|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
689-1272 |
6.75e-162 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 495.84 E-value: 6.75e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 689 SKKVKVTVGRLYSMIRPDWMYGVCGTICAFIAGSQMPLFALGVSQALVSYYSGWDETQkeIKKIAILFCCASVITLIVYT 768
Cdd:COG1132 2 SKSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSA--LLLLLLLLLGLALLRALLSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 769 IEHICFGTMGERLTLRVRENMFRAILKNEIGWFDevDNTSSMLASRLESDATLLKTIVVDRSTILLQNLGLVVTSFIIAF 848
Cdd:COG1132 80 LQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFD--RRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 849 ILNWRLTLVVLATYPLVISGHISEKLFMQGYGGDLNKAYLKANMLAGESVSNIRTVAAFCAEEKILELYSRELLEPSKSS 928
Cdd:COG1132 158 VIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRAN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 929 FRRGQIAGLFYGVSQFFIFSSYGLALWYGSTLMDKGLAGFKSVMkTFMVLIVTAL-AMGETLALAPDLLKGNQMVASVFE 1007
Cdd:COG1132 238 LRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLV-AFILYLLRLFgPLRQLANVLNQLQRALASAERIFE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1008 ILDRKTQIV-GETSEELNNVEGTIELKGVHFSYPSRPDVVifRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTA 1086
Cdd:COG1132 317 LLDEPPEIPdPPGAVPLPPVRGEIEFENVSFSYPGDRPVL--KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTS 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1087 GKVMIEGKDIKKLDLKALRKHIGLVQQEPALFATTIYENILYGNEGASQSEVVESAMLANAHSFITSLPEGYSTKVGERG 1166
Cdd:COG1132 395 GRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1167 VQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVVVAHRLSTIKNADTISVLHGGKIVE 1246
Cdd:COG1132 475 VNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVE 554
|
570 580
....*....|....*....|....*.
gi 79487035 1247 QGSHRKLvLNKSGPYFKLISLQQQQQ 1272
Cdd:COG1132 555 QGTHEEL-LARGGLYARLYRLQFGEE 579
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
55-643 |
2.44e-152 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 470.80 E-value: 2.44e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 55 MTQPKVSLLK-LFSFADFYDcVLMTLGSVGACIHGASVPIFFIFFGKLINIIglaylFPKQASHRVAKYSLDFVYLSVAI 133
Cdd:COG1132 1 MSKSPRKLLRrLLRYLRPYR-GLLILALLLLLLSALLELLLPLLLGRIIDAL-----LAGGDLSALLLLLLLLLGLALLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 134 LFSSWLEVACWMHTGERQAAKMRRAYLRSMLSQDISLFDTeASTGEVISAITSDILVVQDALSEKVGNFLHYISRFIAGF 213
Cdd:COG1132 75 ALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDR-RRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 214 AIGFTSVWQISLVTLSIVPLIALAGGIYAFVAIGLIARVRKSYIKAGEIAEEVIGNVRTVQAFTGEERAVRLYREALENT 293
Cdd:COG1132 154 VVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 294 YKYGRKAGLTKGLGLGSMHCVLFLSWALLVWFTSVVVHKDIADGGK--SFTTMLNVVIAGLS-LGQAapdISAFVRAKAA 370
Cdd:COG1132 234 RRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDlvAFILYLLRLFGPLRqLANV---LNQLQRALAS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 371 AYPIFKMIERnTVTKTSAKSGRKLGKVDGHIQFKDATFSYPSRPDVVifDRLNLAIPAGKIVALVGGSGSGKSTVISLIE 450
Cdd:COG1132 311 AERIFELLDE-PPEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRPVL--KDISLTIPPGETVALVGPSGSGKSTLVNLLL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 451 RFYEPISGAVLLDGNNISELDIKWLRGQIGLVNQEPALFATTIRENILYGKDDATAEEITRAAKLSEAISFINNLPEGFE 530
Cdd:COG1132 388 RFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYD 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 531 TQVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVV 610
Cdd:COG1132 468 TVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVL 547
|
570 580 590
....*....|....*....|....*....|...
gi 79487035 611 HEGKIVEFGNHENLISNpDGAYSSLLRLQETAS 643
Cdd:COG1132 548 DDGRIVEQGTHEELLAR-GGLYARLYRLQFGEE 579
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
76-1269 |
2.94e-151 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 493.78 E-value: 2.94e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 76 LMTLGSVGACIHGASVPIFFIFFGKLINIIGLAylfpkqasHRVAKYSLDFVYLSVAILFSSWLEVACWMHTGERQAAKM 155
Cdd:PTZ00265 61 LLGVSFVCATISGGTLPFFVSVFGVIMKNMNLG--------ENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 156 RRAYLRSMLSQDISLFDTEAStgeviSAITSDILVVQDALSEKVGN----FLHYISRFIAGFAIGFTSVWQISLVTLSIV 231
Cdd:PTZ00265 133 KLEFLKSVFYQDGQFHDNNPG-----SKLTSDLDFYLEQVNAGIGTkfitIFTYASAFLGLYIWSLFKNARLTLCITCVF 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 232 PLIALAGgiyafVAIGLIARVRKSYI-----KAGEIAEEVIGNVRTVQAFTGEERAVRLYREALENTYKYGRKAGLTKGL 306
Cdd:PTZ00265 208 PLIYICG-----VICNKKVKINKKTSllynnNTMSIIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 307 GLGSMHCVLFLSWALLVWFTSVVVHKDIAD--------GGKSFTTMLNVVIAGLSLGQAAPDISAFVRAKAAAYPIFKMI 378
Cdd:PTZ00265 283 HIGMINGFILASYAFGFWYGTRIIISDLSNqqpnndfhGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEII 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 379 ERNTVTKTSaKSGRKLGKVDgHIQFKDATFSYPSRPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISG 458
Cdd:PTZ00265 363 NRKPLVENN-DDGKKLKDIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEG 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 459 AVLL-DGNNISELDIKWLRGQIGLVNQEPALFATTIRENILYG----KD------------------------------- 502
Cdd:PTZ00265 441 DIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslKDlealsnyynedgndsqenknkrnscrakcag 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 503 -------DATAEEITRAAKLSEAIS---------------FINNLPEGFETQVGERGIQLSGGQKQRIAISRAIVKNPSI 560
Cdd:PTZ00265 521 dlndmsnTTDSNELIEMRKNYQTIKdsevvdvskkvlihdFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKI 600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 561 LLLDEATSALDAESEKSVQEALDRVM--VGRTTVVVAHRLSTVRNADIIAVV---------------------------- 610
Cdd:PTZ00265 601 LILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLsnrergstvdvdiigedptkdnkennnk 680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 611 ------------------HEGK-IVEFGNHENLISNPDGAYSSLLRLQETASLQRNPSLNRTLSRPHSIKYS-------- 663
Cdd:PTZ00265 681 nnkddnnnnnnnnnnkinNAGSyIIEQGTHDALMKNKNGIYYTMINNQKVSSKKSSNNDNDKDSDMKSSAYKdsergydp 760
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 664 ---RELSRTRSSFCSERESVTRPDGADPSKKVKVTVGRLYSMIR-----PD---------WMYGVCGTICAF---IAGSQ 723
Cdd:PTZ00265 761 demNGNSKHENESASNKKSCKMSDENASENNAGGKLPFLRNLFKrkpkaPNnlrivyreiFSYKKDVTIIALsilVAGGL 840
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 724 MPLFALGVSQaLVSYYSGWDETQKEIKKIAILFCCASVITLIVYTIEHICFGTMGERLTLRVRENMFRAILKNEIGWFDE 803
Cdd:PTZ00265 841 YPVFALLYAK-YVSTLFDFANLEANSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQ 919
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 804 VDNTSSMLASRLESDATLLKTIVVDRSTILLQNLGLVVTSFIIAFILNWRLTLVVLATY-----------PLVISGHISE 872
Cdd:PTZ00265 920 DKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYFCPIVAAVLTGTYfifmrvfairaRLTANKDVEK 999
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 873 KLFMQG-----YGGDlNKAYLKANMLAGESVSNIRTVAAFCAEEKILELYSRELLEPSKSSFRRGQIAGLFYGVSQ---F 944
Cdd:PTZ00265 1000 KEINQPgtvfaYNSD-DEIFKDPSFLIQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQsaqL 1078
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 945 FIFSsygLALWYGSTLMDKGLAGFKSVMKTFMVLIVTALAMGETLALAPDLLKGNQMVASVFEILDRKTQIV-----GET 1019
Cdd:PTZ00265 1079 FINS---FAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRKSNIDvrdngGIR 1155
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1020 SEELNNVEGTIELKGVHFSYPSRPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYD---------------- 1083
Cdd:PTZ00265 1156 IKNKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtnd 1235
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1084 --------------------------------------PTAGKVMIEGKDIKKLDLKALRKHIGLVQQEPALFATTIYEN 1125
Cdd:PTZ00265 1236 mtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYEN 1315
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1126 ILYGNEGASQSEVVESAMLANAHSFITSLPEGYSTKVGERGVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESER 1205
Cdd:PTZ00265 1316 IKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEK 1395
|
1370 1380 1390 1400 1410 1420 1430
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79487035 1206 VVQQALDRL--MANRTTVVVAHRLSTIKNADTISVLH-----GGKIVEQGSHRKLVLNKSGPYFKLISLQQ 1269
Cdd:PTZ00265 1396 LIEKTIVDIkdKADKTIITIAHRIASIKRSDKIVVFNnpdrtGSFVQAHGTHEELLSVQDGVYKKYVKLAK 1466
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1030-1268 |
6.91e-135 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 411.55 E-value: 6.91e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIG 1109
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1110 LVQQEPALFATTIYENILYGNEGASQSEVVESAMLANAHSFITSLPEGYSTKVGERGVQMSGGQRQRIAIARAILKNPAI 1189
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 1190 LLLDEATSALDVESERVVQQALDRLMANRTTVVVAHRLSTIKNADTISVLHGGKIVEQGSHRKLvLNKSGPYFKLISLQ 1268
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDEL-MAQKGVYAKLVKAQ 238
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
401-639 |
2.10e-134 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 410.01 E-value: 2.10e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIG 480
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 LVNQEPALFATTIRENILYGKDDATAEEITRAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRIAISRAIVKNPSI 560
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 561 LLLDEATSALDAESEKSVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVHEGKIVEFGNHENLISNpDGAYSSLLRLQ 639
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQ-KGVYAKLVKAQ 238
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
680-1269 |
3.00e-122 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 395.36 E-value: 3.00e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 680 VTRPDGADPSKKVKVTVGRLYSMIRPDW-------MYGVCGTICAFIagsqMPLFalgvSQALVSYYSGwDETQKEIKKI 752
Cdd:COG2274 128 LEPTPEFDKRGEKPFGLRWFLRLLRRYRrlllqvlLASLLINLLALA----TPLF----TQVVIDRVLP-NQDLSTLWVL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 753 AILFCCASVITLIVYTIEHICFGTMGERLTLRVRENMFRAILKNEIGWFDevDNTSSMLASRLESDATLLKTIvvdrSTI 832
Cdd:COG2274 199 AIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFE--SRSVGDLASRFRDVESIREFL----TGS 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 833 LLQ---NLGLVVTSFIIAFILNWRLTLVVLATYPLVISghISekLFMQGYGGDLNKAYLKAN-MLAG---ESVSNIRTVA 905
Cdd:COG2274 273 LLTallDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVL--LG--LLFQPRLRRLSREESEASaKRQSllvETLRGIETIK 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 906 AFCAEEKILELYSRELLEPSKSSFRRGQIAGLFYGVSQFFIFSSYGLALWYGSTL-MDKGLagfkSV--MKTFMVLIVTA 982
Cdd:COG2274 349 ALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLvIDGQL----TLgqLIAFNILSGRF 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 983 LA-MGETLALAPDLLKGNQMVASVFEILDRKT-QIVGETSEELNNVEGTIELKGVHFSYPSRPDVVIfRDFDLIVRAGKS 1060
Cdd:COG2274 425 LApVAQLIGLLQRFQDAKIALERLDDILDLPPeREEGRSKLSLPRLKGDIELENVSFRYPGDSPPVL-DNISLTIKPGER 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1061 MALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIGLVQQEPALFATTIYENILYGNEGASQSEVVE 1140
Cdd:COG2274 504 VAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIE 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1141 SAMLANAHSFITSLPEGYSTKVGERGVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANRTT 1220
Cdd:COG2274 584 AARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTV 663
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 79487035 1221 VVVAHRLSTIKNADTISVLHGGKIVEQGSHRKLvLNKSGPYFKLISLQQ 1269
Cdd:COG2274 664 IIIAHRLSTIRLADRIIVLDKGRIVEDGTHEEL-LARKGLYAELVQQQL 711
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
111-639 |
2.98e-121 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 388.29 E-value: 2.98e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 111 FPKQASHRVAKYSLDFVYLSVAILFSSWLEVACWMHTGERQAAKMRRAYLRSMLSQDISLFDTeASTGEVISAITSDILV 190
Cdd:TIGR02204 49 FSKDSSGLLNRYFAFLLVVALVLALGTAARFYLVTWLGERVVADIRRAVFAHLISLSPSFFDK-NRSGEVVSRLTTDTTL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 191 VQDALSEKVGNFLHYISRFIAGFAIGFTSVWQISLVTLSIVPLIALAggiyaFVAIGliARVRK-------SYIKAGEIA 263
Cdd:TIGR02204 128 LQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLP-----ILLFG--RRVRKlsresqdRIADAGSYA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 264 EEVIGNVRTVQAFTGEERAVRLYREALENTYKYGRKAGLTKGLGLGSMHCVLFLSWALLVWFTSVVVHKDIADGGKSFTT 343
Cdd:TIGR02204 201 GETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 344 MLNVVIAGLSLGQAAPDISAFVRAKAAAYPIFKMI-ERNTVTktSAKSGRKLG-KVDGHIQFKDATFSYPSRPDVVIFDR 421
Cdd:TIGR02204 281 VFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLqAEPDIK--APAHPKTLPvPLRGEIEFEQVNFAYPARPDQPALDG 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 422 LNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIGLVNQEPALFATTIRENILYGK 501
Cdd:TIGR02204 359 LNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGR 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 502 DDATAEEITRAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEA 581
Cdd:TIGR02204 439 PDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQA 518
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 582 LDRVMVGRTTVVVAHRLSTVRNADIIAVVHEGKIVEFGNHENLISNpDGAYSSLLRLQ 639
Cdd:TIGR02204 519 LETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAK-GGLYARLARLQ 575
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
690-1257 |
1.10e-120 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 391.39 E-value: 1.10e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 690 KKVKVTVGRLYSMIRPDWMYGVCGTICAFIAGSqmplfalgvSQALVSYYSG----WDETQKEIKKIAI---LFCCASVI 762
Cdd:TIGR00958 143 SETADLLFRLLGLSGRDWPWLISAFVFLTLSSL---------GEMFIPFYTGrvidTLGGDKGPPALASaifFMCLLSIA 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 763 TLIVYTIEHICFGTMGERLTLRVRENMFRAILKNEIGWFDEvdNTSSMLASRLESDATLLKTIVVDRSTILLQNLGLVVT 842
Cdd:TIGR00958 214 SSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDE--NKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLG 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 843 SFIIAFILNWRLTLVVLATYPLVIsghISEKLF---MQGYGGDLNKAYLKANMLAGESVSNIRTVAAFCAEEKILELYsR 919
Cdd:TIGR00958 292 LLGFMLWLSPRLTMVTLINLPLVF---LAEKVFgkrYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRF-K 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 920 ELLEPSKSSFRRGQIAGLFY----GVSQFFIFSsygLALWYGSTLMDKGlAGFKSVMKTFMVL-IVTALAMGETLALAPD 994
Cdd:TIGR00958 368 EALEETLQLNKRKALAYAGYlwttSVLGMLIQV---LVLYYGGQLVLTG-KVSSGNLVSFLLYqEQLGEAVRVLSYVYSG 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 995 LLKGNQMVASVFEILDRKTQIVGETSEELNNVEGTIELKGVHFSYPSRPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSV 1074
Cdd:TIGR00958 444 MMQAVGASEKVFEYLDRKPNIPLTGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTV 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1075 ISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIGLVQQEPALFATTIYENILYGNEGASQSEVVESAMLANAHSFITSL 1154
Cdd:TIGR00958 524 AALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEF 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1155 PEGYSTKVGERGVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQalDRLMANRTTVVVAHRLSTIKNAD 1234
Cdd:TIGR00958 604 PNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERAD 681
|
570 580
....*....|....*....|...
gi 79487035 1235 TISVLHGGKIVEQGSHRKLVLNK 1257
Cdd:TIGR00958 682 QILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
43-636 |
1.60e-120 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 390.62 E-value: 1.60e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 43 PSGDPAPEKEKEMTQPKVSLLKLFSFAD----FYDCVLMTLgsVGACIHGASVPiFFIffGKLINIIGLAYLFPKQAShr 118
Cdd:TIGR00958 130 SAGASEKEAEQGQSETADLLFRLLGLSGrdwpWLISAFVFL--TLSSLGEMFIP-FYT--GRVIDTLGGDKGPPALAS-- 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 119 vAKYSLDFvyLSVAILFSSWLEVACWMHTGERQAAKMRRAYLRSMLSQDISLFDtEASTGEVISAITSDILVVQDALSEK 198
Cdd:TIGR00958 203 -AIFFMCL--LSIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFD-ENKTGELTSRLSSDTQTMSRSLSLN 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 199 VGNFLHYISRFIAGFAIGFTSVWQISLVTLSIVPLIALAGGIYAFVAIGLIARVRKSYIKAGEIAEEVIGNVRTVQAFTG 278
Cdd:TIGR00958 279 VNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAA 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 279 EERAVRLYREALENTYKYGRKAGLTKglglgsmhcvlflswALLVWFTSVVvhkdiadGGKSFTTMLNV----VIAG--- 351
Cdd:TIGR00958 359 EEGEASRFKEALEETLQLNKRKALAY---------------AGYLWTTSVL-------GMLIQVLVLYYggqlVLTGkvs 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 352 -----------LSLGQAAPDISAF----VRAKAAAYPIFKMIERntvTKTSAKSG-RKLGKVDGHIQFKDATFSYPSRPD 415
Cdd:TIGR00958 417 sgnlvsfllyqEQLGEAVRVLSYVysgmMQAVGASEKVFEYLDR---KPNIPLTGtLAPLNLEGLIEFQDVSFSYPNRPD 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 416 VVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIGLVNQEPALFATTIRE 495
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRE 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 496 NILYGKDDATAEEITRAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESE 575
Cdd:TIGR00958 574 NIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECE 653
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79487035 576 KSVQEalDRVMVGRTTVVVAHRLSTVRNADIIAVVHEGKIVEFGNHENLISNPDgAYSSLL 636
Cdd:TIGR00958 654 QLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQG-CYKHLV 711
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
776-1268 |
4.02e-120 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 385.21 E-value: 4.02e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 776 TMGERLTLRVRENMFRAILKNEIGWFDEvdNTSSMLASRLESDATLLKTIVVDRSTILLQNLGLVVTSFIIAFILNWRLT 855
Cdd:TIGR02204 84 WLGERVVADIRRAVFAHLISLSPSFFDK--NRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLT 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 856 LVVLATYPLVIsghisekLFMQGYGGDLNKA-------YLKANMLAGESVSNIRTVAAFCAEEKILELYSRELLEPSKSS 928
Cdd:TIGR02204 162 SLVLLAVPLVL-------LPILLFGRRVRKLsresqdrIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 929 FRRGQIAGLFYGVSQFFIFSSYGLALWYGSTLMdkgLAGFKSVMKTFMVLIVTALAMGETLALAP---DLLKGNQMVASV 1005
Cdd:TIGR02204 235 RQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDV---IAGKMSAGTLGQFVFYAVMVAGSIGTLSEvwgELQRAAGAAERL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1006 FEILDRKTQIVGETSEEL--NNVEGTIELKGVHFSYPSRPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYD 1083
Cdd:TIGR02204 312 IELLQAEPDIKAPAHPKTlpVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYD 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1084 PTAGKVMIEGKDIKKLDLKALRKHIGLVQQEPALFATTIYENILYGNEGASQSEVVESAMLANAHSFITSLPEGYSTKVG 1163
Cdd:TIGR02204 392 PQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLG 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1164 ERGVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVVVAHRLSTIKNADTISVLHGGK 1243
Cdd:TIGR02204 472 ERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGR 551
|
490 500
....*....|....*....|....*
gi 79487035 1244 IVEQGSHRKLVlNKSGPYFKLISLQ 1268
Cdd:TIGR02204 552 IVAQGTHAELI-AKGGLYARLARLQ 575
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
129-639 |
4.33e-113 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 370.70 E-value: 4.33e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 129 LSVAILFSSWLEVA---CWMHTGERQAAKMRRAYLRSMLSQDISLFDTeASTGEVISAItSDILVVQDALSEKVGNFLHY 205
Cdd:COG2274 202 LLLALLFEGLLRLLrsyLLLRLGQRIDLRLSSRFFRHLLRLPLSFFES-RSVGDLASRF-RDVESIREFLTGSLLTALLD 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 206 ISRFIAGFAIGFTSVWQISLVTLSIVPLIALaggIYAFVAIGLIARVRKSYIKAGEIA---EEVIGNVRTVQAFTGEERA 282
Cdd:COG2274 280 LLFVLIFLIVLFFYSPPLALVVLLLIPLYVL---LGLLFQPRLRRLSREESEASAKRQsllVETLRGIETIKALGAESRF 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 283 VRLYREALENTYKYGRKAGLTKGLGLGSMHCVLFLSWALLVWFTSVVVHKD-------IAdggksFTTMLNVVIAGL-SL 354
Cdd:COG2274 357 RRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGqltlgqlIA-----FNILSGRFLAPVaQL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 355 GQAapdISAFVRAKAAAYPIFKMIErNTVTKTSAKSGRKLGKVDGHIQFKDATFSYPSRPDVVIfDRLNLAIPAGKIVAL 434
Cdd:COG2274 432 IGL---LQRFQDAKIALERLDDILD-LPPEREEGRSKLSLPRLKGDIELENVSFRYPGDSPPVL-DNISLTIKPGERVAI 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 435 VGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIGLVNQEPALFATTIRENILYGKDDATAEEITRAAK 514
Cdd:COG2274 507 VGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAAR 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 515 LSEAISFINNLPEGFETQVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRVMVGRTTVVV 594
Cdd:COG2274 587 LAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIII 666
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 79487035 595 AHRLSTVRNADIIAVVHEGKIVEFGNHENLISNpDGAYSSLLRLQ 639
Cdd:COG2274 667 AHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR-KGLYAELVQQQ 710
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1030-1264 |
3.32e-112 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 350.76 E-value: 3.32e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRPDVVIfRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIG 1109
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVL-RDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1110 LVQQEPALFATTIYENILYGNEGASQSEVVESAMLANAHSFITSLPEGYSTKVGERGVQMSGGQRQRIAIARAILKNPAI 1189
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79487035 1190 LLLDEATSALDVESERVVQQALDRLMANRTTVVVAHRLSTIKNADTISVLHGGKIVEQGSHRKLvLNKSGPYFKL 1264
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEEL-LAQGGVYAKL 233
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
401-635 |
1.70e-107 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 338.05 E-value: 1.70e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPDVVIfDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIG 480
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVL-RDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 LVNQEPALFATTIRENILYGKDDATAEEITRAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRIAISRAIVKNPSI 560
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79487035 561 LLLDEATSALDAESEKSVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVHEGKIVEFGNHENLISNpDGAYSSL 635
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQ-GGVYAKL 233
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
837-1272 |
4.53e-107 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 350.66 E-value: 4.53e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 837 LGLVVTSFIIAFILNWRLTLVVLAT---YpLVISGHISE---KLFMQgyggdLNKAYLKANMLAGESVSNIRTVAAFCAE 910
Cdd:COG5265 164 LEIALVAGILLVKYDWWFALITLVTvvlY-IAFTVVVTEwrtKFRRE-----MNEADSEANTRAVDSLLNYETVKYFGNE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 911 EKILELYSRELLEPSKSSfRRGQIAGLFYGVSQFFIFSSyGLALwygstLMdkGLAGFKSVMKTF----MVLiVTALAMG 986
Cdd:COG5265 238 AREARRYDEALARYERAA-VKSQTSLALLNFGQALIIAL-GLTA-----MM--LMAAQGVVAGTMtvgdFVL-VNAYLIQ 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 987 ETL--------------ALApDLlkgNQMvasvFEILDRKTQIVG-ETSEELNNVEGTIELKGVHFSY-PSRPdvvIFRD 1050
Cdd:COG5265 308 LYIplnflgfvyreirqALA-DM---ERM----FDLLDQPPEVADaPDAPPLVVGGGEVRFENVSFGYdPERP---ILKG 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1051 FDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIGLVQQEPALFATTIYENILYGN 1130
Cdd:COG5265 377 VSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGR 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1131 EGASQSEVVESAMLANAHSFITSLPEGYSTKVGERGVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQA 1210
Cdd:COG5265 457 PDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAA 536
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79487035 1211 LDRLMANRTTVVVAHRLSTIKNADTISVLHGGKIVEQGSHRKLvLNKSGPYFKLISLQQQQQ 1272
Cdd:COG5265 537 LREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAEL-LAQGGLYAQMWARQQEEE 597
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
698-1268 |
1.37e-106 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 348.24 E-value: 1.37e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 698 RLYSMIRPDWMYGVCGTICAFIAGSQMPLFAlGVSQALVSYYSGWDETQKeikkiaILFCCASVITLIVytIEHIC--FG 775
Cdd:TIGR02203 4 RLWSYVRPYKAGLVLAGVAMILVAATESTLA-ALLKPLLDDGFGGRDRSV------LWWVPLVVIGLAV--LRGICsfVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 776 TM-----GERLTLRVRENMFRAILKNEIGWFDEvdNTSSMLASRLESDATLLKTIVVDRSTILLQNLGLVVTSFIIAFIL 850
Cdd:TIGR02203 75 TYllswvSNKVVRDIRVRMFEKLLGLPVSFFDR--QPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 851 NWRLTLVVLATYPLV--ISGHISEKL-----FMQGYGGDLNKAylkanmlAGESVSNIRTVAAFCAEEKILELYSRELLE 923
Cdd:TIGR02203 153 SWQLTLIVVVMLPVLsiLMRRVSKRLrriskEIQNSMGQVTTV-------AEETLQGYRVVKLFGGQAYETRRFDAVSNR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 924 PSKSSFRRGQIAGLFYGVSQFFIFSSYGLALWygstlmdkgLAGFKSVMKT-----FMVLIVTALAMGETLA----LAPD 994
Cdd:TIGR02203 226 NRRLAMKMTSAGSISSPITQLIASLALAVVLF---------IALFQAQAGSltagdFTAFITAMIALIRPLKsltnVNAP 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 995 LLKGNQMVASVFEILDrKTQIVGETSEELNNVEGTIELKGVHFSYPSRpDVVIFRDFDLIVRAGKSMALVGQSGSGKSSV 1074
Cdd:TIGR02203 297 MQRGLAAAESLFTLLD-SPPEKDTGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTL 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1075 ISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIGLVQQEPALFATTIYENILYGN-EGASQSEVVESAMLANAHSFITS 1153
Cdd:TIGR02203 375 VNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDK 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1154 LPEGYSTKVGERGVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVVVAHRLSTIKNA 1233
Cdd:TIGR02203 455 LPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKA 534
|
570 580 590
....*....|....*....|....*....|....*
gi 79487035 1234 DTISVLHGGKIVEQGSHRKLvLNKSGPYFKLISLQ 1268
Cdd:TIGR02203 535 DRIVVMDDGRIVERGTHNEL-LARNGLYAQLHNMQ 568
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
700-1015 |
2.23e-106 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 338.27 E-value: 2.23e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 700 YSMIRPDWMYGVCGTICAFIAGSQMPLFALGVSQALVSYY-SGWDETQKEIKKIAILFCCASVITLIVYTIEHICFGTMG 778
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSlPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 779 ERLTLRVRENMFRAILKNEIGWFDEVDNTSSMLASRLESDATLLKTIVVDRSTILLQNLGLVVTSFIIAFILNWRLTLVV 858
Cdd:cd18578 81 ERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 859 LATYPLVISGHISEKLFMQGYGGDLNKAYLKANMLAGESVSNIRTVAAFCAEEKILELYSRELLEPSKSSFRRGQIAGLF 938
Cdd:cd18578 161 LATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLG 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79487035 939 YGVSQFFIFSSYGLALWYGSTLMDKGLAGFKSVMKTFMVLIVTALAMGETLALAPDLLKGNQMVASVFEILDRKTQI 1015
Cdd:cd18578 241 FGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1030-1268 |
6.02e-105 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 331.12 E-value: 6.02e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSY-PSRPdvvIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHI 1108
Cdd:cd03253 1 IEFENVTFAYdPGRP---VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1109 GLVQQEPALFATTIYENILYGNEGASQSEVVESAMLANAHSFITSLPEGYSTKVGERGVQMSGGQRQRIAIARAILKNPA 1188
Cdd:cd03253 78 GVVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1189 ILLLDEATSALDVESERVVQQALDRLMANRTTVVVAHRLSTIKNADTISVLHGGKIVEQGSHRKLvLNKSGPYFKLISLQ 1268
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEEL-LAKGGLYAEMWKAQ 236
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
77-374 |
2.51e-103 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 329.44 E-value: 2.51e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 77 MTLGSVGACIHGASVPIFFIFFGKLINII---GLAYLFPKQASHRVAKYSLDFVYLSVAILFSSWLEVACWMHTGERQAA 153
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFtdfGSGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 154 KMRRAYLRSMLSQDISLFDTeASTGEVISAITSDILVVQDALSEKVGNFLHYISRFIAGFAIGFTSVWQISLVTLSIVPL 233
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDK-NGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 234 IALAGGIYAFVAIGLIARVRKSYIKAGEIAEEVIGNVRTVQAFTGEERAVRLYREALENTYKYGRKAGLTKGLGLGSMHC 313
Cdd:cd18577 160 IAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFF 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79487035 314 VLFLSWALLVWFTSVVVHKDIADGGKSFTTMLNVVIAGLSLGQAAPDISAFVRAKAAAYPI 374
Cdd:cd18577 240 IIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
401-639 |
2.61e-99 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 316.09 E-value: 2.61e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSY-PSRPdvvIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQI 479
Cdd:cd03253 1 IEFENVTFAYdPGRP---VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 480 GLVNQEPALFATTIRENILYGKDDATAEEITRAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRIAISRAIVKNPS 559
Cdd:cd03253 78 GVVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 560 ILLLDEATSALDAESEKSVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVHEGKIVEFGNHENLIsNPDGAYSSLLRLQ 639
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELL-AKGGLYAEMWKAQ 236
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
154-639 |
3.74e-99 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 328.21 E-value: 3.74e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 154 KMRRAYLRSMLSQDISLFDtEASTGEVISAITSDILVVQDALSEKVGNFLHYISRFIAGFAIGFTSVWQISLVTLSIVPL 233
Cdd:TIGR02203 88 DIRVRMFEKLLGLPVSFFD-RQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 234 IALAGGIYAFVAIGLIARVRKSYIKAGEIAEEVIGNVRTVQAFTGEERAVRLYREALENTYKYGRKAGLTKGLGLGSMHC 313
Cdd:TIGR02203 167 LSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 314 VLFLSWALLVWFTSVVVHKDIADGGkSFTTMLNVVIAGLSLGQAAPDISA-FVRAKAAAYPIFKMIERntvTKTSAKSGR 392
Cdd:TIGR02203 247 IASLALAVVLFIALFQAQAGSLTAG-DFTAFITAMIALIRPLKSLTNVNApMQRGLAAAESLFTLLDS---PPEKDTGTR 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 393 KLGKVDGHIQFKDATFSYPSRpDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDI 472
Cdd:TIGR02203 323 AIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTL 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 473 KWLRGQIGLVNQEPALFATTIRENILYGK-DDATAEEITRAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRIAIS 551
Cdd:TIGR02203 402 ASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIA 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 552 RAIVKNPSILLLDEATSALDAESEKSVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVHEGKIVEFGNHENLISNpDGA 631
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLAR-NGL 560
|
....*...
gi 79487035 632 YSSLLRLQ 639
Cdd:TIGR02203 561 YAQLHNMQ 568
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
398-639 |
1.07e-97 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 325.24 E-value: 1.07e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 398 DGHIQFKDATFSY-PSRPdvvIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLR 476
Cdd:COG5265 355 GGEVRFENVSFGYdPERP---ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 477 GQIGLVNQEPALFATTIRENILYGKDDATAEEITRAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRIAISRAIVK 556
Cdd:COG5265 432 AAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLK 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 557 NPSILLLDEATSALDAESEKSVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVHEGKIVEFGNHENLISNpDGAYSSLL 636
Cdd:COG5265 512 NPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQ-GGLYAQMW 590
|
...
gi 79487035 637 RLQ 639
Cdd:COG5265 591 ARQ 593
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1028-1257 |
1.71e-95 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 305.30 E-value: 1.71e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1028 GTIELKGVHFSYpsRPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKH 1107
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1108 IGLVQQEPALFATTIYENILYGNEGASQSEVVESAMLANAHSFITSLPEGYSTKVGERGVQMSGGQRQRIAIARAILKNP 1187
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1188 AILLLDEATSALDVESERVVQQALDRLMANRTTVVVAHRLSTIKNADTISVLHGGKIVEQGSHRKLVLNK 1257
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
399-625 |
2.31e-93 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 299.53 E-value: 2.31e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 399 GHIQFKDATFSYpsRPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQ 478
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 479 IGLVNQEPALFATTIRENILYGKDDATAEEITRAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRIAISRAIVKNP 558
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79487035 559 SILLLDEATSALDAESEKSVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVHEGKIVEFGNHENLI 625
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
155-639 |
2.54e-93 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 312.34 E-value: 2.54e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 155 MRRAYLRSMLSQDISLFDTEaSTGEVISAITSDILVVQDALSEKVGNFLHYISRFIAGFAIGFTSVWQISLVTLSIVPLI 234
Cdd:PRK11176 100 MRRRLFGHMMGMPVSFFDKQ-STGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVIAPIV 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 235 AlaggiyafVAIGLIARVRKSYIK-----AGEI---AEEVIGNVRTVQAFTGEERAVRLYREALENTYKYGRKAGLTKGL 306
Cdd:PRK11176 179 S--------IAIRVVSKRFRNISKnmqntMGQVttsAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASSI 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 307 GLGSMHCVLFLSWALLVWFTSVVVHKDIADGGkSFTTMLNVVIAGLSLGQAAPDISA-FVRAKAAAYPIFKMIERNTvTK 385
Cdd:PRK11176 251 SDPIIQLIASLALAFVLYAASFPSVMDTLTAG-TITVVFSSMIALMRPLKSLTNVNAqFQRGMAACQTLFAILDLEQ-EK 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 386 TSAKsgRKLGKVDGHIQFKDATFSYPSRpDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGN 465
Cdd:PRK11176 329 DEGK--RVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGH 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 466 NISELDIKWLRGQIGLVNQEPALFATTIRENILYGKDDA-TAEEITRAAKLSEAISFINNLPEGFETQVGERGIQLSGGQ 544
Cdd:PRK11176 406 DLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQ 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 545 KQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVHEGKIVEFGNHENL 624
Cdd:PRK11176 486 RQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAEL 565
|
490
....*....|....*
gi 79487035 625 ISNpDGAYSSLLRLQ 639
Cdd:PRK11176 566 LAQ-NGVYAQLHKMQ 579
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
698-1254 |
3.74e-93 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 311.31 E-value: 3.74e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 698 RLYSMIRPDWMYGVCGTICAFIAGSQMPLFALGVSQALVSYYSGWDETQKEIKKIAILFCCASVITLIVYTIEHICFgTM 777
Cdd:COG4988 7 RLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAF-RA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 778 GERLTLRVRENMFRAILKNEIGWfdevdntssmlaSRLESDATLLkTIVVDR--------STILLQNLGLVVTSFII--- 846
Cdd:COG4988 86 AARVKRRLRRRLLEKLLALGPAW------------LRGKSTGELA-TLLTEGvealdgyfARYLPQLFLAALVPLLIlva 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 847 AFILNWRLTLVVLATYPLVIsghisekLFMQ--GYG-GDLNKAYLKA-NMLAG---ESVSNIRTVAAFCAEEKilelYSR 919
Cdd:COG4988 153 VFPLDWLSGLILLVTAPLIP-------LFMIlvGKGaAKASRRQWRAlARLSGhflDRLRGLTTLKLFGRAKA----EAE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 920 ELLEPSKSsFRRG-----QIAGLFYGVSQFFIFSSYGLALWY-GSTLMDKGLagfkSVMKTFMVLIvtalamgetlaLAP 993
Cdd:COG4988 222 RIAEASED-FRKRtmkvlRVAFLSSAVLEFFASLSIALVAVYiGFRLLGGSL----TLFAALFVLL-----------LAP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 994 DL--------------LKGNQMVASVFEILDRKTQIVGETSEELNNVEG-TIELKGVHFSYPSRPDVVifRDFDLIVRAG 1058
Cdd:COG4988 286 EFflplrdlgsfyharANGIAAAEKIFALLDAPEPAAPAGTAPLPAAGPpSIELEDVSFSYPGGRPAL--DGLSLTIPPG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1059 KSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIGLVQQEPALFATTIYENILYGNEGASQSEV 1138
Cdd:COG4988 364 ERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEEL 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1139 VESAMLANAHSFITSLPEGYSTKVGERGVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANR 1218
Cdd:COG4988 444 EAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR 523
|
570 580 590
....*....|....*....|....*....|....*.
gi 79487035 1219 TTVVVAHRLSTIKNADTISVLHGGKIVEQGSHRKLV 1254
Cdd:COG4988 524 TVILITHRLALLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
221-639 |
1.11e-88 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 299.57 E-value: 1.11e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 221 WQISLVtlsivpLIALAGgiyAFVAIG---------LIARVRKSYIKAGEIAEEVIGNVRTVQAFT---GEERAVRLYRE 288
Cdd:PRK13657 156 WRLSLV------LVVLGI---VYTLITtlvmrktkdGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNrieAETQALRDIAD 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 289 ALENTYK-----YGRKAGLTKGLGLGSMHCVLFLSWALlvwftsvvVHKDIADGGK-----SFTTMLnvvIAGLSLgqaa 358
Cdd:PRK13657 227 NLLAAQMpvlswWALASVLNRAASTITMLAILVLGAAL--------VQKGQLRVGEvvafvGFATLL---IGRLDQ---- 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 359 pdISAFV------RAKAAAYpiFKMIerNTVTKTSAKSG-RKLGKVDGHIQFKDATFSYPSRPDVVifDRLNLAIPAGKI 431
Cdd:PRK13657 292 --VVAFInqvfmaAPKLEEF--FEVE--DAVPDVRDPPGaIDLGRVKGAVEFDDVSFSYDNSRQGV--EDVSFEAKPGQT 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 432 VALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIGLVNQEPALFATTIRENILYGKDDATAEEITR 511
Cdd:PRK13657 364 VAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRA 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 512 AAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRVMVGRTT 591
Cdd:PRK13657 444 AAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTT 523
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 79487035 592 VVVAHRLSTVRNADIIAVVHEGKIVEFGNHENLISNpDGAYSSLLRLQ 639
Cdd:PRK13657 524 FIIAHRLSTVRNADRILVFDNGRVVESGSFDELVAR-GGRFAALLRAQ 570
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
367-627 |
1.90e-88 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 298.21 E-value: 1.90e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 367 AKAAAYPIFKMIERNtVTKTSAKSGRKLGKVDGHIQFKDATFSYPSRPDVVifDRLNLAIPAGKIVALVGGSGSGKSTVI 446
Cdd:COG4988 304 GIAAAEKIFALLDAP-EPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRPAL--DGLSLTIPPGERVALVGPSGAGKSTLL 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 447 SLIERFYEPISGAVLLDGNNISELDIKWLRGQIGLVNQEPALFATTIRENILYGKDDATAEEITRAAKLSEAISFINNLP 526
Cdd:COG4988 381 NLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALP 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 527 EGFETQVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRVMVGRTTVVVAHRLSTVRNADI 606
Cdd:COG4988 461 DGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADR 540
|
250 260
....*....|....*....|.
gi 79487035 607 IAVVHEGKIVEFGNHENLISN 627
Cdd:COG4988 541 ILVLDDGRIVEQGTHEELLAK 561
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
778-1267 |
6.86e-87 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 293.98 E-value: 6.86e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 778 GERL-----TLRV----RENMFRAILKNEIGWFdeVDNTSSMLASRLESDatllktivVDRstilLQNL----------G 838
Cdd:COG4987 74 LERLvshdaTLRLladlRVRLYRRLEPLAPAGL--ARLRSGDLLNRLVAD--------VDA----LDNLylrvllpllvA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 839 LVVTSFIIAFI--LNWRLTLVVLATY-------PLV---ISGHISEKLfmqgyggdlnkAYLKANM--LAGESVSNIRTV 904
Cdd:COG4987 140 LLVILAAVAFLafFSPALALVLALGLllaglllPLLaarLGRRAGRRL-----------AAARAALraRLTDLLQGAAEL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 905 AAFCAEEKILELYSRELLEPSKSSFRRGQIAGLFYGVSQFFIFSSYGLALWYGSTLMDKG-LAGfksvmkTFMVLIV-TA 982
Cdd:COG4987 209 AAYGALDRALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGaLSG------PLLALLVlAA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 983 LAMGETLALAPD-LLKGNQMVAS---VFEILDRKTQIVGETSEELNNVEGTIELKGVHFSYPSRPDVViFRDFDLIVRAG 1058
Cdd:COG4987 283 LALFEALAPLPAaAQHLGRVRAAarrLNELLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRPV-LDGLSLTLPPG 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1059 KSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIGLVQQEPALFATTIYENILYGNEGASQSEV 1138
Cdd:COG4987 362 ERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEEL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1139 VESAMLANAHSFITSLPEGYSTKVGERGVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANR 1218
Cdd:COG4987 442 WAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR 521
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 79487035 1219 TTVVVAHRLSTIKNADTISVLHGGKIVEQGSHRKLvLNKSGPYFKLISL 1267
Cdd:COG4987 522 TVLLITHRLAGLERMDRILVLEDGRIVEQGTHEEL-LAQNGRYRQLYQR 569
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
846-1254 |
2.25e-85 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 290.32 E-value: 2.25e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 846 IAFILNWRLT--LVVLATYPLVISGHISEKLF-MQG----YGGDLNKAylkanmlAGESVSNIRTVAAFC---AEEKILE 915
Cdd:PRK13657 150 LALFMNWRLSlvLVVLGIVYTLITTLVMRKTKdGQAaveeHYHDLFAH-------VSDAIGNVSVVQSYNrieAETQALR 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 916 LYSRELLEpskssfrrgqiaglfygvSQFFIFSSYGLA---------------LWYGSTLMDKGLA---------GFKSV 971
Cdd:PRK13657 223 DIADNLLA------------------AQMPVLSWWALAsvlnraastitmlaiLVLGAALVQKGQLrvgevvafvGFATL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 972 -------MKTFMVLIVTAlamgetlalAPDLLKGNQMVASVFEILDRKTQIvgetseELNNVEGTIELKGVHFSYPSRPD 1044
Cdd:PRK13657 285 ligrldqVVAFINQVFMA---------APKLEEFFEVEDAVPDVRDPPGAI------DLGRVKGAVEFDDVSFSYDNSRQ 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1045 VVifRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIGLVQQEPALFATTIYE 1124
Cdd:PRK13657 350 GV--EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIED 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1125 NILYGNEGASQSEVVESAMLANAHSFITSLPEGYSTKVGERGVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESE 1204
Cdd:PRK13657 428 NIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETE 507
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 79487035 1205 RVVQQALDRLMANRTTVVVAHRLSTIKNADTISVLHGGKIVEQGSHRKLV 1254
Cdd:PRK13657 508 AKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELV 557
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1030-1268 |
7.89e-85 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 276.29 E-value: 7.89e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYpsRPD-VVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHI 1108
Cdd:cd03252 1 ITFEHVRFRY--KPDgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1109 GLVQQEPALFATTIYENILYGNEGASQSEVVESAMLANAHSFITSLPEGYSTKVGERGVQMSGGQRQRIAIARAILKNPA 1188
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1189 ILLLDEATSALDVESERVVQQALDRLMANRTTVVVAHRLSTIKNADTISVLHGGKIVEQGSHRKLvLNKSGPYFKLISLQ 1268
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDEL-LAENGLYAYLYQLQ 237
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
176-638 |
1.53e-82 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 281.65 E-value: 1.53e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 176 STGEVISAITSDILVVQDAlsekvgnFLHYISRFIAGFAIGFTSVWqislVTLSIVPLIALAGGIYAFVAIGLI-ARVRK 254
Cdd:COG4987 110 RSGDLLNRLVADVDALDNL-------YLRVLLPLLVALLVILAAVA----FLAFFSPALALVLALGLLLAGLLLpLLAAR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 255 SYIKAGEIAEEVIGNVRT-----------VQAFTGEERAVRLYREALENTYKYGRKAGLTKGLGLGSMHCVLFLSWALLV 323
Cdd:COG4987 179 LGRRAGRRLAAARAALRArltdllqgaaeLAAYGALDRALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 324 WFTSVVVhkdiADGGKSFTTMLNVVIAGLSLGQA-APDISAFV---RAKAAAYPIFKMIERNTVTKTSAKSGRKLGkvDG 399
Cdd:COG4987 259 WLAAPLV----AAGALSGPLLALLVLAALALFEAlAPLPAAAQhlgRVRAAARRLNELLDAPPAVTEPAEPAPAPG--GP 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 400 HIQFKDATFSYPSRPDVViFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQI 479
Cdd:COG4987 333 SLELEDVSFRYPGAGRPV-LDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRI 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 480 GLVNQEPALFATTIRENILYGKDDATAEEITRAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRIAISRAIVKNPS 559
Cdd:COG4987 412 AVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAP 491
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 560 ILLLDEATSALDAESEKSVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVHEGKIVEFGNHENLISNPdGAYSSLLRL 638
Cdd:COG4987 492 ILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQN-GRYRQLYQR 569
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
783-1268 |
6.21e-82 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 280.37 E-value: 6.21e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 783 LRVRENMFRAILKNEIGWFDEvdNTSSMLASRLESDATL--------LKTIVVDRSTILlqnlGLvvtsFIIAFILNWRL 854
Cdd:PRK11176 98 MTMRRRLFGHMMGMPVSFFDK--QSTGTLLSRITYDSEQvassssgaLITVVREGASII----GL----FIMMFYYSWQL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 855 TLVVLATYPLV-ISGHISEKLF------MQGYGGDLNKAylKANMLAGESVsnirtVAAFCAEEKILELYSRELLEPSKS 927
Cdd:PRK11176 168 SLILIVIAPIVsIAIRVVSKRFrnisknMQNTMGQVTTS--AEQMLKGHKE-----VLIFGGQEVETKRFDKVSNRMRQQ 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 928 SFRRGQIAGLFYGVSQFFifSSYGLA-LWYgstlmdkgLAGFKSVMK-----TFMVLIVTALAMGETL----ALAPDLLK 997
Cdd:PRK11176 241 GMKMVSASSISDPIIQLI--ASLALAfVLY--------AASFPSVMDtltagTITVVFSSMIALMRPLksltNVNAQFQR 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 998 GnqMVA--SVFEILDRKTQiVGETSEELNNVEGTIELKGVHFSYPSRpDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVI 1075
Cdd:PRK11176 311 G--MAAcqTLFAILDLEQE-KDEGKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIA 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1076 SLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIGLVQQEPALFATTIYENILYGNEGA-SQSEVVESAMLANAHSFITSL 1154
Cdd:PRK11176 387 NLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKM 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1155 PEGYSTKVGERGVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVVVAHRLSTIKNAD 1234
Cdd:PRK11176 467 DNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKAD 546
|
490 500 510
....*....|....*....|....*....|....
gi 79487035 1235 TISVLHGGKIVEQGSHRKLvLNKSGPYFKLISLQ 1268
Cdd:PRK11176 547 EILVVEDGEIVERGTHAEL-LAQNGVYAQLHKMQ 579
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
401-639 |
1.41e-80 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 264.35 E-value: 1.41e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYpsRPD-VVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQI 479
Cdd:cd03252 1 ITFEHVRFRY--KPDgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 480 GLVNQEPALFATTIRENILYGKDDATAEEITRAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRIAISRAIVKNPS 559
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 560 ILLLDEATSALDAESEKSVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVHEGKIVEFGNHENLISNpDGAYSSLLRLQ 639
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE-NGLYAYLYQLQ 237
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
397-615 |
1.93e-80 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 263.56 E-value: 1.93e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 397 VDGHIQFKDATFSYPSRPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLR 476
Cdd:cd03248 8 LKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 477 GQIGLVNQEPALFATTIRENILYGKDDATAEEITRAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRIAISRAIVK 556
Cdd:cd03248 88 SKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 557 NPSILLLDEATSALDAESEKSVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVHEGKI 615
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1025-1244 |
2.95e-80 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 262.79 E-value: 2.95e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1025 NVEGTIELKGVHFSYPSRPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKAL 1104
Cdd:cd03248 7 HLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1105 RKHIGLVQQEPALFATTIYENILYGNEGASQSEVVESAMLANAHSFITSLPEGYSTKVGERGVQMSGGQRQRIAIARAIL 1184
Cdd:cd03248 87 HSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1185 KNPAILLLDEATSALDVESERVVQQALDRLMANRTTVVVAHRLSTIKNADTISVLHGGKI 1244
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1030-1243 |
5.26e-77 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 251.53 E-value: 5.26e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRPDVViFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIG 1109
Cdd:cd03228 1 IEFKNVSFSYPGRPKPV-LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1110 LVQQEPALFATTIYENILygnegasqsevvesamlanahsfitslpegystkvgergvqmSGGQRQRIAIARAILKNPAI 1189
Cdd:cd03228 80 YVPQDPFLFSGTIRENIL------------------------------------------SGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 79487035 1190 LLLDEATSALDVESERVVQQALDRLMANRTTVVVAHRLSTIKNADTISVLHGGK 1243
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
123-639 |
1.08e-75 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 265.84 E-value: 1.08e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 123 SLDFVYLSVAILFSSWLEVACWMHTGERQAAKMRRAYLRSMLSQDISLFdTEASTGEVISAITSdilvvqdalsekvgnf 202
Cdd:TIGR01846 182 ALAMLAVAIFEPALGGLRTYLFAHLTSRIDVELGARLYRHLLGLPLGYF-ESRRVGDTVARVRE---------------- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 203 LHYISRFIAG----------FAIGFTSVWQISLVTLSIVPLIALAggIYAFVAIGLIARVRK----SYIKAGE----IAE 264
Cdd:TIGR01846 245 LEQIRNFLTGsaltvvldllFVVVFLAVMFFYSPTLTGVVIGSLV--CYALLSVFVGPILRKrvedKFERSAAatsfLVE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 265 EVIGnVRTVQAFTGEERAVRLYREALENTYKYGRKAGLTKGLGLGSMHCVLFLSWALLVWF-TSVVVHKDIADGGKSFTT 343
Cdd:TIGR01846 323 SVTG-IETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFgAHLVIGGALSPGQLVAFN 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 344 MLNVVIAG--LSLGQAAPDisaFVRAKAAaypifkmIER-----NTVTKTSAKSGRKLGKVDGHIQFKDATFSYpsRPDV 416
Cdd:TIGR01846 402 MLAGRVTQpvLRLAQLWQD---FQQTGIA-------LERlgdilNSPTEPRSAGLAALPELRGAITFENIRFRY--APDS 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 417 -VIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIGLVNQEPALFATTIRE 495
Cdd:TIGR01846 470 pEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRD 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 496 NILYGKDDATAEEITRAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESE 575
Cdd:TIGR01846 550 NIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESE 629
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79487035 576 KSVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVHEGKIVEFGNHENLISNpDGAYSSLLRLQ 639
Cdd:TIGR01846 630 ALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLAL-QGLYARLWQQQ 692
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
833-1268 |
5.38e-75 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 263.91 E-value: 5.38e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 833 LLQNLGLVVTSFIIAFILNWRLTLVVLATYP------LVISGHISEKLFMQGYGGDLNKAYLKanmlagESVSNIRTVAA 906
Cdd:TIGR01846 259 VVLDLLFVVVFLAVMFFYSPTLTGVVIGSLVcyallsVFVGPILRKRVEDKFERSAAATSFLV------ESVTGIETIKA 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 907 FCAEEKILELYSRELLEPSKSSFRRGQIAGLFYGVSQFFIFSSYGLALWYGSTLMdkgLAGFKSVMKTFMVLIVTALAMG 986
Cdd:TIGR01846 333 TATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLV---IGGALSPGQLVAFNMLAGRVTQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 987 ETLALAP---DLLKGNQMVASVFEILDRKTQIVGETSEELNNVEGTIELKGVHFSYpsRPDV-VIFRDFDLIVRAGKSMA 1062
Cdd:TIGR01846 410 PVLRLAQlwqDFQQTGIALERLGDILNSPTEPRSAGLAALPELRGAITFENIRFRY--APDSpEVLSNLNLDIKPGEFIG 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1063 LVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIGLVQQEPALFATTIYENILYGNEGASQSEVVESA 1142
Cdd:TIGR01846 488 IVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAA 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1143 MLANAHSFITSLPEGYSTKVGERGVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVV 1222
Cdd:TIGR01846 568 KLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVII 647
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 79487035 1223 VAHRLSTIKNADTISVLHGGKIVEQGSHRKLvLNKSGPYFKLISLQ 1268
Cdd:TIGR01846 648 IAHRLSTVRACDRIIVLEKGQIAESGRHEEL-LALQGLYARLWQQQ 692
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
401-614 |
8.83e-75 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 245.37 E-value: 8.83e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPDVVIFDrLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIG 480
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKD-VSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 LVNQEPALFATTIRENIlygkddataeeitraaklseaisfinnlpegfetqvgergiqLSGGQKQRIAISRAIVKNPSI 560
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 79487035 561 LLLDEATSALDAESEKSVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVHEGK 614
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1028-1248 |
3.97e-70 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 234.02 E-value: 3.97e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1028 GTIELKGVHFSYPSRPDVVIfRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKH 1107
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPAL-DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1108 IGLVQQEPALFATTIYENILYGNEGASQSEVVESAMLANAHSFITSLPEGYSTKVGERGVQMSGGQRQRIAIARAILKNP 1187
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79487035 1188 AILLLDEATSALDVESERVVQQALDRLMANRTTVVVAHRLSTIKNADTISVLHGGKIVEQG 1248
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
745-1265 |
8.81e-70 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 245.95 E-value: 8.81e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 745 TQKEIKKIAILFCCASVITLIVYTIEHICFGTMGERLTLRVRENMFRAILKNEIGWFDEvDNTSSMLASRLESDATLLKT 824
Cdd:TIGR01192 51 SKSDVLPTLALWAGFGVFNTIAYVLVAREADRLAHGRRATLLTEAFGRIISMPLSWHQQ-RGTSNALHTLLRATETLFGL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 825 IVvdrsTILLQNLGLVVTSFII---AFILNWRLT--LVVLATYPLVISghiseKLFMQ-GYGGDLNKAYLKANMLA--GE 896
Cdd:TIGR01192 130 WL----EFMRQHLATFVALFLLiptAFAMDWRLSivLMVLGILYILIA-----KLVMQrTKNGQAAVEHHYHNVFKhvSD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 897 SVSNIRTVAAF---CAEEKILELYSRELLEpskssfrrgqiaglfygvSQFFIFSSYGLAlwygstlmdKGLAGFKSVMK 973
Cdd:TIGR01192 201 SISNVSVVHSYnriEAETSALKQFTNNLLS------------------AQYPVLDWWALA---------SGLNRMASTIS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 974 TFMVLIVTA-------LAMGETLALA--PDLLKG--NQMVASVFEILDRKTQI---------VGETSE-----ELNNVEG 1028
Cdd:TIGR01192 254 MMCILVIGTvlvikgeLSVGEVIAFIgfANLLIGrlDQMSGFITQIFEARAKLedffdledsVFQREEpadapELPNVKG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1029 TIELKGVHFSYPSRPDVVifRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHI 1108
Cdd:TIGR01192 334 AVEFRHITFEFANSSQGV--FDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSI 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1109 GLVQQEPALFATTIYENILYGNEGASQSEVVESAMLANAHSFITSLPEGYSTKVGERGVQMSGGQRQRIAIARAILKNPA 1188
Cdd:TIGR01192 412 ATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAP 491
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79487035 1189 ILLLDEATSALDVESERVVQQALDRLMANRTTVVVAHRLSTIKNADTISVLHGGKIVEQGSHRKLVlNKSGPYFKLI 1265
Cdd:TIGR01192 492 ILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELI-QKDGRFYKLL 567
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
399-616 |
9.19e-70 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 232.87 E-value: 9.19e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 399 GHIQFKDATFSYPSRPDVVIfDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQ 478
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPAL-DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 479 IGLVNQEPALFATTIRENILYGKDDATAEEITRAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRIAISRAIVKNP 558
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 559 SILLLDEATSALDAESEKSVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVHEGKIV 616
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
715-1239 |
2.77e-67 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 236.80 E-value: 2.77e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 715 ICAFIAGSQMPLFALGVSQALVSYYS---GWDETQKEIKKIAILFCCASVITLIVytiehicfGTMGERLTLRV----RE 787
Cdd:TIGR02857 10 LLGVLGALLIIAQAWLLARVVDGLISagePLAELLPALGALALVLLLRALLGWLQ--------ERAAARAAAAVksqlRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 788 NMFRAILKNEIGWFDEVD--NTSSMLASRLES-DATLLKTIVVdrstillQNLGLVVTSFIIAFIL--NWRLTLVVLATY 862
Cdd:TIGR02857 82 RLLEAVAALGPRWLQGRPsgELATLALEGVEAlDGYFARYLPQ-------LVLAVIVPLAILAAVFpqDWISGLILLLTA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 863 PLVIsghisekLFMQ--GYGG-DLNKAYLKA-NMLAG---ESVSNIRTVAAFCAEEKilelySRELLEPSKSSFRRG--- 932
Cdd:TIGR02857 155 PLIP-------IFMIliGWAAqAAARKQWAAlSRLSGhflDRLRGLPTLKLFGRAKA-----QAAAIRRSSEEYRERtmr 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 933 --QIAGLFYGVSQFFIFSSYGL-ALWYGSTLMDKGLAGFKSvmktFMVLIvtalamgetlaLAPDL-------------- 995
Cdd:TIGR02857 223 vlRIAFLSSAVLELFATLSVALvAVYIGFRLLAGDLDLATG----LFVLL-----------LAPEFylplrqlgaqyhar 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 996 LKGNQMVASVFEILDRKTQIVGETSEELNNVEGTIELKGVHFSYPSRPDVVifRDFDLIVRAGKSMALVGQSGSGKSSVI 1075
Cdd:TIGR02857 288 ADGVAAAEALFAVLDAAPRPLAGKAPVTAAPASSLEFSGVSVAYPGRRPAL--RPVSFTVPPGERVALVGPSGAGKSTLL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1076 SLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIGLVQQEPALFATTIYENILYGNEGASQSEVVESAMLANAHSFITSLP 1155
Cdd:TIGR02857 366 NLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALP 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1156 EGYSTKVGERGVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVVVAHRLSTIKNADT 1235
Cdd:TIGR02857 446 QGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADR 525
|
....
gi 79487035 1236 ISVL 1239
Cdd:TIGR02857 526 IVVL 529
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
780-1266 |
4.46e-67 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 241.00 E-value: 4.46e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 780 RLTLRVRENMFRAILKNEIGWFDEvdNTSSMLASRLESDATLLKTIVVDRSTILLqNLGLVVTSFIIAFILNWRLTLVVL 859
Cdd:TIGR03796 224 KLAVGMSARFLWHILRLPVRFFAQ--RHAGDIASRVQLNDQVAEFLSGQLATTAL-DAVMLVFYALLMLLYDPVLTLIGI 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 860 ATYPLVIsghisekLFMQGYGG---DLN-KAYLKANMLAGESVS---NIRTVAAFCAEE----KILELYSRELLEPSKSS 928
Cdd:TIGR03796 301 AFAAINV-------LALQLVSRrrvDANrRLQQDAGKLTGVAISglqSIETLKASGLESdffsRWAGYQAKLLNAQQELG 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 929 fRRGQIAGLfygVSQFFIFSSYGLALWYGSTLMDKG------LAGFKSVMKTFMVLIVTALAMGETLA-LAPDLLKGNQM 1001
Cdd:TIGR03796 374 -VLTQILGV---LPTLLTSLNSALILVVGGLRVMEGqltigmLVAFQSLMSSFLEPVNNLVGFGGTLQeLEGDLNRLDDV 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1002 VASVFEILDRKTQIVGETSEELNNVEGTIELKGVHFSYpSRPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRF 1081
Cdd:TIGR03796 450 LRNPVDPLLEEPEGSAATSEPPRRLSGYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGL 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1082 YDPTAGKVMIEGKDIKKLDLKALRKHIGLVQQEPALFATTIYENILYGNEGASQSEVVESAMLANAHSFITSLPEGYSTK 1161
Cdd:TIGR03796 529 YQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAE 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1162 VGERGVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRlmanR--TTVVVAHRLSTIKNADTISVL 1239
Cdd:TIGR03796 609 LAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRR----RgcTCIIVAHRLSTIRDCDEIIVL 684
|
490 500
....*....|....*....|....*..
gi 79487035 1240 HGGKIVEQGSHRKLvLNKSGPYFKLIS 1266
Cdd:TIGR03796 685 ERGKVVQRGTHEEL-WAVGGAYARLIR 710
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
711-998 |
6.64e-66 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 225.05 E-value: 6.64e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 711 VCGTICAFIAGSQMPLFAL---GVSQALVSYYSGW---DETQKEIKKIAILFCCASVITLIVYTIEHICFGTMGERLTLR 784
Cdd:cd18577 2 IIGLLAAIAAGAALPLMTIvfgDLFDAFTDFGSGEsspDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQARR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 785 VRENMFRAILKNEIGWFDEvdNTSSMLASRLESDATLLKTIVVDRSTILLQNLGLVVTSFIIAFILNWRLTLVVLATYPL 864
Cdd:cd18577 82 IRKRYLKALLRQDIAWFDK--NGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 865 -VISGHISEKlFMQGYGGDLNKAYLKANMLAGESVSNIRTVAAFCAEEKILELYSRELLEPSKSSFRRGQIAGLFYGVSQ 943
Cdd:cd18577 160 iAIVGGIMGK-LLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLF 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 79487035 944 FFIFSSYGLALWYGSTLMDKGLAGFKSVMKTFMVLIVTALAMGETLALAPDLLKG 998
Cdd:cd18577 239 FIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKA 293
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
76-380 |
8.37e-66 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 225.41 E-value: 8.37e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 76 LMTLGSVGACIHGASVPIFFIFFGKLINIigLAYLFPKQASHRVAKYSLDFVYLSVAILFSSWLEVACWMHTGERQAAKM 155
Cdd:cd18578 10 LLLLGLIGAIIAGAVFPVFAILFSKLISV--FSLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAGERLTRRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 156 RRAYLRSMLSQDISLFDTEA-STGEVISAITSDILVVQDALSEKVGNFLHYISRFIAGFAIGFTSVWQISLVTLSIVPLI 234
Cdd:cd18578 88 RKLAFRAILRQDIAWFDDPEnSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVGLATVPLL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 235 ALAGGIYAFVAIGLIARVRKSYIKAGEIAEEVIGNVRTVQAFTGEERAVRLYREALENTYKYGRKAGLTKGLGLGSMHCV 314
Cdd:cd18578 168 LLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGFGLSQSL 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 315 LFLSWALLVWFTSVVVHKDIADGGKSFTTMLNVVIAGLSLGQA---APDISafvRAKAAAYPIFKMIER 380
Cdd:cd18578 248 TFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAfsfAPDIA---KAKAAAARIFRLLDR 313
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
298-1254 |
7.08e-64 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 239.46 E-value: 7.08e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 298 RKAGLTKGLGLGSMHCVLFLSWALLVWFTSVVVHKDIADGGKSFTTMLNVVIAGLSLGQAAPDISAFVRAKAA--AYPIF 375
Cdd:TIGR00957 534 KKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDENNILDAEKAFVSLALFNILRFPLNILPMVISSIVQASVSlkRLRIF 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 376 ---KMIERNTVTKTSAKSGRklgkvDGHIQFKDATFSYpSRPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERF 452
Cdd:TIGR00957 614 lshEELEPDSIERRTIKPGE-----GNSITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAE 687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 453 YEPISGAVLLdgnniseldikwlRGQIGLVNQEPALFATTIRENILYGKddatAEEITRAAKLSEAISFINNL---PEGF 529
Cdd:TIGR00957 688 MDKVEGHVHM-------------KGSVAYVPQQAWIQNDSLRENILFGK----ALNEKYYQQVLEACALLPDLeilPSGD 750
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 530 ETQVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEAL---DRVMVGRTTVVVAHRLSTVRNADI 606
Cdd:TIGR00957 751 RTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDV 830
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 607 IAVVHEGKIVEFGNHENLISNpDGAYSSLLRLQETASLQRNPSLNRTLSRPHSIKYS--------------RELSRTRSS 672
Cdd:TIGR00957 831 IIVMSGGKISEMGSYQELLQR-DGAFAEFLRTYAPDEQQGHLEDSWTALVSGEGKEAkliengmlvtdvvgKQLQRQLSA 909
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 673 FCSERESVTRPDGadPSKKVKVTVGRL--YSMIRPD------------WMYgvCGTICAFIAGSQMPLFALGVSQALVSY 738
Cdd:TIGR00957 910 SSSDSGDQSRHHG--SSAELQKAEAKEetWKLMEADkaqtgqvelsvyWDY--MKAIGLFITFLSIFLFVCNHVSALASN 985
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 739 Y--SGW------DETQKEIKKIAILFCCASVITLIVYTIEHICFGTMGERLTLRVRENMFRAILKNEIGWFDEvdNTSSM 810
Cdd:TIGR00957 986 YwlSLWtddpmvNGTQNNTSLRLSVYGALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFER--TPSGN 1063
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 811 LASRLESDATLLKTIVVDRSTILLQNLGLVVTSFIIAFILNWRLTLVVLatyPLVISghiseKLFMQGYGGDLNKAYLKA 890
Cdd:TIGR00957 1064 LVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIP---PLGLL-----YFFVQRFYVASSRQLKRL 1135
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 891 NMLA--------GESVSNIRTVAAFcAEEKILELYSRELLEPSKSSFRRGQIAGLFYGVSQFFIFSSYGL--ALW--YGS 958
Cdd:TIGR00957 1136 ESVSrspvyshfNETLLGVSVIRAF-EEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLfaALFavISR 1214
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 959 TLMDKGLAGFkSVMKTfmvLIVTAlAMGETLALAPDLLKGNQMVASVFEILDRKT----QIVGETSEELNNVEGTIELKG 1034
Cdd:TIGR00957 1215 HSLSAGLVGL-SVSYS---LQVTF-YLNWLVRMSSEMETNIVAVERLKEYSETEKeapwQIQETAPPSGWPPRGRVEFRN 1289
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1035 VHFSYpsRPDV-VIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIGLVQQ 1113
Cdd:TIGR00957 1290 YCLRY--REDLdLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQ 1367
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1114 EPALFATTIYENiLYGNEGASQSEVVESAMLANAHSFITSLPEGYSTKVGERGVQMSGGQRQRIAIARAILKNPAILLLD 1193
Cdd:TIGR00957 1368 DPVLFSGSLRMN-LDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLD 1446
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79487035 1194 EATSALDVESERVVQQALDRLMANRTTVVVAHRLSTIKNADTISVLHGGKIVEQGSHRKLV 1254
Cdd:TIGR00957 1447 EATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLL 1507
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
367-610 |
4.77e-63 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 224.47 E-value: 4.77e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 367 AKAAAYPIFKMIERNTVTKTSAKSgrKLGKVDGHIQFKDATFSYPSRPDVVifDRLNLAIPAGKIVALVGGSGSGKSTVI 446
Cdd:TIGR02857 290 GVAAAEALFAVLDAAPRPLAGKAP--VTAAPASSLEFSGVSVAYPGRRPAL--RPVSFTVPPGERVALVGPSGAGKSTLL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 447 SLIERFYEPISGAVLLDGNNISELDIKWLRGQIGLVNQEPALFATTIRENILYGKDDATAEEITRAAKLSEAISFINNLP 526
Cdd:TIGR02857 366 NLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALP 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 527 EGFETQVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRVMVGRTTVVVAHRLSTVRNADI 606
Cdd:TIGR02857 446 QGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADR 525
|
....
gi 79487035 607 IAVV 610
Cdd:TIGR02857 526 IVVL 529
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
784-1269 |
9.31e-63 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 225.75 E-value: 9.31e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 784 RVRENMFRAILKNEIGWFDevDNTSSMLASRLESDATLLKTIVVDRSTILLQNLGLVVTSFIIAFILNWRLTLVVLATYP 863
Cdd:PRK10790 99 QLRTDVMDAALRQPLSAFD--TQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAIMIFP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 864 LV-----ISGHISEKLF--MQGYGGDLNKAYlkanmlaGESVSNIRTVAAFCAEEKilelYSRELLEPSKSSFR-RGQIA 935
Cdd:PRK10790 177 AVlvvmvIYQRYSTPIVrrVRAYLADINDGF-------NEVINGMSVIQQFRQQAR----FGERMGEASRSHYMaRMQTL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 936 GL--FYGVSQFFIFSsyglALWYGSTLMdkgLAGFKSVmKTFMVLIVTALA--MGE------TLALAPDLLKgnQMVAS- 1004
Cdd:PRK10790 246 RLdgFLLRPLLSLFS----ALILCGLLM---LFGFSAS-GTIEVGVLYAFIsyLGRlnepliELTTQQSMLQ--QAVVAg 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1005 --VFEILDRKTQIVGETSEELNNveGTIELKGVHFSYpsRPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFY 1082
Cdd:PRK10790 316 erVFELMDGPRQQYGNDDRPLQS--GRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYY 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1083 DPTAGKVMIEGKDIKKLDLKALRKHIGLVQQEPALFATTIYENILYGNEGASQS--EVVESAMLAnahSFITSLPEGYST 1160
Cdd:PRK10790 392 PLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQvwQALETVQLA---ELARSLPDGLYT 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1161 KVGERGVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVVVAHRLSTIKNADTISVLH 1240
Cdd:PRK10790 469 PLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLH 548
|
490 500
....*....|....*....|....*....
gi 79487035 1241 GGKIVEQGSHRKLvLNKSGPYFKLISLQQ 1269
Cdd:PRK10790 549 RGQAVEQGTHQQL-LAAQGRYWQMYQLQL 576
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
401-1265 |
1.19e-62 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 235.26 E-value: 1.19e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLdgnniseldikwLRGQIG 480
Cdd:PLN03232 615 ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV------------IRGSVA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 LVNQEPALFATTIRENILYGKDdATAEEITRAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRIAISRAIVKNPSI 560
Cdd:PLN03232 683 YVPQVSWIFNATVRENILFGSD-FESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDI 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 561 LLLDEATSALDAESEKSV-QEALDRVMVGRTTVVVAHRLSTVRNADIIAVVHEGKIVEFGNHENLISNPDgAYSSLL--- 636
Cdd:PLN03232 762 YIFDDPLSALDAHVAHQVfDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGS-LFKKLMena 840
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 637 -RLQETASLQRNPSLNRTLSRPHSIKYS-RELSRT------RSSFCSERESVTRPDGADPSKKVKVTVGRLYSMIrpdwM 708
Cdd:PLN03232 841 gKMDATQEVNTNDENILKLGPTVTIDVSeRNLGSTkqgkrgRSVLVKQEERETGIISWNVLMRYNKAVGGLWVVM----I 916
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 709 YGVCGTICAFIAGSQMPLFALGVSQA-LVSYYSGWdetqkeikkiailfccasviTLIVYTIehICFGTMGERLT----- 782
Cdd:PLN03232 917 LLVCYLTTEVLRVSSSTWLSIWTDQStPKSYSPGF--------------------YIVVYAL--LGFGQVAVTFTnsfwl 974
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 783 --------LRVRENMFRAILKNEIGWFDEvdNTSSMLASRLESDATLLKTIVVDRSTILLQNLGLVVTSFIIAFILNwrl 854
Cdd:PLN03232 975 issslhaaKRLHDAMLNSILRAPMLFFHT--NPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVS--- 1049
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 855 TLVVLATYPLVISGHiSEKLFMQGYGGDLNK--AYLKANMLA--GESVSNIRTVAAFCAEEKILELYSRELLE------P 924
Cdd:PLN03232 1050 TISLWAIMPLLILFY-AAYLYYQSTSREVRRldSVTRSPIYAqfGEALNGLSSIRAYKAYDRMAKINGKSMDNnirftlA 1128
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 925 SKSSFRRGQIAGLFYGVSQFFIFSSYGLaLWYGSTlmdKGLAGFKSVMKTFM--VLIVTALAMG--ETLALAPDLLKGNQ 1000
Cdd:PLN03232 1129 NTSSNRWLTIRLETLGGVMIWLTATFAV-LRNGNA---ENQAGFASTMGLLLsyTLNITTLLSGvlRQASKAENSLNSVE 1204
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1001 MVASVFEILDRKTQIVgETSEELNN--VEGTIELKGVHFSY-PSRPDVVifRDFDLIVRAGKSMALVGQSGSGKSSVISL 1077
Cdd:PLN03232 1205 RVGNYIDLPSEATAII-ENNRPVSGwpSRGSIKFEDVHLRYrPGLPPVL--HGLSFFVSPSEKVGVVGRTGAGKSSMLNA 1281
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1078 ILRFYDPTAGKVMIEGKDIKKLDLKALRKHIGLVQQEPALFATTIYENI--LYGNEGASQSEVVESAMLANAhsfITSLP 1155
Cdd:PLN03232 1282 LFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIdpFSEHNDADLWEALERAHIKDV---IDRNP 1358
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1156 EGYSTKVGERGVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVVVAHRLSTIKNADT 1235
Cdd:PLN03232 1359 FGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDK 1438
|
890 900 910
....*....|....*....|....*....|
gi 79487035 1236 ISVLHGGKIVEQGSHRKLVLNKSGPYFKLI 1265
Cdd:PLN03232 1439 ILVLSSGQVLEYDSPQELLSRDTSAFFRMV 1468
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
51-638 |
1.94e-62 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 234.54 E-value: 1.94e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 51 KEKEMTQPKVSLLKLFSFADfyDCVLMTLGSVGAcihGASVPIFFIFFGKLIN-IIGLAYLfpkqaSHRVAKYSLDFVYL 129
Cdd:PTZ00265 806 KPKAPNNLRIVYREIFSYKK--DVTIIALSILVA---GGLYPVFALLYAKYVStLFDFANL-----EANSNKYSLYILVI 875
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 130 SVAILFSSWLEVACWMHTGERQAAKMRRAYLRSMLSQDISLFDTEASTGEVISA-ITSDILVVQDALSEKVGNFLHYISR 208
Cdd:PTZ00265 876 AIAMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQDKHAPGLLSAhINRDVHLLKTGLVNNIVIFTHFIVL 955
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 209 FIAGFAIGFTsvwqislvtlsIVPLIA--LAGGIYAFVAIGLI-ARVRKS----------------YIKAGEI------- 262
Cdd:PTZ00265 956 FLVSMVMSFY-----------FCPIVAavLTGTYFIFMRVFAIrARLTANkdvekkeinqpgtvfaYNSDDEIfkdpsfl 1024
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 263 AEEVIGNVRTVQAFTGEERAVRLYREALENTYKYGRKAGLTKGLGLGSMHCVLFLSWALLVWFTSVVVHK---DIADGGK 339
Cdd:PTZ00265 1025 IQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRgtiLVDDFMK 1104
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 340 S-FTTMLNVVIAG--LSLGQAAPDisafvrAKAAAYPIFKMIERNTVTKTSAKSGRKLGK---VDGHIQFKDATFSYPSR 413
Cdd:PTZ00265 1105 SlFTFLFTGSYAGklMSLKGDSEN------AKLSFEKYYPLIIRKSNIDVRDNGGIRIKNkndIKGKIEIMDVNFRYISR 1178
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 414 PDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYE--------------------------------------- 454
Cdd:PTZ00265 1179 PNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnef 1258
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 455 ---------------PISGAVLLDGNNISELDIKWLRGQIGLVNQEPALFATTIRENILYGKDDATAEEITRAAKLSEAI 519
Cdd:PTZ00265 1259 sltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAID 1338
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 520 SFINNLPEGFETQVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRV--MVGRTTVVVAHR 597
Cdd:PTZ00265 1339 EFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHR 1418
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 79487035 598 LSTVRNADIIAVVHE----GKIVEF-GNHENLISNPDGAYSSLLRL 638
Cdd:PTZ00265 1419 IASIKRSDKIVVFNNpdrtGSFVQAhGTHEELLSVQDGVYKKYVKL 1464
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
154-639 |
2.04e-62 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 224.60 E-value: 2.04e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 154 KMRRAYLRSMLSQDISLFDTEAsTGEVISAITSDILVVQDALSEKVGNFLHYISRFIAGFAIGFTSVWQISLVTLSIVPL 233
Cdd:PRK10790 99 QLRTDVMDAALRQPLSAFDTQP-VGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAIMIFPA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 234 IALAGGIYAFVAIGLIARVRkSYIkaGEIAE---EVIGNVRTVQAFTGEERAVRLYREALENTYKYGRKAGLTKGLGLG- 309
Cdd:PRK10790 178 VLVVMVIYQRYSTPIVRRVR-AYL--ADINDgfnEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFLLRp 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 310 --SMHCVLFLSWALLVW-FTSV------VVHKDIadggkSFTTMLNVVIAGLSLGQaapdiSAFVRAKAAAYPIFKMIER 380
Cdd:PRK10790 255 llSLFSALILCGLLMLFgFSASgtievgVLYAFI-----SYLGRLNEPLIELTTQQ-----SMLQQAVVAGERVFELMDG 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 381 ntVTKTSAKSGRKLGKvdGHIQFKDATFSYpsRPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAV 460
Cdd:PRK10790 325 --PRQQYGNDDRPLQS--GRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEI 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 461 LLDGNNISELDIKWLRGQIGLVNQEPALFATTIRENILYGKDdATAEEITRAAKLSEAISFINNLPEGFETQVGERGIQL 540
Cdd:PRK10790 399 RLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRD-ISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNL 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 541 SGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVHEGKIVEFGN 620
Cdd:PRK10790 478 SVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGT 557
|
490
....*....|....*....
gi 79487035 621 HENLISNpDGAYSSLLRLQ 639
Cdd:PRK10790 558 HQQLLAA-QGRYWQMYQLQ 575
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
836-1268 |
6.24e-60 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 219.44 E-value: 6.24e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 836 NLGLVvtsfiiaFILNWRLTLV--VLATYPLVISGHISEKLF-----MQGYGGDLNKayLKANMLAGesVSNIRtVAAfc 908
Cdd:TIGR03797 266 NLGLM-------FYYSWKLALVavALALVAIAVTLVLGLLQVrkerrLLELSGKISG--LTVQLING--ISKLR-VAG-- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 909 AEEKILELYSRELLEPSKSSFRRGQIAGLFYGVSQFF-IFSS---YGLALW-YGSTLMDKG-LAGFKSVMKTFMVlIVTA 982
Cdd:TIGR03797 332 AENRAFARWAKLFSRQRKLELSAQRIENLLTVFNAVLpVLTSaalFAAAISlLGGAGLSLGsFLAFNTAFGSFSG-AVTQ 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 983 LAMG--ETLALAPDLLKGNQMVASVFEILDRKTQiVGETSeelnnveGTIELKGVHFSYpsRPD-VVIFRDFDLIVRAGK 1059
Cdd:TIGR03797 411 LSNTliSILAVIPLWERAKPILEALPEVDEAKTD-PGKLS-------GAIEVDRVTFRY--RPDgPLILDDVSLQIEPGE 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1060 SMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIGLVQQEPALFATTIYENILyGNEGASQSEVV 1139
Cdd:TIGR03797 481 FVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIA-GGAPLTLDEAW 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1140 ESAMLANAHSFITSLPEGYSTKVGERGVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANRt 1219
Cdd:TIGR03797 560 EAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR- 638
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 79487035 1220 tVVVAHRLSTIKNADTISVLHGGKIVEQGSHRKLvLNKSGPYFKLISLQ 1268
Cdd:TIGR03797 639 -IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDEL-MAREGLFAQLARRQ 685
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
221-639 |
1.10e-59 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 218.67 E-value: 1.10e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 221 WQISLVTLSIvplIALAGGIYAFVAIGLIARVRKSYIKAGEIAEEvignvrTVQAFTG---------EERA----VRLYR 287
Cdd:TIGR03797 275 WKLALVAVAL---ALVAIAVTLVLGLLQVRKERRLLELSGKISGL------TVQLINGisklrvagaENRAfarwAKLFS 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 288 EALENTYKYGRKAGltkglGLGSMHCVL-FLSWALLVWFTSVVVHKDIADGGK--SFTTMLNVVIAG-LSLGQAAPDISA 363
Cdd:TIGR03797 346 RQRKLELSAQRIEN-----LLTVFNAVLpVLTSAALFAAAISLLGGAGLSLGSflAFNTAFGSFSGAvTQLSNTLISILA 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 364 FVRAKAAAYPIFKMIERNTVTKTSAksgrklGKVDGHIQFKDATFSYpsRPD-VVIFDRLNLAIPAGKIVALVGGSGSGK 442
Cdd:TIGR03797 421 VIPLWERAKPILEALPEVDEAKTDP------GKLSGAIEVDRVTFRY--RPDgPLILDDVSLQIEPGEFVAIVGPSGSGK 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 443 STVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIGLVNQEPALFATTIRENILyGKDDATAEEITRAAKLSEAISFI 522
Cdd:TIGR03797 493 STLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIA-GGAPLTLDEAWEAARMAGLAEDI 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 523 NNLPEGFETQVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRVMVGRttVVVAHRLSTVR 602
Cdd:TIGR03797 572 RAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIR 649
|
410 420 430
....*....|....*....|....*....|....*..
gi 79487035 603 NADIIAVVHEGKIVEFGNHENLISNPdGAYSSLLRLQ 639
Cdd:TIGR03797 650 NADRIYVLDAGRVVQQGTYDELMARE-GLFAQLARRQ 685
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1028-1249 |
2.38e-58 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 200.41 E-value: 2.38e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1028 GTIELKGVHFSYPSRPDVVIfRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKH 1107
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVL-KNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1108 IGLVQQEPALFATTIYENILYGNEgASQSEVVESAMLANAHSFITSLPEGYSTKVGERGVQMSGGQRQRIAIARAILKNP 1187
Cdd:cd03244 80 ISIIPQDPVLFSGTIRSNLDPFGE-YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79487035 1188 AILLLDEATSALDVESERVVQQALDRLMANRTTVVVAHRLSTIKNADTISVLHGGKIVEQGS 1249
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
839-1269 |
2.60e-58 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 211.88 E-value: 2.60e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 839 LVVTSFIIAfilnWRLTLVVLATYPLVisghiseKLFMQGYGGDLNK-------AYLKANMLAGESVSNIRTVAAFCAEE 911
Cdd:PRK10789 128 LIVMSTQIS----WQLTLLALLPMPVM-------AIMIKRYGDQLHErfklaqaAFSSLNDRTQESLTSIRMIKAFGLED 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 912 KILELYSRELLEPSKSSFRRGQIAGLFYGVSQFFIFSSYGLALWYGSTLmdkglagfksVMKTFMVL-IVTALAMGETLA 990
Cdd:PRK10789 197 RQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGMANLLAIGGGSWM----------VVNGSLTLgQLTSFVMYLGLM 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 991 LAPDLlkgnqMVASVFEILDR-------------KTQIVGETSEELNNVEGTIELKGVHFSYPSRpDVVIFRDFDLIVRA 1057
Cdd:PRK10789 267 IWPML-----ALAWMFNIVERgsaaysriramlaEAPVVKDGSEPVPEGRGELDVNIRQFTYPQT-DHPALENVNFTLKP 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1058 GKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIGLVQQEPALFATTIYENILYGNEGASQSE 1137
Cdd:PRK10789 341 GQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQE 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1138 VVESAMLANAHSFITSLPEGYSTKVGERGVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMAN 1217
Cdd:PRK10789 421 IEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEG 500
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 79487035 1218 RTTVVVAHRLSTIKNADTISVLHGGKIVEQGSHRKLVlNKSGPYFKLISLQQ 1269
Cdd:PRK10789 501 RTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLA-QQSGWYRDMYRYQQ 551
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
399-620 |
4.54e-58 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 199.64 E-value: 4.54e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 399 GHIQFKDATFSYPSRPDVVIFDrLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQ 478
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKN-ISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 479 IGLVNQEPALFATTIRENI-LYGKddATAEEITRAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRIAISRAIVKN 557
Cdd:cd03244 80 ISIIPQDPVLFSGTIRSNLdPFGE--YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79487035 558 PSILLLDEATSALDAESEKSVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVHEGKIVEFGN 620
Cdd:cd03244 158 SKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
401-1265 |
7.25e-58 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 220.38 E-value: 7.25e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLdgnniseldikwLRGQIG 480
Cdd:PLN03130 615 ISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 LVNQEPALFATTIRENILYGK--DDATAEEITRAAKLSEAISFinnLPEGFETQVGERGIQLSGGQKQRIAISRAIVKNP 558
Cdd:PLN03130 683 YVPQVSWIFNATVRDNILFGSpfDPERYERAIDVTALQHDLDL---LPGGDLTEIGERGVNISGGQKQRVSMARAVYSNS 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 559 SILLLDEATSALDAESEKSV-QEALDRVMVGRTTVVVAHRLSTVRNADIIAVVHEGKIVEFGNHENLISNPDgAYSSLL- 636
Cdd:PLN03130 760 DVYIFDDPLSALDAHVGRQVfDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGP-LFQKLMe 838
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 637 ---RLQETASLQRNPSLNRTLSRPHSIKYSRELSRTRSSFCSERE--SVTRPDGADPSKKVKVTVGRLYSmirpDWMYGV 711
Cdd:PLN03130 839 nagKMEEYVEENGEEEDDQTSSKPVANGNANNLKKDSSSKKKSKEgkSVLIKQEERETGVVSWKVLERYK----NALGGA 914
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 712 CGTICAFIAGSQMPLFALGVSQALvsyySGW-DETQKEIKKiailfccaSVITLIVYTIehICFG----TMGERLTL--- 783
Cdd:PLN03130 915 WVVMILFLCYVLTEVFRVSSSTWL----SEWtDQGTPKTHG--------PLFYNLIYAL--LSFGqvlvTLLNSYWLims 980
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 784 ------RVRENMFRAILKNEIGWFDEvdNTSSMLASRLESDatllkTIVVDRSTILLQNLGLV-----VTSFIIAFILNw 852
Cdd:PLN03130 981 slyaakRLHDAMLGSILRAPMSFFHT--NPLGRIINRFAKD-----LGDIDRNVAVFVNMFLGqifqlLSTFVLIGIVS- 1052
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 853 rlTLVVLATYPLVISGHiSEKLFMQGYGGDLNK--AYLKANMLA--GESVSNIRTVAAFCAEEKILELYSRELLEPSK-- 926
Cdd:PLN03130 1053 --TISLWAIMPLLVLFY-GAYLYYQSTAREVKRldSITRSPVYAqfGEALNGLSTIRAYKAYDRMAEINGRSMDNNIRft 1129
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 927 ----SSFRRGQIAGLFYGvsqffifssyGLALWYGSTL--MDKGLA----GFKSVMKTFM--VLIVTALaMGETLALApd 994
Cdd:PLN03130 1130 lvnmSSNRWLAIRLETLG----------GLMIWLTASFavMQNGRAenqaAFASTMGLLLsyALNITSL-LTAVLRLA-- 1196
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 995 llkgnQMVASVFEILDRKTQIVGETSEELNNVE-----------GTIELKGVHFSY-PSRPDVVIFRDFDliVRAGKSMA 1062
Cdd:PLN03130 1197 -----SLAENSLNAVERVGTYIDLPSEAPLVIEnnrpppgwpssGSIKFEDVVLRYrPELPPVLHGLSFE--ISPSEKVG 1269
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1063 LVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIGLVQQEPALFATTIYENILYGNE--GASQSEVVE 1140
Cdd:PLN03130 1270 IVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEhnDADLWESLE 1349
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1141 SAMLANAhsfITSLPEGYSTKVGERGVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANRTT 1220
Cdd:PLN03130 1350 RAHLKDV---IRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTM 1426
|
890 900 910 920
....*....|....*....|....*....|....*....|....*
gi 79487035 1221 VVVAHRLSTIKNADTISVLHGGKIVEQGSHRKLVLNKSGPYFKLI 1265
Cdd:PLN03130 1427 LIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKMV 1471
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1055-1272 |
7.36e-58 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 210.86 E-value: 7.36e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1055 VRAGKSMALVGQSGSGKSSVISLILRFYdPTAGKVMIEGKDIKKLDLKALRKHIGLVQQEPALFATTIYENILYGNEGAS 1134
Cdd:PRK11174 373 LPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDAS 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1135 QSEVVESAMLANAHSFITSLPEGYSTKVGERGVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRL 1214
Cdd:PRK11174 452 DEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAA 531
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 1215 MANRTTVVVAHRLSTIKNADTISVLHGGKIVEQGSHRKLVlNKSGPYFKLISLQQQQQ 1272
Cdd:PRK11174 532 SRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELS-QAGGLFATLLAHRQEEI 588
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
975-1265 |
1.05e-57 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 210.07 E-value: 1.05e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 975 FMVLIV-TALAMGETLA-LAPDLLKGNQMVAS---VFEILDRKTQIVGETSEELNNVEGTIELKGVHFSYPSRPDVVIfR 1049
Cdd:PRK11160 279 LIALFVfAALAAFEALMpVAGAFQHLGQVIASarrINEITEQKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQPVL-K 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1050 DFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIGLVQQEPALFATTIYENILYG 1129
Cdd:PRK11160 358 GLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1130 NEGASQ---SEVVESAMLANahsfITSLPEGYSTKVGERGVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERV 1206
Cdd:PRK11160 438 APNASDealIEVLQQVGLEK----LLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQ 513
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 1207 VQQALDRLMANRTTVVVAHRLSTIKNADTISVLHGGKIVEQGSHRKLvLNKSGPYFKLI 1265
Cdd:PRK11160 514 ILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQEL-LAQQGRYYQLK 571
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
150-598 |
2.17e-56 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 205.29 E-value: 2.17e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 150 RQAAKMRrAYLRSMLSQDISLFDTEASTGEVISAITSDILVVQD----ALSEKVGNFLHYISR--FIAGFAIGFTSVWQI 223
Cdd:TIGR02868 83 RSLGALR-VRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDlyvrVIVPAGVALVVGAAAvaAIAVLSVPAALILAA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 224 SL-VTLSIVPLIALAGGIYAFVAIgliARVRKSYIKAgeiAEEVIGNVRTVQAFTGEERAVRLYREALENTYKYGRKAGL 302
Cdd:TIGR02868 162 GLlLAGFVAPLVSLRAARAAEQAL---ARLRGELAAQ---LTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 303 TKGLGLGSMHCVLFLSWALLVWFTSVVVhkdiADGGKSFTTMLNVVIAGLSLGQA-APDISAFV---RAKAAAYPIFKMI 378
Cdd:TIGR02868 236 ATALGAALTLLAAGLAVLGALWAGGPAV----ADGRLAPVTLAVLVLLPLAAFEAfAALPAAAQqltRVRAAAERIVEVL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 379 ERNTVTKTSAKSGRKLGKVDG-HIQFKDATFSYPSRPDVviFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPIS 457
Cdd:TIGR02868 312 DAAGPVAEGSAPAAGAVGLGKpTLELRDLSAGYPGAPPV--LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQ 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 458 GAVLLDGNNISELDIKWLRGQIGLVNQEPALFATTIRENILYGKDDATAEEITRAAKLSEAISFINNLPEGFETQVGERG 537
Cdd:TIGR02868 390 GEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGG 469
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79487035 538 IQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRVMVGRTTVVVAHRL 598
Cdd:TIGR02868 470 ARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
316-642 |
4.15e-55 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 202.77 E-value: 4.15e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 316 FLSWALLVWFTSV---VV----------HKDIADGGKSFTtmlnvVIAGLSLGQAAP-------DISAFVRAKA----AA 371
Cdd:PRK11174 247 FLSSAVLEFFASIsiaLVavyfgfsylgELNFGHYGTGVT-----LFAGFFVLILAPefyqplrDLGTFYHAKAqavgAA 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 372 YPIFKMIERNTvtkTSAKSGRKLGKVDGHIQFKDATFSYPSRPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIER 451
Cdd:PRK11174 322 ESLVTFLETPL---AHPQQGEKELASNDPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 452 FYePISGAVLLDGNNISELDIKWLRGQIGLVNQEPALFATTIRENILYGKDDATAEEITRAAKLSEAISFINNLPEGFET 531
Cdd:PRK11174 399 FL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDT 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 532 QVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVH 611
Cdd:PRK11174 478 PIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQ 557
|
330 340 350
....*....|....*....|....*....|.
gi 79487035 612 EGKIVEFGNHENLiSNPDGAYSSLLRLQETA 642
Cdd:PRK11174 558 DGQIVQQGDYAEL-SQAGGLFATLLAHRQEE 587
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
399-637 |
2.68e-54 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 200.05 E-value: 2.68e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 399 GHIQFKDATFSYPSRPDVVIfDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQ 478
Cdd:PRK11160 337 VSLTLNNVSFTYPDQPQPVL-KGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 479 IGLVNQEPALFATTIRENILYGKDDATAEEITRA------AKLSEAisfinnlPEGFETQVGERGIQLSGGQKQRIAISR 552
Cdd:PRK11160 416 ISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVlqqvglEKLLED-------DKGLNAWLGEGGRQLSGGEQRRLGIAR 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 553 AIVKNPSILLLDEATSALDAESEKSVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVHEGKIVEFGNHENLISNpDGAY 632
Cdd:PRK11160 489 ALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQ-QGRY 567
|
....*
gi 79487035 633 SSLLR 637
Cdd:PRK11160 568 YQLKQ 572
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
407-640 |
7.69e-54 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 198.78 E-value: 7.69e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 407 TFSYPSRpDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIGLVNQEP 486
Cdd:PRK10789 320 QFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTP 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 487 ALFATTIRENILYGKDDATAEEITRAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEA 566
Cdd:PRK10789 399 FLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDA 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79487035 567 TSALDAESEKSVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVHEGKIVEFGNHENLISNPdGAYSSLLRLQE 640
Cdd:PRK10789 479 LSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS-GWYRDMYRYQQ 551
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1027-1257 |
9.51e-54 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 198.05 E-value: 9.51e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1027 EGTIELKGVHFSYPSRpDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRK 1106
Cdd:COG4618 328 KGRLSVENLTVVPPGS-KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1107 HIGLVQQEPALFATTIYENI-LYGNegASQSEVVESAMLANAHSFITSLPEGYSTKVGERGVQMSGGQRQRIAIARAILK 1185
Cdd:COG4618 407 HIGYLPQDVELFDGTIAENIaRFGD--ADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYG 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79487035 1186 NPAILLLDEATSALDVESERVVQQALDRLMANRTTVVV-AHRLSTIKNADTISVLHGGKIVEQGShRKLVLNK 1257
Cdd:COG4618 485 DPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVViTHRPSLLAAVDKLLVLRDGRVQAFGP-RDEVLAR 556
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
233-619 |
1.20e-52 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 194.97 E-value: 1.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 233 LIALAGGIyAFVAIGLI---------ARVRKSYIKAGEIAEEVIGNVRTVQA--FTGE--ERAVRLYREALENTYKYGRK 299
Cdd:COG4618 159 LLALVGAL-VLVALALLnerltrkplKEANEAAIRANAFAEAALRNAEVIEAmgMLPAlrRRWQRANARALALQARASDR 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 300 AG----LTKGLGLGSMHCVLFLSwALLVwftsvvVHKDIADGgksfttmlnVVIAGlS--LGQA-AP------DISAFVR 366
Cdd:COG4618 238 AGgfsaLSKFLRLLLQSAVLGLG-AYLV------IQGEITPG---------AMIAA-SilMGRAlAPieqaigGWKQFVS 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 367 AKAAAYPIFKMIERNTvtktSAKSGRKLGKVDGHIQFKDATFSYPSRpDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVI 446
Cdd:COG4618 301 ARQAYRRLNELLAAVP----AEPERMPLPRPKGRLSVENLTVVPPGS-KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLA 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 447 SLIERFYEPISGAVLLDGNNISELDIKWLRGQIGLVNQEPALFATTIRENI--LygkDDATAEEITRAAKLSEAISFINN 524
Cdd:COG4618 376 RLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIarF---GDADPEKVVAAAKLAGVHEMILR 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 525 LPEGFETQVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRV-MVGRTTVVVAHRLSTVRN 603
Cdd:COG4618 453 LPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAA 532
|
410
....*....|....*.
gi 79487035 604 ADIIAVVHEGKIVEFG 619
Cdd:COG4618 533 VDKLLVLRDGRVQAFG 548
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
777-1265 |
1.50e-52 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 197.65 E-value: 1.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 777 MGERLTLRVRENMFRAILKNEIGWFdEVDNTSSMLaSRLESDATLLKTIVVDRSTILLQNLGLVVTSFIIAFiLNWRLTL 856
Cdd:TIGR01193 223 LGQRLSIDIILSYIKHLFELPMSFF-STRRTGEIV-SRFTDASSIIDALASTILSLFLDMWILVIVGLFLVR-QNMLLFL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 857 VVLATYPLVISGHIsekLFMQGYGGDLNKAYLKANMLAG---ESVSNIRTVAAFCAEE----KILELYSrELLEPSKSSF 929
Cdd:TIGR01193 300 LSLLSIPVYAVIII---LFKRTFNKLNHDAMQANAVLNSsiiEDLNGIETIKSLTSEAerysKIDSEFG-DYLNKSFKYQ 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 930 RRGQIAGLFYGVSQFFIFSsygLALWYGSTLMDKGLAGFKSVMkTFMVLIVTALAMGETLA-LAPDLLKG---NQMVASV 1005
Cdd:TIGR01193 376 KADQGQQAIKAVTKLILNV---VILWTGAYLVMRGKLTLGQLI-TFNALLSYFLTPLENIInLQPKLQAArvaNNRLNEV 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1006 FeiLDRKTQIVGETSEELNNVEGTIELKGVHFSYPSRPDVVifRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPT 1085
Cdd:TIGR01193 452 Y--LVDSEFINKKKRTELNNLNGDIVINDVSYSYGYGSNIL--SDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQAR 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1086 AGKVMIEGKDIKKLDLKALRKHIGLVQQEPALFATTIYENILYGN-EGASQSEVVESAMLANAHSFITSLPEGYSTKVGE 1164
Cdd:TIGR01193 528 SGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAkENVSQDEIWAACEIAEIKDDIENMPLGYQTELSE 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1165 RGVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVqqaLDRL--MANRTTVVVAHRLSTIKNADTISVLHGG 1242
Cdd:TIGR01193 608 EGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKI---VNNLlnLQDKTIIFVAHRLSVAKQSDKIIVLDHG 684
|
490 500
....*....|....*....|...
gi 79487035 1243 KIVEQGSHRKLvLNKSGPYFKLI 1265
Cdd:TIGR01193 685 KIIEQGSHDEL-LDRNGFYASLI 706
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
77-374 |
2.93e-51 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 183.63 E-value: 2.93e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 77 MTLGSVGACIHGASVPIFFIFFGKLI-------------NIIGLAYLF--PKQASHRVAKYSLDFVYLSVAILFSSWLEV 141
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTdsftnggmtnitgNSSGLNSSAgpFEKLEEEMTLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 142 ACWMHTGERQAAKMRRAYLRSMLSQDISLFDTEaSTGEVISAITSDILVVQDALSEKVGNFLHYISRFIAGFAIGFTSVW 221
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVN-DTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 222 QISLVTLSIVPLIALAGGIYAFVAIGLIARVRKSYIKAGEIAEEVIGNVRTVQAFTGEERAVRLYREALENTYKYGRKAG 301
Cdd:cd18558 160 KLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKA 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79487035 302 LTKGLGLGSMHCVLFLSWALLVWFTSVVVHKDIADGGKSFTTMLNVVIAGLSLGQAAPDISAFVRAKAAAYPI 374
Cdd:cd18558 240 ITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAAYHI 312
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
778-1244 |
3.69e-51 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 190.25 E-value: 3.69e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 778 GERLTLRVRENMFRAILKNEIgwfdevdNTSSMLASRLESDATLLKTIVVDRSTILLQNLGLVVTSFIIAFILNWRLTLV 857
Cdd:TIGR01842 74 GEKLDGALNQPIFAASFSATL-------RRGSGDGLQALRDLDQLRQFLTGPGLFAFFDAPWMPIYLLVCFLLHPWIGIL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 858 VLATYPLVISGHISEKLFMQGYGGDLNKAYLKANMLAGESVSNIRTVAAFC----AEEKILELYSRELLEPSKSSFRrgq 933
Cdd:TIGR01842 147 ALGGAVVLVGLALLNNRATKKPLKEATEASIRANNLADSALRNAEVIEAMGmmgnLTKRWGRFHSKYLSAQSAASDR--- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 934 iAGLFYGVSQFFIFSSYGLALWYGSTLMDKGLAgfksvmkTFMVLIVTALAMGEtlALAP-DLLKGN--QMVASVfEILD 1010
Cdd:TIGR01842 224 -AGMLSNLSKYFRIVLQSLVLGLGAYLAIDGEI-------TPGMMIAGSILVGR--ALAPiDGAIGGwkQFSGAR-QAYK 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1011 RKTQIVGETSE-----ELNNVEGTIELKGVHFSYPSrPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPT 1085
Cdd:TIGR01842 293 RLNELLANYPSrdpamPLPEPEGHLSVENVTIVPPG-GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPT 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1086 AGKVMIEGKDIKKLDLKALRKHIGLVQQEPALFATTIYENILYGNEGASQSEVVESAMLANAHSFITSLPEGYSTKVGER 1165
Cdd:TIGR01842 372 SGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPG 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1166 GVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANR-TTVVVAHRLSTIKNADTISVLHGGKI 1244
Cdd:TIGR01842 452 GATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGiTVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
410-1258 |
1.56e-50 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 196.54 E-value: 1.56e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 410 YPSRPDVVIFDrLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVlldgnniseldikWLRGQIGLVNQEPALF 489
Cdd:PTZ00243 668 FELEPKVLLRD-VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIM 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 490 ATTIRENILYgKDDATAEEITRAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEATSA 569
Cdd:PTZ00243 734 NATVRGNILF-FDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 570 LDAE-SEKSVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVHEGKIVEFGNHENLISNPdgAYSSLlrlqeTASLQRNP 648
Cdd:PTZ00243 813 LDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS--LYATL-----AAELKENK 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 649 SLNRTLSRPHSIKYSRELSRTRSSFCSERESVTRPDGADPSKKvKVTVGRLysMIRPD-------W-MY----GVCGTIC 716
Cdd:PTZ00243 886 DSKEGDADAEVAEVDAAPGGAVDHEPPVAKQEGNAEGGDGAAL-DAAAGRL--MTREEkasgsvpWsTYvaylRFCGGLH 962
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 717 AfiAGSQMPLFA----LGVSQAL-VSYYS----GWDETQKEIKKIAILFCCASVITLIVYTiehiCFGTM--GERltlrv 785
Cdd:PTZ00243 963 A--AGFVLATFAvtelVTVSSGVwLSMWStrsfKLSAATYLYVYLGIVLLGTFSVPLRFFL----SYEAMrrGSR----- 1031
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 786 reNMFRAILKN----EIGWFDevdnTSSM--LASRLESDATLLKTIVVDrSTILLQNLGLVVTSFIIAFILNWRLTLVVL 859
Cdd:PTZ00243 1032 --NMHRDLLRSvsrgTMSFFD----TTPLgrILNRFSRDIDILDNTLPM-SYLYLLQCLFSICSSILVTSASQPFVLVAL 1104
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 860 ATyplviSGHISEKLfMQGYGGD-----LNKAYLKANM--LAGESVSNIRTVAAF-CAEEKILELYSRELLEPSkssfrr 931
Cdd:PTZ00243 1105 VP-----CGYLYYRL-MQFYNSAnreirRIKSVAKSPVftLLEEALQGSATITAYgKAHLVMQEALRRLDVVYS------ 1172
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 932 gqiAGLFYGVSQFFIfssyGLALWYGSTLMDKGLAgFKSVMKTFMV-------LIVTALAMGETLALAPDLLKgnQMVA- 1003
Cdd:PTZ00243 1173 ---CSYLENVANRWL----GVRVEFLSNIVVTVIA-LIGVIGTMLRatsqeigLVSLSLTMAMQTTATLNWLV--RQVAt 1242
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1004 ------SVFEILDRKTQIVGETSEELN--------------NVEGTIELKGVHFS----YPSRPDVVIFRDFDLIVRAGK 1059
Cdd:PTZ00243 1243 veadmnSVERLLYYTDEVPHEDMPELDeevdalerrtgmaaDVTGTVVIEPASPTsaapHPVQAGSLVFEGVQMRYREGL 1322
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1060 SMAL---------------VGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIGLVQQEPALFATTIYE 1124
Cdd:PTZ00243 1323 PLVLrgvsfriaprekvgiVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQ 1402
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1125 NILYGNEgASQSEVVESAMLANAHSFITSLPEGYSTKVGERGVQMSGGQRQRIAIARAILK-NPAILLLDEATSALDVES 1203
Cdd:PTZ00243 1403 NVDPFLE-ASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKkGSGFILMDEATANIDPAL 1481
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*
gi 79487035 1204 ERVVQQALDRLMANRTTVVVAHRLSTIKNADTISVLHGGKIVEQGSHRKLVLNKS 1258
Cdd:PTZ00243 1482 DRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQ 1536
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
401-619 |
1.00e-49 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 175.83 E-value: 1.00e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPsrpDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYE-----PISGAVLLDGNNISELDIK-- 473
Cdd:cd03260 1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 474 WLRGQIGLVNQEPALFATTIRENILYG------KDDATAEEITRAAkLSEAisfinNLPEGFETQVGERGiqLSGGQKQR 547
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDERVEEA-LRKA-----ALWDEVKDRLHALG--LSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79487035 548 IAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRVMVGRTTVVVAHRLSTV-RNADIIAVVHEGKIVEFG 619
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAaRVADRTAFLLNGRLVEFG 222
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
918-1227 |
1.34e-49 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 185.26 E-value: 1.34e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 918 SRELLEPSKssfRRGQIAGLFYGVSQFFIFSSYGLALWYGST-LMDKGLAGfksvmKTFMVLIVTALAMGETLALAPD-- 994
Cdd:TIGR02868 223 DRELTRAER---RAAAATALGAALTLLAAGLAVLGALWAGGPaVADGRLAP-----VTLAVLVLLPLAAFEAFAALPAaa 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 995 --LLKGNQMVASVFEILDRKtQIVGETSEELNNVEG----TIELKGVHFSYPSRPDVviFRDFDLIVRAGKSMALVGQSG 1068
Cdd:TIGR02868 295 qqLTRVRAAAERIVEVLDAA-GPVAEGSAPAAGAVGlgkpTLELRDLSAGYPGAPPV--LDGVSLDLPPGERVAILGPSG 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1069 SGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIGLVQQEPALFATTIYENILYGNEGASQSEVVESAMLANAH 1148
Cdd:TIGR02868 372 SGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLA 451
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 1149 SFITSLPEGYSTKVGERGVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVVVAHRL 1227
Cdd:TIGR02868 452 DWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1030-1244 |
1.25e-48 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 170.86 E-value: 1.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRPDVVIfRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIG 1109
Cdd:cd03246 1 LEVENVSFRYPGAEPPVL-RNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1110 LVQQEPALFATTIYENILygnegasqsevvesamlanahsfitslpegystkvgergvqmSGGQRQRIAIARAILKNPAI 1189
Cdd:cd03246 80 YLPQDDELFSGSIAENIL------------------------------------------SGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 79487035 1190 LLLDEATSALDVESERVVQQALDRL-MANRTTVVVAHRLSTIKNADTISVLHGGKI 1244
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
399-635 |
5.58e-48 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 183.79 E-value: 5.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 399 GHIQFKDATFSYPSRPDVVifDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQ 478
Cdd:TIGR01193 472 GDIVINDVSYSYGYGSNIL--SDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQF 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 479 IGLVNQEPALFATTIRENILYG-KDDATAEEITRAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRIAISRAIVKN 557
Cdd:TIGR01193 550 INYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTD 629
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 558 PSILLLDEATSALDAESEKSVQEALDRvMVGRTTVVVAHRLSTVRNADIIAVVHEGKIVEFGNHENLIsNPDGAYSSL 635
Cdd:TIGR01193 630 SKVLILDESTSNLDTITEKKIVNNLLN-LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELL-DRNGFYASL 705
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1030-1253 |
1.86e-47 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 169.44 E-value: 1.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPsrPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIG 1109
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1110 LVQQEPA--LFATTIYENILYG--NEGASQSEV---VESAM-------LANAHSFitslpegystkvgergvQMSGGQRQ 1175
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGpeNLGLPREEIrerVEEALelvglehLADRPPH-----------------ELSGGQKQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1176 RIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVVVA-HRLSTI-KNADTISVLHGGKIVEQGSHRKL 1253
Cdd:COG1122 142 RVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVaELADRVIVLDDGRIVADGTPREV 221
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
393-626 |
5.35e-47 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 177.93 E-value: 5.35e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 393 KLGKVDGHIQFKDATFSYPSrPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDI 472
Cdd:TIGR01842 309 PLPEPEGHLSVENVTIVPPG-GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDR 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 473 KWLRGQIGLVNQEPALFATTIRENILYGKDDATAEEITRAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRIAISR 552
Cdd:TIGR01842 388 ETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALAR 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79487035 553 AIVKNPSILLLDEATSALDAESEKSVQEALDRVMV-GRTTVVVAHRLSTVRNADIIAVVHEGKIVEFGNHENLIS 626
Cdd:TIGR01842 468 ALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKArGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLA 542
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1030-1261 |
2.71e-46 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 175.09 E-value: 2.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRP--DVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKL---DLKAL 1104
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLsrrSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1105 RKHIGLVQQEP--ALFAT-TIYENILYG---NEGASQSEV---VESAMLAnahsfiTSLPEGYSTKvgeRGVQMSGGQRQ 1175
Cdd:COG1123 341 RRRVQMVFQDPysSLNPRmTVGDIIAEPlrlHGLLSRAERrerVAELLER------VGLPPDLADR---YPHELSGGQRQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1176 RIAIARAILKNPAILLLDEATSALDVeseRVVQQALDRLMA-----NRTTVVVAHRLSTIKN-ADTISVLHGGKIVEQGS 1249
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALDV---SVQAQILNLLRDlqrelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGP 488
|
250
....*....|..
gi 79487035 1250 HRKLVLNKSGPY 1261
Cdd:COG1123 489 TEEVFANPQHPY 500
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1030-1225 |
3.44e-46 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 164.99 E-value: 3.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRPdvvIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIG 1109
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1110 LVQQEPALFATTIYENILYGNEGASQSEVVE--SAMLANAHsfitsLPEGY-STKVGErgvqMSGGQRQRIAIARAILKN 1186
Cdd:COG4619 78 YVPQEPALWGGTVRDNLPFPFQLRERKFDREraLELLERLG-----LPPDIlDKPVER----LSGGERQRLALIRALLLQ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 79487035 1187 PAILLLDEATSALDVESERVVQQALDRLMA--NRTTVVVAH 1225
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYLAeeGRAVLWVSH 189
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
401-629 |
1.98e-45 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 163.66 E-value: 1.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPsrPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIG 480
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 LVNQEPA--LFATTIRENILYG-----KDDATAEEitRAAKLSEAIsfinNLpEGFEtqvgERGI-QLSGGQKQRIAISR 552
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGpenlgLPREEIRE--RVEEALELV----GL-EHLA----DRPPhELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 553 AIVKNPSILLLDEATSALDAESEKSVQEALDRVMVGRTTVVVA-HRLSTV-RNADIIAVVHEGKIVEFGNHENLISNPD 629
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVaELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
401-632 |
3.26e-45 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 171.62 E-value: 3.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRP--DVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISEL---DIKWL 475
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLsrrSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 476 RGQIGLVNQEP--ALFAT-TIRENILYG---KDDATAEEIT-RAAKLSEAIsfinNLPEGFEtqvgERGI-QLSGGQKQR 547
Cdd:COG1123 341 RRRVQMVFQDPysSLNPRmTVGDIIAEPlrlHGLLSRAERReRVAELLERV----GLPPDLA----DRYPhELSGGQRQR 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 548 IAISRAIVKNPSILLLDEATSALDAesekSVQEALDRVMV------GRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFGN 620
Cdd:COG1123 413 VAIARALALEPKLLILDEPTSALDV----SVQAQILNLLRdlqrelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGP 488
|
250
....*....|..
gi 79487035 621 HENLISNPDGAY 632
Cdd:COG1123 489 TEEVFANPQHPY 500
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1030-1248 |
3.71e-45 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 160.94 E-value: 3.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRpDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDlKALRKHIG 1109
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1110 LVQQEPALFATTIYENIlygnegasqsevvesamlanahsfitslpegystkvgerGVQMSGGQRQRIAIARAILKNPAI 1189
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 1190 LLLDEATSALDVESERVVQQALDRLMANRTTVVVAHRLSTIKNADTISVLHGGKIVEQG 1248
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
401-628 |
3.86e-45 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 163.24 E-value: 3.86e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPDVVifDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIG 480
Cdd:cd03295 1 IEFENVTKRYGGGKKAV--NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 LVNQEPALFA-TTIRENI-LYGKDDATAEEiTRAAKLSEAISFINNLPEGFetqvGER-GIQLSGGQKQRIAISRAIVKN 557
Cdd:cd03295 79 YVIQQIGLFPhMTVEENIaLVPKLLKWPKE-KIRERADELLALVGLDPAEF----ADRyPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79487035 558 PSILLLDEATSALDAESEKSVQEALDRV--MVGRTTVVVAHRL-STVRNADIIAVVHEGKIVEFGNHENLISNP 628
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLqqELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
401-614 |
6.79e-45 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 161.10 E-value: 6.79e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPDV--VIFDRLNLAIPAGKIVALVGGSGSGKSTVISLI--ErfYEPISGAVlldgnniseldikWLR 476
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSV-------------SVP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 477 GQIGLVNQEPALFATTIRENILYGK--DDATAEEITRAAKLSEAISfinNLPEGFETQVGERGIQLSGGQKQRIAISRAI 554
Cdd:cd03250 66 GSIAYVSQEPWIQNGTIRENILFGKpfDEERYEKVIKACALEPDLE---ILPDGDLTEIGEKGINLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79487035 555 VKNPSILLLDEATSALDAES-----EKSVQEALdrvMVGRTTVVVAHRLSTVRNADIIAVVHEGK 614
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVgrhifENCILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
401-596 |
1.43e-44 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 160.37 E-value: 1.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPdvvIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIG 480
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 LVNQEPALFATTIRENILYG---KDDATAEEitRAAKLSEAIsfinNLPEGF-ETQVGErgiqLSGGQKQRIAISRAIVK 556
Cdd:COG4619 78 YVPQEPALWGGTVRDNLPFPfqlRERKFDRE--RALELLERL----GLPPDIlDKPVER----LSGGERQRLALIRALLL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 79487035 557 NPSILLLDEATSALDAESEKSVQEALDRVM--VGRTTVVVAH 596
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYLaeEGRAVLWVSH 189
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
415-619 |
1.70e-44 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 160.38 E-value: 1.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 415 DVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKwlRGQIGLVNQEPALFAT-TI 493
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFPHlTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 494 RENILYGKDDATAEEITRAAKLSEAISFInnlpeGFETQVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAE 573
Cdd:cd03259 90 AENIAFGLKLRGVPKAEIRARVRELLELV-----GLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 79487035 574 SEKSVQEALDRVM--VGRTTVVVAHRLS-TVRNADIIAVVHEGKIVEFG 619
Cdd:cd03259 165 LREELREELKELQreLGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
401-615 |
2.59e-44 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 158.53 E-value: 2.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPDVVIFDrLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIG 480
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRN-VSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 LVNQEPALFATTIRENILygkddataeeitraaklseaisfinnlpegfetqvgergiqlSGGQKQRIAISRAIVKNPSI 560
Cdd:cd03246 80 YLPQDDELFSGSIAENIL------------------------------------------SGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 79487035 561 LLLDEATSALDAESEKSVQEALDRV-MVGRTTVVVAHRLSTVRNADIIAVVHEGKI 615
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
401-619 |
4.04e-44 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 157.86 E-value: 4.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRpDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDiKWLRGQIG 480
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 LVNQEPALFATTIRENIlygkddataeeitraaklseaisfinnlpegfetqvgerGIQLSGGQKQRIAISRAIVKNPSI 560
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 561 LLLDEATSALDAESEKSVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVHEGKIVEFG 619
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
401-628 |
6.08e-44 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 159.67 E-value: 6.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRP-DVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRG-- 477
Cdd:cd03258 2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 478 -QIGLVNQEPALFAT-TIRENILYGKDDATAEEITRAAKLSEAISFInnlpeGFETQVGERGIQLSGGQKQRIAISRAIV 555
Cdd:cd03258 82 rRIGMIFQHFNLLSSrTVFENVALPLEIAGVPKAEIEERVLELLELV-----GLEDKADAYPAQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79487035 556 KNPSILLLDEATSALDAESEKSVQEALDRV--MVGRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFGNHENLISNP 628
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILALLRDInrELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1030-1249 |
7.39e-44 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 159.46 E-value: 7.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPsrpDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKlDLKALRKHIG 1109
Cdd:COG1131 1 IEVRGLTKRYG---DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1110 LVQQEPALFAT-TIYENI-----LYGNEGASQSEVVEsAMLAnahsfITSLPEGYSTKVGergvQMSGGQRQRIAIARAI 1183
Cdd:COG1131 77 YVPQEPALYPDlTVRENLrffarLYGLPRKEARERID-ELLE-----LFGLTDAADRKVG----TLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 1184 LKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVVVA-HRLSTI-KNADTISVLHGGKIVEQGS 1249
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAeRLCDRVAIIDKGRIVADGT 214
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1030-1253 |
9.45e-44 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 158.88 E-value: 9.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPsrpDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYD-----PTAGKVMIEGKDIKKLDLK-- 1102
Cdd:cd03260 1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1103 ALRKHIGLVQQEPALFATTIYENILYG------NEGASQSEVVESAmLANAHsfitsLPEGYSTKVGERGvqMSGGQRQR 1176
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDERVEEA-LRKAA-----LWDEVKDRLHALG--LSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 1177 IAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVVVAHRLSTIKN-ADTISVLHGGKIVEQGSHRKL 1253
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1030-1248 |
1.05e-43 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 158.82 E-value: 1.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRPDVV-IFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLD---LKALR 1105
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1106 KHIGLVQQEP--ALFAT-TIYENI------LYGNEGASQSEVVESAMLA---NAHSFITSLPEgystkvgergvQMSGGQ 1173
Cdd:cd03257 82 KEIQMVFQDPmsSLNPRmTIGEQIaeplriHGKLSKKEARKEAVLLLLVgvgLPEEVLNRYPH-----------ELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 1174 RQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANR-TTVV-VAHRLSTIKN-ADTISVLHGGKIVEQG 1248
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELgLTLLfITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1030-1249 |
1.65e-43 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 158.60 E-value: 1.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRpdvVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLD---LKALRK 1106
Cdd:COG1127 6 IEVRNLTKSFGDR---VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1107 HIGLVQQEPALF-ATTIYENILYG---NEGASQSEVVESAMLANAHsfitslpegystkVGERGV------QMSGGQRQR 1176
Cdd:COG1127 83 RIGMLFQGGALFdSLTVFENVAFPlreHTDLSEAEIRELVLEKLEL-------------VGLPGAadkmpsELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1177 IAIARAILKNPAILLLDEATSALDVESERVvqqaLDRLMANR------TTVVVAHRLSTIKN-ADTISVLHGGKIVEQGS 1249
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAV----IDELIRELrdelglTSVVVTHDLDSAFAiADRVAVLADGKIIAEGT 225
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1030-1249 |
1.77e-43 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 158.43 E-value: 1.77e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRpdvVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKL---DLKALRK 1106
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLseaELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1107 HIGLVQQEPALF-ATTIYENI---LYGNEGASQSEVVESAMLANAhsfitslpegystKVGERGV------QMSGGQRQR 1176
Cdd:cd03261 78 RMGMLFQSGALFdSLTVFENVafpLREHTRLSEEEIREIVLEKLE-------------AVGLRGAedlypaELSGGMKKR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79487035 1177 IAIARAILKNPAILLLDEATSALDVESERVVQQALDRL--MANRTTVVVAHRLSTI-KNADTISVLHGGKIVEQGS 1249
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGT 220
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1030-1247 |
1.88e-43 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 157.90 E-value: 1.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPS-RPDVVIFRDFDLIVRAGKSMALVGQSGSGKS---SVISLILRfydPTAGKVMIEGKDIKKLDLKAL- 1104
Cdd:COG1136 5 LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKStllNILGGLDR---PTSGEVLIDGQDISSLSERELa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1105 ---RKHIGLVQQEPALFAT-TIYENILYGNE--GASQSEVVESAM-------LAN-AHSFITslpegystkvgergvQMS 1170
Cdd:COG1136 82 rlrRRHIGFVFQFFNLLPElTALENVALPLLlaGVSRKERRERARellervgLGDrLDHRPS---------------QLS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 1171 GGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMA--NRTTVVVAHRLSTIKNADTISVLHGGKIVEQ 1247
Cdd:COG1136 147 GGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1031-1243 |
2.91e-43 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 156.86 E-value: 2.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1031 ELKGVHFSYPSRpDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIGL 1110
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1111 VQQEPA--LFATTIYENILYG--NEGASQSEVVESAMLANAHSFITSLPEgYSTKvgergvQMSGGQRQRIAIARAILKN 1186
Cdd:cd03225 80 VFQNPDdqFFGPTVEEEVAFGleNLGLPEEEIEERVEEALELVGLEGLRD-RSPF------TLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 1187 PAILLLDEATSALDVESERVVQQALDRLMANRTTVVVA-HRLSTIKN-ADTISVLHGGK 1243
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLEDGK 211
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1028-1249 |
4.07e-43 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 156.42 E-value: 4.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1028 GTIELKGVHFSY-PSRPDVVifRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRK 1106
Cdd:cd03369 5 GEIEVENLSVRYaPDLPPVL--KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1107 HIGLVQQEPALFATTIYENILYGNEgASQSEVVESamlanahsfitslpegysTKVGERGVQMSGGQRQRIAIARAILKN 1186
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLDPFDE-YSDEEIYGA------------------LRVSEGGLNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79487035 1187 PAILLLDEATSALDVESERVVQQALDRLMANRTTVVVAHRLSTIKNADTISVLHGGKIVEQGS 1249
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
402-614 |
8.02e-43 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 155.70 E-value: 8.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 402 QFKDATFSYPSRpDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIGL 481
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 482 VNQEPA--LFATTIRENILYG------KDDATAEEITRAAKLSEAISFINNLPEgfetqvgergiQLSGGQKQRIAISRA 553
Cdd:cd03225 80 VFQNPDdqFFGPTVEEEVAFGlenlglPEEEIEERVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79487035 554 IVKNPSILLLDEATSALDAESEKSVQEALDRVM-VGRTTVVVAHRLSTVRN-ADIIAVVHEGK 614
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKLKaEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
419-568 |
1.58e-42 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 152.42 E-value: 1.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 419 FDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIGLVNQEPALF-ATTIRENI 497
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79487035 498 LYGkddATAEEITRAAKLSEAISFINNLPEGF--ETQVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEATS 568
Cdd:pfam00005 81 RLG---LLLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
401-619 |
3.88e-42 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 154.20 E-value: 3.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPDVV-IFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELD---IKWLR 476
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 477 GQIGLVNQEP--ALFAT-TIRENI-----LYGKDDATAEEITRAAKLSEAIsfinNLPEGFETQvgeRGIQLSGGQKQRI 548
Cdd:cd03257 82 KEIQMVFQDPmsSLNPRmTIGEQIaeplrIHGKLSKKEARKEAVLLLLVGV----GLPEEVLNR---YPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79487035 549 AISRAIVKNPSILLLDEATSALDAESEKSVQEALD--RVMVGRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFG 619
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKklQEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1030-1256 |
5.22e-42 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 153.89 E-value: 5.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRP-DVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKL---DLKALR 1105
Cdd:cd03258 2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLsgkELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1106 KHIGLVQQEPALFAT-TIYENILYGNE--GASQSEVVESamlanahsfITSLPE--GYSTKVGERGVQMSGGQRQRIAIA 1180
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALPLEiaGVPKAEIEER---------VLELLElvGLEDKADAYPAQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1181 RAILKNPAILLLDEATSALDVESERVVQQALDRLmaNR----TTVVVAHRLSTIKN-ADTISVLHGGKIVEQGSHRKLVL 1255
Cdd:cd03258 153 RALANNPKVLLCDEATSALDPETTQSILALLRDI--NRelglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFA 230
|
.
gi 79487035 1256 N 1256
Cdd:cd03258 231 N 231
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1030-1248 |
6.66e-42 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 153.06 E-value: 6.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSrpdVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIkkLDLKALRKHIG 1109
Cdd:cd03259 1 LELKGLSKTYGS---VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV--TGVPPERRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1110 LVQQEPALFAT-TIYENILYG------NEGASQSEVVESAMLANAHSFITSLPEgystkvgergvQMSGGQRQRIAIARA 1182
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGlklrgvPKAEIRARVRELLELVGLEGLLNRYPH-----------ELSGGQQQRVALARA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 1183 ILKNPAILLLDEATSALDVESERVVQQALDRLMANR--TTVVVAHRLS-TIKNADTISVLHGGKIVEQG 1248
Cdd:cd03259 145 LAREPSLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1030-1263 |
8.69e-42 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 153.81 E-value: 8.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRP-DVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHI 1108
Cdd:COG1124 2 LEVRNLSVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1109 GLVQQEPAL-------FATTIYENILYGNEGASQSEVVEsaMLANAHsfitsLPEGYSTKvgeRGVQMSGGQRQRIAIAR 1181
Cdd:COG1124 82 QMVFQDPYAslhprhtVDRILAEPLRIHGLPDREERIAE--LLEQVG-----LPPSFLDR---YPHQLSGGQRQRVAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1182 AILKNPAILLLDEATSALDVeserVVQ----QALDRLMANR--TTVVVAHRLSTIKN-ADTISVLHGGKIVEQGSHRKLV 1254
Cdd:COG1124 152 ALILEPELLLLDEPTSALDV----SVQaeilNLLKDLREERglTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLL 227
|
....*....
gi 79487035 1255 LNKSGPYFK 1263
Cdd:COG1124 228 AGPKHPYTR 236
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1030-1243 |
9.40e-42 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 152.24 E-value: 9.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRPDV--VIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKdikkldlkalrkh 1107
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1108 IGLVQQEPALFATTIYENILYGNEGASQ--SEVVESAMLanaHSFITSLPEGYSTKVGERGVQMSGGQRQRIAIARAILK 1185
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPFDEEryEKVIKACAL---EPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1186 NPAILLLDEATSALDVE-SERVVQQAL-DRLMANRTTVVVAHRLSTIKNADTISVLHGGK 1243
Cdd:cd03250 145 DADIYLLDDPLSAVDAHvGRHIFENCIlGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
711-993 |
1.87e-41 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 155.13 E-value: 1.87e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 711 VCGTICAFIAGSQMPLFALGVSQALVSYYSG------------------WDETQKEIKKIAILFCCASVITLIVYTIEHI 772
Cdd:cd18558 2 VVGILCAIIHGGLLPAFMVIFGDMTDSFTNGgmtnitgnssglnssagpFEKLEEEMTLYAYYYLIIGAIVLITAYIQGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 773 CFGTMGERLTLRVRENMFRAILKNEIGWFDEvdNTSSMLASRLESDATLLKTIVVDRSTILLQNLGLVVTSFIIAFILNW 852
Cdd:cd18558 82 FWGLAAGRQTKKIRYKFFHAIMRQEIGWFDV--NDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 853 RLTLVVLATYPLV-ISGHISEKLfMQGYGGDLNKAYLKANMLAGESVSNIRTVAAFCAEEKILELYSRELLEPSKSSFRR 931
Cdd:cd18558 160 KLTLVILAISPVLgLSAVVWAKI-LSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKK 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79487035 932 GQIAGLFYGVSQFFIFSSYGLALWYGSTL-MDKGLAGFKSVMKTFMVLIVTALAMGETLALAP 993
Cdd:cd18558 239 AITFNISMGAAFLLIYASYALAFWYGTYLvTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEA 301
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1030-1244 |
2.30e-41 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 151.49 E-value: 2.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRPD-VVIFRDFDLIVRAGKSMALVGQSGSGKS---SVISLILRfydPTAGKVMIEGKDIKKLDLKAL- 1104
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKStllNILGGLDR---PTSGEVRVDGTDISKLSEKELa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1105 ---RKHIGLVQQEPALFAT-TIYENILYGNEGASqseVVESAMLANAHSFITS--LPEGYSTKVGergvQMSGGQRQRIA 1178
Cdd:cd03255 78 afrRRHIGFVFQSFNLLPDlTALENVELPLLLAG---VPKKERRERAEELLERvgLGDRLNHYPS----ELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 1179 IARAILKNPAILLLDEATSALDVESERVVQQALDRL--MANRTTVVVAHRLSTIKNADTISVLHGGKI 1244
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
401-629 |
2.42e-41 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 152.44 E-value: 2.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRpdvVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIK---WLRG 477
Cdd:COG1127 6 IEVRNLTKSFGDR---VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 478 QIGLVNQEPALF-ATTIRENILY------GKDDATAEEITRaAKLSeaisfinnlpegfetQVGERGI------QLSGGQ 544
Cdd:COG1127 83 RIGMLFQGGALFdSLTVFENVAFplrehtDLSEAEIRELVL-EKLE---------------LVGLPGAadkmpsELSGGM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 545 KQRIAISRAIVKNPSILLLDEATSALDAESE-------KSVQEALdrvmvGRTTVVVAHRLSTVRN-ADIIAVVHEGKIV 616
Cdd:COG1127 147 RKRVALARALALDPEILLYDEPTAGLDPITSavideliRELRDEL-----GLTSVVVTHDLDSAFAiADRVAVLADGKII 221
|
250
....*....|...
gi 79487035 617 EFGNHENLISNPD 629
Cdd:COG1127 222 AEGTPEELLASDD 234
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
400-628 |
2.51e-41 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 155.62 E-value: 2.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 400 HIQFKDATFSYPSRP-DVVIFDRLNLAIPAGKIVALVGGSGSGKST---VISLIERfyePISGAVLLDGNNISELDIKWL 475
Cdd:COG1135 1 MIELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLER---PTSGSVLVDGVDLTALSEREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 476 RG---QIGLVNQEPALFAT-TIRENILY-----GKDDATAEEitRAAKLseaISFI------NNLPEgfetqvgergiQL 540
Cdd:COG1135 78 RAarrKIGMIFQHFNLLSSrTVAENVALpleiaGVPKAEIRK--RVAEL---LELVglsdkaDAYPS-----------QL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 541 SGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRV---MvGRTTVVVAHRLSTVRN-ADIIAVVHEGKIV 616
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDInreL-GLTIVLITHEMDVVRRiCDRVAVLENGRIV 220
|
250
....*....|..
gi 79487035 617 EFGNHENLISNP 628
Cdd:COG1135 221 EQGPVLDVFANP 232
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1030-1249 |
2.70e-41 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 152.51 E-value: 2.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRPdvvIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIG 1109
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1110 LV-QQEPALFATTIYENILYG---------NEGASQSEVVESAM-LANAHSFItslpegystkvgERGV-QMSGGQRQRI 1177
Cdd:COG1120 79 YVpQEPPAPFGLTVRELVALGryphlglfgRPSAEDREAVEEALeRTGLEHLA------------DRPVdELSGGERQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79487035 1178 AIARAILKNPAILLLDEATSALDVESERVVQQALDRL--MANRTTVVVAHRLS-TIKNADTISVLHGGKIVEQGS 1249
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGP 221
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
401-617 |
3.60e-41 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 151.35 E-value: 3.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPS-RPDVVIFDRLNLAIPAGKIVALVGGSGSGKST---VISLIERfyePISGAVLLDGNNISELDIK--- 473
Cdd:COG1136 5 LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDISSLSERela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 474 WLRGQ-IGLVNQEPALFAT-TIRENILY-----GKDDATAEEitRAAKLSEAI---SFINNLPEgfetqvgergiQLSGG 543
Cdd:COG1136 82 RLRRRhIGFVFQFFNLLPElTALENVALplllaGVSRKERRE--RARELLERVglgDRLDHRPS-----------QLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79487035 544 QKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRV--MVGRTTVVVAHRLSTVRNADIIAVVHEGKIVE 617
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
401-628 |
4.71e-41 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 155.26 E-value: 4.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPsrpDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIkWLRGqIG 480
Cdd:COG3842 6 LELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPP-EKRN-VG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 LVNQEPALFA-TTIRENILYG--KDDATAEEItrAAKLSEAISFINnLpEGFEtqvgERGI-QLSGGQKQRIAISRAIVK 556
Cdd:COG3842 81 MVFQDYALFPhLTVAENVAFGlrMRGVPKAEI--RARVAELLELVG-L-EGLA----DRYPhQLSGGQQQRVALARALAP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79487035 557 NPSILLLDEATSALDAESEKSVQEALDRVM--VGRTTVVVAHRLS---TVrnADIIAVVHEGKIVEFGNHENLISNP 628
Cdd:COG3842 153 EPRVLLLDEPLSALDAKLREEMREELRRLQreLGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEEIYERP 227
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
401-614 |
6.42e-41 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 148.87 E-value: 6.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPsrpDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELD--IKWLRGQ 478
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 479 IGLVNQEPALFAT-TIRENILYGkddataeeitraaklseaisfinnlpegfetqvgergiqLSGGQKQRIAISRAIVKN 557
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 558 PSILLLDEATSALDAESEKSVQEALDRV--MVGRTTVVVAHRLSTVRN-ADIIAVVHEGK 614
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
401-629 |
6.74e-41 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 150.73 E-value: 6.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRpdvVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISEL---DIKWLRG 477
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLseaELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 478 QIGLVNQEPALF-ATTIRENI---LYGKDDATAEEITRAA--KLSEAisfinnlpeGFETQVGERGIQLSGGQKQRIAIS 551
Cdd:cd03261 78 RMGMLFQSGALFdSLTVFENVafpLREHTRLSEEEIREIVleKLEAV---------GLRGAEDLYPAELSGGMKKRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 552 RAIVKNPSILLLDEATSALD-------AESEKSVQEALdrvmvGRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFGNHEN 623
Cdd:cd03261 149 RALALDPELLLYDEPTAGLDpiasgviDDLIRSLKKEL-----GLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEE 223
|
....*.
gi 79487035 624 LISNPD 629
Cdd:cd03261 224 LRASDD 229
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
415-628 |
1.21e-40 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 150.14 E-value: 1.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 415 DVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNI--SELDIKWLRGQIGLVNQEPALFA-T 491
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKVGMVFQQFNLFPhL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 492 TIRENILY------GKDDATAEEITRAA----KLSEaisFINNLPEgfetqvgergiQLSGGQKQRIAISRAIVKNPSIL 561
Cdd:COG1126 93 TVLENVTLapikvkKMSKAEAEERAMELlervGLAD---KADAYPA-----------QLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79487035 562 LLDEATSALDAEsekSVQEALDrVMV-----GRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFGNHENLISNP 628
Cdd:COG1126 159 LFDEPTSALDPE---LVGEVLD-VMRdlakeGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEFFENP 227
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
77-349 |
1.28e-40 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 151.64 E-value: 1.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 77 MTLGSVGACIHGASVPIFFIFFGKLINIIglaylFPKQASH--RVAKYSLDFVYLSVAILFSSWLEVACWMHTGERQAAK 154
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVL-----LPDGDPEtqALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 155 MRRAYLRSMLSQDISLFDTeASTGEVISAITSDILVVQDALSEKVGNFLHYISRFIAGFAIGFTSVWQISLVTLSIVPLI 234
Cdd:pfam00664 76 LRRKLFKKILRQPMSFFDT-NSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 235 ALAGGIYAFVAIGLIARVRKSYIKAGEIAEEVIGNVRTVQAFTGEERAVRLYREALENTYKYGRKAGLTKGLGLGSMHCV 314
Cdd:pfam00664 155 ILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFI 234
|
250 260 270
....*....|....*....|....*....|....*
gi 79487035 315 LFLSWALLVWFTSVVVHKDIADGGKSFTTMLNVVI 349
Cdd:pfam00664 235 GYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQ 269
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1030-1249 |
1.31e-40 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 150.39 E-value: 1.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSrpdVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKAlRKHIG 1109
Cdd:COG4555 2 IEVENLSKKYGK---VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREA-RRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1110 LVQQEPALFAT-TIYENI-----LYGNEGASQSEVVESAmlanAHSFItsLPEGYSTKVGErgvqMSGGQRQRIAIARAI 1183
Cdd:COG4555 78 VLPDERGLYDRlTVRENIryfaeLYGLFDEELKKRIEEL----IELLG--LEEFLDRRVGE----LSTGMKKKVALARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 1184 LKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVVVA-HRLSTIKN-ADTISVLHGGKIVEQGS 1249
Cdd:COG4555 148 VHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGS 215
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
398-619 |
2.25e-40 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 148.33 E-value: 2.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 398 DGHIQFKDATFSY-PSRPDVVifDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLR 476
Cdd:cd03369 4 HGEIEVENLSVRYaPDLPPVL--KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 477 GQIGLVNQEPALFATTIRENiLYGKDDATAEEITRAAKLSEAisfinnlpegfetqvgerGIQLSGGQKQRIAISRAIVK 556
Cdd:cd03369 82 SSLTIIPQDPTLFSGTIRSN-LDPFDEYSDEEIYGALRVSEG------------------GLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79487035 557 NPSILLLDEATSALDAESEKSVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVHEGKIVEFG 619
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
401-626 |
3.58e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 148.67 E-value: 3.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPsrpDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRgQIG 480
Cdd:COG1131 1 IEVRGLTKRYG---DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRR-RIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 LVNQEPALFAT-TIRENI-----LYGKDDATAEEitRAAKLSEAIsfinNLPEGFETQVGergiQLSGGQKQRIAISRAI 554
Cdd:COG1131 77 YVPQEPALYPDlTVRENLrffarLYGLPRKEARE--RIDELLELF----GLTDAADRKVG----TLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79487035 555 VKNPSILLLDEATSALDAESEKSVQEALDRVMVGRTTVVVA-HRLSTV-RNADIIAVVHEGKIVEFGNHENLIS 626
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAeRLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
401-630 |
1.36e-39 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 155.06 E-value: 1.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPDVVIfDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEP---ISGAVLLDGNNISELDIKWLRG 477
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAV-DGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 478 QIGLVNQEP--ALFATTIRENI---LYGKDDATAEEITRAAKLSEAIsfinnlpeGFETQVGERGIQLSGGQKQRIAISR 552
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIaeaLENLGLSRAEARARVLELLEAV--------GLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 553 AIVKNPSILLLDEATSALDAESEKSVQEALDRVMV--GRTTVVVAHRLSTV-RNADIIAVVHEGKIVEFGNHENLISNPD 629
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
.
gi 79487035 630 G 630
Cdd:COG1123 236 A 236
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
401-617 |
1.61e-39 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 146.46 E-value: 1.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPS-RPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELdikwlRGQI 479
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP-----GPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 480 GLVNQEPALFA-TTIRENILYG---KDDATAEEITRAAKLSEAI---SFINNLPEgfetqvgergiQLSGGQKQRIAISR 552
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGlelQGVPKAEARERAEELLELVglsGFENAYPH-----------QLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 553 AIVKNPSILLLDEATSALDAESEKSVQEALDRVMV--GRTTVVVAHRLS-TVRNADIIAVV--HEGKIVE 617
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTHDIDeAVFLADRVVVLsaRPGRIVA 214
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1048-1197 |
6.82e-39 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 142.02 E-value: 6.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1048 FRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIGLVQQEPALF-ATTIYENI 1126
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79487035 1127 LYGNEGASQSEVVESAMLANAHSFItSLPEGYSTKVGERGVQMSGGQRQRIAIARAILKNPAILLLDEATS 1197
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKL-GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
401-619 |
7.41e-39 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 145.57 E-value: 7.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPdvvIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIG 480
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 LVNQEPAL-FATTIRENILYG-------------KDDATAEEITRAAKLSE-AisfinnlpegfetqvgERGI-QLSGGQ 544
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGryphlglfgrpsaEDREAVEEALERTGLEHlA----------------DRPVdELSGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 545 KQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRV--MVGRTTVVVAHRLS-TVRNADIIAVVHEGKIVEFG 619
Cdd:COG1120 143 RQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQG 220
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1030-1249 |
7.90e-39 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 148.71 E-value: 7.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPsrpDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIkkLDLKALRKHIG 1109
Cdd:COG3842 6 LELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV--TGLPPEKRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1110 LVQQEPALFA-TTIYENILYG--NEGASQSEVVESA--MLAnahsfITSLpEGYstkvGERGV-QMSGGQRQRIAIARAI 1183
Cdd:COG3842 81 MVFQDYALFPhLTVAENVAFGlrMRGVPKAEIRARVaeLLE-----LVGL-EGL----ADRYPhQLSGGQQQRVALARAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79487035 1184 LKNPAILLLDEATSALDVESERVVQQALDRLMANR--TTVVVAHRLS---TIknADTISVLHGGKIVEQGS 1249
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLREEMREELRRLQRELgiTFIYVTHDQEealAL--ADRIAVMNDGRIEQVGT 219
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
423-632 |
8.84e-39 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 145.86 E-value: 8.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 423 NLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRG----QIGLVNQEPALFA-TTIRENI 497
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLPhRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 498 LYGKDDATAEEITRAAKLSEAISFINnlPEGFETQVGErgiQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKS 577
Cdd:cd03294 124 AFGLEVQGVPRAEREERAAEALELVG--LEGWEHKYPD---ELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRRE 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 578 VQEALDRV--MVGRTTVVVAHRLS-TVRNADIIAVVHEGKIVEFGNHENLISNPDGAY 632
Cdd:cd03294 199 MQDELLRLqaELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTNPANDY 256
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
97-372 |
9.47e-39 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 146.55 E-value: 9.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 97 FFGKLINIIGLaylfpKQASHRVAKYSLDFVYLSVAILFSSWLEVACWMHTGERQAAKMRRAYLRSMLSQDISLFDtEAS 176
Cdd:cd18557 18 LIGRLIDTIIK-----GGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFD-KHK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 177 TGEVISAITSDILVVQDALSEKVGNFLHYISRFIAGFAIGFTSVWQISLVTLSIVPLIALAGGIYAFVAIGLIARVRKSY 256
Cdd:cd18557 92 TGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDAL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 257 IKAGEIAEEVIGNVRTVQAFTGEERAVRLYREALENTYKYGRKAGLTKGLGLGSMHCVLFLSWALLVWF-TSVVVHKDIA 335
Cdd:cd18557 172 AKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYgGYLVLSGQLT 251
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 79487035 336 DGgksftTMLNVVIAGLSLGQAAPDISAF----VRAKAAAY 372
Cdd:cd18557 252 VG-----ELTSFILYTIMVASSVGGLSSLladiMKALGASE 287
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1030-1249 |
2.15e-38 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 147.15 E-value: 2.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRP-DVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLD---LKALR 1105
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSereLRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1106 KHIGLVQQEPALFAT-TIYENILYGNE--GASQSE----VVEsaML--------ANAHsfitslPEgystkvgergvQMS 1170
Cdd:COG1135 82 RKIGMIFQHFNLLSSrTVAENVALPLEiaGVPKAEirkrVAE--LLelvglsdkADAY------PS-----------QLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1171 GGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLmaNR----TTVVVAHRLSTIKN-ADTISVLHGGKIV 1245
Cdd:COG1135 143 GGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDI--NRelglTIVLITHEMDVVRRiCDRVAVLENGRIV 220
|
....
gi 79487035 1246 EQGS 1249
Cdd:COG1135 221 EQGP 224
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1030-1249 |
2.18e-38 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 143.60 E-value: 2.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPsrpDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDI--KKLDLKALRKH 1107
Cdd:COG1126 2 IEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1108 IGLVQQEPALFA-TTIYENILYGNE---GASQSEVVESAM--LAnahsfitslpegystKVG--ERG----VQMSGGQRQ 1175
Cdd:COG1126 79 VGMVFQQFNLFPhLTVLENVTLAPIkvkKMSKAEAEERAMelLE---------------RVGlaDKAdaypAQLSGGQQQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79487035 1176 RIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLmANR--TTVVVAHRLSTIKN-ADTISVLHGGKIVEQGS 1249
Cdd:COG1126 144 RVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDL-AKEgmTMVVVTHEMGFAREvADRVVFMDGGRIVEEGP 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1030-1244 |
2.27e-38 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 141.38 E-value: 2.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRPdvvIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKlDLKALRKHIG 1109
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1110 LVQQEPALFAT-TIYENILYgnegasqsevvesamlanahsfitslpegystkvgergvqmSGGQRQRIAIARAILKNPA 1188
Cdd:cd03230 77 YLPEEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 1189 ILLLDEATSALDVESERVVQQALDRLMANRTTVVVA-HRLSTIKN-ADTISVLHGGKI 1244
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKEGKTILLSsHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
415-628 |
3.12e-38 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 143.15 E-value: 3.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 415 DVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKwlRGQIGLVNQEPALFA-TTI 493
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTVFQNYALFPhLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 494 RENILYGKDDATAEEITRAAKLSEAISFINnlPEGFEtqvgERGI-QLSGGQKQRIAISRAIVKNPSILLLDEATSALDA 572
Cdd:cd03300 90 FENIAFGLRLKKLPKAEIKERVAEALDLVQ--LEGYA----NRKPsQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79487035 573 ESEKSVQEALDRV--MVGRTTVVVAHRLS---TVrnADIIAVVHEGKIVEFGNHENLISNP 628
Cdd:cd03300 164 KLRKDMQLELKRLqkELGITFVFVTHDQEealTM--SDRIAVMNKGKIQQIGTPEEIYEEP 222
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
401-628 |
3.58e-38 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 143.64 E-value: 3.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPdvVIFDrLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGA-----VLLDGNNI--SELDIK 473
Cdd:COG1117 12 IEVRNLNVYYGDKQ--ALKD-INLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGArvegeILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 474 WLRGQIGLVNQEPALFATTIRENILYG------KDDATAEEITRAAkLSEAisfinNLPEgfetQVGER----GIQLSGG 543
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIVEES-LRKA-----ALWD----EVKDRlkksALGLSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 544 QKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRvMVGRTTVV-VAHRLS-TVRNADIIAVVHEGKIVEFGNH 621
Cdd:COG1117 159 QQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILE-LKKDYTIViVTHNMQqAARVSDYTAFFYLGELVEFGPT 237
|
....*..
gi 79487035 622 ENLISNP 628
Cdd:COG1117 238 EQIFTNP 244
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
711-983 |
4.22e-38 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 144.32 E-value: 4.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 711 VCGTICAFIAGSQMPLFALGVSQALVSYYSGWDETQKEIKKIAILFCCASVITLIVYTIEHICFGTMGERLTLRVRENMF 790
Cdd:pfam00664 2 ILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 791 RAILKNEIGWFDevDNTSSMLASRLESDATLLKTIVVDRSTILLQNLGLVVTSFIIAFILNWRLTLVVLATYPLVISGHI 870
Cdd:pfam00664 82 KKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 871 SEKLFMQGYGGDLNKAYLKANMLAGESVSNIRTVAAFCAEEKILELYSRELLEPSKSSFRRGQIAGLFYGVSQFFIFSSY 950
Cdd:pfam00664 160 VFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSY 239
|
250 260 270
....*....|....*....|....*....|....*
gi 79487035 951 GLALWYGSTLMDKGLAGFKS--VMKTFMVLIVTAL 983
Cdd:pfam00664 240 ALALWFGAYLVISGELSVGDlvAFLSLFAQLFGPL 274
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1030-1243 |
6.04e-38 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 140.40 E-value: 6.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPsrpDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLD--LKALRKH 1107
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1108 IGLVQQEPALFAT-TIYENILYGnegasqsevvesamlanahsfitslpegystkvgergvqMSGGQRQRIAIARAILKN 1186
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1187 PAILLLDEATSALDVESERVVQQALDRLMAN--RTTVVVAHRLS-TIKNADTISVLHGGK 1243
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDeAARLADRVVVLRDGK 178
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1030-1256 |
9.05e-38 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 142.05 E-value: 9.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRPDVVifRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIG 1109
Cdd:cd03295 1 IEFENVTKRYGGGKKAV--NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1110 LVQQEPALFA-TTIYENI--LYGNEGASQSEVVESA--MLANAHSFITSLPEGYSTkvgergvQMSGGQRQRIAIARAIL 1184
Cdd:cd03295 79 YVIQQIGLFPhMTVEENIalVPKLLKWPKEKIRERAdeLLALVGLDPAEFADRYPH-------ELSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79487035 1185 KNPAILLLDEATSALDVESERVVQQALDRLMA--NRTTVVVAHRL-STIKNADTISVLHGGKIVEQGSHRKLVLN 1256
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
401-615 |
1.34e-37 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 140.70 E-value: 1.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPD-VVIFDRLNLAIPAGKIVALVGGSGSGKST---VISLIERfyePISGAVLLDGNNISELD----I 472
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVRVDGTDISKLSekelA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 473 KWLRGQIGLVNQEPALFAT-TIRENI-----LYGKDDATAEEitRAAKLSEAIsfinNLPEGFETQVGergiQLSGGQKQ 546
Cdd:cd03255 78 AFRRRHIGFVFQSFNLLPDlTALENVelpllLAGVPKKERRE--RAEELLERV----GLGDRLNHYPS----ELSGGQQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79487035 547 RIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRV--MVGRTTVVVAHRLSTVRNADIIAVVHEGKI 615
Cdd:cd03255 148 RVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1030-1249 |
1.59e-37 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 148.90 E-value: 1.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRPDVVIfRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTA---GKVMIEGKDIKKLDLKALRK 1106
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAV-DGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1107 HIGLVQQEP--ALFATTIYENILYG--NEGASQSEVVESAMLANAHSFITSLPEGYSTkvgergvQMSGGQRQRIAIARA 1182
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEAleNLGLSRAEARARVLELLEAVGLERRLDRYPH-------QLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1183 ILKNPAILLLDEATSALDVESERVVQQALDRLMANR--TTVVVAHRLSTIKN-ADTISVLHGGKIVEQGS 1249
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEiADRVVVMDDGRIVEDGP 226
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1030-1249 |
1.81e-37 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 143.66 E-value: 1.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRPDVV-IFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDP---TAGKVMIEGKDIKKLDLKALR 1105
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1106 ----KHIGLVQQEPalFAT-----TIYENI---LYGNEGASQSEV---VESAM----LANAHSFITSLPegystkvgerg 1166
Cdd:COG0444 82 kirgREIQMIFQDP--MTSlnpvmTVGDQIaepLRIHGGLSKAEArerAIELLervgLPDPERRLDRYP----------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1167 VQMSGGQRQRIAIARAILKNPAILLLDEATSALDVeserVVQ-QALDrLMAN-----RTTVV-VAHRLSTIKN-ADTISV 1238
Cdd:COG0444 149 HELSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQaQILN-LLKDlqrelGLAILfITHDLGVVAEiADRVAV 223
|
250
....*....|.
gi 79487035 1239 LHGGKIVEQGS 1249
Cdd:COG0444 224 MYAGRIVEEGP 234
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1045-1261 |
2.35e-37 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 142.01 E-value: 2.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1045 VVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKAL----RKHIGLVQQEPALFA- 1119
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPh 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1120 TTIYENILYGNE--GASQSEVVESAM----LANAHSFITSLPEgystkvgergvQMSGGQRQRIAIARAILKNPAILLLD 1193
Cdd:cd03294 117 RTVLENVAFGLEvqGVPRAEREERAAealeLVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79487035 1194 EATSALDVESERVVQQALDRLMAN--RTTVVVAHRLS-TIKNADTISVLHGGKIVEQGSHRKLVLNKSGPY 1261
Cdd:cd03294 186 EAFSALDPLIRREMQDELLRLQAElqKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTNPANDY 256
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
402-614 |
2.80e-37 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 137.76 E-value: 2.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 402 QFKDATFSYPSRPdvvIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIGL 481
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 482 VnqepalfattirenilygkddataeeitraaklseaisfinnlpegfetqvgergIQLSGGQKQRIAISRAIVKNPSIL 561
Cdd:cd00267 78 V-------------------------------------------------------PQLSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 79487035 562 LLDEATSALDAESEKSVQEALDRVMV-GRTTVVVAHRLSTVRNA-DIIAVVHEGK 614
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
401-637 |
2.92e-37 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 140.71 E-value: 2.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRP-DVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQI 479
Cdd:COG1124 2 LEVRNLSVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 480 GLVNQEPalFAT-----TIRENI-----LYGKDDATAeeitRAAKLSEAIsfinNLPEGFETQvgeRGIQLSGGQKQRIA 549
Cdd:COG1124 82 QMVFQDP--YASlhprhTVDRILaeplrIHGLPDREE----RIAELLEQV----GLPPSFLDR---YPHQLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 550 ISRAIVKNPSILLLDEATSALDAesekSVQ-EALD-----RVMVGRTTVVVAHRLSTV-RNADIIAVVHEGKIVEFGNHE 622
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDV----SVQaEILNllkdlREERGLTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTVA 224
|
250
....*....|....*
gi 79487035 623 NLISNPDGAYSSLLR 637
Cdd:COG1124 225 DLLAGPKHPYTRELL 239
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
398-587 |
3.58e-37 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 141.00 E-value: 3.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 398 DGHIQFKDATFSYPSRP-DVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDikwlr 476
Cdd:COG1116 5 APALELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 477 GQIGLVNQEPALFA-TTIRENILYG---KDDATAEEITRAAKLSEAI---SFINNLPEgfetqvgergiQLSGGQKQRIA 549
Cdd:COG1116 80 PDRGVVFQEPALLPwLTVLDNVALGlelRGVPKAERRERARELLELVglaGFEDAYPH-----------QLSGGMRQRVA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79487035 550 ISRAIVKNPSILLLDEATSALDA--------------ESEK--------SVQEAL---DRVMV 587
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDAltrerlqdellrlwQETGktvlfvthDVDEAVflaDRVVV 211
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1030-1256 |
5.47e-37 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 140.56 E-value: 5.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRPdvvIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYD--PTA---GKVMIEGKDI--KKLDLK 1102
Cdd:COG1117 12 IEVRNLNVYYGDKQ---ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGArveGEILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1103 ALRKHIGLVQQEPALFATTIYENILYG---NEGASQS---EVVESAmLANAHsfitsLPEGYSTKVGERGVQMSGGQRQR 1176
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNVAYGlrlHGIKSKSeldEIVEES-LRKAA-----LWDEVKDRLKKSALGLSGGQQQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1177 IAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVVVAH------RLStiknaDTISVLHGGKIVEQGSH 1250
Cdd:COG1117 163 LCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHnmqqaaRVS-----DYTAFFYLGELVEFGPT 237
|
....*.
gi 79487035 1251 RKLVLN 1256
Cdd:COG1117 238 EQIFTN 243
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1030-1246 |
6.70e-37 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 139.03 E-value: 6.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPsrPDVVIFRDFDLIVRAGkSMA-LVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKL---DLKALR 1105
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKG-EFVfLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1106 KHIGLVQQEPALFAT-TIYENILYGNE--GASQSEV---VESAM----LAN-AHSFitslPEgystkvgergvQMSGGQR 1174
Cdd:COG2884 79 RRIGVVFQDFRLLPDrTVYENVALPLRvtGKSRKEIrrrVREVLdlvgLSDkAKAL----PH-----------ELSGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79487035 1175 QRIAIARAILKNPAILLLDEATSALDVE-SERVVqQALDRLMANRTTVVVA-HRLSTIKNAD--TIsVLHGGKIVE 1246
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLDPEtSWEIM-ELLEEINRRGTTVLIAtHDLELVDRMPkrVL-ELEDGRLVR 217
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1031-1243 |
7.52e-37 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 136.22 E-value: 7.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1031 ELKGVHFSYPSRPdvvIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIGL 1110
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1111 VqqepalfattiyenilygnegasqsevvesamlanahsfitslpegystkvgergVQMSGGQRQRIAIARAILKNPAIL 1190
Cdd:cd00267 78 V-------------------------------------------------------PQLSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 79487035 1191 LLDEATSALDVESERVVQQALDRLMA-NRTTVVVAHRLSTIKNA-DTISVLHGGK 1243
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1030-1246 |
1.21e-36 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 139.45 E-value: 1.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRP-DVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDlkalrKHI 1108
Cdd:COG1116 8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG-----PDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1109 GLVQQEPALFA-TTIYENILYGNE--GASQSEVVESAM-------LANahsFITSLPEgystkvgergvQMSGGQRQRIA 1178
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGLElrGVPKAERRERARellelvgLAG---FEDAYPH-----------QLSGGMRQRVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 1179 IARAILKNPAILLLDEATSALDVESERVVQQALDRL-MANRTTVV-VAH------RLstiknADTISVL--HGGKIVE 1246
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLfVTHdvdeavFL-----ADRVVVLsaRPGRIVE 221
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
726-983 |
2.17e-36 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 139.62 E-value: 2.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 726 LFALGVSQALVSYYSGW-------DETQKEIKKIAILFCCASVITLIVYTIEHICFGTMGERLTLRVRENMFRAILKNEI 798
Cdd:cd18557 5 LLISSAAQLLLPYLIGRlidtiikGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 799 GWFDEvdNTSSMLASRLESDATLLKTIVVDRSTILLQNLGLVVTSFIIAFILNWRLTLVVLATYPLVISGHISEKLFMQG 878
Cdd:cd18557 85 AFFDK--HKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 879 YGGDLNKAYLKANMLAGESVSNIRTVAAFCAEEKILELYSRELLEPSKSSFRRGQIAGLFYGVSQFFIFSSYGLALWYGS 958
Cdd:cd18557 163 LSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGG 242
|
250 260
....*....|....*....|....*
gi 79487035 959 TLMdkgLAGFKSVMKTFMVLIVTAL 983
Cdd:cd18557 243 YLV---LSGQLTVGELTSFILYTIM 264
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1013-1265 |
3.44e-36 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 138.12 E-value: 3.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1013 TQIVGETSEELNNVEGTIELKGVHFSYPSRPDVVIfRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIE 1092
Cdd:cd03288 3 ASISGSSNSGLVGLGGEIKIHDLCVRYENNLKPVL-KHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1093 GKDIKKLDLKALRKHIGLVQQEPALFATTIYENiLYGNEGASQSEVVESAMLANAHSFITSLPEGYSTKVGERGVQMSGG 1172
Cdd:cd03288 82 GIDISKLPLHTLRSRLSIILQDPILFSGSIRFN-LDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1173 QRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVVVAHRLSTIKNADTISVLHGGKIVEQGSHRK 1252
Cdd:cd03288 161 QRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPEN 240
|
250
....*....|...
gi 79487035 1253 LVLNKSGPYFKLI 1265
Cdd:cd03288 241 LLAQEDGVFASLV 253
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1030-1247 |
3.51e-36 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 136.83 E-value: 3.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPS-RPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKkldlkALRKHI 1108
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT-----GPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1109 GLVQQEPALFA-TTIYENILYGNE--GASQSEVVESAmlanahsfitslpEGYSTKVGERGV------QMSGGQRQRIAI 1179
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLElqGVPKAEARERA-------------EELLELVGLSGFenayphQLSGGMRQRVAL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79487035 1180 ARAILKNPAILLLDEATSALDVESERVVQQALDRLMA-NRTTVV-VAHRLS-TIKNADTISVLHG--GKIVEQ 1247
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWReTGKTVLlVTHDIDeAVFLADRVVVLSArpGRIVAE 215
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1030-1245 |
6.52e-36 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 137.11 E-value: 6.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSrpDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKL---DLKALRK 1106
Cdd:COG3638 3 LELRNLSKRYPG--GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALrgrALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1107 HIGLVQQEPALFA-TTIYENILYGnegasqsevvesamLANAHSFITSLPEGYST-----------KVG------ERGVQ 1168
Cdd:COG3638 81 RIGMIFQQFNLVPrLSVLTNVLAG--------------RLGRTSTWRSLLGLFPPedreralealeRVGladkayQRADQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1169 MSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMA--NRTTVVVAHRLSTIKN-ADTISVLHGGKIV 1245
Cdd:COG3638 147 LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQVDLARRyADRIIGLRDGRVV 226
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
401-620 |
9.73e-36 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 136.14 E-value: 9.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSrpdVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRgQIG 480
Cdd:COG4555 2 IEVENLSKKYGK---VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARR-QIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 LVNQEPALFAT-TIRENI-----LYGKDDATAEEitRAAKLSEAisfiNNLPEGFETQVGErgiqLSGGQKQRIAISRAI 554
Cdd:COG4555 78 VLPDERGLYDRlTVRENIryfaeLYGLFDEELKK--RIEELIEL----LGLEEFLDRRVGE----LSTGMKKKVALARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 555 VKNPSILLLDEATSALDAESEKSVQEALDRVM-VGRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFGN 620
Cdd:COG4555 148 VHDPKVLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGS 215
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
382-637 |
1.65e-35 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 136.19 E-value: 1.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 382 TVTKTSAKSGRKLGKVDGHIQFKDATFSYPSRPDVVIfDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVL 461
Cdd:cd03288 1 AIASISGSSNSGLVGLGGEIKIHDLCVRYENNLKPVL-KHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 462 LDGNNISELDIKWLRGQIGLVNQEPALFATTIRENiLYGKDDATAEEITRAAKLSEAISFINNLPEGFETQVGERGIQLS 541
Cdd:cd03288 80 IDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFN-LDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 542 GGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVHEGKIVEFGNH 621
Cdd:cd03288 159 VGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTP 238
|
250
....*....|....*.
gi 79487035 622 ENLISNPDGAYSSLLR 637
Cdd:cd03288 239 ENLLAQEDGVFASLVR 254
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
404-619 |
7.87e-35 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 131.40 E-value: 7.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 404 KDATFSYPSRpdvVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIGLVN 483
Cdd:cd03214 3 ENLSVGYGGR---TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 484 QepALfattirenilygkddataeEITRAAKLSeaisfinnlpegfetqvgERGI-QLSGGQKQRIAISRAIVKNPSILL 562
Cdd:cd03214 80 Q--AL-------------------ELLGLAHLA------------------DRPFnELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79487035 563 LDEATSALDAeseKSVQEALDRVM-----VGRTTVVVAHRLS-TVRNADIIAVVHEGKIVEFG 619
Cdd:cd03214 121 LDEPTSHLDI---AHQIELLELLRrlareRGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
96-370 |
8.60e-35 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 135.07 E-value: 8.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 96 IFFGKLINIIGLAYLFPKQASHRVAKYS-----LDFVYLSVAILFSSWLEVAcwmhTGERQAAKMRRAYLRSMLSQDISL 170
Cdd:cd18780 17 YFFGQVIDAVTNHSGSGGEEALRALNQAvlillGVVLIGSIATFLRSWLFTL----AGERVVARLRKRLFSAIIAQEIAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 171 FDTeASTGEVISAITSDILVVQDALSEKVGNFLHYISRFIAGFAIGFTSVWQISLVTLSIVPLIALAGGIYAFVAIGLIA 250
Cdd:cd18780 93 FDV-TRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 251 RVRKSYIKAGEIAEEVIGNVRTVQAFTGEERAVRLYREALENTYKYGRKAGLTKGLGLGSMHCVLFLSWALLVWFTSV-V 329
Cdd:cd18780 172 KFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRlV 251
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 79487035 330 VHKDIADGG-KSFttMLNVVIAGLSLGQAAPDISAFVRAKAA 370
Cdd:cd18780 252 IDGELTTGLlTSF--LLYTLTVAMSFAFLSSLYGDFMQAVGA 291
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1031-1248 |
1.22e-34 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 131.02 E-value: 1.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1031 ELKGVHFSYPSRpdvVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIGL 1110
Cdd:cd03214 1 EVENLSVGYGGR---TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1111 VQQepALfattiyenilygnegasqsEVVEsaMLANAHSFITSLpegystkvgergvqmSGGQRQRIAIARAILKNPAIL 1190
Cdd:cd03214 78 VPQ--AL-------------------ELLG--LAHLADRPFNEL---------------SGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79487035 1191 LLDEATSALDVEServvQQALDRLMA------NRTTVVVAHRLS-TIKNADTISVLHGGKIVEQG 1248
Cdd:cd03214 120 LLDEPTSHLDIAH----QIELLELLRrlarerGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1030-1244 |
1.31e-34 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 131.88 E-value: 1.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRpdvVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDI--KKLDLKALRKH 1107
Cdd:cd03262 1 IEIKNLHKSFGDF---HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1108 IGLVQQEPALFA-TTIYENILYGN---EGASQSEVVESAMlanahsfitslpeGYSTKVG------ERGVQMSGGQRQRI 1177
Cdd:cd03262 78 VGMVFQQFNLFPhLTVLENITLAPikvKGMSKAEAEERAL-------------ELLEKVGladkadAYPAQLSGGQQQRV 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 1178 AIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANRTT-VVVAHRLSTIKN-ADTISVLHGGKI 1244
Cdd:cd03262 145 AIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTmVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
401-617 |
1.67e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 132.10 E-value: 1.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPsrPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISEL---DIKWLRG 477
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 478 QIGLVNQEPALFAT-TIRENILY-----GKDDATAEEITRAA----KLSEaisFINNLPegfetqvgergIQLSGGQKQR 547
Cdd:COG2884 80 RIGVVFQDFRLLPDrTVYENVALplrvtGKSRKEIRRRVREVldlvGLSD---KAKALP-----------HELSGGEQQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79487035 548 IAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRV-MVGrTTVVVA-HRLSTVRNAD--IIAVVHeGKIVE 617
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEInRRG-TTVLIAtHDLELVDRMPkrVLELED-GRLVR 217
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
401-615 |
2.07e-34 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 131.50 E-value: 2.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRpdvVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNI--SELDIKWLRGQ 478
Cdd:cd03262 1 IEIKNLHKSFGDF---HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 479 IGLVNQEPALFA-TTIRENILY------GKDDATAEEitRAAKLSEAIsfinnlpeGFETQVGERGIQLSGGQKQRIAIS 551
Cdd:cd03262 78 VGMVFQQFNLFPhLTVLENITLapikvkGMSKAEAEE--RALELLEKV--------GLADKADAYPAQLSGGQQQRVAIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 552 RAIVKNPSILLLDEATSALDAEsekSVQEALDrVMV-----GRTTVVVAHRLSTVRN-ADIIAVVHEGKI 615
Cdd:cd03262 148 RALAMNPKVMLFDEPTSALDPE---LVGEVLD-VMKdlaeeGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
409-628 |
2.33e-34 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 134.80 E-value: 2.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 409 SYPSRPDVV-IFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEP---ISGAVLLDGNNISELD---IKWLRG-QIG 480
Cdd:COG0444 10 YFPTRRGVVkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSekeLRKIRGrEIQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 LVNQEP--AL---------FATTIRENILYGKDDAT--AEEITRAAKLSEAISFINNLPEgfetqvgergiQLSGGQKQR 547
Cdd:COG0444 90 MIFQDPmtSLnpvmtvgdqIAEPLRIHGGLSKAEARerAIELLERVGLPDPERRLDRYPH-----------ELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 548 IAISRAIVKNPSILLLDEATSALDAesekSVQ-EALDrVMV------GRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFG 619
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDV----TIQaQILN-LLKdlqrelGLAILFITHDLGVVAEiADRVAVMYAGRIVEEG 233
|
....*....
gi 79487035 620 NHENLISNP 628
Cdd:COG0444 234 PVEELFENP 242
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1030-1249 |
3.06e-34 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 131.92 E-value: 3.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSrpDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKL---DLKALRK 1106
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgkALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1107 HIGLVQQEPALFA-TTIYENILYGnegasqsevvesamLANAHSFITSLPEGYS-----------TKVG------ERGVQ 1168
Cdd:cd03256 79 QIGMIFQQFNLIErLSVLENVLSG--------------RLGRRSTWRSLFGLFPkeekqralaalERVGlldkayQRADQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1169 MSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMA--NRTTVVVAHRLSTIK-NADTISVLHGGKIV 1245
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDLAReYADRIVGLKDGRIV 224
|
....
gi 79487035 1246 EQGS 1249
Cdd:cd03256 225 FDGP 228
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
401-628 |
6.68e-34 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 130.92 E-value: 6.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPDVvifDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKwlRGQIG 480
Cdd:cd03296 3 IEVRNVSKRFGDFVAL---DDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 LVNQEPALFA-TTIRENILYG----KDDATAEEITRAAKLSEAISFINnlPEGFETQVGErgiQLSGGQKQRIAISRAIV 555
Cdd:cd03296 78 FVFQHYALFRhMTVFDNVAFGlrvkPRSERPPEAEIRAKVHELLKLVQ--LDWLADRYPA---QLSGGQRQRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79487035 556 KNPSILLLDEATSALDAESEKSVQEALDRVM--VGRTTVVVAHRLS-TVRNADIIAVVHEGKIVEFGNHENLISNP 628
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHdeLHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEVYDHP 228
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
401-616 |
8.32e-34 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 130.77 E-value: 8.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSrpDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWL---RG 477
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 478 QIGLVNQEPALFA-TTIRENILYGKDDA-----------TAEEITRAAKLSEAIsfinnlpeGFETQVGERGIQLSGGQK 545
Cdd:cd03256 79 QIGMIFQQFNLIErLSVLENVLSGRLGRrstwrslfglfPKEEKQRALAALERV--------GLLDKAYQRADQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79487035 546 QRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRV--MVGRTTVVVAHRLSTVR-NADIIAVVHEGKIV 616
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAReYADRIVGLKDGRIV 224
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1050-1261 |
8.88e-34 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 133.32 E-value: 8.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1050 DFDliVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKL---DLKALRKHIGLVQQEPalFAT-----T 1121
Cdd:COG4608 38 SFD--IRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLsgrELRPLRRRMQMVFQDP--YASlnprmT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1122 IYENILYG---NEGASQSEVVESA--MLAnahsfitslpegystKVGERGVQM-------SGGQRQRIAIARAILKNPAI 1189
Cdd:COG4608 114 VGDIIAEPlriHGLASKAERRERVaeLLE---------------LVGLRPEHAdryphefSGGQRQRIGIARALALNPKL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 1190 LLLDEATSALDVeServVQ-QALDRLMA-----NRTTVVVAHRLSTIKN-ADTISVLHGGKIVEQGSHRKLVLNKSGPY 1261
Cdd:COG4608 179 IVCDEPVSALDV-S---IQaQVLNLLEDlqdelGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYARPLHPY 253
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
124-645 |
2.58e-33 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 140.50 E-value: 2.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 124 LDFVYLSVAILFSSWLeVACWMHTGERqaakMRRAYLRSMLSQDISLFDTEAsTGEVISAITSDILVVQDALSEKVGNFL 203
Cdd:PLN03232 959 LGFGQVAVTFTNSFWL-ISSSLHAAKR----LHDAMLNSILRAPMLFFHTNP-TGRVINRFSKDIGDIDRNVANLMNMFM 1032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 204 HYISRFIAGFA-IGFTSVwqISLvtLSIVPLIALAGGIYAFVA-----IGLIARVRKSYIKAgeIAEEVIGNVRTVQAFT 277
Cdd:PLN03232 1033 NQLWQLLSTFAlIGTVST--ISL--WAIMPLLILFYAAYLYYQstsreVRRLDSVTRSPIYA--QFGEALNGLSSIRAYK 1106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 278 GEERAVRLYREALENTYKYGRKAGLTKG------LGLGSMHCVLFLSWALL--------VWFTSVVvhKDIADGGKSFTT 343
Cdd:PLN03232 1107 AYDRMAKINGKSMDNNIRFTLANTSSNRwltirlETLGGVMIWLTATFAVLrngnaenqAGFASTM--GLLLSYTLNITT 1184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 344 MLNVVIAGLSLGQ----AAPDISAFVRAKAAAYPIfkmIERNtvtktSAKSGRKLGkvdGHIQFKDATFSY-PSRPDVVi 418
Cdd:PLN03232 1185 LLSGVLRQASKAEnslnSVERVGNYIDLPSEATAI---IENN-----RPVSGWPSR---GSIKFEDVHLRYrPGLPPVL- 1252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 419 fDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIGLVNQEPALFATTIRENI- 497
Cdd:PLN03232 1253 -HGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNId 1331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 498 -LYGKDDATAEEITRAAKLSEAISfinNLPEGFETQVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEK 576
Cdd:PLN03232 1332 pFSEHNDADLWEALERAHIKDVID---RNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDS 1408
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 577 SVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVHEGKIVEFGNHENLISNPDGAYSSLLRLQETASLQ 645
Cdd:PLN03232 1409 LIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGPANAQ 1477
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
401-636 |
3.30e-33 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 128.72 E-value: 3.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPDvvifdRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIkwlrGQ-- 478
Cdd:COG3840 2 LRLDDLTYRYGDFPL-----RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP----AErp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 479 IGLVNQEPALFA-TTIRENILYGKDDA---TAEEITRAAKLSEAIS---FINNLPEgfetqvgergiQLSGGQKQRIAIS 551
Cdd:COG3840 73 VSMLFQENNLFPhLTVAQNIGLGLRPGlklTAEQRAQVEQALERVGlagLLDRLPG-----------QLSGGQRQRVALA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 552 RAIVKNPSILLLDEATSALD----AESEKSVQEALDRvmVGRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFGNHENLIS 626
Cdd:COG3840 142 RCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRE--RGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLD 219
|
250
....*....|.
gi 79487035 627 -NPDGAYSSLL 636
Cdd:COG3840 220 gEPPPALAAYL 230
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
401-628 |
3.51e-33 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 132.12 E-value: 3.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPsrpDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKwLRGqIG 480
Cdd:COG3839 4 LELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK-DRN-IA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 LVNQEPALF-ATTIRENILYG-------KDDAtAEEITRAAKLSEAISFINNLPEgfetqvgergiQLSGGQKQRIAISR 552
Cdd:COG3839 79 MVFQSYALYpHMTVYENIAFPlklrkvpKAEI-DRRVREAAELLGLEDLLDRKPK-----------QLSGGQRQRVALGR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 553 AIVKNPSILLLDEATSALDAE------SE-KSVQEALdrvmvGRTTVVVAH------RLstvrnADIIAVVHEGKIVEFG 619
Cdd:COG3839 147 ALVREPKVFLLDEPLSNLDAKlrvemrAEiKRLHRRL-----GTTTIYVTHdqveamTL-----ADRIAVMNDGRIQQVG 216
|
....*....
gi 79487035 620 NHENLISNP 628
Cdd:COG3839 217 TPEELYDRP 225
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1028-1249 |
4.24e-33 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 132.12 E-value: 4.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1028 GTIELKGVHFSYPsrpDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIkkLDLKALRKH 1107
Cdd:COG3839 2 ASLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV--TDLPPKDRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1108 IGLVQQEPALF-ATTIYENILYG--NEGASQSEV---VESA--MLAnahsfITSL----PEgystkvgergvQMSGGQRQ 1175
Cdd:COG3839 77 IAMVFQSYALYpHMTVYENIAFPlkLRKVPKAEIdrrVREAaeLLG-----LEDLldrkPK-----------QLSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1176 RIAIARAILKNPAILLLDEATSALDVESeRV--------VQQALdrlmaNRTTVVVAHRLS---TIknADTISVLHGGKI 1244
Cdd:COG3839 141 RVALGRALVREPKVFLLDEPLSNLDAKL-RVemraeikrLHRRL-----GTTTIYVTHDQVeamTL--ADRIAVMNDGRI 212
|
....*
gi 79487035 1245 VEQGS 1249
Cdd:COG3839 213 QQVGT 217
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
401-624 |
5.38e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 128.28 E-value: 5.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPdvvIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELdikwlRGQIG 480
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 LVNQEPAL---FATTIRENILYG-------------KDDATAEEITRAAKLSEaisFINnlpegfeTQVGErgiqLSGGQ 544
Cdd:COG1121 79 YVPQRAEVdwdFPITVRDVVLMGrygrrglfrrpsrADREAVDEALERVGLED---LAD-------RPIGE----LSGGQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 545 KQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDR-VMVGRTTVVVAHRLSTVR-NADIIA-----VVHEGKIVE 617
Cdd:COG1121 145 QQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVReYFDRVLllnrgLVAHGPPEE 224
|
....*..
gi 79487035 618 FGNHENL 624
Cdd:COG1121 225 VLTPENL 231
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
422-628 |
5.58e-33 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 128.22 E-value: 5.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 422 LNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELdiKWLRGQIGLVNQEPALFA-TTIRENILYG 500
Cdd:cd03299 18 VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNL--PPEKRDISYVPQNYALFPhMTVYKNIAYG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 501 KDDATAEEITRAAKLSEAISFInnlpeGFETQVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQE 580
Cdd:cd03299 96 LKKRKVDKKEIERKVLEIAEML-----GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLRE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 79487035 581 ALDRVM--VGRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFGNHENLISNP 628
Cdd:cd03299 171 ELKKIRkeFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
401-615 |
8.40e-33 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 125.20 E-value: 8.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPdvvIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISElDIKWLRGQIG 480
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 LVNQEPALFAT-TIRENIlygkddataeeitraaklseaisfinnlpegfetqvgergiQLSGGQKQRIAISRAIVKNPS 559
Cdd:cd03230 77 YLPEEPSLYENlTVRENL-----------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 560 ILLLDEATSALDAESEKSVQEALDRVMVGRTTVVVA-HRLSTVRN-ADIIAVVHEGKI 615
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKEGKTILLSsHILEEAERlCDRVAILNNGRI 173
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
399-626 |
9.15e-33 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 138.93 E-value: 9.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 399 GHIQFKDATFSYpsRPDV-VIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRG 477
Cdd:TIGR00957 1283 GRVEFRNYCLRY--REDLdLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRF 1360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 478 QIGLVNQEPALFATTIRENiLYGKDDATAEEITRAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRIAISRAIVKN 557
Cdd:TIGR00957 1361 KITIIPQDPVLFSGSLRMN-LDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRK 1439
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 558 PSILLLDEATSALDAESEKSVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVHEGKIVEFGNHENLIS 626
Cdd:TIGR00957 1440 TKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQ 1508
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1030-1249 |
1.30e-32 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 126.97 E-value: 1.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPsrpDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIkkLDLKALRKHIG 1109
Cdd:cd03300 1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1110 LVQQEPALFA-TTIYENILYGNE--GASQSEVVE--SAMLAnahsfITSLpEGYSTKvgeRGVQMSGGQRQRIAIARAIL 1184
Cdd:cd03300 76 TVFQNYALFPhLTVFENIAFGLRlkKLPKAEIKErvAEALD-----LVQL-EGYANR---KPSQLSGGQQQRVAIARALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 1185 KNPAILLLDEATSALDVESERVVQQALDRLMANR--TTVVVAHRLS-TIKNADTISVLHGGKIVEQGS 1249
Cdd:cd03300 147 NEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELgiTFVFVTHDQEeALTMSDRIAVMNKGKIQQIGT 214
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1030-1257 |
1.63e-32 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 125.98 E-value: 1.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPsrPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKA---LRK 1106
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1107 HIGLVQQEPALFAT-TIYENILYGNE--GASQSEVVESAMLANAHSfitslpeGYSTKVGERGVQMSGGQRQRIAIARAI 1183
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFALEvtGVPPREIRKRVPAALELV-------GLSHKHRALPAELSGGEQQRVAIARAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79487035 1184 LKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVVVAhrlstiknadtisvLHGGKIVEQGSHRKLVLNK 1257
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA--------------THAKELVDTTRHRVIALER 211
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
401-619 |
2.07e-32 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 127.55 E-value: 2.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPDVVIfDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKW-LRGQI 479
Cdd:TIGR04520 1 IEVENVSFSYPESEKPAL-KNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWeIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 480 GLVNQEP--ALFATTIRENILYG------KDDATAEEITRAAKLSEAISFINNLPEgfetqvgergiQLSGGQKQRIAIS 551
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGlenlgvPREEMRKRVDEALKLVGMEDFRDREPH-----------LLSGGQKQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 552 RAIVKNPSILLLDEATSALDAESEKSVQEALDRVM--VGRTTVVVAHRLSTVRNADIIAVVHEGKIVEFG 619
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEG 218
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
124-637 |
2.13e-32 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 137.56 E-value: 2.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 124 LDFVYLSVAILFSSWLevacwMHTGERQAAKMRRAYLRSMLSQDISLFDTEAsTGEVISAITSDILVVQDALSEKVGNFL 203
Cdd:PLN03130 962 LSFGQVLVTLLNSYWL-----IMSSLYAAKRLHDAMLGSILRAPMSFFHTNP-LGRIINRFAKDLGDIDRNVAVFVNMFL 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 204 HYISRFIAGFA-IGFTSVwqISLvtLSIVPLIALAGGIYAFVAIglIARVRK---SYIKAGEIAE--EVIGNVRTVQAFT 277
Cdd:PLN03130 1036 GQIFQLLSTFVlIGIVST--ISL--WAIMPLLVLFYGAYLYYQS--TAREVKrldSITRSPVYAQfgEALNGLSTIRAYK 1109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 278 GEERAVRLYREALENTYKYGrkagltkglgLGSMHCVLFLS------WALLVWFTS--VVVHKDIADGGKSF-------- 341
Cdd:PLN03130 1110 AYDRMAEINGRSMDNNIRFT----------LVNMSSNRWLAirletlGGLMIWLTAsfAVMQNGRAENQAAFastmglll 1179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 342 ------TTMLNVVIAGLSLGQ----AAPDISAFVRAKAAAYPIfkmIERNTVTKTSAKSGRklgkvdghIQFKDATFSYp 411
Cdd:PLN03130 1180 syalniTSLLTAVLRLASLAEnslnAVERVGTYIDLPSEAPLV---IENNRPPPGWPSSGS--------IKFEDVVLRY- 1247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 412 sRPDVV-IFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIGLVNQEPALFA 490
Cdd:PLN03130 1248 -RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFS 1326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 491 TTIRENI--LYGKDDATAEEITRAAKLSEAISfiNNlPEGFETQVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEATS 568
Cdd:PLN03130 1327 GTVRFNLdpFNEHNDADLWESLERAHLKDVIR--RN-SLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATA 1403
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 569 ALDAESEKSVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVHEGKIVEFGNHENLISNPDGAYSSLLR 637
Cdd:PLN03130 1404 AVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKMVQ 1472
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
420-628 |
2.19e-32 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 129.08 E-value: 2.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 420 DRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISEL---DIKWLRGQIGLVNQEPalFA------ 490
Cdd:COG4608 35 DGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLsgrELRPLRRRMQMVFQDP--YAslnprm 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 491 ---TTIRENILYGKDDATAEEITRAAKLSEAI----SFINNLPEgfetqvgergiQLSGGQKQRIAISRAIVKNPSILLL 563
Cdd:COG4608 113 tvgDIIAEPLRIHGLASKAERRERVAELLELVglrpEHADRYPH-----------EFSGGQRQRIGIARALALNPKLIVC 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79487035 564 DEATSALDaeseKSVQ-------EALDRVMvGRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFGNHENLISNP 628
Cdd:COG4608 182 DEPVSALD----VSIQaqvlnllEDLQDEL-GLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYARP 249
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
401-628 |
3.26e-32 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 129.15 E-value: 3.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYP-SRPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRG-- 477
Cdd:PRK11153 2 IELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 478 -QIGLVNQEPALFAT-TIRENI-----LYGKDDAtaeEI-TRAAKLSEAIsfinnlpeGFETQVGERGIQLSGGQKQRIA 549
Cdd:PRK11153 82 rQIGMIFQHFNLLSSrTVFDNValpleLAGTPKA---EIkARVTELLELV--------GLSDKADRYPAQLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 550 ISRAIVKNPSILLLDEATSALDAESEKSVQEALDRV--MVGRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFGNHENLIS 626
Cdd:PRK11153 151 IARALASNPKVLLCDEATSALDPATTRSILELLKDInrELGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGTVSEVFS 230
|
..
gi 79487035 627 NP 628
Cdd:PRK11153 231 HP 232
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
401-619 |
4.14e-32 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 124.67 E-value: 4.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPsrpDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKwLRGqIG 480
Cdd:cd03301 1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK-DRD-IA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 LVNQEPALFA-TTIRENILYG------KDDATAEEITRAAKLSEAISFINNLPEgfetqvgergiQLSGGQKQRIAISRA 553
Cdd:cd03301 76 MVFQNYALYPhMTVYDNIAFGlklrkvPKDEIDERVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79487035 554 IVKNPSILLLDEATSALDAE------SE-KSVQEALdrvmvGRTTVVVAH-RLSTVRNADIIAVVHEGKIVEFG 619
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDAKlrvqmrAElKRLQQRL-----GTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
401-595 |
7.45e-32 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 124.06 E-value: 7.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPsrPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELD---IKWLRG 477
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 478 QIGLVNQEPALFAT-TIRENIlygkddATAEEITRAA------KLSEAISFInnlpeGFETQVGERGIQLSGGQKQRIAI 550
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENV------AFALEVTGVPpreirkRVPAALELV-----GLSHKHRALPAELSGGEQQRVAI 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 79487035 551 SRAIVKNPSILLLDEATSALDAESEKSVQEALDRVMVGRTTVVVA 595
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1030-1249 |
9.12e-32 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 127.61 E-value: 9.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYP-SRPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLD---LKALR 1105
Cdd:PRK11153 2 IELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekeLRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1106 KHIGLVQQEPALFAT-TIYENILYGNEGASQSEvvesamlANAHSFITSLPE--GYSTKVGERGVQMSGGQRQRIAIARA 1182
Cdd:PRK11153 82 RQIGMIFQHFNLLSSrTVFDNVALPLELAGTPK-------AEIKARVTELLElvGLSDKADRYPAQLSGGQKQRVAIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79487035 1183 ILKNPAILLLDEATSALDVESERVVQQALDRLmaNR----TTVVVAHRLSTIKN-ADTISVLHGGKIVEQGS 1249
Cdd:PRK11153 155 LASNPKVLLCDEATSALDPATTRSILELLKDI--NRelglTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1030-1244 |
1.00e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 124.82 E-value: 1.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRPdvvIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLdlkalRKHIG 1109
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1110 LVQQEPAL---FATTIYENI---LYGNEG------ASQSEVVESA-----MLANAHSFITSLpegystkvgergvqmSGG 1172
Cdd:COG1121 79 YVPQRAEVdwdFPITVRDVVlmgRYGRRGlfrrpsRADREAVDEAlervgLEDLADRPIGEL---------------SGG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79487035 1173 QRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRL-MANRTTVVVAHRLSTI-KNADTISVLHGGKI 1244
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVrEYFDRVLLLNRGLV 217
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1023-1257 |
1.11e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 125.49 E-value: 1.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1023 LNNVEGTIELKGVHFSYPSRPDVVIfRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLK 1102
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPNSENNAL-KNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1103 ALRKHIGLVQQEP--ALFATTIYENILYG--NEGASQSEvvesamlanahsfITSLPEGYSTKVG-----ERGVQ-MSGG 1172
Cdd:PRK13632 80 EIRKKIGIIFQNPdnQFIGATVEDDIAFGleNKKVPPKK-------------MKDIIDDLAKKVGmedylDKEPQnLSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1173 QRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRL--MANRTTVVVAHRLSTIKNADTISVLHGGKIVEQGSH 1250
Cdd:PRK13632 147 QKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLrkTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKP 226
|
....*..
gi 79487035 1251 RKLVLNK 1257
Cdd:PRK13632 227 KEILNNK 233
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
401-640 |
1.55e-31 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 124.05 E-value: 1.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPsrpDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNI--SELDIKWLRGQ 478
Cdd:PRK09493 2 IEFKNVSKHFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 479 IGLVNQEPALFA-TTIRENILYGKDDataeeiTRAAKLSEAisfiNNLPEGFETQVG--ERG----IQLSGGQKQRIAIS 551
Cdd:PRK09493 79 AGMVFQQFYLFPhLTALENVMFGPLR------VRGASKEEA----EKQARELLAKVGlaERAhhypSELSGGQQQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 552 RAIVKNPSILLLDEATSALDAESEksvQEALdRVMV-----GRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFGNHENLI 625
Cdd:PRK09493 149 RALAVKPKLMLFDEPTSALDPELR---HEVL-KVMQdlaeeGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
250
....*....|....*
gi 79487035 626 SNPDGAyssllRLQE 640
Cdd:PRK09493 225 KNPPSQ-----RLQE 234
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
258-1258 |
1.87e-31 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 134.27 E-value: 1.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 258 KAGEIAE------EVIGNVRTVQAFTGEERAVRLYREALENTYKYGRKAGLTKGLGLGSmhcvLFLSwALLVWFTSVVVH 331
Cdd:TIGR01271 252 RAGKISErlaitsEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAYLRYFYSSA----FFFS-GFFVVFLSVVPY 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 332 KDIAD--GGKSFTTMLNVVIAGLSLGQAAP-DISAFVRAKAAAYPI--------FKMIERNTVTK------TSAKSGRKL 394
Cdd:TIGR01271 327 ALIKGiiLRRIFTTISYCIVLRMTVTRQFPgAIQTWYDSLGAITKIqdflckeeYKTLEYNLTTTevemvnVTASWDEGI 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 395 GKVDGHIQFKDATFSYPSRPDVVIFDRL-----------NLAIPAGKIVALVGGSGSGKSTVISLIERFYEPisgavlld 463
Cdd:TIGR01271 407 GELFEKIKQNNKARKQPNGDDGLFFSNFslyvtpvlkniSFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEP-------- 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 464 gnniSELDIKWlRGQIGLVNQEPALFATTIRENILYG--KDDATAEEITRAAKLSEAISFinnLPEGFETQVGERGIQLS 541
Cdd:TIGR01271 479 ----SEGKIKH-SGRISFSPQTSWIMPGTIKDNIIFGlsYDEYRYTSVIKACQLEEDIAL---FPEKDKTVLGEGGITLS 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 542 GGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEA-LDRVMVGRTTVVVAHRLSTVRNADIIAVVHEGKIVEFGN 620
Cdd:TIGR01271 551 GGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGT 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 621 HENLIS-NPDgaYSSLL----RLQETASLQRNPSLNRTLSR------------PHSIKYS-----------RELSRTRSS 672
Cdd:TIGR01271 631 FSELQAkRPD--FSSLLlgleAFDNFSAERRNSILTETLRRvsidgdstvfsgPETIKQSfkqpppefaekRKQSIILNP 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 673 FCSERE------SVTRPDGADPSKKVKVTVGRLYSMIrPDWMYGVCGTICAFIAGSQMPLFAlGVSQALVSYYSGWDETQ 746
Cdd:TIGR01271 709 IASARKfsfvqmGPQKAQATTIEDAVREPSERKFSLV-PEDEQGEESLPRGNQYHHGLQHQA-QRRQSVLQLMTHSNRGE 786
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 747 KEIKKIAILFCCASVITLIVYTIEHICFGT--MGERLTLRVRENMFRAILKNeiGWFDEVDNTSSMlasrlESDATLLKT 824
Cdd:TIGR01271 787 NRREQLQTSFRKKSSITQQNELASELDIYSrrLSKDSVYEISEEINEEDLKE--CFADERENVFET-----TTWNTYLRY 859
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 825 IVVDRSTILLQNLGLVV------TSFIIAFIL------------NWRLTLVVLATYPLVISGH-----------ISEKLF 875
Cdd:TIGR01271 860 ITTNRNLVFVLIFCLVIflaevaASLLGLWLItdnpsapnyvdqQHANASSPDVQKPVIITPTsayyifyiyvgTADSVL 939
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 876 MQGY-------------GGDLNK----AYLKANMLAGESVSNIRTVAAFCAEEKILE--------------------LYS 918
Cdd:TIGR01271 940 ALGFfrglplvhtlltvSKRLHEqmlhSVLQAPMAVLNTMKAGRILNRFTKDMAIIDdmlpltlfdfiqltlivlgaIFV 1019
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 919 RELLEPSkSSFRRGQIAGLFYGVSQFFIFSSYGL--------------------ALW---------YGSTLMDKGLAG-- 967
Cdd:TIGR01271 1020 VSVLQPY-IFIAAIPVAVIFIMLRAYFLRTSQQLkqlesearspifshlitslkGLWtirafgrqsYFETLFHKALNLht 1098
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 968 -----FKSVMKTFMVLI----------VTALAMGET----------LALAPDLLKGNQM--------------VASVFEI 1008
Cdd:TIGR01271 1099 anwflYLSTLRWFQMRIdiifvfffiaVTFIAIGTNqdgegevgiiLTLAMNILSTLQWavnssidvdglmrsVSRVFKF 1178
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1009 LDRKTQIVGETSEELNNVEGT---IELKGVHFSYPSRPDVV--------------IFRDFDLIVRAGKSMALVGQSGSGK 1071
Cdd:TIGR01271 1179 IDLPQEEPRPSGGGGKYQLSTvlvIENPHAQKCWPSGGQMDvqgltakyteagraVLQDLSFSVEGGQRVGLLGRTGSGK 1258
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1072 SSVISLILRFYDpTAGKVMIEGKDIKKLDLKALRKHIGLVQQEPALFATTIYENiLYGNEGASQSEVVESAMLANAHSFI 1151
Cdd:TIGR01271 1259 STLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKN-LDPYEQWSDEEIWKVAEEVGLKSVI 1336
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1152 TSLPEGYSTKVGERGVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVVVAHRLSTIK 1231
Cdd:TIGR01271 1337 EQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALL 1416
|
1210 1220
....*....|....*....|....*..
gi 79487035 1232 NADTISVLHGGKIVEQGSHRKLVLNKS 1258
Cdd:TIGR01271 1417 ECQQFLVIEGSSVKQYDSIQKLLNETS 1443
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
401-628 |
2.80e-31 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 126.41 E-value: 2.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPdvvIFDRLNLAIPAGKIVALVGGSGSGKSTVISLI---ERfyePISGAVLLDGNNI-SELDIKwlR 476
Cdd:COG1118 3 IEVRNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTLLRIIaglET---PDSGRIVLNGRDLfTNLPPR--E 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 477 GQIGLVNQEPALFA-TTIRENILYG---KDDATAEEITRAAKLSEAIsfinNLpEGFEtqvGERGIQLSGGQKQRIAISR 552
Cdd:COG1118 75 RRVGFVFQHYALFPhMTVAENIAFGlrvRPPSKAEIRARVEELLELV----QL-EGLA---DRYPSQLSGGQRQRVALAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 553 AIVKNPSILLLDEATSALDA----ESEKSVQEALDRvmVGRTTVVVAH-RLSTVRNADIIAVVHEGKIVEFGNHENLISN 627
Cdd:COG1118 147 ALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHDE--LGGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDEVYDR 224
|
.
gi 79487035 628 P 628
Cdd:COG1118 225 P 225
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1030-1248 |
3.78e-31 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 121.92 E-value: 3.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRpdvVIFRDFDLIVRAGKSmALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKlDLKALRKHIG 1109
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1110 LVQQEPALFAT-TIYE-----NILYGNEGASQSEVVEsAMLANAHsfitsLPEGYSTKVGergvQMSGGQRQRIAIARAI 1183
Cdd:cd03264 76 YLPQEFGVYPNfTVREfldyiAWLKGIPSKEVKARVD-EVLELVN-----LGDRAKKKIG----SLSGGMRRRVGIAQAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79487035 1184 LKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVVVAHRLSTIKN-ADTISVLHGGKIVEQG 1248
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
97-325 |
1.06e-30 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 123.39 E-value: 1.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 97 FFGKLINIIGLAYLFPKQAShrvakYSLDFVYLSVAILF-----SSWLEVACWMHTGERQAAKMRRAYLRSMLSQDISLF 171
Cdd:cd18573 18 AIGKLIDVASKESGDIEIFG-----LSLKTFALALLGVFvvgaaANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 172 DTeASTGEVISAITSDILVVQDALSEKVGNFLHYISRFIAGFAIGFTSVWQISLVTLSIVPLIALAGGIYAFVAIGLIAR 251
Cdd:cd18573 93 DK-NKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQ 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79487035 252 VRKSYIKAGEIAEEVIGNVRTVQAFTGEERAVRLYREALENTYKYGRKAGLTKGLGLGSMHCVLFLSWALLVWF 325
Cdd:cd18573 172 VQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYY 245
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1049-1262 |
1.29e-30 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 121.29 E-value: 1.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1049 RDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKklDLKALRKHIGLVQQEPALFA-TTIYENIL 1127
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISYVPQNYALFPhMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1128 YG--NEGASQSEVVE-----SAMLANAHsFITSLPEgystkvgergvQMSGGQRQRIAIARAILKNPAILLLDEATSALD 1200
Cdd:cd03299 94 YGlkKRKVDKKEIERkvleiAEMLGIDH-LLNRKPE-----------TLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79487035 1201 VESERVVQQALDRLMANRTTVV--VAHRLSTIKN-ADTISVLHGGKIVEQGSHRKlVLNKSGPYF 1262
Cdd:cd03299 162 VRTKEKLREELKKIRKEFGVTVlhVTHDFEEAWAlADKVAIMLNGKLIQVGKPEE-VFKKPKNEF 225
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
402-619 |
1.78e-30 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 119.95 E-value: 1.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 402 QFKDATFSYPSRPdvvIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELdikwlRGQIGL 481
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 482 VNQEPAL---FATTIRENIL------------YGKDDAtaEEITRAAKLSEAISFINNlpegfetQVGErgiqLSGGQKQ 546
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVLmglyghkglfrrLSKADK--AKVDEALERVGLSELADR-------QIGE----LSGGQQQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79487035 547 RIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRV-MVGRTTVVVAHRLSTV-RNADIIAVVhEGKIVEFG 619
Cdd:cd03235 140 RVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVlEYFDRVLLL-NRTVVASG 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1029-1249 |
2.25e-30 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 123.72 E-value: 2.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1029 TIELKGVHFSYPSRPdvvIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKkLDLKALRKHI 1108
Cdd:COG1118 2 SIEVRNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF-TNLPPRERRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1109 GLVQQEPALFA-TTIYENILYG--NEGASQSEVVESAM----LANAHSFITSLPEgystkvgergvQMSGGQRQRIAIAR 1181
Cdd:COG1118 78 GFVFQHYALFPhMTVAENIAFGlrVRPPSKAEIRARVEelleLVQLEGLADRYPS-----------QLSGGQRQRVALAR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 1182 AILKNPAILLLDEATSALDV----ESERVVQQALDRLmaNRTTVVVAH------RLstiknADTISVLHGGKIVEQGS 1249
Cdd:COG1118 147 ALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHDEL--GGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGT 217
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
726-964 |
3.51e-30 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 121.50 E-value: 3.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 726 LFALGVSQALVSYYSG-------WDETQKEIKKIAILFCCASVITLIVYTIEHICFGTMGERLTLRVRENMFRAILKNEI 798
Cdd:cd18572 5 LVVAALSELAIPHYTGavidavvADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 799 GWFDEvdNTSSMLASRLESDATLLKTIVVDRSTILLQNLGLVVTSFIIAFILNWRLTLVVLATYPLV-----ISGHISEK 873
Cdd:cd18572 85 AFFDA--TKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIalitkVYGRYYRK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 874 L--FMQgyggdlnKAYLKANMLAGESVSNIRTVAAFCAEEKILELYSRELLEPSKSSFRRGQIAGLFYGVSQFFIFSSYG 951
Cdd:cd18572 163 LskEIQ-------DALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQV 235
|
250
....*....|...
gi 79487035 952 LALWYGSTLMDKG 964
Cdd:cd18572 236 LVLFYGGHLVLSG 248
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1030-1246 |
4.78e-30 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 119.46 E-value: 4.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRP-DVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLD---LKALR 1105
Cdd:COG4181 9 IELRGLTKTVGTGAgELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedaRARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1106 -KHIGLVQQEPALFAT-TIYENILYGNEGASQSEVVESA--MLAnahsfitslpegystKVG--ERG----VQMSGGQRQ 1175
Cdd:COG4181 89 aRHVGFVFQSFQLLPTlTALENVMLPLELAGRRDARARAraLLE---------------RVGlgHRLdhypAQLSGGEQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79487035 1176 RIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANR-TT-VVVAHRLSTIKNADTISVLHGGKIVE 1246
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgTTlVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1030-1251 |
9.02e-30 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 122.75 E-value: 9.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRPdvvIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKklDLKALRKHIG 1109
Cdd:PRK09452 15 VELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT--HVPAENRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1110 LVQQEPALFA-TTIYENILYG--NEGASQSEVVESAMLANAhsfITSLpEGYSTKvgeRGVQMSGGQRQRIAIARAILKN 1186
Cdd:PRK09452 90 TVFQSYALFPhMTVFENVAFGlrMQKTPAAEITPRVMEALR---MVQL-EEFAQR---KPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 1187 PAILLLDEATSALDVESERVVQQALDRLMA--NRTTVVVAH-RLSTIKNADTISVLHGGKIVEQGSHR 1251
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPR 230
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1029-1249 |
1.25e-29 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 118.60 E-value: 1.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1029 TIELKGVHFSYPSRPDVvifRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKalRKHI 1108
Cdd:cd03296 2 SIEVRNVSKRFGDFVAL---DDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1109 GLVQQEPALFA-TTIYENILYG----------NEGASQSEVVESAMLANAHSFITSLPEgystkvgergvQMSGGQRQRI 1177
Cdd:cd03296 77 GFVFQHYALFRhMTVFDNVAFGlrvkprserpPEAEIRAKVHELLKLVQLDWLADRYPA-----------QLSGGQRQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79487035 1178 AIARAILKNPAILLLDEATSALDVESERVVQQALDRLM--ANRTTVVVAHRLS-TIKNADTISVLHGGKIVEQGS 1249
Cdd:cd03296 146 ALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHdeLHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGT 220
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1062-1248 |
2.26e-29 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 117.01 E-value: 2.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1062 ALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDI----KKLDLKALRKHIGLVQQEPALFA-TTIYENILYGNEGASQS 1136
Cdd:cd03297 27 GIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrKKINLPPQQRKIGLVFQQYALFPhLNVRENLAFGLKRKRNR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1137 E--VVESAMLANAHsfITSLPEGYSTkvgergvQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRL 1214
Cdd:cd03297 107 EdrISVDELLDLLG--LDHLLNRYPA-------QLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQI 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 79487035 1215 MA--NRTTVVVAHRLSTI-KNADTISVLHGGKIVEQG 1248
Cdd:cd03297 178 KKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
401-613 |
2.63e-29 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 117.05 E-value: 2.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPsrPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWL----R 476
Cdd:cd03290 1 VQVTNGYFSWG--SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 477 GQIGLVNQEPALFATTIRENILYGK--DDATAEEITRAAKLSEAISFinnLPEGFETQVGERGIQLSGGQKQRIAISRAI 554
Cdd:cd03290 79 YSVAYAAQKPWLLNATVEENITFGSpfNKQRYKAVTDACSLQPDIDL---LPFGDQTEIGERGINLSGGQRQRICVARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79487035 555 VKNPSILLLDEATSALDAE-SEKSVQEALDRVMVG--RTTVVVAHRLSTVRNADIIAVVHEG 613
Cdd:cd03290 156 YQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1050-1252 |
3.97e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 118.61 E-value: 3.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1050 DFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDI--KKLDLKALRKHIGLVQQEP--ALFATTIYEN 1125
Cdd:PRK13637 25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFEETIEKD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1126 ILYG--NEGASQSEV---VESAMLANAHSFitslpEGYSTKvgeRGVQMSGGQRQRIAIARAILKNPAILLLDEATSALD 1200
Cdd:PRK13637 105 IAFGpiNLGLSEEEIenrVKRAMNIVGLDY-----EDYKDK---SPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 79487035 1201 VESERVVQQALDRLMA--NRTTVVVAHRLSTI-KNADTISVLHGGKIVEQGSHRK 1252
Cdd:PRK13637 177 PKGRDEILNKIKELHKeyNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPRE 231
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
1063-1253 |
4.67e-29 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 119.52 E-value: 4.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1063 LVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIkkLDLKALRKHIGLVQQEPALFA-TTIYENILYG----NEGASQ-- 1135
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV--TNVPPHLRHINMVFQSYALFPhMTVEENVAFGlkmrKVPRAEik 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1136 SEVVESAMLANAHSFITSLPegystkvgergVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLM 1215
Cdd:TIGR01187 79 PRVLEALRLVQLEEFADRKP-----------HQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQ 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 79487035 1216 ANR--TTVVVAHRLS-TIKNADTISVLHGGKIVEQGSHRKL 1253
Cdd:TIGR01187 148 EQLgiTFVFVTHDQEeAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
415-628 |
4.96e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 117.32 E-value: 4.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 415 DVVIFDRLNLAIPAGKIVALVGGSGSGKSTVIS----LIERFYEP-ISGAVLLDGNNISELDIKWLRGQIGLVNQEPALF 489
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRvfnrLIELYPEArVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 490 AT-TIRENILYG-------KDDATAEEITRAAkLSEAisfinNLPEGFETQVGERGIQLSGGQKQRIAISRAIVKNPSIL 561
Cdd:PRK14247 95 PNlSIFENVALGlklnrlvKSKKELQERVRWA-LEKA-----QLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 562 LLDEATSALDAESEKSVQEALDRVMVGRTTVVVAH-RLSTVRNADIIAVVHEGKIVEFGNHENLISNP 628
Cdd:PRK14247 169 LADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
401-619 |
4.99e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 117.78 E-value: 4.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPDVVIfDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIG 480
Cdd:PRK13632 8 IKVENVSFSYPNSENNAL-KNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 LVNQEP--ALFATTIRENILYG------KDDATAEEITRAAKLSEAISFINNLPEgfetqvgergiQLSGGQKQRIAISR 552
Cdd:PRK13632 87 IIFQNPdnQFIGATVEDDIAFGlenkkvPPKKMKDIIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIAS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 553 AIVKNPSILLLDEATSALDAESEKSVQEALD--RVMVGRTTVVVAHRLSTVRNADIIAVVHEGKIVEFG 619
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVdlRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQG 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
431-628 |
7.00e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 116.80 E-value: 7.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 431 IVALVGGSGSGKSTVISLIERFYE-----PISGAVLLDGNNI--SELDIKWLRGQIGLVNQEPALFATTIRENILYG--- 500
Cdd:PRK14239 33 ITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPNPFPMSIYENVVYGlrl 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 501 ---KD----DATAEEITRAAKLSEAIsfinnlpegfETQVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAE 573
Cdd:PRK14239 113 kgiKDkqvlDEAVEKSLKGASIWDEV----------KDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPI 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 79487035 574 SEKSVQEALDRVMVGRTTVVVAHRLSTV-RNADIIAVVHEGKIVEFGNHENLISNP 628
Cdd:PRK14239 183 SAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDTKQMFMNP 238
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1030-1248 |
8.42e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 122.05 E-value: 8.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSrpdVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLD-LKALRKHI 1108
Cdd:COG1129 5 LEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1109 GLVQQEPALFAT-TIYENILYGNEGASQSEVVESAMLANAHSFITSL-----PEgysTKVGErgvqMSGGQRQRIAIARA 1182
Cdd:COG1129 82 AIIHQELNLVPNlSVAENIFLGREPRRGGLIDWRAMRRRARELLARLgldidPD---TPVGD----LSVAQQQLVEIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 1183 ILKNPAILLLDEATSAL-DVESERVVQQaLDRLMANRTTVV-VAHRLSTIKN-ADTISVLHGGKIVEQG 1248
Cdd:COG1129 155 LSRDARVLILDEPTASLtEREVERLFRI-IRRLKAQGVAIIyISHRLDEVFEiADRVTVLRDGRLVGTG 222
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
753-1261 |
8.43e-29 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 125.83 E-value: 8.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 753 AILFCCASVITLIVYTIEHICFGTmGERLTLRVRENMFRAIL--------KNEIGwfdEVDNTSSMLASRLESDATLLKT 824
Cdd:TIGR00957 362 GLLFVCACLQTLILHQYFHICFVS-GMRIKTAVMGAVYRKALvitnsarkSSTVG---EIVNLMSVDAQRFMDLATYINM 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 825 I------VVDRSTILLQNLGLVVTSFIIAFILnwrltlvvlaTYPLviSGHISEKLfmqgyggdlnKAYLKANMLAGESv 898
Cdd:TIGR00957 438 IwsaplqVILALYFLWLNLGPSVLAGVAVMVL----------MVPL--NAVMAMKT----------KTYQVAHMKSKDN- 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 899 sNIRTVAAFCAEEKILELYSRELlepsksSFRRgQIAGLFYGVSQFFIFSSY----GLALWYGSTlmdkglagFKSVMKT 974
Cdd:TIGR00957 495 -RIKLMNEILNGIKVLKLYAWEL------AFLD-KVEGIRQEELKVLKKSAYlhavGTFTWVCTP--------FLVALIT 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 975 FMVLIV-------------TALAMGETLALAPDLLKgnQMVASVFEI---LDRKTQIVGETSEELNNVE---------GT 1029
Cdd:TIGR00957 559 FAVYVTvdennildaekafVSLALFNILRFPLNILP--MVISSIVQAsvsLKRLRIFLSHEELEPDSIErrtikpgegNS 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYpSRPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKdikkldlkalrkhIG 1109
Cdd:TIGR00957 637 ITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VA 702
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1110 LVQQEPALFATTIYENILYG---NEGASQSEVVESAMLANahsfITSLPEGYSTKVGERGVQMSGGQRQRIAIARAILKN 1186
Cdd:TIGR00957 703 YVPQQAWIQNDSLRENILFGkalNEKYYQQVLEACALLPD----LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSN 778
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1187 PAILLLDEATSALDVEserVVQQALDR------LMANRTTVVVAHRLSTIKNADTISVLHGGKIVEQGSHRKLvLNKSGP 1260
Cdd:TIGR00957 779 ADIYLFDDPLSAVDAH---VGKHIFEHvigpegVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQEL-LQRDGA 854
|
.
gi 79487035 1261 Y 1261
Cdd:TIGR00957 855 F 855
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
713-960 |
1.12e-28 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 117.35 E-value: 1.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 713 GTICAFI-AGSQM--PLFALGVSQALVSYYSGWDETQKE-IKKIAILFCCASVITLIVYTIEHICFGTMGERLTLRVREN 788
Cdd:cd18780 1 GTIALLVsSGTNLalPYFFGQVIDAVTNHSGSGGEEALRaLNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 789 MFRAILKNEIGWFDEvdNTSSMLASRLESDATLLKTIVVDRSTILLQNLGLVVTSFIIAFILNWRLTLVVLATYPLVISG 868
Cdd:cd18780 81 LFSAIIAQEIAFFDV--TRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 869 HISEKLFMQGYGGDLNKAYLKANMLAGESVSNIRTVAAFCAEEKILELYSRELLEPSKSSFRRGQIAGLFYGVSQFFIFS 948
Cdd:cd18780 159 AVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQL 238
|
250
....*....|..
gi 79487035 949 SYGLALWYGSTL 960
Cdd:cd18780 239 AIVLVLWYGGRL 250
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1031-1244 |
1.20e-28 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 114.94 E-value: 1.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1031 ELKGVHFSYPSRPdvvIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLdlkalRKHIGL 1110
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1111 VQQEPAL---FATTIYENILYGNEG---------ASQSEVVESA-----MLANAHSFITSLpegystkvgergvqmSGGQ 1173
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVLMGLYGhkglfrrlsKADKAKVDEAlervgLSELADRQIGEL---------------SGGQ 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79487035 1174 RQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRL-MANRTTVVVAHRLSTI-KNADTISVLHGGKI 1244
Cdd:cd03235 138 QQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVlEYFDRVLLLNRTVV 210
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
403-619 |
1.28e-28 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 114.19 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 403 FKDATFSYPSRPDVV---IFDRLNLAIPAGKIVALVGGSGSGKSTVISLI--ERFYEPISGAVLLDGNNiseLDIKWLRG 477
Cdd:cd03213 6 FRNLTVTVKSSPSKSgkqLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRP---LDKRSFRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 478 QIGLVNQEPALFAT-TIRENILYgkddataeeitrAAKLseaisfinnlpegfetqvgeRGIqlSGGQKQRIAISRAIVK 556
Cdd:cd03213 83 IIGYVPQDDILHPTlTVRETLMF------------AAKL--------------------RGL--SGGERKRVSIALELVS 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79487035 557 NPSILLLDEATSALDAESEKSVQEALDR-VMVGRTTVVVAHRLST--VRNADIIAVVHEGKIVEFG 619
Cdd:cd03213 129 NPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1030-1248 |
1.49e-28 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 114.66 E-value: 1.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPsrpDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKklDLKALRKHIG 1109
Cdd:cd03301 1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT--DLPPKDRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1110 LVQQEPALFA-TTIYENILYGNE--GASQSEVVESAMLANAHSFITSLPEGYSTkvgergvQMSGGQRQRIAIARAILKN 1186
Cdd:cd03301 76 MVFQNYALYPhMTVYDNIAFGLKlrKVPKDEIDERVREVAELLQIEHLLDRKPK-------QLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79487035 1187 PAILLLDEATSALDVESERVVQQALDRLMAN--RTTVVVAH-RLSTIKNADTISVLHGGKIVEQG 1248
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlgTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1030-1249 |
1.50e-28 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 122.10 E-value: 1.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSR--------PDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFyDPTAGKVMIEGKDIKKLD- 1100
Cdd:COG4172 276 LEARDLKVWFPIKrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSr 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1101 --LKALRKHIGLVQQEPalFAT-----TIYENILygnEG----------ASQSEVVESAMlanahsfitslpegysTKVG 1163
Cdd:COG4172 355 raLRPLRRRMQVVFQDP--FGSlsprmTVGQIIA---EGlrvhgpglsaAERRARVAEAL----------------EEVG 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1164 -ERGV------QMSGGQRQRIAIARAILKNPAILLLDEATSALDVeserVVQ-QALD---RLMANR--TTVVVAHRLSTI 1230
Cdd:COG4172 414 lDPAArhryphEFSGGQRQRIAIARALILEPKLLVLDEPTSALDV----SVQaQILDllrDLQREHglAYLFISHDLAVV 489
|
250 260
....*....|....*....|
gi 79487035 1231 KN-ADTISVLHGGKIVEQGS 1249
Cdd:COG4172 490 RAlAHRVMVMKDGKVVEQGP 509
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
383-634 |
1.57e-28 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 119.17 E-value: 1.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 383 VTKTSAKSGRKLGKVdghIQFKDATFSYPSRPDVvifDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLL 462
Cdd:PRK11607 5 IPRPQAKTRKALTPL---LEIRNLTKSFDGQHAV---DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 463 DGNNISELDiKWLRgQIGLVNQEPALFA-TTIRENILYG--KDDATAEEITraAKLSEAISFINnlpegFETQVGERGIQ 539
Cdd:PRK11607 79 DGVDLSHVP-PYQR-PINMMFQSYALFPhMTVEQNIAFGlkQDKLPKAEIA--SRVNEMLGLVH-----MQEFAKRKPHQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 540 LSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQ-EALDRV-MVGRTTVVVAH-RLSTVRNADIIAVVHEGKIV 616
Cdd:PRK11607 150 LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQlEVVDILeRVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFV 229
|
250
....*....|....*...
gi 79487035 617 EFGNHENLISNPDGAYSS 634
Cdd:PRK11607 230 QIGEPEEIYEHPTTRYSA 247
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1030-1253 |
3.50e-28 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 114.08 E-value: 3.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRPdvviFRdFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDlKALRKhIG 1109
Cdd:COG3840 2 LRLDDLTYRYGDFP----LR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP-PAERP-VS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1110 LVQQEPALFA-TTIYENILYG-----NEGASQSEVVESAM----LANahsFITSLPEgystkvgergvQMSGGQRQRIAI 1179
Cdd:COG3840 75 MLFQENNLFPhLTVAQNIGLGlrpglKLTAEQRAQVEQALervgLAG---LLDRLPG-----------QLSGGQRQRVAL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 1180 ARAILKNPAILLLDEATSALD----VESERVVQQALDRLmaNRTTVVVAHRLSTIKN-ADTISVLHGGKIVEQGSHRKL 1253
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRER--GLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAAL 217
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1030-1248 |
3.60e-28 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 114.80 E-value: 3.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRPdvvIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGK-VMIEGKDIKKLDLKALRKHI 1108
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1109 GLVQqePALFA-----TTIYENIL---YGNEGASQSevVESAMLANAHSFITSLpeGYSTKVGERGVQMSGGQRQRIAIA 1180
Cdd:COG1119 81 GLVS--PALQLrfprdETVLDVVLsgfFDSIGLYRE--PTDEQRERARELLELL--GLAHLADRPFGTLSQGEQRRVLIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79487035 1181 RAILKNPAILLLDEATSALDVESERVVQQALDRLMAN--RTTVVVAHRLSTIknADTIS---VLHGGKIVEQG 1248
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHVEEI--PPGIThvlLLKDGRVVAAG 225
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1030-1246 |
3.71e-28 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 113.66 E-value: 3.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRPdvvIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIG 1109
Cdd:PRK10247 8 LQLQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1110 LVQQEPALFATTIYENILYGNEGASQSeVVESAMLANAHSFitSLPEGYSTKvgeRGVQMSGGQRQRIAIARAILKNPAI 1189
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIFPWQIRNQQ-PDPAIFLDDLERF--ALPDTILTK---NIAELSGGEKQRISLIRNLQFMPKV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79487035 1190 LLLDEATSALDVESERVVQQALDRLMANRTTVV--VAHRLSTIKNADTISVL--HGGKIVE 1246
Cdd:PRK10247 159 LLLDEITSALDESNKHNVNEIIHRYVREQNIAVlwVTHDKDEINHADKVITLqpHAGEMQE 219
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1062-1256 |
4.83e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 114.49 E-value: 4.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1062 ALVGQSGSGKSSVISLILRFYD-----PTAGKVMIEGKDI--KKLDLKALRKHIGLVQQEPALFATTIYENILYG----- 1129
Cdd:PRK14239 35 ALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPNPFPMSIYENVVYGlrlkg 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1130 -NEGASQSEVVESAMLAnahsfiTSLPEGYSTKVGERGVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQ 1208
Cdd:PRK14239 115 iKDKQVLDEAVEKSLKG------ASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIE 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 79487035 1209 QALDRLMANRTTVVVAHRL---STIknADTISVLHGGKIVEQGSHRKLVLN 1256
Cdd:PRK14239 189 ETLLGLKDDYTMLLVTRSMqqaSRI--SDRTGFFLDGDLIEYNDTKQMFMN 237
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
401-619 |
7.32e-28 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 116.97 E-value: 7.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPdvvIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKwlRGQIG 480
Cdd:PRK09452 15 VELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 LVNQEPALFA-TTIRENILYG--KDDATAEEITRaaKLSEAISFINnlPEGFetqvGERGI-QLSGGQKQRIAISRAIVK 556
Cdd:PRK09452 90 TVFQSYALFPhMTVFENVAFGlrMQKTPAAEITP--RVMEALRMVQ--LEEF----AQRKPhQLSGGQQQRVAIARAVVN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 557 NPSILLLDEATSALDAESEKSVQ---EALDRVMvGRTTVVVAH----RLSTvrnADIIAVVHEGKIVEFG 619
Cdd:PRK09452 162 KPKVLLLDESLSALDYKLRKQMQnelKALQRKL-GITFVFVTHdqeeALTM---SDRIVVMRDGRIEQDG 227
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1050-1253 |
7.86e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 114.73 E-value: 7.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1050 DFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDI----KKLDLKALRKHIGLVQQ--EPALFATTIY 1123
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKPLRKKVGIVFQfpEHQLFEETVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1124 ENILYG--NEGASQSEVVESA--MLAnahsfITSLPEGYSTKvgeRGVQMSGGQRQRIAIARAILKNPAILLLDEATSAL 1199
Cdd:PRK13634 105 KDICFGpmNFGVSEEDAKQKAreMIE-----LVGLPEELLAR---SPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 79487035 1200 DVESERVVQQALDRLM--ANRTTVVVAHRLSTIKN-ADTISVLHGGKIVEQGSHRKL 1253
Cdd:PRK13634 177 DPKGRKEMMEMFYKLHkeKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREI 233
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
416-628 |
8.13e-28 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 116.36 E-value: 8.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 416 VVIfDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKwlRGQIGLVNQEPALFA-TTIR 494
Cdd:PRK11432 20 TVI-DNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFPhMSLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 495 ENILYG--KDDATAEEitRAAKLSEAISFINnlPEGFEtqvgERGI-QLSGGQKQRIAISRAIVKNPSILLLDEATSALD 571
Cdd:PRK11432 97 ENVGYGlkMLGVPKEE--RKQRVKEALELVD--LAGFE----DRYVdQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79487035 572 AESEKSVQEALDRVM--VGRTTVVVAHRLS---TVrnADIIAVVHEGKIVEFGNHENLISNP 628
Cdd:PRK11432 169 ANLRRSMREKIRELQqqFNITSLYVTHDQSeafAV--SDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1030-1253 |
1.11e-27 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 112.21 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRPDVVIfRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKlDLKALRKHIG 1109
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAV-DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1110 LVQQEPALFAT-TIYENI-----LYGNEGASQSEVVESAMLanahsfITSLPEGYSTKVGergvQMSGGQRQRIAIARAI 1183
Cdd:cd03263 79 YCPQFDALFDElTVREHLrfyarLKGLPKSEIKEEVELLLR------VLGLTDKANKRAR----TLSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79487035 1184 LKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVVVAHRLSTIKN-ADTISVLHGGKIVEQGSHRKL 1253
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
401-619 |
1.38e-27 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 111.90 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRpdvVIFDRLNLAIPAGkIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISElDIKWLRGQIG 480
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 LVNQEPALFAT-TIRE-----NILYGKDDATAEEitRAAKLSEAIsfinNLPEGFETQVGergiQLSGGQKQRIAISRAI 554
Cdd:cd03264 76 YLPQEFGVYPNfTVREfldyiAWLKGIPSKEVKA--RVDEVLELV----NLGDRAKKKIG----SLSGGMRRRVGIAQAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79487035 555 VKNPSILLLDEATSALDAESEKSVQEALDRVMVGRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFG 619
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
401-630 |
1.63e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 113.31 E-value: 1.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPDVVIfDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIG 480
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTL-KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 LVNQEP--ALFATTIRENILYGKDDATAEEITRAAKLSEAISFINNLPEG-FETQvgergiQLSGGQKQRIAISRAIVKN 557
Cdd:PRK13648 87 IVFQNPdnQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERAdYEPN------ALSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79487035 558 PSILLLDEATSALDAESEKSVQEALDRVMVGR--TTVVVAHRLSTVRNADIIAVVHEGKIVEFGNHENLISNPDG 630
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEE 235
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
401-609 |
1.74e-27 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 111.42 E-value: 1.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPdvvIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWlRGQIG 480
Cdd:COG4133 3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 LVNQEPALFAT-TIRENI-----LYGkDDATAEEITRAAklsEAIsfinNLPEGFETQVGergiQLSGGQKQRIAISRAI 554
Cdd:COG4133 79 YLGHADGLKPElTVRENLrfwaaLYG-LRADREAIDEAL---EAV----GLAGLADLPVR----QLSAGQKRRVALARLL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 555 VKNPSILLLDEATSALDAES----EKSVQEALDRvmvGRTTVVVAHRLSTVRNADIIAV 609
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGvallAELIAAHLAR---GGAVLLTTHQPLELAAARVLDL 202
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1030-1242 |
1.77e-27 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 111.65 E-value: 1.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPsrPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKAL----R 1105
Cdd:cd03290 1 VQVTNGYFSWG--SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1106 KHIGLVQQEPALFATTIYENILYGNEGASQ--SEVVESAMLanaHSFITSLPEGYSTKVGERGVQMSGGQRQRIAIARAI 1183
Cdd:cd03290 79 YSVAYAAQKPWLLNATVEENITFGSPFNKQryKAVTDACSL---QPDIDLLPFGDQTEIGERGINLSGGQRQRICVARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79487035 1184 LKNPAILLLDEATSALDVE-SERVVQQALDRLMAN--RTTVVVAHRLSTIKNADTISVLHGG 1242
Cdd:cd03290 156 YQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
401-646 |
2.15e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 113.58 E-value: 2.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSY-PSRPdvviFDRL-----NLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNIS----EL 470
Cdd:PRK13634 3 ITFQKVEHRYqYKTP----FERRalydvNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkkNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 471 DIKWLRGQIGLVNQ--EPALFATTIRENILYGKDDATAEEITRAAKLSEAISFINnLPEgfetQVGERG-IQLSGGQKQR 547
Cdd:PRK13634 79 KLKPLRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELVG-LPE----ELLARSpFELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 548 IAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRVM--VGRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFGNHENL 624
Cdd:PRK13634 154 VAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHkeKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREI 233
|
250 260
....*....|....*....|..
gi 79487035 625 ISNPDGAYSSLLRLQETASLQR 646
Cdd:PRK13634 234 FADPDELEAIGLDLPETVKFKR 255
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1041-1238 |
2.17e-27 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 111.03 E-value: 2.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1041 SRPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLkALRKHIGLVQQEPALFAT 1120
Cdd:COG4133 11 RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE-DYRRRLAYLGHADGLKPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1121 -TIYENI-----LYGNEGAsqSEVVESAMLAnahsfiTSLPEGYSTKVGergvQMSGGQRQRIAIARAILKNPAILLLDE 1194
Cdd:COG4133 90 lTVRENLrfwaaLYGLRAD--REAIDEALEA------VGLAGLADLPVR----QLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 79487035 1195 ATSALDVESERVVQQALDRLMANRTTVVVA-HRLSTIKNADTISV 1238
Cdd:COG4133 158 PFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDL 202
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
401-668 |
2.75e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 112.91 E-value: 2.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSrpDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIG 480
Cdd:PRK13647 5 IEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 LVNQEP--ALFATTIRENILYGKDDA--TAEEITRaaKLSEAISFInnlpeGFETQVGERGIQLSGGQKQRIAISRAIVK 556
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGPVNMglDKDEVER--RVEEALKAV-----RMWDFRDKPPYHLSYGQKKRVAIAGVLAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 557 NPSILLLDEATSALDAESEKSVQEALDRVMVGRTTVVVA-HRLSTVRN-ADIIAVVHEGKIVEFGNHEnLISNPDGAYSS 634
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGDKS-LLTDEDIVEQA 234
|
250 260 270
....*....|....*....|....*....|....*
gi 79487035 635 LLRLQETASL-QRNPSLNRTlSRPHSIKYSRELSR 668
Cdd:PRK13647 235 GLRLPLVAQIfEDLPELGQS-KLPLTVKEAVQIIR 268
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1030-1245 |
2.98e-27 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 109.06 E-value: 2.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSrpdVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLK-ALRKHI 1108
Cdd:cd03216 1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRdARRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1109 GLVQQepalfattiyenilygnegasqsevvesamlanahsfitslpegystkvgergvqMSGGQRQRIAIARAILKNPA 1188
Cdd:cd03216 78 AMVYQ-------------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1189 ILLLDEATSALDV-ESERVVQQaLDRLMANRTTVV-VAHRLSTIKN-ADTISVLHGGKIV 1245
Cdd:cd03216 103 LLILDEPTAALTPaEVERLFKV-IRRLRAQGVAVIfISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1049-1253 |
3.12e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 112.95 E-value: 3.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1049 RDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDI----KKLDLKALRKHIGLVQQ--EPALFATTI 1122
Cdd:PRK13646 24 HDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRPVRKRIGMVFQfpESQLFEDTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1123 YENILYG--NEGASQSEVVEsamlaNAHSFITSLpeGYSTKVGERG-VQMSGGQRQRIAIARAILKNPAILLLDEATSAL 1199
Cdd:PRK13646 104 EREIIFGpkNFKMNLDEVKN-----YAHRLLMDL--GFSRDVMSQSpFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 79487035 1200 DVESERVVQQALDRLMA--NRTTVVVAHRLSTI-KNADTISVLHGGKIVEQGSHRKL 1253
Cdd:PRK13646 177 DPQSKRQVMRLLKSLQTdeNKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKEL 233
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
126-299 |
3.43e-27 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 113.02 E-value: 3.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 126 FVYLSVAILFSSWLEVACWMHTGERQAAKMRRAYLRSMLSQDISLFDTEaSTGEVISAITSDILVVQDALSEKVGNFLHY 205
Cdd:cd18572 42 LLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDAT-KTGELTSRLTSDCQKVSDPLSTNLNVFLRN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 206 ISRFIAGFAIGFTSVWQISLVTLSIVPLIALAGGIYAFVAIGLIARVRKSYIKAGEIAEEVIGNVRTVQAFTGEERAVRL 285
Cdd:cd18572 121 LVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARR 200
|
170
....*....|....
gi 79487035 286 YREALENTYKYGRK 299
Cdd:cd18572 201 YERALDKALKLSVR 214
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
404-596 |
9.22e-27 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 109.27 E-value: 9.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 404 KDATFSYPSRPDVVifDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISEldiKWLRGQIGLVN 483
Cdd:cd03226 3 ENISFSYKKGTEIL--DDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 484 QEP--ALFATTIRENILYGKDDAtAEEITRAAKLSEAISfINNLPEgfetqvgERGIQLSGGQKQRIAISRAIVKNPSIL 561
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGLKEL-DAGNEQAETVLKDLD-LYALKE-------RHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190
....*....|....*....|....*....|....*.
gi 79487035 562 LLDEATSALDAESEKSVQEALDRVM-VGRTTVVVAH 596
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAaQGKAVIVITH 184
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1030-1253 |
1.04e-26 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 109.45 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPsrpDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDL-KALRKHI 1108
Cdd:cd03224 1 LEVENLNAGYG---KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPhERARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1109 GLVQQEPALFAT-TIYENILYGNEGASQSEVveSAMLANAHSFITSLPEGYSTKVGergvQMSGGQRQRIAIARAILKNP 1187
Cdd:cd03224 78 GYVPEGRRIFPElTVEENLLLGAYARRRAKR--KARLERVYELFPRLKERRKQLAG----TLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79487035 1188 AILLLDEATSALdveSERVVQQ---ALDRLMANRTTVVV----AHRLSTIknADTISVLHGGKIVEQGSHRKL 1253
Cdd:cd03224 152 KLLLLDEPSEGL---APKIVEEifeAIRELRDEGVTILLveqnARFALEI--ADRAYVLERGRVVLEGTAAEL 219
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1025-1248 |
1.52e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 110.88 E-value: 1.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1025 NVEGTIELKGVHFSYP--SRPDVvifRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLK 1102
Cdd:PRK13635 1 MKEEIIRVEHISFRYPdaATYAL---KDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1103 ALRKHIGLVQQEP--ALFATTIYENILYG--NEGASQSEVVE---SAM-LANAHSFITSLPEgystkvgergvQMSGGQR 1174
Cdd:PRK13635 78 DVRRQVGMVFQNPdnQFVGATVQDDVAFGleNIGVPREEMVErvdQALrQVGMEDFLNREPH-----------RLSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79487035 1175 QRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVVVA--HRLSTIKNADTISVLHGGKIVEQG 1248
Cdd:PRK13635 147 QRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSitHDLDEAAQADRVIVMNKGEILEEG 222
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1057-1261 |
1.54e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 111.98 E-value: 1.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1057 AGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLD---LKALRKHIGLVQQEPalFAT--------TIYEN 1125
Cdd:PRK11308 40 RGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQNP--YGSlnprkkvgQILEE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1126 ILYGNEGASQSEVVES--AMLAnahsfitslpegystKVG------ERGVQM-SGGQRQRIAIARAILKNPAILLLDEAT 1196
Cdd:PRK11308 118 PLLINTSLSAAERREKalAMMA---------------KVGlrpehyDRYPHMfSGGQRQRIAIARALMLDPDVVVADEPV 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79487035 1197 SALDVEservVQ-QALDRLM-----ANRTTVVVAHRLSTIKN-ADTISVLHGGKIVEQGSHRKLVLNKSGPY 1261
Cdd:PRK11308 183 SALDVS----VQaQVLNLMMdlqqeLGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNNPRHPY 250
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1030-1248 |
1.68e-26 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 108.73 E-value: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRPdvvifRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKalRKHIG 1109
Cdd:cd03298 1 VRLDKIRFSYGEQP-----MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1110 LVQQEPALFA-TTIYENILYG-NEGASQSEVVESAMLANAHSFitslpeGYSTKVGERGVQMSGGQRQRIAIARAILKNP 1187
Cdd:cd03298 74 MLFQENNLFAhLTVEQNVGLGlSPGLKLTAEDRQAIEVALARV------GLAGLEKRLPGELSGGERQRVALARVLVRDK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79487035 1188 AILLLDEATSALDVESERVVQQALDRLMANR--TTVVVAHRLSTIKNADTISV-LHGGKIVEQG 1248
Cdd:cd03298 148 PVLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRLAQRVVfLDNGRIAAQG 211
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
401-620 |
2.00e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 110.52 E-value: 2.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSY-PSRP-DVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKW--LR 476
Cdd:PRK13637 3 IKIENLTHIYmEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLsdIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 477 GQIGLVNQEP--ALFATTIRENILYGKDD--ATAEEITRAAKLSEAISFINnlpegFETQVGERGIQLSGGQKQRIAISR 552
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEKDIAFGPINlgLSEEEIENRVKRAMNIVGLD-----YEDYKDKSPFELSGGQKRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79487035 553 AIVKNPSILLLDEATSALDAeseKSVQEALDRVM-----VGRTTVVVAHRLSTV-RNADIIAVVHEGKIVEFGN 620
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDP---KGRDEILNKIKelhkeYNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGT 228
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
752-964 |
2.43e-26 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 110.72 E-value: 2.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 752 IAILFCCASVITLIVYTIEHICFGTMGERLTLRVRENMFRAILKNEIGWFDEvdNTSSMLASRLESDATLLKTIVVDRST 831
Cdd:cd07346 41 IALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDR--NRTGDLMSRLTSDVDAVQNLVSSGLL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 832 ILLQNLGLVVTSFIIAFILNWRLTLVVLATYPLVIsghisekLFMQGYGGDLNKAYLK-----ANMLAG--ESVSNIRTV 904
Cdd:cd07346 119 QLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYV-------LILRYFRRRIRKASREvreslAELSAFlqESLSGIRVV 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 905 AAFCAEEKILELYSRELLEPSKSSFRRGQIAGLFYGVSQFFIFSSYGLALWYGSTLMDKG 964
Cdd:cd07346 192 KAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQG 251
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
401-628 |
2.48e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 109.74 E-value: 2.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPdvvIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYE-----PISGAVLLDGNNISE--LDIK 473
Cdd:PRK14258 8 IKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIYErrVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 474 WLRGQIGLVNQEPALFATTIRENILYG----------KDDATAEEITRAAKLSEAIsfinnlpegfETQVGERGIQLSGG 543
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwrpklEIDDIVESALKDADLWDEI----------KHKIHKSALDLSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 544 QKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALD--RVMVGRTTVVVAHRLSTV-RNADIIAVVHE-----GKI 615
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVsRLSDFTAFFKGnenriGQL 234
|
250
....*....|...
gi 79487035 616 VEFGNHENLISNP 628
Cdd:PRK14258 235 VEFGLTKKIFNSP 247
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
422-629 |
3.15e-26 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 111.74 E-value: 3.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 422 LNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISE----LDIKWLRGQIGLVNQEPALFA-TTIREN 496
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgIFLPPEKRRIGYVFQEARLFPhLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 497 ILYGKDDATAEEitRAAKLSEAISFInnlpeGFETQVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEK 576
Cdd:TIGR02142 96 LRYGMKRARPSE--RRISFERVIELL-----GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 79487035 577 SVQEALDRVM--VGRTTVVVAHRLSTV-RNADIIAVVHEGKIVEFGNHENLISNPD 629
Cdd:TIGR02142 169 EILPYLERLHaeFGIPILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
422-628 |
3.62e-26 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 108.68 E-value: 3.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 422 LNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISG-----AVLLDGN---NISELDIKWLRGQIGLVNQEPALFA-TT 492
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTArslSQQKGLIRQLRQHVGFVFQNFNLFPhRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 493 IRENILYG----KDDATAEEITRAAKLSEAISFinnlpEGFETQVGERgiqLSGGQKQRIAISRAIVKNPSILLLDEATS 568
Cdd:PRK11264 102 VLENIIEGpvivKGEPKEEATARARELLAKVGL-----AGKETSYPRR---LSGGQQQRVAIARALAMRPEVILFDEPTS 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79487035 569 ALDAEsekSVQEALDRVMV----GRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFGNHENLISNP 628
Cdd:PRK11264 174 ALDPE---LVGEVLNTIRQlaqeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFADP 235
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
423-632 |
4.40e-26 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 112.43 E-value: 4.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 423 NLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWL----RGQIGLVNQEPALFA-TTIRENI 497
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSFALMPhMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 498 LYGKDDATAEEITRAAKLSEAISFInnlpeGFETQVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKS 577
Cdd:PRK10070 128 AFGMELAGINAEERREKALDALRQV-----GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 578 VQEALDRVMVG--RTTVVVAHRL-STVRNADIIAVVHEGKIVEFGNHENLISNPDGAY 632
Cdd:PRK10070 203 MQDELVKLQAKhqRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1031-1245 |
4.51e-26 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 107.34 E-value: 4.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1031 ELKGVHFSYPSRPDVVifRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKldlKALRKHIGL 1110
Cdd:cd03226 1 RIENISFSYKKGTEIL--DDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1111 VQQEP--ALFATTIYENILYGNEGASQS-EVVESAM-------LANAHSFItslpegystkvgergvqMSGGQRQRIAIA 1180
Cdd:cd03226 76 VMQDVdyQLFTDSVREELLLGLKELDAGnEQAETVLkdldlyaLKERHPLS-----------------LSGGQKQRLAIA 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79487035 1181 RAILKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVVVA-HRLSTIKN-ADTISVLHGGKIV 1245
Cdd:cd03226 139 AALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVItHDYEFLAKvCDRVLLLANGAIV 205
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
423-644 |
8.49e-26 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 110.58 E-value: 8.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 423 NLAIPAGKIVALVGGSGSGKSTVISLI---ERfyeP------ISGAVLLDgnniSELDIkWL---RGQIGLVNQEPALFA 490
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIaglER---PdsgrirLGGEVLQD----SARGI-FLpphRRRIGYVFQEARLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 491 T-TIRENILYGKDDATAEEitRAAKLSEAISFInnlpeGFETQVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEATSA 569
Cdd:COG4148 91 HlSVRGNLLYGRKRAPRAE--RRISFDEVVELL-----GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 570 LDAESEKSVQEALDRVmvgRTT-----VVVAHRLSTV-RNADIIAVVHEGKIVEFGNHENLISNPDgaYSSLLRLQETAS 643
Cdd:COG4148 164 LDLARKAEILPYLERL---RDEldipiLYVSHSLDEVaRLADHVVLLEQGRVVASGPLAEVLSRPD--LLPLAGGEEAGS 238
|
.
gi 79487035 644 L 644
Cdd:COG4148 239 V 239
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
401-619 |
9.41e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 108.56 E-value: 9.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYP--SRPDVvifDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQ 478
Cdd:PRK13635 6 IRVEHISFRYPdaATYAL---KDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 479 IGLVNQEP--ALFATTIRENILYGKDDATAEEITRAAKLSEAISFINNlpEGFETQVGERgiqLSGGQKQRIAISRAIVK 556
Cdd:PRK13635 83 VGMVFQNPdnQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGM--EDFLNREPHR---LSGGQKQRVAIAGVLAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79487035 557 NPSILLLDEATSALDAESEKSVQEALdRVMV--GRTTVV-VAHRLSTVRNADIIAVVHEGKIVEFG 619
Cdd:PRK13635 158 QPDIIILDEATSMLDPRGRREVLETV-RQLKeqKGITVLsITHDLDEAAQADRVIVMNKGEILEEG 222
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1049-1263 |
1.36e-25 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 110.89 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1049 RDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALR----KHIGLVQQEPALFA-TTIY 1123
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMPhMTVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1124 ENILYGNE--GASQSEVVESAMLANAHSFITSLPEGYSTkvgergvQMSGGQRQRIAIARAILKNPAILLLDEATSALDV 1201
Cdd:PRK10070 125 DNTAFGMElaGINAEERREKALDALRQVGLENYAHSYPD-------ELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79487035 1202 ESERVVQQALDRLMA--NRTTVVVAHRL-STIKNADTISVLHGGKIVEQGSHRKLVLNKSGPYFK 1263
Cdd:PRK10070 198 LIRTEMQDELVKLQAkhQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1030-1260 |
1.39e-25 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 106.72 E-value: 1.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGV--HFSypsrpDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIK--KLDLKALR 1105
Cdd:PRK09493 2 IEFKNVskHFG-----PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1106 KHIGLVQQEPALFA-TTIYENILYGN---EGASQSEVVESAM--LANAhsfitslpeGYSTKVGERGVQMSGGQRQRIAI 1179
Cdd:PRK09493 77 QEAGMVFQQFYLFPhLTALENVMFGPlrvRGASKEEAEKQARelLAKV---------GLAERAHHYPSELSGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1180 ARAILKNPAILLLDEATSALDVESE----RVVQQALDRLManrTTVVVAHRLS-TIKNADTISVLHGGKIVEQGSHRKLV 1254
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALDPELRhevlKVMQDLAEEGM---TMVIVTHEIGfAEKVASRLIFIDKGRIAEDGDPQVLI 224
|
....*.
gi 79487035 1255 LNKSGP 1260
Cdd:PRK09493 225 KNPPSQ 230
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
424-629 |
1.55e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 107.56 E-value: 1.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 424 LAIPAGKIVALVGGSGSGKSTVI-------SLIERFYepISGAVLLDGNNI--SELDIKWLRGQIGLVNQEPALFATTIR 494
Cdd:PRK14243 31 LDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGFR--VEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPKSIY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 495 ENILYGKD--------DATAEEITRAAKLSEAIsfinnlpegfETQVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEA 566
Cdd:PRK14243 109 DNIAYGARingykgdmDELVERSLRQAALWDEV----------KDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79487035 567 TSALDAESEKSVQEALDRVMVGRTTVVVAHRLSTV-RNADIIAVVH---------EGKIVEFGNHENLISNPD 629
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAaRVSDMTAFFNveltegggrYGYLVEFDRTEKIFNSPQ 251
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
415-628 |
2.21e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 106.67 E-value: 2.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 415 DVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYE------PISGAVLLDGNNISELDIKWLRGQIGLVNQEPAL 488
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 489 FA-TTIRENILYGKDDATAEEITRAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEAT 567
Cdd:PRK14246 102 FPhLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79487035 568 SALDAESEKSVQEALDRVMVGRTTVVVAHRLSTV-RNADIIAVVHEGKIVEFGNHENLISNP 628
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIFTSP 243
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
416-629 |
2.43e-25 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 105.98 E-value: 2.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 416 VVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISEL--DIKWLRGqIGLVNQEPALFAT-T 492
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLppHEIARLG-IGRTFQIPRLFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 493 IRENIL----------YGKDDATAEEITRAAKLSEAISFInNLPEGFETQVGErgiqLSGGQKQRIAISRAIVKNPSILL 562
Cdd:cd03219 92 VLENVMvaaqartgsgLLLARARREEREARERAEELLERV-GLADLADRPAGE----LSYGQQRRLEIARALATDPKLLL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 563 LDEATSALDAESEKSVQEALDRVMV-GRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFGNHENLISNPD 629
Cdd:cd03219 167 LDEPAAGLNPEETEELAELIRELRErGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
429-619 |
2.44e-25 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 105.45 E-value: 2.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 429 GKIVALVGGSGSGKSTVISLIERFYEP------ISGAVLLDGNNisELDIKWLRGQIGLVNQEPALFA-TTIRENILYG- 500
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPdggtivLNGTVLFDSRK--KINLPPQQRKIGLVFQQYALFPhLNVRENLAFGl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 501 KDDATAEEITRAAKLSEAISFinnlpegfeTQVGERGI-QLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQ 579
Cdd:cd03297 101 KRKRNREDRISVDELLDLLGL---------DHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 79487035 580 EALDRVM--VGRTTVVVAHRLSTV-RNADIIAVVHEGKIVEFG 619
Cdd:cd03297 172 PELKQIKknLNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1034-1242 |
2.81e-25 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 107.25 E-value: 2.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1034 GVHFSYPSRPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKdikkldlkalrkhIGLVQQ 1113
Cdd:cd03291 39 NLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1114 EPALFATTIYENILYG---NEGASQSeVVESAMLANAhsfITSLPEGYSTKVGERGVQMSGGQRQRIAIARAILKNPAIL 1190
Cdd:cd03291 106 FSWIMPGTIKENIIFGvsyDEYRYKS-VVKACQLEED---ITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLY 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 79487035 1191 LLDEATSALDVESER-VVQQALDRLMANRTTVVVAHRLSTIKNADTISVLHGG 1242
Cdd:cd03291 182 LLDSPFGYLDVFTEKeIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
418-634 |
3.53e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 106.72 E-value: 3.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 418 IFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGA-----VLLDGNNI-SELDIKWLRGQIGLVNQEPALFAT 491
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIfNYRDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 492 TIRENILYGkddataeeiTRAAKLSEAISFiNNLPEGFETQVG----------ERGIQLSGGQKQRIAISRAIVKNPSIL 561
Cdd:PRK14271 116 SIMDNVLAG---------VRAHKLVPRKEF-RGVAQARLTEVGlwdavkdrlsDSPFRLSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79487035 562 LLDEATSALDAESEKSVQEALDRVMVGRTTVVVAHRLS-TVRNADIIAVVHEGKIVEFGNHENLISNPDGAYSS 634
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETA 259
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
422-656 |
3.56e-25 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 106.86 E-value: 3.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 422 LNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAvlldgnniseldIKWlRGQIGLVNQEPALFATTIRENILYG- 500
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGK------------IKH-SGRISFSSQFSWIMPGTIKENIIFGv 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 501 -KDDATAEEITRAAKLSEAISfinNLPEGFETQVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQ 579
Cdd:cd03291 123 sYDEYRYKSVVKACQLEEDIT---KFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIF 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 580 EA-LDRVMVGRTTVVVAHRLSTVRNADIIAVVHEGKIVEFGNHENLIS-NPDgaYSSLL----RLQETASLQRNPSLNRT 653
Cdd:cd03291 200 EScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSlRPD--FSSKLmgydTFDQFSAERRNSILTET 277
|
...
gi 79487035 654 LSR 656
Cdd:cd03291 278 LRR 280
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
401-644 |
3.70e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 106.70 E-value: 3.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSrpDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISeLDIKWL---RG 477
Cdd:PRK13639 2 LETRDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLlevRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 478 QIGLVNQEP--ALFATTIRENILYGKDDA--TAEEITRAAKlsEAISFINNlpEGFETQVGErgiQLSGGQKQRIAISRA 553
Cdd:PRK13639 79 TVGIVFQNPddQLFAPTVEEDVAFGPLNLglSKEEVEKRVK--EALKAVGM--EGFENKPPH---HLSGGQKKRVAIAGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 554 IVKNPSILLLDEATSALDAESEKSVQEAL-DRVMVGRTTVVVAHRLSTV-RNADIIAVVHEGKIVEFGNHENLISNPDGA 631
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDPMGASQIMKLLyDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSDIETI 231
|
250
....*....|...
gi 79487035 632 YSSLLRLQETASL 644
Cdd:PRK13639 232 RKANLRLPRVAHL 244
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
401-615 |
3.86e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 106.74 E-value: 3.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIG 480
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 LVNQEP--ALFATTIRENILYGKDDATAEEITRAAKLSEAISFINNlpEGFETQVGERgiqLSGGQKQRIAISRAIVKNP 558
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGM--QDFKEREPAR---LSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79487035 559 SILLLDEATSALDAESE----KSVQEALDRvmVGRTTVVVAHRLSTVRNADIIAVVHEGKI 615
Cdd:PRK13650 160 KIIILDEATSMLDPEGRleliKTIKGIRDD--YQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1044-1253 |
4.19e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 105.90 E-value: 4.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1044 DVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRF---YDP---TAGKVMIEGKDIKKLDLKALRKHIGLVQQEPAL 1117
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSkikVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1118 FA-TTIYENILYGNEGASQSEVVESAMLANAHSFITSLPEGYSTKVGERGVQMSGGQRQRIAIARAILKNPAILLLDEAT 1196
Cdd:PRK14246 102 FPhLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 1197 SALDVESERVVQQALDRLMANRTTVVVAHRLSTI-KNADTISVLHGGKIVEQGSHRKL 1253
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
401-617 |
4.47e-25 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 105.21 E-value: 4.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRP-DVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLI---ERfyePISGAVLLDGNNISELD----I 472
Cdd:COG4181 9 IELRGLTKTVGTGAgELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLaglDR---PTSGTVRLAGQDLFALDedarA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 473 KWLRGQIGLVNQEPALFAT-TIRENI-----LYGKDDATAeeitRAAKLSEAISfinnlpegfetqVGERG----IQLSG 542
Cdd:COG4181 86 RLRARHVGFVFQSFQLLPTlTALENVmlpleLAGRRDARA----RARALLERVG------------LGHRLdhypAQLSG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 543 GQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQE---ALDRVMvGRTTVVVAHRLSTVRNADIIAVVHEGKIVE 617
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDllfELNRER-GTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
397-666 |
4.48e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 106.42 E-value: 4.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 397 VDGHIQFKDATFSYPSRPDVVIFDrLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGA---VLLDGNNISELDIK 473
Cdd:PRK13640 2 KDNIVEFKHVSFTYPDSKKPALND-ISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 474 WLRGQIGLVNQEP--ALFATTIRENILYGKDDataeeitRAAKLSEAISFINNLPEgfetQVGERGIQ------LSGGQK 545
Cdd:PRK13640 81 DIREKVGIVFQNPdnQFVGATVGDDVAFGLEN-------RAVPRPEMIKIVRDVLA----DVGMLDYIdsepanLSGGQK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 546 QRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRVMV--GRTTVVVAHRLSTVRNADIIAVVHEGKIVEFGNHEN 623
Cdd:PRK13640 150 QRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVE 229
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 79487035 624 LISNPDGAYSSLLRLQETASLqRNPSLNRTLSRPHSIKYSREL 666
Cdd:PRK13640 230 IFSKVEMLKEIGLDIPFVYKL-KNKLKEKGISVPQEINTEEKL 271
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1030-1249 |
4.56e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 106.32 E-value: 4.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSrpDVVIFRDFDLIVRAGKSMALVGQSGSGKSSvisLILRF---YDPTAGKVMIEGKDIK--KLDLKAL 1104
Cdd:PRK13639 2 LETRDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKST---LFLHFngiLKPTSGEVLIKGEPIKydKKSLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1105 RKHIGLVQQEP--ALFATTIYENILYG--NEGASQSEV---VESAMLANAHsfitslpEGYSTKVGErgvQMSGGQRQRI 1177
Cdd:PRK13639 77 RKTVGIVFQNPddQLFAPTVEEDVAFGplNLGLSKEEVekrVKEALKAVGM-------EGFENKPPH---HLSGGQKKRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79487035 1178 AIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVVVA-HRLSTI-KNADTISVLHGGKIVEQGS 1249
Cdd:PRK13639 147 AIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVpVYADKVYVMSDGKIIKEGT 220
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
401-647 |
4.85e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 106.79 E-value: 4.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSY-PSRP-DVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNIS----ELDIKW 474
Cdd:PRK13646 3 IRFDNVSYTYqKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 475 LRGQIGLVNQ--EPALFATTIRENILYGKDD--ATAEEI-TRAAKLSeaisfinnLPEGFETQVGERG-IQLSGGQKQRI 548
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNfkMNLDEVkNYAHRLL--------MDLGFSRDVMSQSpFQMSGGQMRKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 549 AISRAIVKNPSILLLDEATSALDAESEKSVQEALDRVMV--GRTTVVVAHRLSTV-RNADIIAVVHEGKIVEFGNHENLI 625
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTdeNKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELF 234
|
250 260
....*....|....*....|..
gi 79487035 626 SNPDGAYSSLLRLQETASLQRN 647
Cdd:PRK13646 235 KDKKKLADWHIGLPEIVQLQYD 256
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1048-1249 |
5.34e-25 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 108.26 E-value: 5.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1048 FRDFDLIVR----AGKSMALVGQSGSGKSSVISLI---LRfydPTAGKVMIEGKDI----KKLDLKALRKHIGLVQQEPA 1116
Cdd:COG4148 11 RGGFTLDVDftlpGRGVTALFGPSGSGKTTLLRAIaglER---PDSGRIRLGGEVLqdsaRGIFLPPHRRRIGYVFQEAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1117 LFAT-TIYENILYG-------NEGASQSEVVEsaMLAnahsfITSLPEgystkvgeRGV-QMSGGQRQRIAIARAILKNP 1187
Cdd:COG4148 88 LFPHlSVRGNLLYGrkrapraERRISFDEVVE--LLG-----IGHLLD--------RRPaTLSGGERQRVAIGRALLSSP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79487035 1188 AILLLDEATSALDVESERVVQQALDRLmANRTT---VVVAH------RLstiknADTISVLHGGKIVEQGS 1249
Cdd:COG4148 153 RLLLMDEPLAALDLARKAEILPYLERL-RDELDipiLYVSHsldevaRL-----ADHVVLLEQGRVVASGP 217
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
417-627 |
5.50e-25 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 104.44 E-value: 5.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 417 VIFDrLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISEL---DIkwLRGQIGLVNQEPALFAT-T 492
Cdd:cd03224 15 ILFG-VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLpphER--ARAGIGYVPEGRRIFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 493 IRENILYGKDDATAEEitRAAKLSEAISFINNLPEGFETQVGergiQLSGGQKQRIAISRAIVKNPSILLLDEATSALda 572
Cdd:cd03224 92 VEENLLLGAYARRRAK--RKARLERVYELFPRLKERRKQLAG----TLSGGEQQMLAIARALMSRPKLLLLDEPSEGL-- 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 573 eSEKSVQEALDRVM----VGRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFGNHENLISN 627
Cdd:cd03224 164 -APKIVEEIFEAIRelrdEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLAD 222
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1030-1253 |
9.13e-25 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 107.50 E-value: 9.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSrpDVVIfRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKalRKHIG 1109
Cdd:PRK11432 7 VVLKNITKRFGS--NTVI-DNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1110 LVQQEPALFA-TTIYENILYG--NEGASQSEVVESAMLANAhsfITSLpEGYstkvGERGV-QMSGGQRQRIAIARAILK 1185
Cdd:PRK11432 82 MVFQSYALFPhMSLGENVGYGlkMLGVPKEERKQRVKEALE---LVDL-AGF----EDRYVdQISGGQQQRVALARALIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79487035 1186 NPAILLLDEATSALDV-------ESERVVQQALdrlmaNRTTVVVAHRLS-TIKNADTISVLHGGKIVEQGSHRKL 1253
Cdd:PRK11432 154 KPKVLLFDEPLSNLDAnlrrsmrEKIRELQQQF-----NITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
422-640 |
9.75e-25 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 105.05 E-value: 9.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 422 LNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISEL-------------DIKWLRGQIGLVNQEPAL 488
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLRLLRTRLTMVFQHFNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 489 FA-TTIRENILYGKDDATAeeITRAAKLSEAISFINNLpeGF-ETQVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEA 566
Cdd:PRK10619 104 WShMTVLENVMEAPIQVLG--LSKQEARERAVKYLAKV--GIdERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 567 TSALDAEsekSVQEALdRVMV-----GRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFGNHENLISNPDGAyssllRLQE 640
Cdd:PRK10619 180 TSALDPE---LVGEVL-RIMQqlaeeGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGNPQSP-----RLQQ 250
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
401-617 |
9.97e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 105.56 E-value: 9.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIG 480
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 LVNQEP--ALFATTIRENILYGKDDATAEEITRAAKLSEAISFINNLpeGFETQVGERgiqLSGGQKQRIAISRAIVKNP 558
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNML--DFKTREPAR---LSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79487035 559 SILLLDEATSALD----AESEKSVQEALDRVMVgrTTVVVAHRLSTVRNADIIAVVHEGKIVE 617
Cdd:PRK13642 160 EIIILDESTSMLDptgrQEIMRVIHEIKEKYQL--TVLSITHDLDEAASSDRILVMKAGEIIK 220
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1030-1254 |
1.04e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 105.20 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSrpDVVIFRDFDLIVRAGKSMALVGQSGSGKSSvisLILRF---YDPTAGKVMIEGKDIKKLDLKALRK 1106
Cdd:PRK13647 5 IEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKST---LLLHLngiYLPQRGRVKVMGREVNAENEKWVRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1107 HIGLVQQEP--ALFATTIYENILYG--NEGASQSEV---VESAMLA-NAHSFITSLPEgystkvgergvQMSGGQRQRIA 1178
Cdd:PRK13647 80 KVGLVFQDPddQVFSSTVWDDVAFGpvNMGLDKDEVerrVEEALKAvRMWDFRDKPPY-----------HLSYGQKKRVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 1179 IARAILKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVVVA-HRLS-TIKNADTISVLHGGKIVEQGSHRKLV 1254
Cdd:PRK13647 149 IAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDlAAEWADQVIVLKEGRVLAEGDKSLLT 226
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
401-619 |
1.11e-24 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 104.40 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPdvvIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVL-LDGNNISELDIKWLRGQI 479
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 480 GLVNqePALFA-----TTIRENILYGKDD-------ATAEEITRAAKLSEAIsfinnlpeGFETQVGERGIQLSGGQKQR 547
Cdd:COG1119 81 GLVS--PALQLrfprdETVLDVVLSGFFDsiglyrePTDEQRERARELLELL--------GLAHLADRPFGTLSQGEQRR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 548 IAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRVMV-GRTTVV-VAHRLStvrnaDIIAVVH------EGKIVEFG 619
Cdd:COG1119 151 VLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAeGAPTLVlVTHHVE-----EIPPGIThvlllkDGRVVAAG 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
420-632 |
1.12e-24 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 110.16 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 420 DRLNLAIPAGKIVALVGGSGSGKST----VISLIerfyePISGAVLLDGNNISELD---IKWLRGQIGLVNQEPalFAT- 491
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--FGSl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 492 ----TIRENILYG----KDDATAEEitRAAKLSEAisfinnLPE-GFETQVGERGI-QLSGGQKQRIAISRAIVKNPSIL 561
Cdd:COG4172 376 sprmTVGQIIAEGlrvhGPGLSAAE--RRARVAEA------LEEvGLDPAARHRYPhEFSGGQRQRIAIARALILEPKLL 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 562 LLDEATSALDAesekSVQ----EALDRVMV--GRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFGNHENLISNPDGAY 632
Cdd:COG4172 448 VLDEPTSALDV----SVQaqilDLLRDLQRehGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFDAPQHPY 521
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1052-1256 |
1.17e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 104.45 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1052 DLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDI--------KKLDLKALRKHIGLVQQEPALFA-TTI 1122
Cdd:PRK11264 23 DLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqQKGLIRQLRQHVGFVFQNFNLFPhRTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1123 YENILYG-----NEGASQSEVVESAMLANAhsfitslpeGYSTKVGERGVQMSGGQRQRIAIARAILKNPAILLLDEATS 1197
Cdd:PRK11264 103 LENIIEGpvivkGEPKEEATARARELLAKV---------GLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTS 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79487035 1198 ALDVEserVVQQALD--RLMA--NRTTVVVAHRLSTIKN-ADTISVLHGGKIVEQGSHRKLVLN 1256
Cdd:PRK11264 174 ALDPE---LVGEVLNtiRQLAqeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1030-1249 |
1.37e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 105.21 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRPDV---VIFrDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDI----KKLDLK 1102
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegrALF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1103 ALRKHIGLVQQ--EPALFATTIYENILYG--NEGASQSEVVESAM--LANAhsfitslpeGYSTKVGERG-VQMSGGQRQ 1175
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEETVLKDVAFGpqNFGVSQEEAEALARekLALV---------GISESLFEKNpFELSGGQMR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79487035 1176 RIAIARAILKNPAILLLDEATSALDVESERVVQQALDRL-MANRTTVVVAHRLSTIKN-ADTISVLHGGKIVEQGS 1249
Cdd:PRK13649 153 RVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
1051-1248 |
1.58e-24 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 103.02 E-value: 1.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1051 FDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIkkLDLKALRKHIGLVQQEPALFA-TTIYENILYG 1129
Cdd:TIGR01277 17 FDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSH--TGLAPYQRPVSMLFQENNLFAhLTVRQNIGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1130 -NEG-----ASQSEVVESAMLANAHSFITSLPEgystkvgergvQMSGGQRQRIAIARAILKNPAILLLDEATSALD--- 1200
Cdd:TIGR01277 95 lHPGlklnaEQQEKVVDAAQQVGIADYLDRLPE-----------QLSGGQRQRVALARCLVRPNPILLLDEPFSALDpll 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 79487035 1201 -VESERVVQQALDRlmANRTTVVVAHRLS-TIKNADTISVLHGGKIVEQG 1248
Cdd:TIGR01277 164 rEEMLALVKQLCSE--RQRTLLMVTHHLSdARAIASQIAVVSQGKIKVVS 211
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1045-1249 |
2.53e-24 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 102.90 E-value: 2.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1045 VVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDlKALRKHIGLVQ--QEPALFAT-T 1121
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLP-PHEIARLGIGRtfQIPRLFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1122 IYENILYGNEGASQSEVV-------ESAMLANAHSFITSLpeGYSTKVGERGVQMSGGQRQRIAIARAILKNPAILLLDE 1194
Cdd:cd03219 92 VLENVMVAAQARTGSGLLlararreEREARERAEELLERV--GLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 1195 ATSAL-DVESERVVqQALDRL-MANRTTVVVAHRLSTIKN-ADTISVLHGGKIVEQGS 1249
Cdd:cd03219 170 PAAGLnPEETEELA-ELIRELrERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
771-998 |
2.79e-24 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 104.52 E-value: 2.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 771 HICFGTMGERLTLRVRENMFRAILKNEIGWFDevDNTSSMLASRLESDATLLKTIVVDRSTILLQNLGLVVTSFIIAFIL 850
Cdd:cd18573 62 VYLLRIAGERIVARLRKRLFKSILRQDAAFFD--KNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 851 NWRLTLVVLATYPLVISGHISEKLFMQGYGGDLNKAYLKANMLAGESVSNIRTVAAFCAEEKILELYSRELLEPSKSSFR 930
Cdd:cd18573 140 SPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKK 219
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79487035 931 RGQIAGLFYGVSQFFIFSSYGLALWYGSTLMDKG------LAGFksVMKTFMVlivtALAMGETLALAPDLLKG 998
Cdd:cd18573 220 EALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGeltvgdLTSF--LMYAVYV----GSSVSGLSSFYSELMKG 287
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
401-619 |
3.08e-24 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 102.20 E-value: 3.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPDVVIfDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISElDIKWLRGQIG 480
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAV-DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 LVNQEPALFAT-TIRENI-----LYGKDDATAEEItraaklSEAISFINNLPEGFETQVGergiQLSGGQKQRIAISRAI 554
Cdd:cd03263 79 YCPQFDALFDElTVREHLrfyarLKGLPKSEIKEE------VELLLRVLGLTDKANKRAR----TLSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79487035 555 VKNPSILLLDEATSALDAESEKSVQEALDRVMVGRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFG 619
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIG 214
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
401-629 |
4.11e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 103.73 E-value: 4.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYpsRPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIG 480
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 LVNQEP--ALFATTIRENILYGKDDATAEEITRAAKLSEAISFInnlpeGFETQVGERGIQLSGGQKQRIAISRAIVKNP 558
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHML-----GLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79487035 559 SILLLDEATSALDAESEKSVQEALDRVMV--GRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFGNHENLISNPD 629
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQPD 230
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
401-629 |
5.06e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 103.76 E-value: 5.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSY-PSRP-DVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNI----SELDIKW 474
Cdd:PRK13641 3 IKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 475 LRGQIGLVNQ--EPALFATTIRENILYGKDDATAEEitRAAKlSEAISFINNLpeGFETQVGERG-IQLSGGQKQRIAIS 551
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSE--DEAK-EKALKWLKKV--GLSEDLISKSpFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 552 RAIVKNPSILLLDEATSALDAESEKSVQEA-LDRVMVGRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFGNHENLISNPD 629
Cdd:PRK13641 158 GVMAYEPEILCLDEPAAGLDPEGRKEMMQLfKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1023-1248 |
5.60e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 102.91 E-value: 5.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1023 LNNVEGTIELKGVHFSYPSRPDVVIfRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLK 1102
Cdd:PRK13648 1 MEDKNSIIVFKNVSFQYQSDASFTL-KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1103 ALRKHIGLVQQEP--ALFATTIYENILYGNEGAS------QSEVVES----AMLANAHSFITSLpegystkvgergvqmS 1170
Cdd:PRK13648 80 KLRKHIGIVFQNPdnQFVGSIVKYDVAFGLENHAvpydemHRRVSEAlkqvDMLERADYEPNAL---------------S 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1171 GGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANR--TTVVVAHRLSTIKNADTISVLHGGKIVEQG 1248
Cdd:PRK13648 145 GGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEG 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
401-676 |
6.59e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 103.14 E-value: 6.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPDVVifDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELD-IKWLRGQI 479
Cdd:PRK13644 2 IRLENVSYSYPDGTPAL--ENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 480 GLVNQEP--ALFATTIRENILYGKDDATAEEITRAAKLSEAISFInnlpeGFETQVGERGIQLSGGQKQRIAISRAIVKN 557
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEI-----GLEKYRHRSPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 558 PSILLLDEATSALDAESEKSVQEALDRVM-VGRTTVVVAHRLSTVRNADIIAVVHEGKIVEFGNHENLISNPDGAY---- 632
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLHeKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTlglt 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 79487035 633 -SSLLRLQETAslqrnpslnrtlsRPHSIKYSRELSRTRSSFCSE 676
Cdd:PRK13644 235 pPSLIELAENL-------------KMHGVVIPWENTSSPSSFAEE 266
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
154-323 |
8.03e-24 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 103.16 E-value: 8.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 154 KMRRAYLRSMLSQDISLFDTeASTGEVISAITSDILVVQDALSEKVGNFLHYISRFIAGFAIGFTSVWQISLVTLSIVPL 233
Cdd:cd18784 70 RIRNLLFRSIVSQEIGFFDT-VKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 234 IALAGGIYAFVAIGLIARVRKSYIKAGEIAEEVIGNVRTVQAFTGEERAVRLYREALENTYKYGRKAGLTKGlglGSMHC 313
Cdd:cd18784 149 IAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYG---GYVWS 225
|
170
....*....|
gi 79487035 314 VLFLSWALLV 323
Cdd:cd18784 226 NELTELALTV 235
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1030-1248 |
8.10e-24 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 100.91 E-value: 8.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSY-PSRPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKhI 1108
Cdd:cd03266 2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR-L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1109 GLVQQEPALFA-TTIYENI-----LYGNEGASQSEVVESamLANAHSFitslpEGYSTKvgeRGVQMSGGQRQRIAIARA 1182
Cdd:cd03266 81 GFVSDSTGLYDrLTARENLeyfagLYGLKGDELTARLEE--LADRLGM-----EELLDR---RVGGFSTGMRQKVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 1183 ILKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVVVA-HRLSTIKN-ADTISVLHGGKIVEQG 1248
Cdd:cd03266 151 LVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
425-666 |
8.50e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 103.89 E-value: 8.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 425 AIPAGKIVALVGGSGSGKSTV---ISLIErfyEPISGAVLLDGNNISELD---IKWLRGQIGLVNQEPalFA-------- 490
Cdd:PRK11308 37 TLERGKTLAVVGESGCGKSTLarlLTMIE---TPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQNP--YGslnprkkv 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 491 -TTIRENILYGKDDATAEEITRAAKLSEAI----SFINNLPEGFetqvgergiqlSGGQKQRIAISRAIVKNPSILLLDE 565
Cdd:PRK11308 112 gQILEEPLLINTSLSAAERREKALAMMAKVglrpEHYDRYPHMF-----------SGGQRQRIAIARALMLDPDVVVADE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 566 ATSALDAesekSVQ-EALDRVM-----VGRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFGNHENLISNPDGAYSSLLrl 638
Cdd:PRK11308 181 PVSALDV----SVQaQVLNLMMdlqqeLGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQAL-- 254
|
250 260
....*....|....*....|....*...
gi 79487035 639 qetasLQRNPSLNRTLSRPHsIKYSREL 666
Cdd:PRK11308 255 -----LSATPRLNPDDRRER-IKLTGEL 276
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
401-616 |
8.89e-24 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 100.65 E-value: 8.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPDvvifdRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKwlRGQIG 480
Cdd:cd03298 1 VRLDKIRFSYGEQPM-----HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 LVNQEPALFA-TTIRENILYGKDDA---TAEEITRAAKLSEAISFinnlpEGFETQVGErgiQLSGGQKQRIAISRAIVK 556
Cdd:cd03298 74 MLFQENNLFAhLTVEQNVGLGLSPGlklTAEDRQAIEVALARVGL-----AGLEKRLPG---ELSGGERQRVALARVLVR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79487035 557 NPSILLLDEATSALDAESEKSVQEALDRV--MVGRTTVVVAHRLSTVRN-ADIIAVVHEGKIV 616
Cdd:cd03298 146 DKPVLLLDEPFAALDPALRAEMLDLVLDLhaETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIA 208
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1047-1249 |
9.05e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 102.01 E-value: 9.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1047 IFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIGLV-QQEPALFATTIYEN 1125
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLpQHHLTPEGITVREL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1126 ILYGNE---------GASQSEVVESAMlanAHSFITSLPEgystkvgERGVQMSGGQRQRIAIARAILKNPAILLLDEAT 1196
Cdd:PRK11231 97 VAYGRSpwlslwgrlSAEDNARVNQAM---EQTRINHLAD-------RRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 1197 SALDVEServvQQALDRLM-----ANRTTVVVAHRLS-TIKNADTISVLHGGKIVEQGS 1249
Cdd:PRK11231 167 TYLDINH----QVELMRLMrelntQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGT 221
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
412-573 |
9.94e-24 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 100.63 E-value: 9.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 412 SRPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEP---ISGAVLLDGNNISELDIkwLRGQIGLVNQEPAL 488
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPA--EQRRIGILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 489 FA-TTIRENILYgkddATAEEITRAAK-------LSEAisfinNLPeGFetqvGERGI-QLSGGQKQRIAISRAIVKNPS 559
Cdd:COG4136 88 FPhLSVGENLAF----ALPPTIGRAQRrarveqaLEEA-----GLA-GF----ADRDPaTLSGGQRARVALLRALLAEPR 153
|
170
....*....|....
gi 79487035 560 ILLLDEATSALDAE 573
Cdd:COG4136 154 ALLLDEPFSKLDAA 167
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
401-622 |
9.94e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 101.63 E-value: 9.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSrpDVVIFDrLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGN------NISELDIKW 474
Cdd:PRK11124 3 IQLNGINCFYGA--HQALFD-ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdfskTPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 475 LRGQIGLVNQE----PALfatTIRENIL------YGKDDATAeeITRAAKLSEAISfINNLPEGFEtqvgergIQLSGGQ 544
Cdd:PRK11124 80 LRRNVGMVFQQynlwPHL---TVQQNLIeapcrvLGLSKDQA--LARAEKLLERLR-LKPYADRFP-------LHLSGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 545 KQRIAISRAIVKNPSILLLDEATSALDAE-SEKSVQEALDRVMVGRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFGNHE 622
Cdd:PRK11124 147 QQRVAIARALMMEPQVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1047-1247 |
1.09e-23 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 102.19 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1047 IFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLD---LKALRKHIGLVQQE------PAL 1117
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkqRRAFRRDVQLVFQDspsavnPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1118 FATTIYENILYGNEGASQSEVVE--SAMLAnahsfITSLPEGYSTKvgeRGVQMSGGQRQRIAIARAILKNPAILLLDEA 1195
Cdd:TIGR02769 106 TVRQIIGEPLRHLTSLDESEQKAriAELLD-----MVGLRSEDADK---LPRQLSGGQLQRINIARALAVKPKLIVLDEA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 79487035 1196 TSALDVESERVVQQALDRLMANRTT--VVVAHRLSTIKN-ADTISVLHGGKIVEQ 1247
Cdd:TIGR02769 178 VSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSfCQRVAVMDKGQIVEE 232
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1030-1248 |
1.13e-23 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 100.43 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPsrpDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDlkalRKHIG 1109
Cdd:cd03269 1 LEVENVTKRFG---RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1110 LVQQEPALF-ATTIYENILYgneGASQSEVVESAMLANAHSFITSLpeGYSTKVGERGVQMSGGQRQRIAIARAILKNPA 1188
Cdd:cd03269 74 YLPEERGLYpKMKVIDQLVY---LAQLKGLKKEEARRRIDEWLERL--ELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79487035 1189 ILLLDEATSALDVESERVVQQALDRLMANRTTVV-VAHRLSTIKN-ADTISVLHGGKIVEQG 1248
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRELARAGKTVIlSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1029-1257 |
1.13e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 102.60 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1029 TIELKGVHFSY-PSRP------DVVIFRdfdliVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIK---- 1097
Cdd:PRK13641 2 SIKFENVDYIYsPGTPmekkglDNISFE-----LEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1098 KLDLKALRKHIGLVQQ--EPALFATTIYENILYG--NEGASQSEVVESAMlanahSFITSLpeGYSTKVGERG-VQMSGG 1172
Cdd:PRK13641 77 NKNLKKLRKKVSLVFQfpEAQLFENTVLKDVEFGpkNFGFSEDEAKEKAL-----KWLKKV--GLSEDLISKSpFELSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1173 QRQRIAIARAILKNPAILLLDEATSALDVES-ERVVQQALDRLMANRTTVVVAHRLSTI-KNADTISVLHGGKIVEQGSH 1250
Cdd:PRK13641 150 QMRRVAIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASP 229
|
....*..
gi 79487035 1251 RKLVLNK 1257
Cdd:PRK13641 230 KEIFSDK 236
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1030-1256 |
1.32e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 101.53 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPsrpDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYD--PTA---GKVMIEGKDIKKLDLKAL 1104
Cdd:PRK14247 4 IEIRDLKVSFG---QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEArvsGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1105 RKHIGLVQQEPALFAT-TIYENILYGNE----GASQSEVVESAMLANAHSfitSLPEGYSTKVGERGVQMSGGQRQRIAI 1179
Cdd:PRK14247 81 RRRVQMVFQIPNPIPNlSIFENVALGLKlnrlVKSKKELQERVRWALEKA---QLWDEVKDRLDAPAGKLSGGQQQRLCI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1180 ARAILKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVVVAH------RLStiknaDTISVLHGGKIVEQGSHRKL 1253
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWGPTREV 232
|
...
gi 79487035 1254 VLN 1256
Cdd:PRK14247 233 FTN 235
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1020-1249 |
1.35e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 101.78 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1020 SEELNNVEGTIELKGVHFSYPSRPDVvifRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYD--PTA---GKVMIEGK 1094
Cdd:PRK14243 1 TSTLNGTETVLRTENLNVYYGSFLAV---KNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGFrveGKVTFHGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1095 DI--KKLDLKALRKHIGLVQQEPALFATTIYENILYGNE----GASQSEVVESAMLANAhsfitsLPEGYSTKVGERGVQ 1168
Cdd:PRK14243 78 NLyaPDVDPVEVRRRIGMVFQKPNPFPKSIYDNIAYGARingyKGDMDELVERSLRQAA------LWDEVKDKLKQSGLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1169 MSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVVVAHRLSTIKNADTISVLHGGKIVEQG 1248
Cdd:PRK14243 152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGG 231
|
.
gi 79487035 1249 S 1249
Cdd:PRK14243 232 G 232
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1050-1248 |
1.44e-23 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 99.98 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1050 DFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLdlKALRKHIGLVQQEPALFAT-TIYENI-- 1126
Cdd:cd03268 18 DISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKN--IEALRRIGALIEAPGFYPNlTARENLrl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1127 ---LYGNEGASQSEVVESAMLANAHSfitslpegysTKVGergvQMSGGQRQRIAIARAILKNPAILLLDEATSALDVES 1203
Cdd:cd03268 96 larLLGIRKKRIDEVLDVVGLKDSAK----------KKVK----GFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 79487035 1204 ERVVQQALDRLMANRTTVVVA-HRLSTI-KNADTISVLHGGKIVEQG 1248
Cdd:cd03268 162 IKELRELILSLRDQGITVLISsHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1031-1253 |
1.55e-23 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 100.83 E-value: 1.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1031 ELKGVHFSYPsrpDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKAL-RKHIG 1109
Cdd:COG0410 5 EVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1110 LVQQEPALFAT-TIYENILYGNEGASQSEVVESAMlanahSFITSL-PEgystkVGER----GVQMSGGQRQRIAIARAI 1183
Cdd:COG0410 82 YVPEGRRIFPSlTVEENLLLGAYARRDRAEVRADL-----ERVYELfPR-----LKERrrqrAGTLSGGEQQMLAIGRAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79487035 1184 LKNPAILLLDEATSALdveSERVVQQ---ALDRLMANRTTVVV----AHRLSTIknADTISVLHGGKIVEQGSHRKL 1253
Cdd:COG0410 152 MSRPKLLLLDEPSLGL---APLIVEEifeIIRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAAEL 223
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1030-1253 |
2.27e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 101.35 E-value: 2.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIG 1109
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1110 LVQQEP--ALFATTIYENILYG--NEGASQSE----VVESAMLANAHSFITSLPegystkvgergVQMSGGQRQRIAIAR 1181
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGleNKGIPHEEmkerVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79487035 1182 AILKNPAILLLDEATSALDVESERVVQQALDRLMA--NRTTVVVAHRLSTIKNADTISVLHGGKIVEQGSHRKL 1253
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
401-619 |
2.30e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 101.36 E-value: 2.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPDV---VIFDrLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISEL----DIK 473
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegrALFD-VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 474 WLRGQIGLVNQ--EPALFATTIRENILYGKDD--ATAEEITRAAKLSEAISFINnlpegfETQVGERGIQLSGGQKQRIA 549
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79487035 550 ISRAIVKNPSILLLDEATSALDAESEKSVQEALDRV-MVGRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFG 619
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSG 227
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1047-1248 |
2.52e-23 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 98.78 E-value: 2.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1047 IFRDFDLIVRAGKSMALVGQSGSGKSSVISLI--LRFYDPTAGKVMIEGKdikKLDLKALRKHIGLVQQEPALFAT-TIY 1123
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGR---PLDKRSFRKIIGYVPQDDILHPTlTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1124 ENILYgnegasqsevveSAMLanahsfitslpegystkvgeRGVqmSGGQRQRIAIARAILKNPAILLLDEATSALDVES 1203
Cdd:cd03213 101 ETLMF------------AAKL--------------------RGL--SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSS 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 79487035 1204 ERVVQQALDRLM-ANRTTVVVAHRLST--IKNADTISVLHGGKIVEQG 1248
Cdd:cd03213 147 ALQVMSLLRRLAdTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
399-670 |
2.81e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 101.62 E-value: 2.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 399 GHIQFKDATFSYPSRP--DVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISL-----IERFYEPISGAVLLDGNNISELD 471
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLtngliISETGQTIVGDYAIPANLKKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 472 IKWLRGQIGLVNQEP--ALFATTIRENILYGKDDATAEEITRAAKLSEAISFINnLPEGFetqVGERGIQLSGGQKQRIA 549
Cdd:PRK13645 85 VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQ-LPEDY---VKRSPFELSGGQKRRVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 550 ISRAIVKNPSILLLDEATSALDAESEKSVQEALDRV--MVGRTTVVVAHRLSTV-RNADIIAVVHEGKIVEFGNHENLIS 626
Cdd:PRK13645 161 LAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnkEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSPFEIFS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 79487035 627 N----------PDGAYSSLLRLQETASLQRNPSLnRTLSrphsiKYSRELSRTR 670
Cdd:PRK13645 241 NqelltkieidPPKLYQLMYKLKNKGIDLLNKNI-RTIE-----EFAKELAKVL 288
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
400-585 |
2.95e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 100.71 E-value: 2.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 400 HIQFKDATFSYP-SRPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDikwlrGQ 478
Cdd:COG4525 3 MLTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG-----AD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 479 IGLVNQEPALFA-TTIRENILYGKDDATAEEITRAAKLSEAISFInnlpeGFEtQVGERGI-QLSGGQKQRIAISRAIVK 556
Cdd:COG4525 78 RGVVFQKDALLPwLNVLDNVAFGLRLRGVPKAERRARAEELLALV-----GLA-DFARRRIwQLSGGMRQRVGIARALAA 151
|
170 180
....*....|....*....|....*....
gi 79487035 557 NPSILLLDEATSALDAESEKSVQEALDRV 585
Cdd:COG4525 152 DPRFLLMDEPFGALDALTREQMQELLLDV 180
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
426-636 |
3.36e-23 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 107.56 E-value: 3.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 426 IPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIGLVNQEPALFATTIRENIlygkD--- 502
Cdd:PTZ00243 1333 IAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV----Dpfl 1408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 503 DATAEEITRAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRIAISRAIVKNPS-ILLLDEATSALDAESEKSVQEA 581
Cdd:PTZ00243 1409 EASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSgFILMDEATANIDPALDRQIQAT 1488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 79487035 582 LDRVMVGRTTVVVAHRLSTVRNADIIAVVHEGKIVEFGNHENLISNPDGAYSSLL 636
Cdd:PTZ00243 1489 VMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMV 1543
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1029-1250 |
5.13e-23 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 99.32 E-value: 5.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1029 TIELKGVHFSYPSrpDVVIFrDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEG------KDIKKLDLK 1102
Cdd:PRK11124 2 SIQLNGINCFYGA--HQALF-DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1103 ALRKHIGLVQQE----PALfatTIYENILygnE------GASQSEVVESAM--LANAH--SFITSLPegystkvgergVQ 1168
Cdd:PRK11124 79 ELRRNVGMVFQQynlwPHL---TVQQNLI---EapcrvlGLSKDQALARAEklLERLRlkPYADRFP-----------LH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1169 MSGGQRQRIAIARAILKNPAILLLDEATSALDVE-SERVVQQALDRLMANRTTVVVAHRLSTIKNADTISV-LHGGKIVE 1246
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVyMENGHIVE 221
|
....
gi 79487035 1247 QGSH 1250
Cdd:PRK11124 222 QGDA 225
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
407-619 |
5.66e-23 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 98.59 E-value: 5.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 407 TFSYPSRPDVVIfDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGqIGLVNQEP 486
Cdd:cd03266 10 RFRDVKKTVQAV-DGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR-LGFVSDST 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 487 ALFA-TTIRENI-----LYG-KDDATAEEITRAAKLSEAISFINNLPEGFETqvgergiqlsgGQKQRIAISRAIVKNPS 559
Cdd:cd03266 88 GLYDrLTARENLeyfagLYGlKGDELTARLEELADRLGMEELLDRRVGGFST-----------GMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79487035 560 ILLLDEATSALDAESEKSVQEALDRVMVGRTTVVVA-HRLSTV-RNADIIAVVHEGKIVEFG 619
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
711-964 |
5.88e-23 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 100.70 E-value: 5.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 711 VCGTICAFIAGSQMPLfALG-----VSQALVSYYSG-WDETQKEIKKIAILFCCASVITLIvytieHICF-GTMGERLTL 783
Cdd:cd18574 2 VLSALAAALVNIQIPL-LLGdlvnvISRSLKETNGDfIEDLKKPALKLLGLYLLQSLLTFA-----YISLlSVVGERVAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 784 RVRENMFRAILKNEIGWFDEvdNTSSMLASRLESDATLLKTIVVDRSTILLQNLGLVVTSFIIAFILNWRLTLVVLATYP 863
Cdd:cd18574 76 RLRNDLFSSLLRQDIAFFDT--HRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIVP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 864 LVIsghisekLFMQGYGGDLNK-------AYLKANMLAGESVSNIRTVAAFCAEEKILELYSRELLEPSKSSFRRGQIAG 936
Cdd:cd18574 154 VVV-------LVGTLYGSFLRKlsrraqaQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEKLGLGIG 226
|
250 260
....*....|....*....|....*...
gi 79487035 937 LFYGVSQFFIFSSYGLALWYGSTLMDKG 964
Cdd:cd18574 227 IFQGLSNLALNGIVLGVLYYGGSLVSRG 254
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
402-628 |
6.12e-23 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 99.91 E-value: 6.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 402 QFKDATfSYPSRPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWL------ 475
Cdd:COG4167 13 TFKYRT-GLFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRckhirm 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 476 -----------RGQIGLVNQEPALFATtirenilygkdDATAEEitRAAKLSEAISFINNLPE--GFETQVgergiqLSG 542
Cdd:COG4167 92 ifqdpntslnpRLNIGQILEEPLRLNT-----------DLTAEE--REERIFATLRLVGLLPEhaNFYPHM------LSS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 543 GQKQRIAISRAIVKNPSILLLDEATSALDAeSEKS--------VQEALdrvmvGRTTVVVAHRLSTVRN-ADIIAVVHEG 613
Cdd:COG4167 153 GQKQRVALARALILQPKIIIADEALAALDM-SVRSqiinlmleLQEKL-----GISYIYVSQHLGIVKHiSDKVLVMHQG 226
|
250
....*....|....*
gi 79487035 614 KIVEFGNHENLISNP 628
Cdd:COG4167 227 EVVEYGKTAEVFANP 241
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
418-628 |
6.29e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 102.08 E-value: 6.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 418 IFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKwlRGQIGLVNQEPALFA-TTIREN 496
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFRhMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 497 ILYG------KDDATAEEI-TRAAKLSEAISfINNLPEGFETQvgergiqLSGGQKQRIAISRAIVKNPSILLLDEATSA 569
Cdd:PRK10851 95 IAFGltvlprRERPNAAAIkAKVTQLLEMVQ-LAHLADRYPAQ-------LSGGQKQRVALARALAVEPQILLLDEPFGA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79487035 570 LDAESEKSVQEALDRVM--VGRTTVVVAH-RLSTVRNADIIAVVHEGKIVEFGNHENLISNP 628
Cdd:PRK10851 167 LDAQVRKELRRWLRQLHeeLKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1030-1253 |
6.52e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 100.17 E-value: 6.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIG 1109
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1110 LVQQEP--ALFATTIYENILYG--NEGASQSEV---VESAMLA-NAHSFITSLPegystkvgergVQMSGGQRQRIAIAR 1181
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGmeNQGIPREEMikrVDEALLAvNMLDFKTREP-----------ARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79487035 1182 AILKNPAILLLDEATSALD----VESERVVQQALDRLmaNRTTVVVAHRLSTIKNADTISVLHGGKIVEQGSHRKL 1253
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDptgrQEIMRVIHEIKEKY--QLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1030-1256 |
7.70e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 99.73 E-value: 7.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRPdvvIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDpTAGKVMIEGK------DI--KKLDL 1101
Cdd:PRK14258 8 IKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRveffnqNIyeRRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1102 KALRKHIGLVQQEPALFATTIYENILYG------NEGASQSEVVESAMLAnahsfiTSLPEGYSTKVGERGVQMSGGQRQ 1175
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIVESALKD------ADLWDEIKHKIHKSALDLSGGQQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1176 RIAIARAILKNPAILLLDEATSALD----VESERVVQQAldRLMANRTTVVVAHRLSTIKN-ADTISVLHG-----GKIV 1245
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSL--RLRSELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQLV 235
|
250
....*....|.
gi 79487035 1246 EQGSHRKLVLN 1256
Cdd:PRK14258 236 EFGLTKKIFNS 246
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1041-1241 |
8.13e-23 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 97.94 E-value: 8.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1041 SRPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDP---TAGKVMIEGKDIkkLDLKALRKHIGLVQQEPAL 1117
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRL--TALPAEQRRIGILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1118 FA-TTIYENILYG-----NEGASQSEVveSAMLANAhsfitSLpegysTKVGERGV-QMSGGQRQRIAIARAILKNPAIL 1190
Cdd:COG4136 88 FPhLSVGENLAFAlpptiGRAQRRARV--EQALEEA-----GL-----AGFADRDPaTLSGGQRARVALLRALLAEPRAL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 79487035 1191 LLDEATSALDVE-SERVVQQALDRL-MANRTTVVVAHRLSTIKNADTISVLHG 1241
Cdd:COG4136 156 LLDEPFSKLDAAlRAQFREFVFEQIrQRGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
420-617 |
8.17e-23 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 97.67 E-value: 8.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 420 DRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWlrGQIGLVNQEPALFAT-TIRENI- 497
Cdd:cd03268 17 DDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIGALIEAPGFYPNlTARENLr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 498 ----LYGKDDATAEEITRAAKLSEAisfinnlpegfetqvGERGI-QLSGGQKQRIAISRAIVKNPSILLLDEATSALDA 572
Cdd:cd03268 95 llarLLGIRKKRIDEVLDVVGLKDS---------------AKKKVkGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 79487035 573 ESEKSVQEALDRVM-VGRTTVVVAHRLSTVRN-ADIIAVVHEGKIVE 617
Cdd:cd03268 160 DGIKELRELILSLRdQGITVLISSHLLSEIQKvADRIGIINKGKLIE 206
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
147-371 |
9.60e-23 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 99.87 E-value: 9.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 147 TGERQAAKMRRAYLRSMLSQDISLFDtEASTGEVISAITSDILVVQDALSEKVGNFLHYISRFIAGFAIGFTSVWQISLV 226
Cdd:cd18576 63 VGERVVADLRKDLYRHLQRLPLSFFH-ERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 227 TLSIVPLIALaggiyafVAIGLIARVRK-------SYIKAGEIAEEVIGNVRTVQAFTGEERAVRLYREALENTYKYGRK 299
Cdd:cd18576 142 MLATVPVVVL-------VAVLFGRRIRKlskkvqdELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALK 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79487035 300 AGLTKGLGLGSMHCVLFLSWALLVWFTSVVVHKDIADGGKSFTTMLNVVIAGLSLGQAAPDISAFVRAKAAA 371
Cdd:cd18576 215 RARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGAS 286
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1029-1250 |
9.83e-23 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 98.55 E-value: 9.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1029 TIELKGVHFSYPSRPdvvIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEG------KDIKKLDLK 1102
Cdd:COG4161 2 SIQLKNINCFYGSHQ---ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1103 ALRKHIGLVQQE----PALfatTIYENILygnE------GASQSEVVESAMlanahSFITSLpeGYSTKVGERGVQMSGG 1172
Cdd:COG4161 79 LLRQKVGMVFQQynlwPHL---TVMENLI---EapckvlGLSKEQAREKAM-----KLLARL--RLTDKADRFPLHLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1173 QRQRIAIARAILKNPAILLLDEATSALDVE-SERVVQQALDRLMANRTTVVVAHRLSTI-KNADTISVLHGGKIVEQGSH 1250
Cdd:COG4161 146 QQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFArKVASQVVYMEKGRIIEQGDA 225
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
415-612 |
9.85e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 98.25 E-value: 9.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 415 DVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIGLVNQEPALFATTIR 494
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 495 ENIL--YGKDDATAEEITRAAKLSEaisFinNLPEgfetQVGERGI-QLSGGQKQRIAISRAIVKNPSILLLDEATSALD 571
Cdd:PRK10247 99 DNLIfpWQIRNQQPDPAIFLDDLER---F--ALPD----TILTKNIaELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 79487035 572 AESEKSVQEaldrvmvgrttvvVAHRLSTVRNADIIAVVHE 612
Cdd:PRK10247 170 ESNKHNVNE-------------IIHRYVREQNIAVLWVTHD 197
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
893-1263 |
1.07e-22 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 105.83 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 893 LAGESVSNIRTVAAFcAEEKILELYSRELLEPSKSSFRRGQIAGLFYGvsqfFIFSSYGLALwygsTLMDKG----LAGF 968
Cdd:PLN03232 481 IINEILASMDTVKCY-AWEKSFESRIQGIRNEELSWFRKAQLLSAFNS----FILNSIPVVV----TLVSFGvfvlLGGD 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 969 KSVMKTFMVLIVTALaMGETLALAPDLL----KGNQMVASVFEILDRKTQIVGEtSEELNNVEGTIELKGVHFSYPSRPD 1044
Cdd:PLN03232 552 LTPARAFTSLSLFAV-LRSPLNMLPNLLsqvvNANVSLQRIEELLLSEERILAQ-NPPLQPGAPAISIKNGYFSWDSKTS 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1045 VVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIegkdikkldlkaLRKHIGLVQQEPALFATTIYE 1124
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV------------IRGSVAYVPQVSWIFNATVRE 697
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1125 NILYGNEgaSQSEVVESAMLANAHSFITSLPEGYS-TKVGERGVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVEs 1203
Cdd:PLN03232 698 NILFGSD--FESERYWRAIDVTALQHDLDLLPGRDlTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAH- 774
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79487035 1204 erVVQQALDRLMAN----RTTVVVAHRLSTIKNADTISVLHGGKIVEQGSHRKlvLNKSGPYFK 1263
Cdd:PLN03232 775 --VAHQVFDSCMKDelkgKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAE--LSKSGSLFK 834
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
409-605 |
1.19e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 96.92 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 409 SYPSRPdvvIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNniseldikwlrGQIGLVNQ---E 485
Cdd:NF040873 1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG-----------ARVAYVPQrseV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 486 PALFATTIRENILYGK-------------DDATAEEITRAAKLseaisfinnlpEGFET-QVGErgiqLSGGQKQRIAIS 551
Cdd:NF040873 67 PDSLPLTVRDLVAMGRwarrglwrrltrdDRAAVDDALERVGL-----------ADLAGrQLGE----LSGGQRQRALLA 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 79487035 552 RAIVKNPSILLLDEATSALDAESEKSVQEALDR-VMVGRTTVVVAHRLSTVRNAD 605
Cdd:NF040873 132 QGLAQEADLLLLDEPTTGLDAESRERIIALLAEeHARGATVVVVTHDLELVRRAD 186
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1029-1249 |
1.69e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 98.31 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1029 TIELKGVHFSYPSRPdvvIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHI 1108
Cdd:PRK13548 2 MLEARNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1109 GLVQQEPAL-FATTIYENILYG-----NEGASQSEVVESAM-----LANAHSFITSLpegystkvgergvqmSGGQRQRI 1177
Cdd:PRK13548 79 AVLPQHSSLsFPFTVEEVVAMGraphgLSRAEDDALVAAALaqvdlAHLAGRDYPQL---------------SGGEQQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1178 AIARAIL------KNPAILLLDEATSALDVEServvQQALDRLMANRTT------VVVAHRLstikN-----ADTISVLH 1240
Cdd:PRK13548 144 QLARVLAqlwepdGPPRWLLLDEPTSALDLAH----QHHVLRLARQLAHerglavIVVLHDL----NlaaryADRIVLLH 215
|
....*....
gi 79487035 1241 GGKIVEQGS 1249
Cdd:PRK13548 216 QGRLVADGT 224
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
420-596 |
1.75e-22 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 97.54 E-value: 1.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 420 DRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLrgqigLVNQEPALFA-TTIRENIL 498
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 499 YGKDDA--TAEEITRAAKLSEAISFINnLPEGFETQVGergiQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEK 576
Cdd:TIGR01184 77 LAVDRVlpDLSKSERRAIVEEHIALVG-LTEAADKRPG----QLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180
....*....|....*....|..
gi 79487035 577 SVQEALDRVM--VGRTTVVVAH 596
Cdd:TIGR01184 152 NLQEELMQIWeeHRVTVLMVTH 173
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1049-1261 |
1.85e-22 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 103.23 E-value: 1.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1049 RDFDLIVRAGKSMALVGQSGSGKSsVISL-ILRFYDPTA----GKVMIEGKDIKKLDLKALRK----HIGLVQQEP---- 1115
Cdd:COG4172 27 KGVSFDIAAGETLALVGESGSGKS-VTALsILRLLPDPAahpsGSILFDGQDLLGLSERELRRirgnRIAMIFQEPmtsl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1116 -ALFatTIYENI-----LYG--NEGASQSEVVEsaMLA-----NAHSFITSLPEgystkvgergvQMSGGQRQRIAIARA 1182
Cdd:COG4172 106 nPLH--TIGKQIaevlrLHRglSGAAARARALE--LLErvgipDPERRLDAYPH-----------QLSGGQRQRVMIAMA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1183 ILKNPAILLLDEATSALDVeserVVQ-QALDRL--------MAnrtTVVVAHRLSTIKN-ADTISVLHGGKIVEQGSHRK 1252
Cdd:COG4172 171 LANEPDLLIADEPTTALDV----TVQaQILDLLkdlqrelgMA---LLLITHDLGVVRRfADRVAVMRQGEIVEQGPTAE 243
|
....*....
gi 79487035 1253 LVLNKSGPY 1261
Cdd:COG4172 244 LFAAPQHPY 252
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1050-1249 |
2.04e-22 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 100.57 E-value: 2.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1050 DFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDI----KKLDLKALRKHIGLVQQEPALFA-TTIYE 1124
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrKGIFLPPEKRRIGYVFQEARLFPhLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1125 NILYG-------NEGASQSEVVEsaMLANAHSFitslpegystkvgERGV-QMSGGQRQRIAIARAILKNPAILLLDEAT 1196
Cdd:TIGR02142 95 NLRYGmkrarpsERRISFERVIE--LLGIGHLL-------------GRLPgRLSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 79487035 1197 SALDVESERVVQQALDRLMA--NRTTVVVAHRLSTIKN-ADTISVLHGGKIVEQGS 1249
Cdd:TIGR02142 160 AALDDPRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGP 215
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
401-656 |
2.21e-22 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 103.65 E-value: 2.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPS-RPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWL---- 475
Cdd:PRK10535 5 LELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 476 RGQIGLVNQEPALFA-TTIRENIlygKDDATAEEITRAAKLSEAISFINNLpeGFETQVGERGIQLSGGQKQRIAISRAI 554
Cdd:PRK10535 85 REHFGFIFQRYHLLShLTAAQNV---EVPAVYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 555 VKNPSILLLDEATSALDAESEKSVQEALDRVM-VGRTTVVVAHRLSTVRNADIIAVVHEGKIVefgnhenliSNPDGAYS 633
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAAQAERVIEIRDGEIV---------RNPPAQEK 230
|
250 260
....*....|....*....|...
gi 79487035 634 SLLRLQETASLQRNPSLNRTLSR 656
Cdd:PRK10535 231 VNVAGGTEPVVNTASGWRQFVSG 253
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
420-636 |
2.35e-22 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 102.84 E-value: 2.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 420 DRLNLAIPAGKIVALVGGSGSGKS----TVISLIERFYEPISGAVLLDGNNISELDIKWLRG----QIGLVNQEP--ALf 489
Cdd:COG4172 27 KGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEPmtSL- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 490 attireNILYgkddaTAEE-----------ITRAAKLSEAISFINnlpegfetQVG----ERGI-----QLSGGQKQRIA 549
Cdd:COG4172 106 ------NPLH-----TIGKqiaevlrlhrgLSGAAARARALELLE--------RVGipdpERRLdayphQLSGGQRQRVM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 550 ISRAIVKNPSILLLDEATSALDAesekSVQ-EALD--RVMVGRTTVVVA---HRLSTVRN-ADIIAVVHEGKIVEFGNHE 622
Cdd:COG4172 167 IAMALANEPDLLIADEPTTALDV----TVQaQILDllKDLQRELGMALLlitHDLGVVRRfADRVAVMRQGEIVEQGPTA 242
|
250
....*....|....
gi 79487035 623 NLISNPDGAYSSLL 636
Cdd:COG4172 243 ELFAAPQHPYTRKL 256
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
402-612 |
2.50e-22 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 97.94 E-value: 2.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 402 QFKDATFSYPSRpdvVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIG- 480
Cdd:PRK10575 13 ALRNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 LVNQEPALFATTIRENIL------------YGKDDataeeitrAAKLSEAISFINNLPegfetqVGERGI-QLSGGQKQR 547
Cdd:PRK10575 90 LPQQLPAAEGMTVRELVAigrypwhgalgrFGAAD--------REKVEEAISLVGLKP------LAHRLVdSLSGGERQR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79487035 548 IAISRAIVKNPSILLLDEATSALDAESEKSVqealdrvmvgrttVVVAHRLSTVRNADIIAVVHE 612
Cdd:PRK10575 156 AWIAMLVAQDSRCLLLDEPTSALDIAHQVDV-------------LALVHRLSQERGLTVIAVLHD 207
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
422-629 |
2.86e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 97.61 E-value: 2.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 422 LNLAIPAGKIVALVGGSGSGKSTVISLIERFYE-----PISGAVLLDGNNI--SELDIKWLRGQIGLVNQEPALFA-TTI 493
Cdd:PRK14267 23 VDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIysPDVDPIEVRREVGMVFQYPNPFPhLTI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 494 RENILYGK------------DDATAEEITRAAKLSEAISFINNLPEgfetqvgergiQLSGGQKQRIAISRAIVKNPSIL 561
Cdd:PRK14267 103 YDNVAIGVklnglvkskkelDERVEWALKKAALWDEVKDRLNDYPS-----------NLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 562 LLDEATSALDAESEKSVQEALDRVMVGRTTVVVAHR-LSTVRNADIIAVVHEGKIVEFGNHENLISNPD 629
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVFENPE 240
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
401-616 |
2.97e-22 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 94.80 E-value: 2.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSrpdVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGnniseldikwlrgqig 480
Cdd:cd03216 1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 lvnqEPALFATTirenilygkddataeeitraaklSEAIsfinnlpegfetqvgERGI----QLSGGQKQRIAISRAIVK 556
Cdd:cd03216 62 ----KEVSFASP-----------------------RDAR---------------RAGIamvyQLSVGERQMVEIARALAR 99
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79487035 557 NPSILLLDEATSALDAESEKSVQEALDRVMV-GRTTVVVAHRLSTVRN-ADIIAVVHEGKIV 616
Cdd:cd03216 100 NARLLILDEPTAALTPAEVERLFKVIRRLRAqGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
1051-1255 |
3.22e-22 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 97.22 E-value: 3.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1051 FDLIVRAGKSMALVGQSGSGKSSVISLILRFYdPTAGKVMIEGKDIKKLDLKALRKHIG-LVQQEPALFATTIYENI-LY 1128
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAyLSQQQSPPFAMPVFQYLaLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1129 GNEGASqSEVVESAMLANAHSFitslpeGYSTKVGERGVQMSGGQRQRIAIARAILK-----NP--AILLLDEATSALDv 1201
Cdd:COG4138 94 QPAGAS-SEAVEQLLAQLAEAL------GLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptiNPegQLLLLDEPMNSLD- 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79487035 1202 eserVVQQ-ALDRLM-----ANRTTVVVAHRLS-TIKNADTISVLHGGKIVEQGShRKLVL 1255
Cdd:COG4138 166 ----VAQQaALDRLLrelcqQGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGE-TAEVM 221
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
418-626 |
3.66e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 97.39 E-value: 3.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 418 IFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIGLVNQE-PALFATTIREN 496
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHhLTPEGITVREL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 497 ILYGKD----------DATAEEITRAAKLSEAISFINNLPEgfetqvgergiQLSGGQKQRIAISRAIVKNPSILLLDEA 566
Cdd:PRK11231 97 VAYGRSpwlslwgrlsAEDNARVNQAMEQTRINHLADRRLT-----------DLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79487035 567 TSALDAesekSVQEALDRVM-----VGRTTVVVAHRLSTV-RNADIIAVVHEGKIVEFGNHENLIS 626
Cdd:PRK11231 166 TTYLDI----NHQVELMRLMrelntQGKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
421-626 |
3.71e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 96.57 E-value: 3.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 421 RLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKwlRGQIGLVNQEPALFA-TTIRENI-- 497
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFShLTVAQNIgl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 498 -------LYGKDDATAEEITRAAKLSEaisFINNLPEgfetqvgergiQLSGGQKQRIAISRAIVKNPSILLLDEATSAL 570
Cdd:PRK10771 95 glnpglkLNAAQREKLHAIARQMGIED---LLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 571 DAESEKSVQEALDRVMVGR--TTVVVAHRLS-TVRNADIIAVVHEGKIVEFGNHENLIS 626
Cdd:PRK10771 161 DPALRQEMLTLVSQVCQERqlTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1047-1269 |
4.17e-22 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 97.35 E-value: 4.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1047 IFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIK-------------KLDLKALRKHIGLVQQ 1113
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1114 EPALFA-TTIYENILYGNE---GASQSEVVESAMLanahsfitslpegYSTKVG--ERG-----VQMSGGQRQRIAIARA 1182
Cdd:PRK10619 100 HFNLWShMTVLENVMEAPIqvlGLSKQEARERAVK-------------YLAKVGidERAqgkypVHLSGGQQQRVSIARA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1183 ILKNPAILLLDEATSALDV----ESERVVQQALDRlmaNRTTVVVAHRLSTIKNADT-ISVLHGGKIVEQGSHRKLVLNK 1257
Cdd:PRK10619 167 LAMEPEVLLFDEPTSALDPelvgEVLRIMQQLAEE---GKTMVVVTHEMGFARHVSShVIFLHQGKIEEEGAPEQLFGNP 243
|
250
....*....|..
gi 79487035 1258 SGPyfkliSLQQ 1269
Cdd:PRK10619 244 QSP-----RLQQ 250
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
773-964 |
4.20e-22 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 98.18 E-value: 4.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 773 CFGTMGERLTLRVRENMFRAILKNEIGWFDEvdNTSSMLASRLESDATLLKTIVVDRSTILLQNLGLVVTSFIIAFILNW 852
Cdd:cd18590 59 LFMCTLSRLNLRLRHQLFSSLVQQDIGFFEK--TKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSW 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 853 RLTLVVLATYPLVIsghISEKLF---MQGYGGDLNKAYLKANMLAGESVSNIRTVAAFCAEEKILELYSRELLEPSKSSF 929
Cdd:cd18590 137 QLTLLTLIEMPLTA---IAQKVYntyHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKD 213
|
170 180 190
....*....|....*....|....*....|....*
gi 79487035 930 RRGQIAGLFYGVSQFFIFSSYGLALWYGSTLMDKG 964
Cdd:cd18590 214 RRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSG 248
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1051-1254 |
4.45e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 96.57 E-value: 4.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1051 FDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLdlKALRKHIGLVQQEPALFA-TTIYENILYG 1129
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTT--PPSRRPVSMLFQENNLFShLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1130 -NEG----ASQSEVVES-AMLANAHSFITSLPEgystkvgergvQMSGGQRQRIAIARAILKNPAILLLDEATSALDVES 1203
Cdd:PRK10771 96 lNPGlklnAAQREKLHAiARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSALDPAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 79487035 1204 ERVVQQALDRLMANR--TTVVVAHRLS-TIKNADTISVLHGGKIVEQGSHRKLV 1254
Cdd:PRK10771 165 RQEMLTLVSQVCQERqlTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
412-628 |
6.15e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 99.92 E-value: 6.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 412 SRPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIGLVNQEPAL-FA 490
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 491 TTIRENILYGKDD-----ATAEEITRAAkLSEAISfinnlpEGFETQVGERGI-QLSGGQKQRIAISRAIVKNPSILLLD 564
Cdd:PRK09536 92 FDVRQVVEMGRTPhrsrfDTWTETDRAA-VERAME------RTGVAQFADRPVtSLSGGERQRVLLARALAQATPVLLLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79487035 565 EATSALDAESE-KSVQEALDRVMVGRTTVVVAHRLS-TVRNADIIAVVHEGKIVEFGNHENLISNP 628
Cdd:PRK09536 165 EPTASLDINHQvRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1042-1246 |
6.71e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 97.06 E-value: 6.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1042 RPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLD---LKALRKHIGLVQQEpALF 1118
Cdd:PRK10419 22 HQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQD-SIS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1119 AT----TIYENI------LYGNEGASQSEVVESAMLAnahsfiTSLPEGYSTKvgeRGVQMSGGQRQRIAIARAILKNPA 1188
Cdd:PRK10419 101 AVnprkTVREIIreplrhLLSLDKAERLARASEMLRA------VDLDDSVLDK---RPPQLSGGQLQRVCLARALAVEPK 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79487035 1189 ILLLDEATSALDVESERVVQQALDRLMANRTT--VVVAHRLSTIKN-ADTISVLHGGKIVE 1246
Cdd:PRK10419 172 LLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1030-1245 |
9.01e-22 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 101.72 E-value: 9.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPS-RPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISlILRFYD-PTAGKVMIEGKDIKKLDLKAL--- 1104
Cdd:PRK10535 5 LELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLDkPTSGTYRVAGQDVATLDADALaql 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1105 -RKHIGLVQQEPALFA-TTIYENI----LYGNEGASQSevvesamLANAHSFITSLpeGYSTKVGERGVQMSGGQRQRIA 1178
Cdd:PRK10535 84 rREHFGFIFQRYHLLShLTAAQNVevpaVYAGLERKQR-------LLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 1179 IARAILKNPAILLLDEATSALDVESERVVQQALDRLMAN-RTTVVVAHRLSTIKNADTISVLHGGKIV 1245
Cdd:PRK10535 155 IARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRgHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1027-1249 |
1.41e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 96.01 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1027 EGTIELKGVHFSYPSRpdvVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKAL-R 1105
Cdd:PRK10575 9 DTTFALRNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFaR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1106 KHIGLVQQEPALFATTIYENILYGNE---------GASQSEVVESA-----MLANAHSFITSLpegystkvgergvqmSG 1171
Cdd:PRK10575 86 KVAYLPQQLPAAEGMTVRELVAIGRYpwhgalgrfGAADREKVEEAislvgLKPLAHRLVDSL---------------SG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1172 GQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANR--TTVVVAHRLS-TIKNADTISVLHGGKIVEQG 1248
Cdd:PRK10575 151 GERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINmAARYCDYLVALRGGEMIAQG 230
|
.
gi 79487035 1249 S 1249
Cdd:PRK10575 231 T 231
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1028-1249 |
2.03e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 96.23 E-value: 2.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1028 GTIELKGVHFSYPSRP--DVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEG----KDIKKL-D 1100
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIkE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1101 LKALRKHIGLVQQEP--ALFATTIYENILYG--NEGASQSEVVESA--MLAnahsfITSLPEGYSTKvgeRGVQMSGGQR 1174
Cdd:PRK13645 85 VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGpvNLGENKQEAYKKVpeLLK-----LVQLPEDYVKR---SPFELSGGQK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 1175 QRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMAN--RTTVVVAHRLSTI-KNADTISVLHGGKIVEQGS 1249
Cdd:PRK13645 157 RRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGS 234
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1030-1249 |
2.13e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 95.15 E-value: 2.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPsrpDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIG 1109
Cdd:COG4604 2 IEIKNVSKRYG---GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1110 LVQQEPAlFAT--TIYENILYG----NEG---ASQSEVVESAM----LAN-AHSFITSLpegystkvgergvqmSGGQRQ 1175
Cdd:COG4604 79 ILRQENH-INSrlTVRELVAFGrfpySKGrltAEDREIIDEAIayldLEDlADRYLDEL---------------SGGQRQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1176 RIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLM--ANRTTVVVAHRLstikN-----ADTISVLHGGKIVEQG 1248
Cdd:COG4604 143 RAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLAdeLGKTVVIVLHDI----NfascyADHIVAMKDGRVVAQG 218
|
.
gi 79487035 1249 S 1249
Cdd:COG4604 219 T 219
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1047-1256 |
2.29e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 94.91 E-value: 2.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1047 IFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYD--PTA---GKVMIEGKDIKKLDLKAL--RKHIGLVQQEPALFA 1119
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElnEEArveGEVRLFGRNIYSPDVDPIevRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1120 -TTIYENILYG----NEGASQSEVVESAMLANAHSfitSLPEGYSTKVGERGVQMSGGQRQRIAIARAILKNPAILLLDE 1194
Cdd:PRK14267 99 hLTIYDNVAIGvklnGLVKSKKELDERVEWALKKA---ALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79487035 1195 ATSALDVESERVVQQALDRLMANRTTVVVAHR-LSTIKNADTISVLHGGKIVEQGSHRKLVLN 1256
Cdd:PRK14267 176 PTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVFEN 238
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1030-1253 |
3.23e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 95.25 E-value: 3.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRPDVVIfRDFDLIVRAGKSMALVGQSGSGKSSVISLI---LRFYDPTAGKVMIEGKDIKKLDLKALRK 1106
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPAL-NDISFSIPRGSWTALIGHNGSGKSTISKLInglLLPDDNPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1107 HIGLVQQEP--ALFATTIYENILYG--NEGASQSEVV--------ESAMLanahSFITSLPEgystkvgergvQMSGGQR 1174
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGleNRAVPRPEMIkivrdvlaDVGML----DYIDSEPA-----------NLSGGQK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1175 QRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMA--NRTTVVVAHRLSTIKNADTISVLHGGKIVEQGSHRK 1252
Cdd:PRK13640 150 QRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVE 229
|
.
gi 79487035 1253 L 1253
Cdd:PRK13640 230 I 230
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1050-1249 |
3.54e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 97.21 E-value: 3.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1050 DFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKklDLKALRKHIGLVQQEPALFA-TTIYENILY 1128
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQRPINMMFQSYALFPhMTVEQNIAF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1129 G------NEGASQSEVVESAMLANAHSFITSLPEgystkvgergvQMSGGQRQRIAIARAILKNPAILLLDEATSALDVE 1202
Cdd:PRK11607 115 GlkqdklPKAEIASRVNEMLGLVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 79487035 1203 -SERVVQQALDRL-MANRTTVVVAH-RLSTIKNADTISVLHGGKIVEQGS 1249
Cdd:PRK11607 184 lRDRMQLEVVDILeRVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGE 233
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
748-964 |
3.87e-21 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 95.24 E-value: 3.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 748 EIKKIAILFCCASVITLIVYTIEHICFGTMGERLTLRVRENMFRAILKNEIGWFDEvdNTSSMLASRLESDATLLKTIVV 827
Cdd:cd18576 34 SLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHE--RRVGELTSRLSNDVTQIQDTLT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 828 DRSTILLQNLGLVVTSFIIAFILNWRLTLVVLATYPLVIsghISEKLF---MQGYGGDLNKAYLKANMLAGESVSNIRTV 904
Cdd:cd18576 112 TTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVV---LVAVLFgrrIRKLSKKVQDELAEANTIVEETLQGIRVV 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 905 AAFCAEEKILELYSRELLEPSKSSFRRGQIAGLFYGVSQFFIFSSYGLALWYGSTLMDKG 964
Cdd:cd18576 189 KAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAG 248
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
401-638 |
4.23e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 94.91 E-value: 4.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPDVVifDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNI--SELDIKWLRGQ 478
Cdd:PRK13636 6 LKVEELNYNYSDGTHAL--KGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 479 IGLVNQEP--ALFATTIRENILYG------KDDATAEEITRAAKLSeAISFINNLPEGFetqvgergiqLSGGQKQRIAI 550
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGavnlklPEDEVRKRVDNALKRT-GIEHLKDKPTHC----------LSFGQKKRVAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 551 SRAIVKNPSILLLDEATSALDAESEKSVQEALDRVM--VGRTTVVVAHRLSTVR-NADIIAVVHEGKIVEFGNHENLISN 627
Cdd:PRK13636 153 AGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQkeLGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAE 232
|
250
....*....|.
gi 79487035 628 PDGAYSSLLRL 638
Cdd:PRK13636 233 KEMLRKVNLRL 243
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
407-619 |
4.36e-21 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 93.37 E-value: 4.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 407 TFSYPSRPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIkwlrgQIGLvnqEP 486
Cdd:cd03220 26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGL-----GGGF---NP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 487 ALfatTIRENI-----LYGKDDAtaeEItrAAKLSEAISFiNNLPEGFETQVGErgiqLSGGQKQRIAISRAIVKNPSIL 561
Cdd:cd03220 98 EL---TGRENIylngrLLGLSRK---EI--DEKIDEIIEF-SELGDFIDLPVKT----YSSGMKARLAFAIATALEPDIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 562 LLDEATSALDAE-SEKSVQEALDRVMVGRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFG 619
Cdd:cd03220 165 LIDEVLAVGDAAfQEKCQRRLRELLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
726-960 |
4.82e-21 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 95.07 E-value: 4.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 726 LFALGVSQALVSYYSGW-------DETQKEIKKIAILFCCASVITLIVYTIEHICFGTMGERLTLRVRENMFRAILKNEI 798
Cdd:cd18784 5 LLAAAVGEIFIPYYTGQvidgiviEKSQDKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 799 GWFDEVdNTSSMLaSRLESDATLLKTIVVDRSTILLQNLGLVVTSFIIAFILNWRLTLVVLATYPLVIS-----GHISEK 873
Cdd:cd18784 85 GFFDTV-KTGDIT-SRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIvskvyGDYYKK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 874 LfmqgyGGDLNKAYLKANMLAGESVSNIRTVAAFCAEEKILELYSRELLEPSKSSFRRGQIAGLFYGVSQFFIFSSYGLA 953
Cdd:cd18784 163 L-----SKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVST 237
|
....*..
gi 79487035 954 LWYGSTL 960
Cdd:cd18784 238 LYYGGHL 244
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1030-1249 |
4.84e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 94.67 E-value: 4.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRPDVVifRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLD-LKALRKHI 1108
Cdd:PRK13644 2 IRLENVSYSYPDGTPAL--ENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1109 GLVQQEP--ALFATTIYENILYGNEGASQSEVVESAMLANAhsfitsLPEGYSTKVGERGVQ-MSGGQRQRIAIARAILK 1185
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRA------LAEIGLEKYRHRSPKtLSGGQGQCVALAGILTM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79487035 1186 NPAILLLDEATSALDVESERVVQQALDRLM-ANRTTVVVAHRLSTIKNADTISVLHGGKIVEQGS 1249
Cdd:PRK13644 154 EPECLIFDEVTSMLDPDSGIAVLERIKKLHeKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1030-1245 |
5.53e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 98.18 E-value: 5.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSrpdVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKdikKLDLK----ALR 1105
Cdd:COG3845 6 LELRGITKRFGG---VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGK---PVRIRsprdAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1106 KHIGLVQQEPALFAT-TIYENILYGNEGASQseVVESamLANAHSFITSLPEGY------STKVGergvQMSGGQRQRIA 1178
Cdd:COG3845 80 LGIGMVHQHFMLVPNlTVAENIVLGLEPTKG--GRLD--RKAARARIRELSERYgldvdpDAKVE----DLSVGEQQRVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1179 IARAILKNPAILLLDEATSAL-DVESERVVqQALDRLMANRTTVV-VAHRLSTIK-NADTISVLHGGKIV 1245
Cdd:COG3845 152 ILKALYRGARILILDEPTAVLtPQEADELF-EILRRLAAEGKSIIfITHKLREVMaIADRVTVLRRGKVV 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
423-617 |
5.73e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 98.17 E-value: 5.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 423 NLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIK--WLRGqIGLVNQEPALFAT-TIRENILY 499
Cdd:COG1129 24 SLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRdaQAAG-IAIIHQELNLVPNlSVAENIFL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 500 GKDDAT------AEEITRAAKLSEAIsfinNLPEGFETQVGErgiqLSGGQKQRIAISRAIVKNPSILLLDEATSALDaE 573
Cdd:COG1129 103 GREPRRgglidwRAMRRRARELLARL----GLDIDPDTPVGD----LSVAQQQLVEIARALSRDARVLILDEPTASLT-E 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 79487035 574 SEKsvqEALDRVMV-----GRTTVVVAHRLSTVRN-ADIIAVVHEGKIVE 617
Cdd:COG1129 174 REV---ERLFRIIRrlkaqGVAIIYISHRLDEVFEiADRVTVLRDGRLVG 220
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
409-629 |
6.92e-21 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 92.99 E-value: 6.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 409 SYPSRPdvvIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDI-KWLRGQIGLVNQEPA 487
Cdd:cd03218 9 RYGKRK---VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYLPQEAS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 488 LFAT-TIRENILygkddATAEEITRAAKlsEAISFINNLPEGF--ETQVGERGIQLSGGQKQRIAISRAIVKNPSILLLD 564
Cdd:cd03218 86 IFRKlTVEENIL-----AVLEIRGLSKK--EREEKLEELLEEFhiTHLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79487035 565 EATSALD----AESEKSVQEALDR---VMVG----RTTVVVAHRlstvrnadiIAVVHEGKIVEFGNHENLISNPD 629
Cdd:cd03218 159 EPFAGVDpiavQDIQKIIKILKDRgigVLITdhnvRETLSITDR---------AYIIYEGKVLAEGTPEEIAANEL 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
403-574 |
7.21e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.83 E-value: 7.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 403 FKDATFSYPSRPdvvIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNniseldikwLRgqIGLV 482
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG---------LR--IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 483 NQEPALFAT-TIRENI----------------LYGKDDATAEEITRAAKLSEAISFIN---------------NLPEG-F 529
Cdd:COG0488 67 PQEPPLDDDlTVLDTVldgdaelraleaeleeLEAKLAEPDEDLERLAELQEEFEALGgweaearaeeilsglGFPEEdL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 79487035 530 ETQVGErgiqLSGGQKQRIAISRAIVKNPSILLLDEATSALDAES 574
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
418-615 |
8.24e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 93.59 E-value: 8.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 418 IFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELdikwlRGQIGLVNQEPALFA-TTIREN 496
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-----REDTRLMFQDARLLPwKKVIDN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 497 I---LYGKDDATAEEITRAAKLSEaisfinnlpegfetQVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAE 573
Cdd:PRK11247 102 VglgLKGQWRDAALQALAAVGLAD--------------RANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 79487035 574 SEKSVQEALDRVMV--GRTTVVVAHRLS-TVRNADIIAVVHEGKI 615
Cdd:PRK11247 168 TRIEMQDLIESLWQqhGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1045-1249 |
1.07e-20 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 93.18 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1045 VVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLkALRKHIGLVQ--QEPALFAT-T 1121
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP-HRIARLGIARtfQNPRLFPElT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1122 IYENILYGNEGASQSEVV------------ESAMLANAHSFITSLpeGYSTKVGERGVQMSGGQRQRIAIARAILKNPAI 1189
Cdd:COG0411 96 VLENVLVAAHARLGRGLLaallrlprarreEREARERAEELLERV--GLADRADEPAGNLSYGQQRRLEIARALATEPKL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79487035 1190 LLLDEATSAL-DVESERVVqQALDRLMANR--TTVVVAHRLSTIKN-ADTISVLHGGKIVEQGS 1249
Cdd:COG0411 174 LLLDEPAAGLnPEETEELA-ELIRRLRDERgiTILLIEHDMDLVMGlADRIVVLDFGRVIAEGT 236
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
418-617 |
1.18e-20 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 93.33 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 418 IFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELD---IKWLRGQIGLVNQE-PALF---- 489
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkqRRAFRRDVQLVFQDsPSAVnprm 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 490 --ATTIRENILYGKDDATAEEITRAAKLSEAI----SFINNLPEgfetqvgergiQLSGGQKQRIAISRAIVKNPSILLL 563
Cdd:TIGR02769 106 tvRQIIGEPLRHLTSLDESEQKARIAELLDMVglrsEDADKLPR-----------QLSGGQLQRINIARALAVKPKLIVL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 79487035 564 DEATSALDAESEKSVQEALD--RVMVGRTTVVVAHRLSTV-RNADIIAVVHEGKIVE 617
Cdd:TIGR02769 175 DEAVSNLDMVLQAVILELLRklQQAFGTAYLFITHDLRLVqSFCQRVAVMDKGQIVE 231
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1044-1249 |
1.25e-20 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 92.05 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1044 DVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKlDLKALRKHIGLVQQEPAL-FATTI 1122
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVdDELTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1123 YENI-----LYGNEGASQSEVVESAMlanahSFItSLPEGYSTKVGergvQMSGGQRQRIAIARAILKNPAILLLDEATS 1197
Cdd:cd03265 91 WENLyiharLYGVPGAERRERIDELL-----DFV-GLLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 79487035 1198 ALDVESERVVQQALDRLMA--NRTTVVVAHRLSTI-KNADTISVLHGGKIVEQGS 1249
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEefGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGT 215
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1047-1228 |
1.36e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 92.19 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1047 IFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKA---LRKH-IGLVQQEPALFAT-T 1121
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQFHHLLPDfT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1122 IYENI----LYGNEGASQSEVVESAMLANAhsfitslpeGYSTKVGERGVQMSGGQRQRIAIARAILKNPAILLLDEATS 1197
Cdd:PRK11629 104 ALENVamplLIGKKKPAEINSRALEMLAAV---------GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTG 174
|
170 180 190
....*....|....*....|....*....|...
gi 79487035 1198 ALDVESERVVQQALDRLMANRTT--VVVAHRLS 1228
Cdd:PRK11629 175 NLDARNADSIFQLLGELNRLQGTafLVVTHDLQ 207
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
999-1246 |
1.52e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.06 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 999 NQMVASVFEILDRKTQIVGETSEELNNVegTIELKGVHFSYPSRPdvvIFRDFDLIVRAGKSMALVGQSGSGKSSVISLI 1078
Cdd:COG0488 287 EKLEREEPPRRDKTVEIRFPPPERLGKK--VLELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLL 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1079 LRFYDPTAGKVmIEGKDIKkldlkalrkhIGLVQQEPALFAT--TIYENILYGNEGASQSEVveSAMLAnahSFITSlPE 1156
Cdd:COG0488 362 AGELEPDSGTV-KLGETVK----------IGYFDQHQEELDPdkTVLDELRDGAPGGTEQEV--RGYLG---RFLFS-GD 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1157 GYSTKVGErgvqMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLmaNRTTVVVAH-R--LSTIknA 1233
Cdd:COG0488 425 DAFKPVGV----LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF--PGTVLLVSHdRyfLDRV--A 496
|
250
....*....|...
gi 79487035 1234 DTISVLHGGKIVE 1246
Cdd:COG0488 497 TRILEFEDGGVRE 509
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1029-1249 |
1.61e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 93.63 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1029 TIELKGVHFSYPsrpDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDlkalRKHI 1108
Cdd:COG4152 1 MLELKGLTKRFG---DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1109 GLVQQEPALFAT-TIYENILYGNE--GASQSEVVESAM-LANAHSfitsLPEGYSTKVGErgvqMSGGQRQRIAIARAIL 1184
Cdd:COG4152 74 GYLPEERGLYPKmKVGEQLVYLARlkGLSKAEAKRRADeWLERLG----LGDRANKKVEE----LSKGNQQKVQLIAALL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79487035 1185 KNPAILLLDEATSALDVESERVVQQALDRLMANRTTVVVA-HRLSTI-KNADTISVLHGGKIVEQGS 1249
Cdd:COG4152 146 HDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSsHQMELVeELCDRIVIINKGRKVLSGS 212
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
401-629 |
1.94e-20 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 92.52 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPdvvIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWL---RG 477
Cdd:PRK11831 8 VDMRGVSFTRGNRC---IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 478 QIGLVNQEPALFA-TTIRENILYGKDDATA--EEITRAA---KLsEAisfinnlpegfetqVGERGI------QLSGGQK 545
Cdd:PRK11831 85 RMSMLFQSGALFTdMNVFDNVAYPLREHTQlpAPLLHSTvmmKL-EA--------------VGLRGAaklmpsELSGGMA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 546 QRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRV--MVGRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFGNHE 622
Cdd:PRK11831 150 RRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELnsALGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQ 229
|
....*..
gi 79487035 623 NLISNPD 629
Cdd:PRK11831 230 ALQANPD 236
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
415-619 |
1.97e-20 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 91.19 E-value: 1.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 415 DVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDikwlRGQIGLVNQEPALF-ATTI 493
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLPEERGLYpKMKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 494 RENILYGKDdataeeiTRAAKLSEAISFINNLPEGFE-TQVGERGI-QLSGGQKQRIAISRAIVKNPSILLLDEATSALD 571
Cdd:cd03269 88 IDQLVYLAQ-------LKGLKKEEARRRIDEWLERLElSEYANKRVeELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 79487035 572 AESEKSVQEALDRVM-VGRTTVVVAHRLSTV-RNADIIAVVHEGKIVEFG 619
Cdd:cd03269 161 PVNVELLKDVIRELArAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
413-617 |
2.25e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 92.44 E-value: 2.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 413 RPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELD---IKWLRGQIGLVNQEpALF 489
Cdd:PRK10419 22 HQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQD-SIS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 490 AT----TIRENI------LYGKDDAtaEEITRAAKLSEAIsfinNLPEGFETQvgeRGIQLSGGQKQRIAISRAIVKNPS 559
Cdd:PRK10419 101 AVnprkTVREIIreplrhLLSLDKA--ERLARASEMLRAV----DLDDSVLDK---RPPQLSGGQLQRVCLARALAVEPK 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79487035 560 ILLLDEATSALDAESEKSVQEALDRVM--VGRTTVVVAHRLSTV-RNADIIAVVHEGKIVE 617
Cdd:PRK10419 172 LLILDEAVSNLDLVLQAGVIRLLKKLQqqFGTACLFITHDLRLVeRFCQRVMVMDNGQIVE 232
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1047-1247 |
2.38e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 94.38 E-value: 2.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1047 IFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLdlKALRKHIGLVQQEPALFA-TTIYEN 1125
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL--HARDRKVGFVFQHYALFRhMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1126 ILYG----------NEGASQSEVVES-AMLANAHsfitsLPEGYSTkvgergvQMSGGQRQRIAIARAILKNPAILLLDE 1194
Cdd:PRK10851 95 IAFGltvlprrerpNAAAIKAKVTQLlEMVQLAH-----LADRYPA-------QLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 79487035 1195 ATSALDVESERVVQQALDRLMANR--TTVVVAH-RLSTIKNADTISVLHGGKIvEQ 1247
Cdd:PRK10851 163 PFGALDAQVRKELRRWLRQLHEELkfTSVFVTHdQEEAMEVADRVVVMSQGNI-EQ 217
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
401-629 |
2.51e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 92.87 E-value: 2.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSY-PSRP--DVVIFDrLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAV----LLDGNNISELDIK 473
Cdd:PRK13643 2 IKFEKVNYTYqPNSPfaSRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 474 WLRGQIGLVNQEP--ALFATTIRENILYGKDD--ATAEEITRAAklSEAISFInnlpeGFETQVGERG-IQLSGGQKQRI 548
Cdd:PRK13643 81 PVRKKVGVVFQFPesQLFEETVLKDVAFGPQNfgIPKEKAEKIA--AEKLEMV-----GLADEFWEKSpFELSGGQMRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 549 AISRAIVKNPSILLLDEATSALDAESEKSVQEALDRV-MVGRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFGNHENLIS 626
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQ 233
|
...
gi 79487035 627 NPD 629
Cdd:PRK13643 234 EVD 236
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
425-599 |
2.97e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 91.03 E-value: 2.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 425 AIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKW---LRGQ-IGLVNQEPALFAT-TIRENI-- 497
Cdd:PRK11629 31 SIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQFHHLLPDfTALENVam 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 498 --LYGKDdATAEEITRAAKLSEAIsfinnlpeGFETQVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESE 575
Cdd:PRK11629 111 plLIGKK-KPAEINSRALEMLAAV--------GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA 181
|
170 180
....*....|....*....|....*.
gi 79487035 576 KSVQEALDRVMVGRTT--VVVAHRLS 599
Cdd:PRK11629 182 DSIFQLLGELNRLQGTafLVVTHDLQ 207
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1029-1248 |
3.37e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 94.52 E-value: 3.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1029 TIELKGVHFSypsRPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHI 1108
Cdd:PRK09536 3 MIDVSDLSVE---FGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1109 GLVQQEPAL-FATTIYENI---------LYGNEGASQSEVVESAM-LANAHSF----ITSLpegystkvgergvqmSGGQ 1173
Cdd:PRK09536 80 ASVPQDTSLsFEFDVRQVVemgrtphrsRFDTWTETDRAAVERAMeRTGVAQFadrpVTSL---------------SGGE 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79487035 1174 RQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVVVA-HRLS-TIKNADTISVLHGGKIVEQG 1248
Cdd:PRK09536 145 RQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAiHDLDlAARYCDELVLLADGRVRAAG 221
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
410-585 |
3.59e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 91.68 E-value: 3.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 410 YPSRPdvvIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDikwlrGQIGLVNQEPALF 489
Cdd:PRK11248 11 YGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-----AERGVVFQNEGLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 490 A-TTIRENILYGKDDATAEEITRAAKLSEAISFINnlPEGFEtqvgERGI-QLSGGQKQRIAISRAIVKNPSILLLDEAT 567
Cdd:PRK11248 83 PwRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVG--LEGAE----KRYIwQLSGGQRQRVGIARALAANPQLLLLDEPF 156
|
170
....*....|....*...
gi 79487035 568 SALDAESEKSVQEALDRV 585
Cdd:PRK11248 157 GALDAFTREQMQTLLLKL 174
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
401-619 |
6.41e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 90.99 E-value: 6.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPdvvIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIG 480
Cdd:PRK13548 3 LEARNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 LVNQEPAL-FATTIRENILYG---------KDDATAEEITRAAKLSEaisfinnlpegfetqVGERGI-QLSGGQKQRIA 549
Cdd:PRK13548 80 VLPQHSSLsFPFTVEEVVAMGraphglsraEDDALVAAALAQVDLAH---------------LAGRDYpQLSGGEQQRVQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 550 ISRAIV------KNPSILLLDEATSALD-AESEKSVQEALDRVMVGRTTV-VVAHRLS-TVRNADIIAVVHEGKIVEFG 619
Cdd:PRK13548 145 LARVLAqlwepdGPPRWLLLDEPTSALDlAHQHHVLRLARQLAHERGLAViVVLHDLNlAARYADRIVLLHQGRLVADG 223
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1044-1249 |
6.93e-20 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 89.12 E-value: 6.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1044 DVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRF--YDPTAGKVMIEGKDIKKL--DLKAlRKHIGLVQQEPalfa 1119
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLppEERA-RLGIFLAFQYP---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1120 ttiyenilygnegasqsevVESAMLANAHsFITSLPEGYStkvgergvqmsGGQRQRIAIARAILKNPAILLLDEATSAL 1199
Cdd:cd03217 87 -------------------PEIPGVKNAD-FLRYVNEGFS-----------GGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 79487035 1200 DVESERVVQQALDRLM-ANRTTVVVAH--RLSTIKNADTISVLHGGKIVEQGS 1249
Cdd:cd03217 136 DIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGD 188
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
398-597 |
7.77e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 95.26 E-value: 7.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 398 DGHIQFKDATFSYPSrpDVVIFDRLNLAIPAGKIVALVGGSGSGKSTvislierfyepisgavLLDGnnISELdikWL-- 475
Cdd:COG4178 360 DGALALEDLTLRTPD--GRPLLEDLSLSLKPGERLLITGPSGSGKST----------------LLRA--IAGL---WPyg 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 476 RGQIGLVNQEPALFAT--------TIRENILYGK-----DDATAEEITRAAKLSeaisfinNLPEGFETQVgERGIQLSG 542
Cdd:COG4178 417 SGRIARPAGARVLFLPqrpylplgTLREALLYPAtaeafSDAELREALEAVGLG-------HLAERLDEEA-DWDQVLSL 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 79487035 543 GQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRVMVGRTTVVVAHR 597
Cdd:COG4178 489 GEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
111-365 |
8.63e-20 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 91.39 E-value: 8.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 111 FPKQASHRVAKYSLDFVYLSVAILFSSWLEVACWMHTGERQAAKMRRAYLRSMLSQDISLFDTeASTGEVISAITSDILV 190
Cdd:cd18575 27 FAAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFFET-TRTGEVLSRLTTDTTL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 191 VQDALSEKVGNFLHYISRFIAGFAIGFTSVWQISLVTLSIVPLIalaggiyaFVAIGLIAR-VRK-------SYIKAGEI 262
Cdd:cd18575 106 IQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLV--------VLPIILFGRrVRRlsrasqdRLADLSAF 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 263 AEEVIGNVRTVQAFTGEERAVRLYREALENTYKYGRKAGLTKGLGLGSMHCVLFLSWALLVWFtsvvvhkdiadGGKSft 342
Cdd:cd18575 178 AEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWL-----------GAHD-- 244
|
250 260
....*....|....*....|....
gi 79487035 343 tmlnvVIAG-LSLGqaapDISAFV 365
Cdd:cd18575 245 -----VLAGrMSAG----ELSQFV 259
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
415-624 |
9.02e-20 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 89.35 E-value: 9.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 415 DVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISElDIKWLRGQIGLVNQEPAL-FATTI 493
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVdDELTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 494 RENI-----LYGKDDATAEEitraaKLSEAISFINnLPEGFETQVGergiQLSGGQKQRIAISRAIVKNPSILLLDEATS 568
Cdd:cd03265 91 WENLyiharLYGVPGAERRE-----RIDELLDFVG-LLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 569 ALDAESEKSVQEALdRVMV---GRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFGNHENL 624
Cdd:cd03265 161 GLDPQTRAHVWEYI-EKLKeefGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1045-1222 |
9.33e-20 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 89.42 E-value: 9.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1045 VVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMI----EGKDIKKLD---LKALRKH-IGLVQQ--- 1113
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVDLAQASpreILALRRRtIGYVSQflr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1114 ----EPALfaTTIYENILYGNEGASQSEVVESAMLA--NahsfitsLPEGY-----STkvgergvqMSGGQRQRIAIARA 1182
Cdd:COG4778 104 viprVSAL--DVVAEPLLERGVDREEARARARELLArlN-------LPERLwdlppAT--------FSGGEQQRVNIARG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 79487035 1183 ILKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVV 1222
Cdd:COG4778 167 FIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
403-620 |
1.06e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 89.76 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 403 FKDATFS--YPSRPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNniseldIKWLrgqIG 480
Cdd:COG1134 24 LKELLLRrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR------VSAL---LE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 L---VNQEpalfaTTIRENI-----LYGkddATAEEItrAAKLSEAISFiNNLPEGFETQVGergiQLSGGQKQRIAISR 552
Cdd:COG1134 95 LgagFHPE-----LTGRENIylngrLLG---LSRKEI--DEKFDEIVEF-AELGDFIDQPVK----TYSSGMRARLAFAV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 553 AIVKNPSILLLDEATSALDAE-SEKSVQEALDRVMVGRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFGN 620
Cdd:COG1134 160 ATAVDPDILLVDEVLAVGDAAfQKKCLARIRELRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1032-1248 |
1.07e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 92.40 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1032 LKGVHFSYPsrpDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKklDLKALRKHIGLV 1111
Cdd:PRK11000 6 LRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN--DVPPAERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1112 QQEPALFA-TTIYENILYGNE--GASQSEV---VESA--MLANAHsFITSLPEGystkvgergvqMSGGQRQRIAIARAI 1183
Cdd:PRK11000 81 FQSYALYPhLSVAENMSFGLKlaGAKKEEInqrVNQVaeVLQLAH-LLDRKPKA-----------LSGGQRQRVAIGRTL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79487035 1184 LKNPAILLLDEATSALD--------VESERVVQqaldRLmaNRTTVVVAH-RLSTIKNADTISVLHGGKIVEQG 1248
Cdd:PRK11000 149 VAEPSVFLLDEPLSNLDaalrvqmrIEISRLHK----RL--GRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1030-1245 |
1.27e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 90.15 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVH--FsYPSRPD-VVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLdlKALR- 1105
Cdd:COG1101 2 LELKNLSktF-NPGTVNeKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKL--PEYKr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1106 -KHIGLVQQEPAL---FATTIYENI-LYGNEGASQSEV--VESAMLANAHSFITSLPEGY----STKVGergvQMSGGQR 1174
Cdd:COG1101 79 aKYIGRVFQDPMMgtaPSMTIEENLaLAYRRGKRRGLRrgLTKKRRELFRELLATLGLGLenrlDTKVG----LLSGGQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79487035 1175 QRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMA--NRTTVVVAHRLS-TIKNADTISVLHGGKIV 1245
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEenNLTTLMVTHNMEqALDYGNRLIMMHEGRII 228
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
407-616 |
1.42e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 90.15 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 407 TFsYPSRPD-VVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDiKWLR-GQIGLVNQ 484
Cdd:COG1101 10 TF-NPGTVNeKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLP-EYKRaKYIGRVFQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 485 EPAL---FATTIRENIL------------YGKDDAtaeeitRAAKLSEAISFINNlpeGFE----TQVGergiQLSGGQK 545
Cdd:COG1101 88 DPMMgtaPSMTIEENLAlayrrgkrrglrRGLTKK------RRELFRELLATLGL---GLEnrldTKVG----LLSGGQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79487035 546 QRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRVmVGR---TTVVVAHRLS-TVRNADIIAVVHEGKIV 616
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKI-VEEnnlTTLMVTHNMEqALDYGNRLIMMHEGRII 228
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1030-1249 |
1.43e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 90.56 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSY-PSRP--DVVIFrDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKV----MIEGKDIKKLDLK 1102
Cdd:PRK13643 2 IKFEKVNYTYqPNSPfaSRALF-DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1103 ALRKHIGLVQQEP--ALFATTIYENILYG--NEGASQSEVVESAmlANAHSFItslpeGYSTKVGERG-VQMSGGQRQRI 1177
Cdd:PRK13643 81 PVRKKVGVVFQFPesQLFEETVLKDVAFGpqNFGIPKEKAEKIA--AEKLEMV-----GLADEFWEKSpFELSGGQMRRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79487035 1178 AIARAILKNPAILLLDEATSALDVESERVVQQALDRL-MANRTTVVVAHRLSTIKN-ADTISVLHGGKIVEQGS 1249
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT 227
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
129-299 |
1.43e-19 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 90.61 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 129 LSVAILFSSWLEVAC---WMHTGERQAAKMRRAYLRSMLSQDISLFDTeASTGEVISAITSDILVVQDALSEKVGNFLHY 205
Cdd:cd18589 42 MSLLTIASAVSEFVCdliYNITMSRIHSRLQGLVFAAVLRQEIAFFDS-NQTGDIVSRVTTDTEDMSESLSENLSLLMWY 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 206 ISRFIAGFAIGFTSVWQISLVTLSIVPLIALAGGIYAFVAIGLIARVRKSYIKAGEIAEEVIGNVRTVQAFTGEERAVRL 285
Cdd:cd18589 121 LARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQR 200
|
170
....*....|....
gi 79487035 286 YREALENTYKYGRK 299
Cdd:cd18589 201 YRQRLQKTYRLNKK 214
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1044-1257 |
1.46e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 91.45 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1044 DVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIE----GKDI-----------KKL-DLKALRKH 1107
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKnnhelitnpysKKIkNFKELRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1108 IGLVQQEP--ALFATTIYENILYG--NEGASQSEVVESA-----MLANAHSFITSLPEGystkvgergvqMSGGQRQRIA 1178
Cdd:PRK13631 118 VSMVFQFPeyQLFKDTIEKDIMFGpvALGVKKSEAKKLAkfylnKMGLDDSYLERSPFG-----------LSGGQKRRVA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1179 IARAILKNPAILLLDEATSALDVESER-VVQQALDRLMANRTTVVVAHRLSTI-KNADTISVLHGGKIVEQGSHRKLVLN 1256
Cdd:PRK13631 187 IAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEIFTD 266
|
.
gi 79487035 1257 K 1257
Cdd:PRK13631 267 Q 267
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1029-1200 |
1.46e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 89.92 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1029 TIELKGVHFSYP-SRPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDlkALRkh 1107
Cdd:COG4525 3 MLTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG--ADR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1108 iGLVQQEPALFA-TTIYENILYG----NEGASQSEVVESAMLAnahsfitslpegystKVGERGV------QMSGGQRQR 1176
Cdd:COG4525 79 -GVVFQKDALLPwLNVLDNVAFGlrlrGVPKAERRARAEELLA---------------LVGLADFarrriwQLSGGMRQR 142
|
170 180
....*....|....*....|....
gi 79487035 1177 IAIARAILKNPAILLLDEATSALD 1200
Cdd:COG4525 143 VGIARALAADPRFLLMDEPFGALD 166
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1030-1253 |
2.29e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 89.76 E-value: 2.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRPD---VVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKL-DLKALR 1105
Cdd:PRK13633 5 IKCKNVSYKYESNEEsteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1106 KHIGLVQQEP--ALFATTIYENILYG--NEGASQSEV---VESAMLA-NAHSFITSLPEgystkvgergvQMSGGQRQRI 1177
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGpeNLGIPPEEIrerVDESLKKvGMYEYRRHAPH-----------LLSGGQKQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 1178 AIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANR--TTVVVAHRLSTIKNADTISVLHGGKIVEQGSHRKL 1253
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1062-1253 |
2.93e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 89.38 E-value: 2.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1062 ALVGQSGSGKSSVISLILRFYDPTAG-----KVMIEGKDI-KKLDLKALRKHIGLVQQEPALFATTIYENILYGNEGASQ 1135
Cdd:PRK14271 51 SLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfNYRDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1136 SEVVESAMLANAHSFITSLPEGYSTKVGERGVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLM 1215
Cdd:PRK14271 131 VPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA 210
|
170 180 190
....*....|....*....|....*....|....*....
gi 79487035 1216 ANRTTVVVAHRLS-TIKNADTISVLHGGKIVEQGSHRKL 1253
Cdd:PRK14271 211 DRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
984-1250 |
3.09e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 90.66 E-value: 3.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 984 AMGETLALAPDLLKGNQMVASVFEILDRktqIVGETSEElnnvegTIELKGVHFSYPSRPdvvIFRDFDLIVRAGKSMAL 1063
Cdd:PRK13536 5 AVAEEAPRRLELSPIERKHQGISEAKAS---IPGSMSTV------AIDLAGVSKSYGDKA---VVNGLSFTVASGECFGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1064 VGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKlDLKALRKHIGLVQQEPAL-FATTIYENIL----YGNEGASQSEV 1138
Cdd:PRK13536 73 LGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQFDNLdLEFTVRENLLvfgrYFGMSTREIEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1139 VESAMLANAHsfitslpegYSTKVGERGVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANR 1218
Cdd:PRK13536 152 VIPSLLEFAR---------LESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARG 222
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 79487035 1219 TTVVV-------AHRLstiknADTISVLHGG-KIVEQGSH 1250
Cdd:PRK13536 223 KTILLtthfmeeAERL-----CDRLCVLEAGrKIAEGRPH 257
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
415-619 |
3.15e-19 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 87.20 E-value: 3.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 415 DVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERF--YEPISGAVLLDGNNISELDI--KWLRGqIGLVNQEPAlfa 490
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPeeRARLG-IFLAFQYPP--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 491 ttirenilygkddataeEITrAAKLSEaisFINNLPEGFetqvgergiqlSGGQKQRIAISRAIVKNPSILLLDEATSAL 570
Cdd:cd03217 88 -----------------EIP-GVKNAD---FLRYVNEGF-----------SGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 79487035 571 DAESEKSVQEALDRVM-VGRTTVVVAH--RLSTVRNADIIAVVHEGKIVEFG 619
Cdd:cd03217 136 DIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1031-1248 |
3.76e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 88.20 E-value: 3.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1031 ELKGVHFSYPSRPdvvIFRDFDLIVRAGKSMALVGQSGSGKSS---VISLILRfYDPTAGKVMIEGKDIKKL--DLKAlR 1105
Cdd:COG0396 2 EIKNLHVSVEGKE---ILKGVNLTIKPGEVHAIMGPNGSGKSTlakVLMGHPK-YEVTSGSILLDGEDILELspDERA-R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1106 KHIGLVQQEP--------ALFATTIYENILYGNEGASQS--EVVESAMLAN-AHSFIT-SLPEGYStkvgergvqmsGGQ 1173
Cdd:COG0396 77 AGIFLAFQYPveipgvsvSNFLRTALNARRGEELSAREFlkLLKEKMKELGlDEDFLDrYVNEGFS-----------GGE 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 1174 RQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMA-NRTTVVVAH--RLSTIKNADTISVLHGGKIVEQG 1248
Cdd:COG0396 146 KKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSpDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSG 223
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
146-308 |
4.66e-19 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 89.14 E-value: 4.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 146 HTGERQAAKMRRAYLRSMLSQDISLFDTEaSTGEVISAITSDilvVQDALSekvgNFLHYISrfiagfaIGFTSVWQ--- 222
Cdd:cd18574 68 VVGERVAARLRNDLFSSLLRQDIAFFDTH-RTGELVNRLTAD---VQEFKS----SFKQCVS-------QGLRSVTQtvg 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 223 --ISLVTLS---------IVPLIALAGGIYAFVAIGLIARVRKSYIKAGEIAEEVIGNVRTVQAFTGEERAVRLYREALE 291
Cdd:cd18574 133 cvVSLYLISpkltllllvIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVE 212
|
170
....*....|....*..
gi 79487035 292 NTYKYGRKAGLtkGLGL 308
Cdd:cd18574 213 KAAKLNEKLGL--GIGI 227
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
401-627 |
4.77e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 88.99 E-value: 4.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPD---VVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKW-LR 476
Cdd:PRK13633 5 IKCKNVSYKYESNEEsteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 477 GQIGLVNQEP--ALFATTIRENILYGKDD--ATAEEITraAKLSEAISFINNlpegFETQVGERGIqLSGGQKQRIAISR 552
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGPENlgIPPEEIR--ERVDESLKKVGM----YEYRRHAPHL-LSGGQKQRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79487035 553 AIVKNPSILLLDEATSALDAESEKSVQEALDRV--MVGRTTVVVAHRLSTVRNADIIAVVHEGKIVEFGNHENLISN 627
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLDPSGRREVVNTIKELnkKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1048-1244 |
5.29e-19 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 85.95 E-value: 5.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1048 FRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLD-LKALRKHIGLV----QQEPALFATTI 1122
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRAGIAYVpedrKREGLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1123 YENIlygnegasqsevvesamlanahsfitSLPegystkvgergVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVE 1202
Cdd:cd03215 96 AENI--------------------------ALS-----------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 79487035 1203 SERVVQQALDRLMANRTTVVVahrLST-----IKNADTISVLHGGKI 1244
Cdd:cd03215 139 AKAEIYRLIRELADAGKAVLL---ISSeldelLGLCDRILVMYEGRI 182
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
416-588 |
6.04e-19 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 87.10 E-value: 6.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 416 VVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNN-------ISELDIKWLR-GQIGLVNQ--- 484
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdlaqASPREILALRrRTIGYVSQflr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 485 ------------EPALFAttirenilyGKDDATAEEitRAAKLSEAIsfinNLPEG--------FetqvgergiqlSGGQ 544
Cdd:COG4778 104 viprvsaldvvaEPLLER---------GVDREEARA--RARELLARL----NLPERlwdlppatF-----------SGGE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 79487035 545 KQRIAISRAIVKNPSILLLDEATSALDAESEKSV----QEALDR--VMVG 588
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTASLDAANRAVVveliEEAKARgtAIIG 207
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
422-639 |
7.19e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 89.93 E-value: 7.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 422 LNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGN--NISELDIkWL---RGQIGLVNQEPALFA-TTIRE 495
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlFDAEKGI-CLppeKRRIGYVFQDARLFPhYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 496 NILYGKDDATAEEITRAAKLSEAISFINNLPegfetqvgergIQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESE 575
Cdd:PRK11144 96 NLRYGMAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRK 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79487035 576 KSVQEALDRVM--VGRTTVVVAHRLSTV-RNADIIAVVHEGKIVEFGNHENLISN-------PDGAYSSLLRLQ 639
Cdd:PRK11144 165 RELLPYLERLAreINIPILYVSHSLDEIlRLADRVVVLEQGKVKAFGPLEEVWASsamrpwlPKEEQSSILKVT 238
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
422-624 |
7.56e-19 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 86.81 E-value: 7.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 422 LNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWL--RGqIGLVNQEPALFAT-TIRENIL 498
Cdd:TIGR03410 19 VSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERarAG-IAYVPQGREIFPRlTVEENLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 499 YGKDdataeeiTRAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSV 578
Cdd:TIGR03410 98 TGLA-------ALPRRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 79487035 579 QEALDRV--MVGRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFGNHENL 624
Cdd:TIGR03410 171 GRVIRRLraEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1042-1248 |
8.92e-19 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 86.56 E-value: 8.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1042 RPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLI---LRFYDPTAGKVMIEGKDIKKldlKALRKHIGLVQQEPALF 1118
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNGQPRKP---DQFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1119 AT-TIYENILY---------GNEGASQSEVVESAMLANAHSFITslpegystkvGERGVQMSGGQRQRIAIARAILKNPA 1188
Cdd:cd03234 94 PGlTVRETLTYtailrlprkSSDAIRKKRVEDVLLRDLALTRIG----------GNLVKGISGGERRRVSIAVQLLWDPK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79487035 1189 ILLLDEATSALDVESERVVQQALDRLMA-NRTTVVVAH--RLSTIKNADTISVLHGGKIVEQG 1248
Cdd:cd03234 164 VLILDEPTSGLDSFTALNLVSTLSQLARrNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1047-1225 |
9.18e-19 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 86.76 E-value: 9.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1047 IFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLK---ALR-KHIGLVQQEPALFAT-T 1121
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRaKHVGFVFQSFMLIPTlN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1122 IYENI----LYGNEGASQSEVVESAMLANAhsfitslpeGYSTKVGERGVQMSGGQRQRIAIARAILKNPAILLLDEATS 1197
Cdd:PRK10584 105 ALENVelpaLLRGESSRQSRNGAKALLEQL---------GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
|
170 180 190
....*....|....*....|....*....|.
gi 79487035 1198 ALDVES-ERVVQQ--ALDRLMANrTTVVVAH 1225
Cdd:PRK10584 176 NLDRQTgDKIADLlfSLNREHGT-TLILVTH 205
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
1047-1249 |
1.07e-18 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 86.42 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1047 IFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKAL-RKHIGLVQQEPALFAT-TIYE 1124
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIAYVPQGREIFPRlTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1125 NILYGNE--GASQSEVVESA---------MLanahsfitslpegystkvGERGVQMSGGQRQRIAIARAILKNPAILLLD 1193
Cdd:TIGR03410 95 NLLTGLAalPRRSRKIPDEIyelfpvlkeML------------------GRRGGDLSGGQQQQLAIARALVTRPKLLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 1194 EATSALDVESERVVQQALDRLMANR--TTVVVAHRLSTIKN-ADTISVLHGGKIVEQGS 1249
Cdd:TIGR03410 157 EPTEGIQPSIIKDIGRVIRRLRAEGgmAILLVEQYLDFARElADRYYVMERGRVVASGA 215
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1032-1203 |
1.07e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 91.28 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1032 LKGVHFSYPSRPdvvIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEgKDIKkldlkalrkhIGLV 1111
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP-KGLR----------IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1112 QQEPALFAT-TIYENILYGNEGA----SQSEVVESAM---------LANAHSFITSLpEGYS------------------ 1159
Cdd:COG0488 67 PQEPPLDDDlTVLDTVLDGDAELraleAELEELEAKLaepdedlerLAELQEEFEAL-GGWEaearaeeilsglgfpeed 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 79487035 1160 --TKVGErgvqMSGGQRQRIAIARAILKNPAILLLDEATSALDVES 1203
Cdd:COG0488 146 ldRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
77-371 |
1.10e-18 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 87.99 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 77 MTLGSVGACIHGASVPIFFIFFGKLINiiglaYLFPKQASHRVAKYSLDFVYLSVAILFSSWLEVACWMHTGERQAAKMR 156
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLID-----DVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 157 RAYLRSMLSQDISLFDtEASTGEVISAITSDILVVQDALSEKVGNFLHYISRFIAGFAIGFTSVWQISLVTLSIVPLIAL 236
Cdd:cd07346 76 RDLFRHLQRLSLSFFD-RNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 237 AGGIYAFVAIGLIARVRKSYIKAGEIAEEVIGNVRTVQAFTGEERAVRLYREALENTYKYGRKAGLTKGLGLGSMHCVLF 316
Cdd:cd07346 155 ILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTA 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 79487035 317 LSWALLVWFTSVVVHKDIADGGK--SFTTMLNVVIAglSLGQAAPDISAFVRAKAAA 371
Cdd:cd07346 235 LGTALVLLYGGYLVLQGSLTIGElvAFLAYLGMLFG--PIQRLANLYNQLQQALASL 289
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
417-629 |
1.11e-18 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 86.57 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 417 VIFDrLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWL--RGqIGLVNQEPALFAT-TI 493
Cdd:COG0410 18 VLHG-VSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarLG-IGYVPEGRRIFPSlTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 494 RENILYGkddatAEEITRAAKLSEAISFINNL-PEgfetqVGER----GIQLSGGQKQRIAISRAIVKNPSILLLDEATS 568
Cdd:COG0410 96 EENLLLG-----AYARRDRAEVRADLERVYELfPR-----LKERrrqrAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79487035 569 ALdaeSEKSVQEALDRVMV----GRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFGNHENLISNPD 629
Cdd:COG0410 166 GL---APLIVEEIFEIIRRlnreGVTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1027-1226 |
1.24e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 91.41 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1027 EGTIELKGVHFSYPSrpDVVIFRDFDLIVRAGKSMALVGQSGSGKSSvislILR-------FYD-----PTAGKVMiegk 1094
Cdd:COG4178 360 DGALALEDLTLRTPD--GRPLLEDLSLSLKPGERLLITGPSGSGKST----LLRaiaglwpYGSgriarPAGARVL---- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1095 dikkldlkalrkhigLVQQEPALFATTIYENILYGNEGASQS-EVVESAM-LANAHSFITSLPEgystkVGERGVQMSGG 1172
Cdd:COG4178 430 ---------------FLPQRPYLPLGTLREALLYPATAEAFSdAELREALeAVGLGHLAERLDE-----EADWDQVLSLG 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 79487035 1173 QRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVVVAHR 1226
Cdd:COG4178 490 EQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
415-622 |
1.25e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 86.66 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 415 DVVIFDRLNLAIPAGKIVALVGGSGSGKST---VISLIERfYEPISGAVLLDGNNISELDI--KWLRGqIGLVNQEPALF 489
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTlakVLMGHPK-YEVTSGSILLDGEDILELSPdeRARAG-IFLAFQYPVEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 490 ------------ATTIRENILYGKD-DATAEEITRAAKLSEaiSFIN-NLPEGFetqvgergiqlSGGQKQRIAISRAIV 555
Cdd:COG0396 90 pgvsvsnflrtaLNARRGEELSAREfLKLLKEKMKELGLDE--DFLDrYVNEGF-----------SGGEKKRNEILQMLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 556 KNPSILLLDEATSALDAESEKSVQEALDRVMV-GRTTVVVAH--RLSTVRNADIIAVVHEGKIVEFGNHE 622
Cdd:COG0396 157 LEPKLAILDETDSGLDIDALRIVAEGVNKLRSpDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGKE 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1050-1261 |
1.32e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.92 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1050 DFDLIVRAGKSMALVGQSGSGKSSVISLILRFYdPT------AGKVMIEGKDIKKLDLKALRK----HIGLVQQEPAL-- 1117
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQEPMVsl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1118 -----FATTIYEnILYGNEG----ASQSEVV---ESAMLANAHSFITSLPEgystkvgergvQMSGGQRQRIAIARAILK 1185
Cdd:PRK15134 106 nplhtLEKQLYE-VLSLHRGmrreAARGEILnclDRVGIRQAAKRLTDYPH-----------QLSGGERQRVMIAMALLT 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 1186 NPAILLLDEATSALDVESERVVQQALDRLMA--NRTTVVVAHRLSTIKN-ADTISVLHGGKIVEQGSHRKLVLNKSGPY 1261
Cdd:PRK15134 174 RPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFSAPTHPY 252
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1057-1266 |
1.41e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 88.61 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1057 AGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLD---LKALRKHIGLVQQEPalFAT-----TIYENI-- 1126
Cdd:PRK15079 46 EGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKddeWRAVRSDIQMIFQDP--LASlnprmTIGEIIae 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1127 ---LYGNEgASQSEVVE--SAMLANA---HSFITSLPEgystkvgergvQMSGGQRQRIAIARAILKNPAILLLDEATSA 1198
Cdd:PRK15079 124 plrTYHPK-LSRQEVKDrvKAMMLKVgllPNLINRYPH-----------EFSGGQCQRIGIARALILEPKLIICDEPVSA 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79487035 1199 LDVESE-RVVQ--QALDRLMAnRTTVVVAHRLSTIKN-ADTISVLHGGKIVEQGSHRKLVLNKSGPYFK-LIS 1266
Cdd:PRK15079 192 LDVSIQaQVVNllQQLQREMG-LSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHNPLHPYTKaLMS 263
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
366-620 |
1.61e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.51 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 366 RAKAAAypifKMIE-----RNTVTKTSAKSGRKLGK-VdghIQFKDATFSYPSRPdvvIFDRLNLAIPAGKIVALVGGSG 439
Cdd:COG0488 282 RIKALE----KLEReepprRDKTVEIRFPPPERLGKkV---LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 440 SGKSTVISLIERFYEPISGAVLLdGNNIseldikwlrgQIGLVNQEPALFAT--TIRENILYGKDDATaeEITRAAKLSe 517
Cdd:COG0488 352 AGKSTLLKLLAGELEPDSGTVKL-GETV----------KIGYFDQHQEELDPdkTVLDELRDGAPGGT--EQEVRGYLG- 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 518 aiSFinnlpeGF-----ETQVGErgiqLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDR----Vmvg 588
Cdd:COG0488 418 --RF------LFsgddaFKPVGV----LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDfpgtV--- 482
|
250 260 270
....*....|....*....|....*....|....*.
gi 79487035 589 rttVVVAH-R--LSTVrnADIIAVVHEGKIVEF-GN 620
Cdd:COG0488 483 ---LLVSHdRyfLDRV--ATRILEFEDGGVREYpGG 513
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
415-629 |
1.73e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 87.98 E-value: 1.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 415 DVVIFDRLNLAIPAGKIVALVGGSGSGKSTVIS----LIERFYEPISGAVLLDGNNISEL------------DIKWLRGQ 478
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVThfngLIKSKYGTIQVGDIYIGDKKNNHelitnpyskkikNFKELRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 479 IGLVNQEP--ALFATTIRENILYGKDdATAEEITRAAKLseAISFINNLpeGFETQVGERG-IQLSGGQKQRIAISRAIV 555
Cdd:PRK13631 118 VSMVFQFPeyQLFKDTIEKDIMFGPV-ALGVKKSEAKKL--AKFYLNKM--GLDDSYLERSpFGLSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79487035 556 KNPSILLLDEATSALDAESEKS-VQEALDRVMVGRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFGNHENLISNPD 629
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEmMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
429-601 |
1.74e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 85.70 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 429 GKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISEL---DIKWLRGQIGLVNQEPALFAT-TIREN-----ILY 499
Cdd:PRK10908 28 GEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrEVPFLRRQIGMIFQDHHLLMDrTVYDNvaiplIIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 500 GkddATAEEITRaaKLSEAISFInnlpeGFETQVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEATSALD-AESEKSV 578
Cdd:PRK10908 108 G---ASGDDIRR--RVSAALDKV-----GLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDdALSEGIL 177
|
170 180
....*....|....*....|....*
gi 79487035 579 Q--EALDRvmVGRTTVVVAHRLSTV 601
Cdd:PRK10908 178 RlfEEFNR--VGVTVLMATHDIGLI 200
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1050-1226 |
1.83e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 85.70 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1050 DFDLivRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKL---DLKALRKHIGLV-QQEPALFATTIYEN 1125
Cdd:PRK10908 22 TFHM--RPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrEVPFLRRQIGMIfQDHHLLMDRTVYDN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1126 -----ILYGNEGASQSEVVESAM-----LANAHSFitslpegystkvgerGVQMSGGQRQRIAIARAILKNPAILLLDEA 1195
Cdd:PRK10908 100 vaiplIIAGASGDDIRRRVSAALdkvglLDKAKNF---------------PIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 79487035 1196 TSALDVE-SERVVQ--QALDR-----LMANRTTVVVAHR 1226
Cdd:PRK10908 165 TGNLDDAlSEGILRlfEEFNRvgvtvLMATHDIGLISRR 203
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1030-1257 |
2.06e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 87.21 E-value: 2.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRPDVVifRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGK--DIKKLDLKALRKH 1107
Cdd:PRK13636 6 LKVEELNYNYSDGTHAL--KGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1108 IGLVQQEP--ALFATTIYENILYG--NEGASQSEV---VESAMLANAHSFITSLPEGYstkvgergvqMSGGQRQRIAIA 1180
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGavNLKLPEDEVrkrVDNALKRTGIEHLKDKPTHC----------LSFGQKKRVAIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1181 RAILKNPAILLLDEATSALD----VESERVVQQALDRLmaNRTTVVVAHRLSTIK-NADTISVLHGGKIVEQGSHRKLVL 1255
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKEL--GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFA 231
|
..
gi 79487035 1256 NK 1257
Cdd:PRK13636 232 EK 233
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
753-957 |
2.68e-18 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 86.77 E-value: 2.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 753 AILFCCASVITLIVYT-IEHICFGTMGERLTLRVRENMFRAILKNEIGWFDEvdNTSSMLASRLESDATLLKTIVVDRST 831
Cdd:cd18575 38 AFLLLLAVALVLALASaLRFYLVSWLGERVVADLRKAVFAHLLRLSPSFFET--TRTGEVLSRLTTDTTLIQTVVGSSLS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 832 ILLQNLGLVVTSFIIAFILNWRLTLVVLATYPLVIsghisekLFMQGYGGDLNK-------AYLKANMLAGESVSNIRTV 904
Cdd:cd18575 116 IALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVV-------LPIILFGRRVRRlsrasqdRLADLSAFAEETLSAIKTV 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 79487035 905 AAFCAEEKILELYSRELLEPSKSSFRRGQIAGLFYGVSQFFIFSSYGLALWYG 957
Cdd:cd18575 189 QAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWLG 241
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1029-1249 |
2.74e-18 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 85.91 E-value: 2.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1029 TIELKGVHFSypsrPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDP----TAGKVMIEGKDIKKLDLKAl 1104
Cdd:PRK10418 4 QIELRNIALQ----AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALRG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1105 rKHIGLVQQEP-ALF------ATTIYENIL-YGNEGASQS--EVVESAMLANAHSFITSLPegystkvgergVQMSGGQR 1174
Cdd:PRK10418 79 -RKIATIMQNPrSAFnplhtmHTHARETCLaLGKPADDATltAALEAVGLENAARVLKLYP-----------FEMSGGML 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 1175 QRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANRT--TVVVAHRLSTI-KNADTISVLHGGKIVEQGS 1249
Cdd:PRK10418 147 QRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIVEQGD 224
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
414-636 |
2.79e-18 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 85.91 E-value: 2.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 414 PDVVIFDRLNLAIPAGKIVALVGGSGSGKS----TVISLIERFYEPISGAVLLDGNNISELDikwLRGQ-IGLVNQEP-A 487
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCA---LRGRkIATIMQNPrS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 488 LF------ATTIRENIL-YGK--DDATAEEITRAAKLSEAISFINNLPegFEtqvgergiqLSGGQKQRIAISRAIVKNP 558
Cdd:PRK10418 91 AFnplhtmHTHARETCLaLGKpaDDATLTAALEAVGLENAARVLKLYP--FE---------MSGGMLQRMMIALALLCEA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 559 SILLLDEATSALDAESEKSVQEALDRVMVGRT--TVVVAHRLSTV-RNADIIAVVHEGKIVEFGNHENLISNPDGAYSSL 635
Cdd:PRK10418 160 PFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRS 239
|
.
gi 79487035 636 L 636
Cdd:PRK10418 240 L 240
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
126-565 |
2.79e-18 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 90.24 E-value: 2.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 126 FVYLSVAILFSSWLEVACWMHTGERQAAKMRRAYLRSMLSQDISLFDtEASTGEVISAITSDILVVQDALSeKVGNFLHY 205
Cdd:COG4615 54 FAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLE-RIGAARLLAALTEDVRTISQAFV-RLPELLQS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 206 ISRFIAGFA-IGFTSvWQISLVTLSivpLIALAGGIYAFvaigLIARVRKSYIKAGEIAEEVIGNVRTVqaFTG------ 278
Cdd:COG4615 132 VALVLGCLAyLAWLS-PPLFLLTLV---LLGLGVAGYRL----LVRRARRHLRRAREAEDRLFKHFRAL--LEGfkelkl 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 279 -EERAVRLYREALENTY----KYGRKAGLTKGLGLGSMHCVLFLSWALLVWFTSVVVHKDIADGGKSFTTMLNVVIAGLS 353
Cdd:COG4615 202 nRRRRRAFFDEDLQPTAeryrDLRIRADTIFALANNWGNLLFFALIGLILFLLPALGWADPAVLSGFVLVLLFLRGPLSQ 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 354 LGQAAPdisAFVRAKAAaypiFKMIER------NTVTKTSAKSGRKLGKVDGHIQFKDATFSYPSRPDVVIFD--RLNLA 425
Cdd:COG4615 282 LVGALP---TLSRANVA----LRKIEElelalaAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDGDEGFTlgPIDLT 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 426 IPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIGLVNQEPALFATtireniLYGKDDAT 505
Cdd:COG4615 355 IRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDR------LLGLDGEA 428
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79487035 506 AEEITRA----AKLSEAISFINNlpeGFETqvgergIQLSGGQKQRIAISRAIVKNPSILLLDE 565
Cdd:COG4615 429 DPARAREllerLELDHKVSVEDG---RFST------TDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1030-1257 |
2.82e-18 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 85.29 E-value: 2.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRPdvvIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDL-KALRKHI 1108
Cdd:cd03218 1 LRAENLSKRYGKRK---VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1109 GLVQQEPALFAT-TIYENIL-----YGNEGASQSEVVEsAMLANAHsfITSLpegystkVGERGVQMSGGQRQRIAIARA 1182
Cdd:cd03218 78 GYLPQEASIFRKlTVEENILavleiRGLSKKEREEKLE-ELLEEFH--ITHL-------RKSKASSLSGGERRRVEIARA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79487035 1183 ILKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVVVA-HRLS-TIKNADTISVLHGGKIVEQGSHRKLVLNK 1257
Cdd:cd03218 148 LATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
399-626 |
2.91e-18 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 86.45 E-value: 2.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 399 GHIQFKDATFSYPSRPDVVIfDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEpISGAVLLDGNNISELDIKWLRGQ 478
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVL-ENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 479 IGLVNQEPALFATTIRENI-LYGKddATAEEITRAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRIAISRAIVKN 557
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLdPYGK--WSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 558 PSILLLDEATSALDAESEKSVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVHEGKIVEFGNHENLIS 626
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLN 225
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1030-1249 |
4.46e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 86.01 E-value: 4.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYpsRPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIG 1109
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1110 LVQQEP--ALFATTIYENILYG--NEGASQSEV---VESAM-LANAHSFITSLPEgystkvgergvQMSGGQRQRIAIAR 1181
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGpiNLGLDEETVahrVSSALhMLGLEELRDRVPH-----------HLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79487035 1182 AILKNPAILLLDEATSALDVESERVVQQALDRLMAN--RTTVVVAHRLSTIKN-ADTISVLHGGKIVEQGS 1249
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGT 221
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
405-619 |
4.74e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 85.83 E-value: 4.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 405 DATFSYPSRPdvvIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGN--NISELDIKWLRGQIGLV 482
Cdd:PRK13638 6 DLWFRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 483 NQEP--ALFATTIRENILYG-KDDATAE-EITRaaKLSEAISFINnlPEGFETQvgerGIQ-LSGGQKQRIAISRAIVKN 557
Cdd:PRK13638 83 FQDPeqQIFYTDIDSDIAFSlRNLGVPEaEITR--RVDEALTLVD--AQHFRHQ----PIQcLSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79487035 558 PSILLLDEATSALDAESEKSVQEALDRVMV-GRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFG 619
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRIVAqGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHG 218
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1030-1253 |
4.83e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 88.95 E-value: 4.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSrpdVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLD-LKALRKHI 1108
Cdd:PRK15439 12 LCARSISKQYSG---VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKAHQLGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1109 GLVQQEPALFAT-TIYENILYGNEGASQSEVVESAMLANAHSFITSLPEGYSTKVGErgvqmsggqRQRIAIARAILKNP 1187
Cdd:PRK15439 89 YLVPQEPLLFPNlSVKENILFGLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVAD---------RQIVEILRGLMRDS 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 1188 AILLLDEATSALD-VESERVVQQALDRLMANRTTVVVAHRLSTIKN-ADTISVLHGGKIVEQGSHRKL 1253
Cdd:PRK15439 160 RILILDEPTASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
408-646 |
5.81e-18 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 90.46 E-value: 5.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 408 FSYPSRPDVvifDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNIsELDIKWLRGQIGLVNQEPA 487
Cdd:TIGR01257 938 FEPSGRPAV---DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNI 1013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 488 LFA-TTIRENILY-----GKDDATAEeITRAAKLSEAisfinnlpeGFETQVGERGIQLSGGQKQRIAISRAIVKNPSIL 561
Cdd:TIGR01257 1014 LFHhLTVAEHILFyaqlkGRSWEEAQ-LEMEAMLEDT---------GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVV 1083
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 562 LLDEATSALDAESEKSVQEALDRVMVGRTTVVVAHRLStvrNADI----IAVVHEGKIVEFGNH---ENLISNpdGAYSS 634
Cdd:TIGR01257 1084 VLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMD---EADLlgdrIAIISQGRLYCSGTPlflKNCFGT--GFYLT 1158
|
250
....*....|..
gi 79487035 635 LLRLQETASLQR 646
Cdd:TIGR01257 1159 LVRKMKNIQSQR 1170
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
417-626 |
6.78e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 85.04 E-value: 6.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 417 VIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIGLVNQEpalfATTiren 496
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQN----ATT---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 497 ilygKDDATAEEI------------TRAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRIAISRAIVKNPSILLLD 564
Cdd:PRK10253 93 ----PGDITVQELvargryphqplfTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79487035 565 EATSALDAESEKSVQEALDRV--MVGRTTVVVAHRLS-TVRNADIIAVVHEGKIVEFGNHENLIS 626
Cdd:PRK10253 169 EPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVT 233
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
415-616 |
7.22e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 85.55 E-value: 7.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 415 DVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDikwlRGQIGLVNQEPALFAT-TI 493
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYLPEERGLYPKmKV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 494 RENILY-----GKDDATAEEitRAAKLSEAisfinnlpegFEtqVGERG---IQ-LSGGQKQRIAISRAIVKNPSILLLD 564
Cdd:COG4152 89 GEQLVYlarlkGLSKAEAKR--RADEWLER----------LG--LGDRAnkkVEeLSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 79487035 565 EATSALDAESEKSVQEAL-DRVMVGRTTVVVAHRLSTV-RNADIIAVVHEGKIV 616
Cdd:COG4152 155 EPFSGLDPVNVELLKDVIrELAAKGTTVIFSSHQMELVeELCDRIVIINKGRKV 208
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1030-1214 |
7.82e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 84.75 E-value: 7.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRPdvvIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKklDLKALRkhiG 1109
Cdd:PRK11248 2 LQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE--GPGAER---G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1110 LVQQEPALFA-TTIYENILYGNE----GASQSEVVESAMLAnahsfitslpegystKVGERGV------QMSGGQRQRIA 1178
Cdd:PRK11248 74 VVFQNEGLLPwRNVQDNVAFGLQlagvEKMQRLEIAHQMLK---------------KVGLEGAekryiwQLSGGQRQRVG 138
|
170 180 190
....*....|....*....|....*....|....*.
gi 79487035 1179 IARAILKNPAILLLDEATSALDVESERVVQQALDRL 1214
Cdd:PRK11248 139 IARALAANPQLLLLDEPFGALDAFTREQMQTLLLKL 174
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1058-1258 |
8.73e-18 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 84.91 E-value: 8.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1058 GKSMALVGQSGSGKSSVISLILRFYDpTAGKVMIEGKDIKKLDLKALRKHIGLVQQEPALFATTIYENiLYGNEGASQSE 1137
Cdd:cd03289 30 GQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKN-LDPYGKWSDEE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1138 VVESAMLANAHSFITSLPEGYSTKVGERGVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMAN 1217
Cdd:cd03289 108 IWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFAD 187
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 79487035 1218 RTTVVVAHRLSTIKNADTISVLHGGKIVEQGSHRKLVLNKS 1258
Cdd:cd03289 188 CTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKS 228
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
401-572 |
8.91e-18 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 86.44 E-value: 8.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPDVVifDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFyEPI-SGAVLLDGNNISELDIKwLRGqI 479
Cdd:PRK11650 4 LKLQAVRKSYDGKTQVI--KGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGL-ERItSGEIWIGGRVVNELEPA-DRD-I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 480 GLVNQEPALFA-TTIRENILYG-------KDDaTAEEITRAAKLSEAISFINNLPEgfetqvgergiQLSGGQKQRIAIS 551
Cdd:PRK11650 79 AMVFQNYALYPhMSVRENMAYGlkirgmpKAE-IEERVAEAARILELEPLLDRKPR-----------ELSGGQRQRVAMG 146
|
170 180
....*....|....*....|.
gi 79487035 552 RAIVKNPSILLLDEATSALDA 572
Cdd:PRK11650 147 RAIVREPAVFLFDEPLSNLDA 167
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1049-1225 |
1.03e-17 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 83.67 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1049 RDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALrkhigLVQQEPALFA-TTIYENI- 1126
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENIa 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1127 LYGNEGASQSEVVESAMLANAHSFITSLPEGYSTKVGergvQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERV 1206
Cdd:TIGR01184 77 LAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPG----QLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180
....*....|....*....|.
gi 79487035 1207 VQQALDRLM--ANRTTVVVAH 1225
Cdd:TIGR01184 153 LQEELMQIWeeHRVTVLMVTH 173
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1038-1239 |
1.52e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 82.28 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1038 SYPSRPdvvIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKdikkldlkalrKHIGLVQQ---E 1114
Cdd:NF040873 1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG-----------ARVAYVPQrseV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1115 PALFATTIYENI---------LYGNEGASQSEVVESAMLANAhsfITSLpegystkvGERGVQ-MSGGQRQRIAIARAIL 1184
Cdd:NF040873 67 PDSLPLTVRDLVamgrwarrgLWRRLTRDDRAAVDDALERVG---LADL--------AGRQLGeLSGGQRQRALLAQGLA 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 79487035 1185 KNPAILLLDEATSALDVESERVVQQALDRLMA-NRTTVVVAHRLSTIKNADTISVL 1239
Cdd:NF040873 136 QEADLLLLDEPTTGLDAESRERIIALLAEEHArGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
415-619 |
1.64e-17 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 85.85 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 415 DVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKwLRGqIGLVNQEPALFA-TTI 493
Cdd:PRK11000 15 DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA-ERG-VGMVFQSYALYPhLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 494 RENILYGKDDATAEEITRAAKLsEAISFINNLPEGFETQVGErgiqLSGGQKQRIAISRAIVKNPSILLLDEATSALDAe 573
Cdd:PRK11000 93 AENMSFGLKLAGAKKEEINQRV-NQVAEVLQLAHLLDRKPKA----LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA- 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 574 seksvqeALdRVM-----------VGRTTVVVAH-RLSTVRNADIIAVVHEGKIVEFG 619
Cdd:PRK11000 167 -------AL-RVQmrieisrlhkrLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
772-985 |
2.00e-17 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 84.40 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 772 ICFGTMGERLTLRVRENMFRAILKNEIGWFDEvdNTSSMLASRLESDATLLKTIVVDRSTILLQNLGLVVTSFIIAFILN 851
Cdd:cd18552 61 YLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDR--NSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 852 WRLTLVVLATYPLV--ISGHISEKL-----FMQGYGGDLNKaylkanmLAGESVSNIRTVAAFCAEEKILELYSRELLEP 924
Cdd:cd18552 139 WKLTLIALVVLPLAalPIRRIGKRLrkisrRSQESMGDLTS-------VLQETLSGIRVVKAFGAEDYEIKRFRKANERL 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79487035 925 SKSSFRRGQIAGLFYGVSQFFIFSSYGLALWYGSTLMdkgLAGFKSVmKTFMVLIvTALAM 985
Cdd:cd18552 212 RRLSMKIARARALSSPLMELLGAIAIALVLWYGGYQV---ISGELTP-GEFISFI-TALLL 267
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1051-1256 |
2.14e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 83.73 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1051 FDLivRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIGLVQQ----------------- 1113
Cdd:COG4167 34 FTL--EAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMIFQdpntslnprlnigqile 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1114 EPALFATTIyenilygNEGASQSEVVES----AMLANaHSFItslpegYstkvgergVQM-SGGQRQRIAIARAILKNPA 1188
Cdd:COG4167 112 EPLRLNTDL-------TAEEREERIFATlrlvGLLPE-HANF------Y--------PHMlSSGQKQRVALARALILQPK 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79487035 1189 ILLLDEATSALDVeSERvvQQALDRLMANRTT-----VVVAHRLSTIKN-ADTISVLHGGKIVEQGSHRKLVLN 1256
Cdd:COG4167 170 IIIADEALAALDM-SVR--SQIINLMLELQEKlgisyIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVFAN 240
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
378-622 |
3.17e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 84.50 E-value: 3.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 378 IERNTVTKTSAKSGRKLGKVDGHIQFKDATFSYPSRPdvvIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPIS 457
Cdd:PRK13536 19 IERKHQGISEAKASIPGSMSTVAIDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 458 GAVLLDGNNISElDIKWLRGQIGLVNQEPAL-FATTIRENIL-YGKddataeEITRAAKLSEAIsfINNLPE--GFETQV 533
Cdd:PRK13536 96 GKITVLGVPVPA-RARLARARIGVVPQFDNLdLEFTVRENLLvFGR------YFGMSTREIEAV--IPSLLEfaRLESKA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 534 GERGIQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRVMV-GRTTVVVAHRLSTV-RNADIIAVVH 611
Cdd:PRK13536 167 DARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLArGKTILLTTHFMEEAeRLCDRLCVLE 246
|
250
....*....|..
gi 79487035 612 EG-KIVEFGNHE 622
Cdd:PRK13536 247 AGrKIAEGRPHA 258
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1051-1261 |
3.80e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 86.83 E-value: 3.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1051 FDLIvrAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLD---LKALRKHIGLVQQEPalFAT------- 1120
Cdd:PRK10261 345 FDLW--PGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDP--YASldprqtv 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1121 --TIYE-----NILYGNEGASQ-SEVVESAMLANAHSFitSLPEgystkvgergvQMSGGQRQRIAIARAILKNPAILLL 1192
Cdd:PRK10261 421 gdSIMEplrvhGLLPGKAAAARvAWLLERVGLLPEHAW--RYPH-----------EFSGGQRQRICIARALALNPKVIIA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79487035 1193 DEATSALDVE-SERVVQQALD--RLMAnRTTVVVAHRLSTIKN-ADTISVLHGGKIVEQGSHRKLVLNKSGPY 1261
Cdd:PRK10261 488 DEAVSALDVSiRGQIINLLLDlqRDFG-IAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFENPQHPY 559
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
399-649 |
4.57e-17 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 87.27 E-value: 4.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 399 GHIQFKDATFSYPSRPDVVIFDrLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEpISGAVLLDGNNISELDIKWLRGQ 478
Cdd:TIGR01271 1216 GQMDVQGLTAKYTEAGRAVLQD-LSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKA 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 479 IGLVNQEPALFATTIRENiLYGKDDATAEEITRAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRIAISRAIVKNP 558
Cdd:TIGR01271 1294 FGVIPQKVFIFSGTFRKN-LDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKA 1372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 559 SILLLDEATSALDAESEKSVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVHEGKIVEFGNHENLI---SNPDGAYSSL 635
Cdd:TIGR01271 1373 KILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLnetSLFKQAMSAA 1452
|
250
....*....|....
gi 79487035 636 LRLQETASLQRNPS 649
Cdd:TIGR01271 1453 DRLKLFPLHRRNSS 1466
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1030-1243 |
4.69e-17 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 79.03 E-value: 4.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRPdvvIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIeGKDIKkldlkalrkhIG 1109
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVK----------IG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1110 LVQQepalfattiyenilygnegasqsevvesamlanahsfitslpegystkvgergvqMSGGQRQRIAIARAILKNPAI 1189
Cdd:cd03221 67 YFEQ-------------------------------------------------------LSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 79487035 1190 LLLDEATSALDVESERVVQQALDRLmaNRTTVVVAHRLSTIKN-ADTISVLHGGK 1243
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALKEY--PGTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
401-614 |
4.83e-17 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 79.03 E-value: 4.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPdvvIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNiseldikwlrgqig 480
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV-------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 lvnqepalfattireNILYgkddataeeitraaklseaisfinnlpegFEtqvgergiQLSGGQKQRIAISRAIVKNPSI 560
Cdd:cd03221 64 ---------------KIGY-----------------------------FE--------QLSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 79487035 561 LLLDEATSALDAESEKSVQEALDRvmVGRTTVVVAH-R--LSTVrnADIIAVVHEGK 614
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALKE--YPGTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1062-1249 |
5.11e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 84.16 E-value: 5.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1062 ALVGQSGSGKSSVISLILRFYDPTAGKVMIEGK---DI-KKLDLKALRKHIGLVQQEPALFA-TTIYENILYGNEGASQS 1136
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAeKGICLPPEKRRIGYVFQDARLFPhYKVRGNLRYGMAKSMVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1137 E---VVEsaMLAnahsfITSLPEGY-STkvgergvqMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALD 1212
Cdd:PRK11144 108 QfdkIVA--LLG-----IEPLLDRYpGS--------LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 79487035 1213 RLMA--NRTTVVVAHRLSTI-KNADTISVLHGGKIVEQGS 1249
Cdd:PRK11144 173 RLAReiNIPILYVSHSLDEIlRLADRVVVLEQGKVKAFGP 212
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1024-1256 |
5.73e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 82.51 E-value: 5.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1024 NNVEGTIELKGVHFSYPSRPdvvIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLD--- 1100
Cdd:PRK11831 2 QSVANLVDMRGVSFTRGNRC---IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1101 LKALRKHIGLVQQEPALFA-TTIYENILYGNEGASQ--SEVVESAMLANAHSfitslpegystkVGERGV------QMSG 1171
Cdd:PRK11831 79 LYTVRKRMSMLFQSGALFTdMNVFDNVAYPLREHTQlpAPLLHSTVMMKLEA------------VGLRGAaklmpsELSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1172 GQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLmaNR----TTVVVAHRLSTIKN-ADTISVLHGGKIVE 1246
Cdd:PRK11831 147 GMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISEL--NSalgvTCVVVSHDVPEVLSiADHAYIVADKKIVA 224
|
250
....*....|
gi 79487035 1247 QGSHRKLVLN 1256
Cdd:PRK11831 225 HGSAQALQAN 234
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
416-626 |
6.64e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 85.49 E-value: 6.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 416 VVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKwLRGQIG--LVNQEPALFAT-T 492
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGiyLVPQEPLLFPNlS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 493 IRENILYG--KDDATAEEITraAKLSEAISFINnlpegFETQVGergiQLSGGQKQRIAISRAIVKNPSILLLDEATSAL 570
Cdd:PRK15439 103 VKENILFGlpKRQASMQKMK--QLLAALGCQLD-----LDSSAG----SLEVADRQIVEILRGLMRDSRILILDEPTASL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79487035 571 D-AESE---KSVQEALDRvmvGRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFG-----NHENLIS 626
Cdd:PRK15439 172 TpAETErlfSRIRELLAQ---GVGIVFISHKLPEIRQlADRISVMRDGTIALSGktadlSTDDIIQ 234
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
422-642 |
6.82e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 81.98 E-value: 6.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 422 LNLAIPAGKIVALVGGSGSGKSTVI----SLIERFYEPISGAVLLdGNNISEL-----DIKWLRGQIGLVNQEPALF-AT 491
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDKSAGSHIELL-GRTVQREgrlarDIRKSRANTGYIFQQFNLVnRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 492 TIRENILYGKDDATA------EEITRAAKlSEAISFINNLpeGFETQVGERGIQLSGGQKQRIAISRAIVKNPSILLLDE 565
Cdd:PRK09984 102 SVLENVLIGALGSTPfwrtcfSWFTREQK-QRALQALTRV--GMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 566 ATSALDAESEKSVQEALDRVMV--GRTTVVVAHRLS-TVRNADIIAVVHEGKIVEFGNHENLISNP-DGAYSSLLRLQET 641
Cdd:PRK09984 179 PIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQFDNERfDHLYRSINRVEEN 258
|
.
gi 79487035 642 A 642
Cdd:PRK09984 259 A 259
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
420-636 |
7.07e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 85.53 E-value: 7.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 420 DRLNLAIPAGKIVALVGGSGSGKS-TVISLIERFYEP----ISGAVLLDGNNISELDIKWLRG----QIGLVNQEPalfa 490
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQEP---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 491 tTIRENILYGKDDATAEEIT------RAAKLSEAISFINnlpegfetQVGERGI---------QLSGGQKQRIAISRAIV 555
Cdd:PRK15134 102 -MVSLNPLHTLEKQLYEVLSlhrgmrREAARGEILNCLD--------RVGIRQAakrltdyphQLSGGERQRVMIAMALL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 556 KNPSILLLDEATSALDAESE-------KSVQEALDRVMvgrttVVVAHRLSTVRN-ADIIAVVHEGKIVEFGNHENLISN 627
Cdd:PRK15134 173 TRPELLIADEPTTALDVSVQaqilqllRELQQELNMGL-----LFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFSA 247
|
....*....
gi 79487035 628 PDGAYSSLL 636
Cdd:PRK15134 248 PTHPYTQKL 256
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1030-1248 |
8.40e-17 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 81.04 E-value: 8.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPS-------------------RPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVM 1090
Cdd:cd03220 1 IELENVSKSYPTykggssslkklgilgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1091 IEGKDIKKLDLkalrkHIGLvqqEPALfatTIYENI-LYGNE-GASQSEVveSAMLANAHSFiTSLPEGYSTKVGErgvq 1168
Cdd:cd03220 81 VRGRVSSLLGL-----GGGF---NPEL---TGRENIyLNGRLlGLSRKEI--DEKIDEIIEF-SELGDFIDLPVKT---- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1169 MSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVV-VAHRLSTIKN-ADTISVLHGGKIVE 1246
Cdd:cd03220 143 YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVIlVSHDPSSIKRlCDRALVLEKGKIRF 222
|
..
gi 79487035 1247 QG 1248
Cdd:cd03220 223 DG 224
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1043-1243 |
1.03e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 84.98 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1043 PDVVIFRDFDLIVRAGKSMALVGQSGSGKSS---VISLILRF--YDptaGKVMIEGKDIKKLDLK-ALRKHIGLVQQEPA 1116
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTlmkVLSGVYPHgtYE---GEIIFEGEELQASNIRdTERAGIAIIHQELA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1117 LFAT-TIYENILYGNEGASQSEVVESAMLANAHSFITSLPEGYS--TKVGERGvqmsGGQRQRIAIARAILKNPAILLLD 1193
Cdd:PRK13549 93 LVKElSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINpaTPVGNLG----LGQQQLVEIAKALNKQARLLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 79487035 1194 EATSALdVESERVVQQALDRLMANR--TTVVVAHRLSTIKN-ADTISVLHGGK 1243
Cdd:PRK13549 169 EPTASL-TESETAVLLDIIRDLKAHgiACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
401-627 |
1.11e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 82.44 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPDVVI--FDRLNLAIPAGKIVALVGGSGSGKSTVIS-----------LIERFYE-------PISGAV 460
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEhlnalllpdtgTIEWIFKdeknkkkTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 461 LLDGNNISEL------DIKWLRGQIGLVNQ--EPALFATTIRENIL-----YGKDDATAEEitRAAKLSEAIsfinNLPE 527
Cdd:PRK13651 83 VLEKLVIQKTrfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIfgpvsMGVSKEEAKK--RAAKYIELV----GLDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 528 GFetqVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRV-MVGRTTVVVAHRLSTV-RNAD 605
Cdd:PRK13651 157 SY---LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVlEWTK 233
|
250 260
....*....|....*....|..
gi 79487035 606 IIAVVHEGKIVEFGNHENLISN 627
Cdd:PRK13651 234 RTIFFKDGKIIKDGDTYDILSD 255
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1032-1251 |
1.94e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 80.49 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1032 LKGVHFSYPSRpdvVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMiegkdIKKLDLKALRKHIGLV 1111
Cdd:PRK11247 15 LNAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-----AGTAPLAEAREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1112 QQEPALFA-TTIYENI---LYGNEGASQSEVVESAMLANahsfitslpegystKVGERGVQMSGGQRQRIAIARAILKNP 1187
Cdd:PRK11247 87 FQDARLLPwKKVIDNVglgLKGQWRDAALQALAAVGLAD--------------RANEWPAALSGGQKQRVALARALIHRP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 1188 AILLLDEATSALDVESERVVQQALDRLMANR--TTVVVAHRLS-TIKNADTISVLHGGKI-----VE------QGSHR 1251
Cdd:PRK11247 153 GLLLLDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSeAVAMADRVLLIEEGKIgldltVDlprprrRGSAR 230
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1052-1254 |
2.39e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 83.70 E-value: 2.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1052 DLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMI----EGKDIKKL--DLKA-LRKHIGLVQQEPALFA-TTIY 1123
Cdd:TIGR03269 304 SLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPgpDGRGrAKRYIGILHQEYDLYPhRTVL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1124 ENIlygNEGASQSEVVESAMLANAHSFITSlpeGYSTKVGERGV-----QMSGGQRQRIAIARAILKNPAILLLDEATSA 1198
Cdd:TIGR03269 384 DNL---TEAIGLELPDELARMKAVITLKMV---GFDEEKAEEILdkypdELSEGERHRVALAQVLIKEPRIVILDEPTGT 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 1199 LDVESERVVQQAL--DRLMANRTTVVVAHRLSTIKN-ADTISVLHGGKIVEQGSHRKLV 1254
Cdd:TIGR03269 458 MDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIV 516
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
429-636 |
2.41e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 80.36 E-value: 2.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 429 GKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNN--------ISELDIKWL-RGQIGLVNQEPA------------ 487
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdlyaLSEAERRRLlRTEWGFVHQHPRdglrmqvsaggn 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 488 ----LFATTIREnilYGKDDATAEEITRAAKLseAISFINNLPEGFetqvgergiqlSGGQKQRIAISRAIVKNPSILLL 563
Cdd:PRK11701 112 igerLMAVGARH---YGDIRATAGDWLERVEI--DAARIDDLPTTF-----------SGGMQQRLQIARNLVTHPRLVFM 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 564 DEATSALDAesekSVQ-EALD--RVMV---GRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFGNHENLISNPDGAYSSLL 636
Cdd:PRK11701 176 DEPTGGLDV----SVQaRLLDllRGLVrelGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESGLTDQVLDDPQHPYTQLL 251
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
418-617 |
2.63e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 79.23 E-value: 2.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 418 IFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYE--PISGAVLLDGNNISEldikwlrgqiglvnqepalfATTIRE 495
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFGR--------------------EASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 496 NILYGKDDATAEEITRAAKLSEAISFINNLPEgfetqvgergiqLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESE 575
Cdd:COG2401 105 AIGRKGDFKDAVELLNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTA 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 79487035 576 K----SVQEALDRvmVGRTTVVVAHRlSTVRNA---DIIAVVHEGKIVE 617
Cdd:COG2401 173 KrvarNLQKLARR--AGITLVVATHH-YDVIDDlqpDLLIFVGYGGVPE 218
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
401-597 |
3.57e-16 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 77.19 E-value: 3.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRpDVVIFDrLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVlldgnniseldIKWLRGQIG 480
Cdd:cd03223 1 IELENLSLATPDG-RVLLKD-LSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 LVNQEPALFATTIRENILYGKDDAtaeeitraaklseaisfinnlpegfetqvgergiqLSGGQKQRIAISRAIVKNPSI 560
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIYPWDDV-----------------------------------LSGGEQQRLAFARLLLHKPKF 112
|
170 180 190
....*....|....*....|....*....|....*...
gi 79487035 561 LLLDEATSALDAESEKSVQEALDRVMvgrTTVV-VAHR 597
Cdd:cd03223 113 VFLDEATSALDEESEDRLYQLLKELG---ITVIsVGHR 147
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
401-622 |
3.95e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 80.62 E-value: 3.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPsrpDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISElDIKWLRGQIG 480
Cdd:PRK13537 8 IDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 LV----NQEPALfatTIRENIL-----YGKDDATAEEitRAAKLSEaisfINNLPEGFETQVGErgiqLSGGQKQRIAIS 551
Cdd:PRK13537 84 VVpqfdNLDPDF---TVRENLLvfgryFGLSAAAARA--LVPPLLE----FAKLENKADAKVGE----LSGGMKRRLTLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79487035 552 RAIVKNPSILLLDEATSALDAESEKSVQEALDRVMV-GRTTVVVAHRLSTV-RNADIIAVVHEG-KIVEFGNHE 622
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLArGKTILLTTHFMEEAeRLCDRLCVIEEGrKIAEGAPHA 224
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1029-1247 |
4.05e-16 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 81.43 E-value: 4.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1029 TIELKGVHFSYPSRPDVVifRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDlKALRKhI 1108
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVI--KGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELE-PADRD-I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1109 GLVQQEPALFA-TTIYENILYG--NEGASQSE----VVESAMLANAHSFITSLPEgystkvgergvQMSGGQRQRIAIAR 1181
Cdd:PRK11650 79 AMVFQNYALYPhMSVRENMAYGlkIRGMPKAEieerVAEAARILELEPLLDRKPR-----------ELSGGQRQRVAMGR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1182 AILKNPAILLLDEATSALDVE---SERVVQQALDRLMaNRTTVVVAH-RLSTIKNADTISVLHGGKIvEQ 1247
Cdd:PRK11650 148 AIVREPAVFLFDEPLSNLDAKlrvQMRLEIQRLHRRL-KTTSLYVTHdQVEAMTLADRVVVMNGGVA-EQ 215
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1055-1249 |
4.21e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 79.59 E-value: 4.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1055 VRAGKSMALVGQSGSGKSSVISLI---LrfydPTAGKVMIEGKDIKKLDLKALRKHIG-LVQQEPALFATTIYENI-LYG 1129
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMaglL----PGSGSIQFAGQPLEAWSAAELARHRAyLSQQQTPPFAMPVFQYLtLHQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1130 ----NEGASQS---EVVESAMLANahsfitslpegystKVGERGVQMSGGQRQRIAIARAILK-----NPA--ILLLDEA 1195
Cdd:PRK03695 95 pdktRTEAVASalnEVAEALGLDD--------------KLGRSVNQLSGGEWQRVRLAAVVLQvwpdiNPAgqLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79487035 1196 TSALDveserVVQQ-ALDRLM-----ANRTTVVVAHRLS-TIKNADTISVLHGGKIVEQGS 1249
Cdd:PRK03695 161 MNSLD-----VAQQaALDRLLselcqQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGR 216
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1052-1249 |
4.47e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 79.67 E-value: 4.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1052 DLIVRAGKSMALVGQSGSGKSSVISLI--LRFYDPTAG-KVMIEGKDIKKL-----DLKALRKHIGLVQQEPALF-ATTI 1122
Cdd:PRK09984 24 DLNIHHGEMVALLGPSGSGKSTLLRHLsgLITGDKSAGsHIELLGRTVQREgrlarDIRKSRANTGYIFQQFNLVnRLSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1123 YENILYGNEGASqsevvesAMLANAHSFITSLPEGYS----TKVG------ERGVQMSGGQRQRIAIARAILKNPAILLL 1192
Cdd:PRK09984 104 LENVLIGALGST-------PFWRTCFSWFTREQKQRAlqalTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVILA 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1193 DEATSALDVESERVVQQALDRLMANR--TTVVVAHRLS-TIKNADTISVLHGGKIVEQGS 1249
Cdd:PRK09984 177 DEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGHVFYDGS 236
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
414-616 |
5.14e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 82.77 E-value: 5.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 414 PDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNnisELDIK----WLRGQIGLVNQEPALF 489
Cdd:COG3845 16 GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGK---PVRIRsprdAIALGIGMVHQHFMLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 490 AT-TIRENILYGKDDA------TAEEITRAAKLSEAIsfinnlpeGFE----TQVGergiQLSGGQKQRIAISRAIVKNP 558
Cdd:COG3845 93 PNlTVAENIVLGLEPTkggrldRKAARARIRELSERY--------GLDvdpdAKVE----DLSVGEQQRVEILKALYRGA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79487035 559 SILLLDEATSALdaesekSVQEAlDRVMV--------GRTTVVVAHRLSTVR-NADIIAVVHEGKIV 616
Cdd:COG3845 161 RILILDEPTAVL------TPQEA-DELFEilrrlaaeGKSIIFITHKLREVMaIADRVTVLRRGKVV 220
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
412-582 |
5.55e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 77.92 E-value: 5.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 412 SRPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIGLVNQEPALFAT 491
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 492 TIRENILYGKDDATAEEITRAAklseaisfinnlpegfeTQVGERGI------QLSGGQKQRIAISRAIVKNPSILLLDE 565
Cdd:cd03231 89 SVLENLRFWHADHSDEQVEEAL-----------------ARVGLNGFedrpvaQLSAGQQRRVALARLLLSGRPLWILDE 151
|
170
....*....|....*..
gi 79487035 566 ATSALDAESEKSVQEAL 582
Cdd:cd03231 152 PTTALDKAGVARFAEAM 168
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1054-1262 |
5.61e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 83.17 E-value: 5.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1054 IVRAGKSMALVGQSGSGKSSVISlILRFYDPT----AGKVMIEGkdiKKLDLKALRKHIGLVQQEPALFAT-TIYENILY 1128
Cdd:TIGR00955 47 VAKPGELLAVMGSSGAGKTTLMN-ALAFRSPKgvkgSGSVLLNG---MPIDAKEMRAISAYVQQDDLFIPTlTVREHLMF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1129 GNEGASQSEVVESAMLANAHSFIT--SLPEGYSTKVGERGVQ--MSGGQRQRIAIARAILKNPAILLLDEATSALDVESE 1204
Cdd:TIGR00955 123 QAHLRMPRRVTKKEKRERVDEVLQalGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMA 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79487035 1205 RVVQQALDRLMANRTTVVVA-HRLST--IKNADTISVLHGGKIVEQGSHRKLVlnksgPYF 1262
Cdd:TIGR00955 203 YSVVQVLKGLAQKGKTIICTiHQPSSelFELFDKIILMAEGRVAYLGSPDQAV-----PFF 258
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1051-1249 |
5.75e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 82.45 E-value: 5.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1051 FDLivRAGKSMALVGQSGSGKSSVISLILRFYdPTAGKVMIEGKDIKKLDLKAL---RKHIGLVQQEP--ALFATTIYEN 1125
Cdd:PRK15134 307 FTL--RPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPnsSLNPRLNVLQ 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1126 ILygNEG----------ASQSEVVESAML------ANAHSFITslpegystkvgergvQMSGGQRQRIAIARAILKNPAI 1189
Cdd:PRK15134 384 II--EEGlrvhqptlsaAQREQQVIAVMEevgldpETRHRYPA---------------EFSGGQRQRIAIARALILKPSL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79487035 1190 LLLDEATSALDveseRVVQ-QALDRLMANRTT-----VVVAHRLSTIKN-ADTISVLHGGKIVEQGS 1249
Cdd:PRK15134 447 IILDEPTSSLD----KTVQaQILALLKSLQQKhqlayLFISHDLHVVRAlCHQVIVLRQGEVVEQGD 509
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
413-576 |
6.31e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.99 E-value: 6.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 413 RPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNIselDIKWLRGQIGLVNQEPALFAT- 491
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI---DDPDVAEACHYLGHRNAMKPAl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 492 TIRENI-----LYGKDDATAEEITRAAKLSEaisfINNLPEGFetqvgergiqLSGGQKQRIAISRAIVKNPSILLLDEA 566
Cdd:PRK13539 89 TVAENLefwaaFLGGEELDIAAALEAVGLAP----LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEP 154
|
170
....*....|
gi 79487035 567 TSALDAESEK 576
Cdd:PRK13539 155 TAALDAAAVA 164
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
409-629 |
6.33e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 78.53 E-value: 6.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 409 SYPSRPdVVifDRLNLAIPAGKIVALVGGSGSGKSTVislierFY------EPISGAVLLDGNNISELDIkWLRGQ--IG 480
Cdd:COG1137 12 SYGKRT-VV--KDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPM-HKRARlgIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 LVNQEPALFAT-TIRENIL-----YGKDDATAEEitRAAKLSEA--ISFINNLPegfetqvgerGIQLSGGQKQRIAISR 552
Cdd:COG1137 82 YLPQEASIFRKlTVEDNILavlelRKLSKKEREE--RLEELLEEfgITHLRKSK----------AYSLSGGERRRVEIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 553 AIVKNPSILLLDEATSALD----AESEKSVQEALDR----------VmvgRTTvvvahrLSTVRNADIIavvHEGKIVEF 618
Cdd:COG1137 150 ALATNPKFILLDEPFAGVDpiavADIQKIIRHLKERgigvlitdhnV---RET------LGICDRAYII---SEGKVLAE 217
|
250
....*....|.
gi 79487035 619 GNHENLISNPD 629
Cdd:COG1137 218 GTPEEILNNPL 228
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1030-1259 |
7.99e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 79.85 E-value: 7.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPsrpDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKAlRKHIG 1109
Cdd:PRK13537 8 IDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1110 LVQQ----EPALfatTIYENIL----YGNEGASQSEVVESAMLANAHsfitsLPEGYSTKVGErgvqMSGGQRQRIAIAR 1181
Cdd:PRK13537 84 VVPQfdnlDPDF---TVRENLLvfgrYFGLSAAAARALVPPLLEFAK-----LENKADAKVGE----LSGGMKRRLTLAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1182 AILKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVVV-------AHRLstiknADTISVLHGGKIVEQGSHRKLV 1254
Cdd:PRK13537 152 ALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVIEEGRKIAEGAPHALI 226
|
....*
gi 79487035 1255 LNKSG 1259
Cdd:PRK13537 227 ESEIG 231
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
422-616 |
9.32e-16 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 77.70 E-value: 9.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 422 LNLAIPAGKIVALVGGSGSGKSTVISLIERFYEP---ISGAVLLDGnniSELDIKWLRGQIGLVNQEPALFAT-TIRENI 497
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNG---QPRKPDQFQKCVAYVRQDDILLPGlTVRETL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 498 LYGKDDATAEEITRAAKLSEAISFInnLPEGFETQVGERGIQ-LSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEK 576
Cdd:cd03234 103 TYTAILRLPRKSSDAIRKKRVEDVL--LRDLALTRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTAL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 79487035 577 SVQEALDRVMVGRTTVVVA-H--RLSTVRNADIIAVVHEGKIV 616
Cdd:cd03234 181 NLVSTLSQLARRNRIVILTiHqpRSDLFRLFDRILLLSSGEIV 223
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
420-636 |
1.20e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 79.75 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 420 DRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISEL-DIKWL--RGQIGLVNQEPaLFATTIREN 496
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMkDDEWRavRSDIQMIFQDP-LASLNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 497 IlygkDDATAE-------EITRA----------AKLSEAISFINNLPEGFetqvgergiqlSGGQKQRIAISRAIVKNPS 559
Cdd:PRK15079 117 I----GEIIAEplrtyhpKLSRQevkdrvkammLKVGLLPNLINRYPHEF-----------SGGQCQRIGIARALILEPK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 560 ILLLDEATSALDAesekSVQ-------EALDRVMvGRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFGNHENLISNPDGA 631
Cdd:PRK15079 182 LIICDEPVSALDV----SIQaqvvnllQQLQREM-GLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHNPLHP 256
|
....*
gi 79487035 632 YSSLL 636
Cdd:PRK15079 257 YTKAL 261
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1062-1249 |
1.39e-15 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 82.75 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1062 ALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKlDLKALRKHIGLVQQEPALFA-TTIYENILYGNE--GASQSE- 1137
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHhLTVAEHILFYAQlkGRSWEEa 1038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1138 -VVESAMLANAhsfitslpeGYSTKVGERGVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMA 1216
Cdd:TIGR01257 1039 qLEMEAMLEDT---------GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRS 1109
|
170 180 190
....*....|....*....|....*....|....
gi 79487035 1217 NRTTVVVAHRLSTIKN-ADTISVLHGGKIVEQGS 1249
Cdd:TIGR01257 1110 GRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGT 1143
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
401-626 |
2.12e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 80.62 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPS--RPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLL----DGNNISELDIKw 474
Cdd:TIGR03269 280 IKVRNVSKRYISvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPD- 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 475 LRGQ----IGLVNQEPALFA-TTIRENilygkddataeeitraakLSEAISFinNLPE--------------GFETQVGE 535
Cdd:TIGR03269 359 GRGRakryIGILHQEYDLYPhRTVLDN------------------LTEAIGL--ELPDelarmkavitlkmvGFDEEKAE 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 536 RGI-----QLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEAL--DRVMVGRTTVVVAHRLSTVRN-ADII 607
Cdd:TIGR03269 419 EILdkypdELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLDvCDRA 498
|
250
....*....|....*....
gi 79487035 608 AVVHEGKIVEFGNHENLIS 626
Cdd:TIGR03269 499 ALMRDGKIVKIGDPEEIVE 517
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1035-1261 |
2.79e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 78.61 E-value: 2.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1035 VHFSYPSrPDVVIFRDFDLIVRAGKSMALVGQSGSGKS-SVISL--ILRFYDPTAGKVMIEGKDIKKLDLKALRK----H 1107
Cdd:PRK09473 20 VTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALmgLLAANGRIGGSATFNGREILNLPEKELNKlraeQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1108 IGLVQQEPAlfaTTI--YENI-------LYGNEGASQSEVVESA--ML-----ANAHSFITSLPEgystkvgergvQMSG 1171
Cdd:PRK09473 99 ISMIFQDPM---TSLnpYMRVgeqlmevLMLHKGMSKAEAFEESvrMLdavkmPEARKRMKMYPH-----------EFSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1172 GQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMA--NRTTVVVAHRLSTIKN-ADTISVLHGGKIVEQG 1248
Cdd:PRK09473 165 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYG 244
|
250
....*....|...
gi 79487035 1249 SHRKLVLNKSGPY 1261
Cdd:PRK09473 245 NARDVFYQPSHPY 257
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
99-309 |
2.89e-15 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 77.76 E-value: 2.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 99 GKLINIIGLAYLfpkqasHRVAKYSLDFVYL-SVAILFSSWLEVACWMHTGERQAAKMRRAYLRSMLSQDISLFDtEAST 177
Cdd:cd18590 20 GRVIDILGGEYQ------HNAFTSAIGLMCLfSLGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFE-KTKT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 178 GEVISAITSDILVVQDALSEKVGNFLHYISRFIAGFAIGFTSVWQISLVTLSIVPLIALAGGIYAFVAIGLIARVRKSYI 257
Cdd:cd18590 93 GDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 79487035 258 KAGEIAEEVIGNVRTVQAFTGEERAVRLYREALENTYKYGRKAGLTKGLGLG 309
Cdd:cd18590 173 KAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLL 224
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
148-325 |
3.45e-15 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 77.46 E-value: 3.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 148 GERQAAKMRRAYLRSMLSQDISLFDTEaSTGEVISAITSDILVVQDALSEKVGNFLHYISRFIAGFAIGFTSVWQISLVT 227
Cdd:cd18552 67 GQRVVRDLRNDLFDKLLRLPLSFFDRN-SSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 228 LSIVPLIALAggiyafvaIGLIAR-----VRKSYIKAGEIA---EEVIGNVRTVQAFTGEERAVRLYREALENTYKYGRK 299
Cdd:cd18552 146 LVVLPLAALP--------IRRIGKrlrkiSRRSQESMGDLTsvlQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMK 217
|
170 180
....*....|....*....|....*.
gi 79487035 300 AGLTKGLGLGSMHCVLFLSWALLVWF 325
Cdd:cd18552 218 IARARALSSPLMELLGAIAIALVLWY 243
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
408-616 |
3.61e-15 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 76.60 E-value: 3.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 408 FSYPSRPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRgQIGLV----N 483
Cdd:cd03267 26 LFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLR-RIGVVfgqkT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 484 QE----PALFATTIRENIlYGKDDATAEEitRAAKLSEAIsfinNLPEGFETQVgeRgiQLSGGQKQRIAISRAIVKNPS 559
Cdd:cd03267 105 QLwwdlPVIDSFYLLAAI-YDLPPARFKK--RLDELSELL----DLEELLDTPV--R--QLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 560 ILLLDEATSALDAESEKSVQEALDRVMVGRTTVVV--AHRLSTV-RNADIIAVVHEGKIV 616
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLltSHYMKDIeALARRVLVIDKGRLL 233
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1030-1248 |
5.34e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 77.43 E-value: 5.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRPDVVI--FRDFDLIVRAGKSMALVGQSGSGKSSVI----SLILrfydPTAGKVMIEGKDIKKL---- 1099
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELkaLDNVSVEINQGEFIAIIGQTGSGKTTFIehlnALLL----PDTGTIEWIFKDEKNKkktk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1100 --------------------DLKALRKHIGLVQQ--EPALFATTIYENILYG--NEGASQSEVVEsamLANAHSFITSLP 1155
Cdd:PRK13651 79 ekekvleklviqktrfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGpvSMGVSKEEAKK---RAAKYIELVGLD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1156 EGYSTKvgeRGVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMAN-RTTVVVAHRL-STIKNA 1233
Cdd:PRK13651 156 ESYLQR---SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLdNVLEWT 232
|
250
....*....|....*
gi 79487035 1234 DTISVLHGGKIVEQG 1248
Cdd:PRK13651 233 KRTIFFKDGKIIKDG 247
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1048-1248 |
7.66e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 76.12 E-value: 7.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1048 FRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKAL----RKHI-----GLVQQEPA-- 1116
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaeRRRLlrtewGFVHQHPRdg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1117 -LFATTIYENI----------LYGN---EGASQSEVVESAMlanahSFITSLPEGYStkvgergvqmsGGQRQRIAIARA 1182
Cdd:PRK11701 102 lRMQVSAGGNIgerlmavgarHYGDiraTAGDWLERVEIDA-----ARIDDLPTTFS-----------GGMQQRLQIARN 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79487035 1183 ILKNPAILLLDEATSALDVEservVQQALDRLMANRTT------VVVAHRLSTIKN-ADTISVLHGGKIVEQG 1248
Cdd:PRK11701 166 LVTHPRLVFMDEPTGGLDVS----VQARLLDLLRGLVRelglavVIVTHDLAVARLlAHRLLVMKQGRVVESG 234
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
754-957 |
8.87e-15 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 76.32 E-value: 8.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 754 ILFCCASVITLIVYTIEHICFGTMGERLTLRVRENMFRAILKNEIGWFDEvdNTSSMLASRLESDATLLKTIVVDRSTIL 833
Cdd:cd18551 40 ALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDR--RRSGDLVSRVTNDTTLLRELITSGLPQL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 834 LQNLGLVVTSFIIAFILNWRLTLVVLATYPL--VISGHISEKlfMQGYGGDLNKAylKANMLAG--ESVSNIRTVAAFCA 909
Cdd:cd18551 118 VTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLafLIILPLGRR--IRKASKRAQDA--LGELSAAleRALSAIRTVKASNA 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 79487035 910 EEKILELYSRELLEPSKSSFRRGQIAGLFYGVSQFFIFSSYGLALWYG 957
Cdd:cd18551 194 EERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGVG 241
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1058-1254 |
9.01e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 75.79 E-value: 9.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1058 GKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIGLVQQEPA---------LFATTIY-ENIL 1127
Cdd:PRK10253 33 GHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATtpgditvqeLVARGRYpHQPL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1128 YGNEGASQSEVVESAMLANAhsfITSLpegystkVGERGVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVV 1207
Cdd:PRK10253 113 FTRWRKEDEEAVTKAMQATG---ITHL-------ADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 79487035 1208 QQALDRLmaNR----TTVVVAHRLS-TIKNADTISVLHGGKIVEQGSHRKLV 1254
Cdd:PRK10253 183 LELLSEL--NRekgyTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
429-626 |
9.24e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.94 E-value: 9.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 429 GKIVALVGGSGSGKSTVISLIErFYEP----ISGAVLLDGNNIselDIKWLRGQIGLVNQEPALFAT-TIRENILY---- 499
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALA-FRSPkgvkGSGSVLLNGMPI---DAKEMRAISAYVQQDDLFIPTlTVREHLMFqahl 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 500 --GKDDATAEEITRAAKLSEAISFIN--NLpegfETQVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESE 575
Cdd:TIGR00955 127 rmPRRVTKKEKRERVDEVLQALGLRKcaNT----RIGVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMA 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 79487035 576 KSVQEALDRV-MVGRTTVVVAHRLST--VRNADIIAVVHEGKIVEFGNHENLIS 626
Cdd:TIGR00955 203 YSVVQVLKGLaQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
412-574 |
1.06e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 73.93 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 412 SRPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRgQIGLVNQEPALFAT 491
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHE-NILYLGHLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 492 -TIRENILYGKDDATAEEITraakLSEAIsfinnlpegfeTQVGERGI------QLSGGQKQRIAISRAIVKNPSILLLD 564
Cdd:TIGR01189 88 lSALENLHFWAAIHGGAQRT----IEDAL-----------AAVGLTGFedlpaaQLSAGQQRRLALARLWLSRRPLWILD 152
|
170
....*....|
gi 79487035 565 EATSALDAES 574
Cdd:TIGR01189 153 EPTTALDKAG 162
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
422-638 |
1.27e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 78.21 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 422 LNLAIPAGKIVALVGGSGSGKST----VISLIerfyePISGAVLLDGNNISELDIKWL---RGQIGLVNQEP--AL---- 488
Cdd:PRK15134 305 ISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPnsSLnprl 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 489 -FATTIRENILYGKDDATAEEitRAAKLSEAISFINNLPEGFETQVGErgiqLSGGQKQRIAISRAIVKNPSILLLDEAT 567
Cdd:PRK15134 380 nVLQIIEEGLRVHQPTLSAAQ--REQQVIAVMEEVGLDPETRHRYPAE----FSGGQRQRIAIARALILKPSLIILDEPT 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 568 SALDaeseKSVQE---ALDRVMVGR---TTVVVAHRLSTVRN-ADIIAVVHEGKIVEFGNHENLISNPDGAYS-SLLRL 638
Cdd:PRK15134 454 SSLD----KTVQAqilALLKSLQQKhqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFAAPQQEYTrQLLAL 528
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
420-629 |
1.55e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 75.03 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 420 DRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDikwlrGQ----IGLVN--QEPALFAT-T 492
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLP-----GHqiarMGVVRtfQHVRLFREmT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 493 IRENILYGKD------------------DATAEEITRAAKLSEAIsfinNLPEGFETQVGergiQLSGGQKQRIAISRAI 554
Cdd:PRK11300 97 VIENLLVAQHqqlktglfsgllktpafrRAESEALDRAATWLERV----GLLEHANRQAG----NLAYGQQRRLEIARCM 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 555 VKNPSILLLDEATSALDAESEKSVQEALD--RVMVGRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFGNHENLISNPD 629
Cdd:PRK11300 169 VTQPEILMLDEPAAGLNPKETKELDELIAelRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEIRNNPD 246
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1030-1261 |
1.90e-14 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 72.57 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSrpDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMiegkdikkldlKALRKHIG 1109
Cdd:cd03223 1 IELENLSLATPD--GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG-----------MPEGEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1110 LVQQEPALFATTIYENILYgnegASQSEvvesamlanahsfitslpegystkvgergvqMSGGQRQRIAIARAILKNPAI 1189
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIY----PWDDV-------------------------------LSGGEQQRLAFARLLLHKPKF 112
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79487035 1190 LLLDEATSALDVESERVVQQALDRLMAnrTTVVVAHRlstiknaDTISVLHggkiveqgsHRKLVLNKSGPY 1261
Cdd:cd03223 113 VFLDEATSALDEESEDRLYQLLKELGI--TVISVGHR-------PSLWKFH---------DRVLDLDGEGGW 166
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1042-1207 |
2.12e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 73.37 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1042 RPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIG-LVQQEPALfat 1120
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGhRNAMKPAL--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1121 TIYENI-----LYGNEGASQSEVVESAMLANahsfITSLPEGYstkvgergvqMSGGQRQRIAIARAILKNPAILLLDEA 1195
Cdd:PRK13539 89 TVAENLefwaaFLGGEELDIAAALEAVGLAP----LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEP 154
|
170
....*....|..
gi 79487035 1196 TSALDVESERVV 1207
Cdd:PRK13539 155 TAALDAAAVALF 166
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
751-964 |
2.93e-14 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 74.78 E-value: 2.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 751 KIAILFCCASVITLIVYTIEHICFGTMGERLTLRVRENMFRAILKNEIGWFDevDNTSSMLASRLESDATLLKTIVVDRS 830
Cdd:cd18542 40 LLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHD--KARTGDLMSRCTSDVDTIRRFLAFGL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 831 TILLQNLGLVVTSFIIAFILNWRLTLVVLATYPLVIsghisekLFMQGYGGDLNKAYLKA-------NMLAGESVSNIRT 903
Cdd:cd18542 118 VELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIA-------LFSYVFFKKVRPAFEEIreqegelNTVLQENLTGVRV 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79487035 904 VAAFCAEEKILELYSRELLEPSKSSFRRGQIAGLFYGVSQFFIFSSYGLALWYGSTLMDKG 964
Cdd:cd18542 191 VKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVING 251
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1063-1249 |
3.10e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 74.27 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1063 LVGQSGSGKSSV---ISLILRfydPTAGKVMIEGK--DIKKLDLKALRKHIGLVQQEP--ALFATTIYENILYG--NEGA 1133
Cdd:PRK13638 32 LVGANGCGKSTLfmnLSGLLR---PQKGAVLWQGKplDYSKRGLLALRQQVATVFQDPeqQIFYTDIDSDIAFSlrNLGV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1134 SQSEVV----ESAMLANAHSFitslpegystkvGERGVQ-MSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQ 1208
Cdd:PRK13638 109 PEAEITrrvdEALTLVDAQHF------------RHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 79487035 1209 QALDRLMANRTTVVV-AHRLSTIKN-ADTISVLHGGKIVEQGS 1249
Cdd:PRK13638 177 AIIRRIVAQGNHVIIsSHDIDLIYEiSDAVYVLRQGQILTHGA 219
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
147-301 |
3.16e-14 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 74.78 E-value: 3.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 147 TGERQAAKMRRAYLRSMLSQDISLFDTEaSTGEVISAITSDILVVQDALSEKVGNFLHYISRFIAGFAIGFTSVWQISLV 226
Cdd:cd18551 63 TGERVVLDLRRRLWRRLLRLPVSFFDRR-RSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 227 TLSIVPLIALaggiyafVAIGLIARVRKSYIKA-------GEIAEEVIGNVRTVQAFTGEERAVRLYREALENTYKYGRK 299
Cdd:cd18551 142 TLAVVPLAFL-------IILPLGRRIRKASKRAqdalgelSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLK 214
|
..
gi 79487035 300 AG 301
Cdd:cd18551 215 AA 216
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1042-1263 |
3.18e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 77.20 E-value: 3.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1042 RPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKV-------------MIEGKDIKKLDLKALR-KH 1107
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqVIELSEQSAAQMRHVRgAD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1108 IGLVQQEP-----ALFAT--TIYENILYgNEGASQSEVVESA--ML-----ANAHSFITSLPEgystkvgergvQMSGGQ 1173
Cdd:PRK10261 106 MAMIFQEPmtslnPVFTVgeQIAESIRL-HQGASREEAMVEAkrMLdqvriPEAQTILSRYPH-----------QLSGGM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1174 RQRIAIARAILKNPAILLLDEATSALDVESE-------RVVQQALDrlMAnrtTVVVAHRLSTIKN-ADTISVLHGGKIV 1245
Cdd:PRK10261 174 RQRVMIAMALSCRPAVLIADEPTTALDVTIQaqilqliKVLQKEMS--MG---VIFITHDMGVVAEiADRVLVMYQGEAV 248
|
250
....*....|....*...
gi 79487035 1246 EQGSHRKLVLNKSGPYFK 1263
Cdd:PRK10261 249 ETGSVEQIFHAPQHPYTR 266
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1027-1194 |
3.28e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 73.52 E-value: 3.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1027 EGTIELKGVHFSYPSRPdVVifRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDL-KALR 1105
Cdd:COG1137 1 MMTLEAENLVKSYGKRT-VV--KDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMhKRAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1106 KHIGLVQQEPALFAT-TIYENIL-----YGNEGASQSEVVESaMLANAHsfITSLpegYSTKvgerGVQMSGGQRQRIAI 1179
Cdd:COG1137 78 LGIGYLPQEASIFRKlTVEDNILavlelRKLSKKEREERLEE-LLEEFG--ITHL---RKSK----AYSLSGGERRRVEI 147
|
170
....*....|....*
gi 79487035 1180 ARAILKNPAILLLDE 1194
Cdd:COG1137 148 ARALATNPKFILLDE 162
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
415-626 |
4.13e-14 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 76.76 E-value: 4.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 415 DVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERF--YEPISGAVLLD-----------------------GNNISE 469
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcekcgyverpskvgepcpvcGGTLEP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 470 LDIK-W---------LRGQIGLVNQEP-ALFAT-TIRENILYGKDDA---TAEEITRAAKLSEaisfinnlpegfETQVG 534
Cdd:TIGR03269 92 EEVDfWnlsdklrrrIRKRIAIMLQRTfALYGDdTVLDNVLEALEEIgyeGKEAVGRAVDLIE------------MVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 535 ER----GIQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRVMV--GRTTVVVAHRLSTVRNADIIA 608
Cdd:TIGR03269 160 HRithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasGISMVLTSHWPEVIEDLSDKA 239
|
250
....*....|....*....
gi 79487035 609 VVHE-GKIVEFGNHENLIS 626
Cdd:TIGR03269 240 IWLEnGEIKEEGTPDEVVA 258
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
407-628 |
4.84e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 73.67 E-value: 4.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 407 TFSYPS----RPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIGLV 482
Cdd:PRK15112 13 TFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 483 NQEPALfATTIRENI-------LYGKDDATAEEitRAAKLSEAISFINNLPEgfetQVGERGIQLSGGQKQRIAISRAIV 555
Cdd:PRK15112 93 FQDPST-SLNPRQRIsqildfpLRLNTDLEPEQ--REKQIIETLRQVGLLPD----HASYYPHMLAPGQKQRLGLARALI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 556 KNPSILLLDEATSALDAesekSVQEALDRVMV------GRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFGNHENLISNP 628
Cdd:PRK15112 166 LRPKVIIADEALASLDM----SMRSQLINLMLelqekqGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLASP 241
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1029-1261 |
7.66e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 74.01 E-value: 7.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1029 TIELKGVHFSYPSRPdvviFRDFDLI---VRAGKSMALVGQSGSGKSsVISL-ILRFYDpTAGKVMIE-----GKDIKKL 1099
Cdd:PRK11022 5 NVDKLSVHFGDESAP----FRAVDRIsysVKQGEVVGIVGESGSGKS-VSSLaIMGLID-YPGRVMAEklefnGQDLQRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1100 DLKALRKHIG----LVQQEPALFATTIYE------NILYGNEGASQSEVVESAM-------LANAHSFITSLPEgystkv 1162
Cdd:PRK11022 79 SEKERRNLVGaevaMIFQDPMTSLNPCYTvgfqimEAIKVHQGGNKKTRRQRAIdllnqvgIPDPASRLDVYPH------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1163 gergvQMSGGQRQRIAIARAILKNPAILLLDEATSALDVEserVVQQALDRLMA-----NRTTVVVAHRLSTI-KNADTI 1236
Cdd:PRK11022 153 -----QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVT---IQAQIIELLLElqqkeNMALVLITHDLALVaEAAHKI 224
|
250 260
....*....|....*....|....*
gi 79487035 1237 SVLHGGKIVEQGSHRKLVLNKSGPY 1261
Cdd:PRK11022 225 IVMYAGQVVETGKAHDIFRAPRHPY 249
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
415-622 |
8.43e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 72.75 E-value: 8.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 415 DVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERF--YEPISGAVLLDGNNISELDIKwLRGQIGL----------- 481
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHLGIflafqypieip 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 482 -VNQEPALFATTIRENILYGKDDATA----EEITRAAKLSE-AISFIN-NLPEGFetqvgergiqlSGGQKQRIAISRAI 554
Cdd:CHL00131 98 gVSNADFLRLAYNSKRKFQGLPELDPleflEIINEKLKLVGmDPSFLSrNVNEGF-----------SGGEKKRNEILQMA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79487035 555 VKNPSILLLDEATSALDAESEKSVQEALDRVM-VGRTTVVVAH--RLSTVRNADIIAVVHEGKIVEFGNHE 622
Cdd:CHL00131 167 LLDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGDAE 237
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
414-614 |
8.76e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 75.74 E-value: 8.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 414 PDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYeP---ISGAVLLDG-----NNISELDikwlRGQIGLVNQE 485
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PhgtYEGEIIFEGeelqaSNIRDTE----RAGIAIIHQE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 486 PALFAT-TIRENILYGkddataEEITR------AAKLSEAISFINNLpeGFETQVGERGIQLSGGQKQRIAISRAIVKNP 558
Cdd:PRK13549 91 LALVKElSVLENIFLG------NEITPggimdyDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALNKQA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79487035 559 SILLLDEATSALdaeSEKSVQEALDRVM----VGRTTVVVAHRLSTVRN-ADIIAVVHEGK 614
Cdd:PRK13549 163 RLLILDEPTASL---TESETAVLLDIIRdlkaHGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
429-636 |
8.85e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 76.05 E-value: 8.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 429 GKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELD---IKWLRGQIGLVNQEPalFAT-----TIRENIL-- 498
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDP--YASldprqTVGDSIMep 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 499 -----YGKDDATAEeitRAAKLSEAISFinnLPEgfetQVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAE 573
Cdd:PRK10261 428 lrvhgLLPGKAAAA---RVAWLLERVGL---LPE----HAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79487035 574 SEKSVQEA---LDRVMvGRTTVVVAHRLSTV-RNADIIAVVHEGKIVEFGNHENLISNPDGAYSSLL 636
Cdd:PRK10261 498 IRGQIINLlldLQRDF-GIAYLFISHDMAVVeRISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKL 563
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
418-571 |
9.86e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 72.12 E-value: 9.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 418 IFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKW---LRGQ-IGLVNQEPALFAT-T 492
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakLRAKhVGFVFQSFMLIPTlN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 493 IRENI-----LYGKDDATAEEitRAAKLSEAISF---INNLPEgfetqvgergiQLSGGQKQRIAISRAIVKNPSILLLD 564
Cdd:PRK10584 105 ALENVelpalLRGESSRQSRN--GAKALLEQLGLgkrLDHLPA-----------QLSGGEQQRVALARAFNGRPDVLFAD 171
|
....*..
gi 79487035 565 EATSALD 571
Cdd:PRK10584 172 EPTGNLD 178
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1047-1248 |
1.03e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 72.23 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1047 IFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKA-LRKHIGLVQQEPALFAT-TIYE 1124
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARRGIGYLPQEASIFRRlSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1125 NILYGNE-----GASQSEVVESAMLANAHsfITSLPEGYstkvgerGVQMSGGQRQRIAIARAILKNPAILLLDEATSAL 1199
Cdd:PRK10895 98 NLMAVLQirddlSAEQREDRANELMEEFH--IEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDEPFAGV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 79487035 1200 D----VESERVVQQALDRLMAnrtTVVVAHRLStiknaDTISVLHGGKIVEQG 1248
Cdd:PRK10895 169 DpisvIDIKRIIEHLRDSGLG---VLITDHNVR-----ETLAVCERAYIVSQG 213
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
369-619 |
1.51e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 75.30 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 369 AAAYPI-FKMIE---RNTVTKTSAKSGrKLGKVDGHIQ-FKDATFSYPSRpdvVIFDRLNLAIPAGKIVALVGGSGSGKS 443
Cdd:PLN03211 33 SSCYPItLKFMDvcyRVKFENMKNKGS-NIKRILGHKPkISDETRQIQER---TILNGVTGMASPGEILAVLGPSGSGKS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 444 TVISLIE-RFY-EPISGAVLLDGNNISELDIKwlrgQIGLVNQEPALFA-TTIRENILYGKDDATAEEITRAAKLSEAIS 520
Cdd:PLN03211 109 TLLNALAgRIQgNNFTGTILANNRKPTKQILK----RTGFVTQDDILYPhLTVRETLVFCSLLRLPKSLTKQEKILVAES 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 521 FINNL--PEGFETQVGE---RGIqlSGGQKQRIAISRAIVKNPSILLLDEATSALDAESE-KSVQEALDRVMVGRTTVVV 594
Cdd:PLN03211 185 VISELglTKCENTIIGNsfiRGI--SGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAyRLVLTLGSLAQKGKTIVTS 262
|
250 260
....*....|....*....|....*..
gi 79487035 595 AHRLST--VRNADIIAVVHEGKIVEFG 619
Cdd:PLN03211 263 MHQPSSrvYQMFDSVLVLSEGRCLFFG 289
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1044-1245 |
1.62e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 74.86 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1044 DVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYdPTA---GKVMIEGKDIKKLDLKAL-RKHIGLVQQEPALFA 1119
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGtwdGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1120 T-TIYENILYGNEGASQSEVVE-SAMLANAHSFI--TSLPEGYSTK-VGERGvqmsGGQRQRIAIARAILKNPAILLLDE 1194
Cdd:TIGR02633 92 ElSVAENIFLGNEITLPGGRMAyNAMYLRAKNLLreLQLDADNVTRpVGDYG----GGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 79487035 1195 ATSAL-DVESERVVQQALDRLMANRTTVVVAHRLSTIKN-ADTISVLHGGKIV 1245
Cdd:TIGR02633 168 PSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
407-633 |
1.86e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 73.22 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 407 TFSYPSrPDVVIFDRLNLAIPAGKIVALVGGSGSGKS-TVISLIERFYEP--ISGAVLLDGN---NISELDIKWLRG-QI 479
Cdd:PRK09473 21 TFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGReilNLPEKELNKLRAeQI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 480 GLVNQEPalfATT------IRENIL--------YGKDDATAEEITR--AAKLSEAISFINNLPEGFetqvgergiqlSGG 543
Cdd:PRK09473 100 SMIFQDP---MTSlnpymrVGEQLMevlmlhkgMSKAEAFEESVRMldAVKMPEARKRMKMYPHEF-----------SGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 544 QKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRVM--VGRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFGN 620
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKreFNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGN 245
|
250
....*....|...
gi 79487035 621 HENLISNPDGAYS 633
Cdd:PRK09473 246 ARDVFYQPSHPYS 258
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
416-658 |
2.46e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 72.63 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 416 VVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLI------------ERFYepisgavlLDGNNISELDI----KWLRGQI 479
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAIcgitkdnwhvtaDRFR--------WNGIDLLKLSPrerrKIIGREI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 480 GLVNQEPALF---ATTIRENILYGKDDATAE---------EITRAAKL--------SEAIsfINNLPEgfetqvgergiQ 539
Cdd:COG4170 92 AMIFQEPSSCldpSAKIGDQLIEAIPSWTFKgkwwqrfkwRKKRAIELlhrvgikdHKDI--MNSYPH-----------E 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 540 LSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRV-MVGRTTVV-VAHRLSTV-RNADIIAVVHEGKIV 616
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLnQLQGTSILlISHDLESIsQWADTITVLYCGQTV 238
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 79487035 617 EFGNHENLISNPDGAYSSLLrlqetasLQRNPSLNRTLsrPH 658
Cdd:COG4170 239 ESGPTEQILKSPHHPYTKAL-------LRSMPDFRQPL--PH 271
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
418-627 |
3.29e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 70.69 E-value: 3.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 418 IFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDI--KWLRGqIGLVNQEPALFAT-TIR 494
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhaRARRG-IGYLPQEASIFRRlSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 495 EN---ILYGKDDATAEE-ITRAAKLSEAISfINNLPEGFetqvgerGIQLSGGQKQRIAISRAIVKNPSILLLDEATSAL 570
Cdd:PRK10895 97 DNlmaVLQIRDDLSAEQrEDRANELMEEFH-IEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDEPFAGV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79487035 571 DAES----EKSVQEALDRvmvGRTTVVVAHRL-STVRNADIIAVVHEGKIVEFGNHENLISN 627
Cdd:PRK10895 169 DPISvidiKRIIEHLRDS---GLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1043-1246 |
3.67e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.41 E-value: 3.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1043 PDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLK-ALRKHIGLVQQE----PAL 1117
Cdd:PRK11288 15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGVAIIYQElhlvPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1118 fatTIYENILYGNEGASQSEVVESAMLANAHSFITSLPEGY--STKVGErgvqMSGGQRQRIAIARAILKNPAILLLDEA 1195
Cdd:PRK11288 95 ---TVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIdpDTPLKY----LSIGQRQMVEIAKALARNARVIAFDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 79487035 1196 TSALDV-ESE---RVVqqalDRLMAN-RTTVVVAHRLSTI-KNADTISVLHGGKIVE 1246
Cdd:PRK11288 168 TSSLSArEIEqlfRVI----RELRAEgRVILYVSHRMEEIfALCDAITVFKDGRYVA 220
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
753-1194 |
3.89e-13 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 73.68 E-value: 3.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 753 AILFCCASVITLIVYTIEHICFGTMGERLTLRVRENMFRAILKNEIGWFDEVdNTSSMLASrLESDATLLkTIVVDRSTI 832
Cdd:COG4615 51 LLLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLERI-GAARLLAA-LTEDVRTI-SQAFVRLPE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 833 LLQNLGLVVTSFIIAFILNWRLTLVVLATYPLVISGHIS-----EKLFMQ--GYGGDLNKAYlkANMLAGesvsnirtva 905
Cdd:COG4615 128 LLQSVALVLGCLAYLAWLSPPLFLLTLVLLGLGVAGYRLlvrraRRHLRRarEAEDRLFKHF--RALLEG---------- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 906 afCAEEKI-----LELYSRELlEPSKSSFRRGQI-AGLFYGV----SQFFIFSSYGLALWYGSTLmdkgLAGFKSVMKTF 975
Cdd:COG4615 196 --FKELKLnrrrrRAFFDEDL-QPTAERYRDLRIrADTIFALannwGNLLFFALIGLILFLLPAL----GWADPAVLSGF 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 976 mVLIVTALA--MGETLALAPDLLKGN---QMVASVFEILDRKTQIVGETSEELNNVE-GTIELKGVHFSYPSRPDVVIFR 1049
Cdd:COG4615 269 -VLVLLFLRgpLSQLVGALPTLSRANvalRKIEELELALAAAEPAAADAAAPPAPADfQTLELRGVTYRYPGEDGDEGFT 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1050 --DFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIGLVQQEPALFATtiyeniL 1127
Cdd:COG4615 348 lgPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDR------L 421
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79487035 1128 YGNEGASQSEVVES--AMLANAHsfitslpegystKVGERG-----VQMSGGQRQRIAIARAILKNPAILLLDE 1194
Cdd:COG4615 422 LGLDGEADPARAREllERLELDH------------KVSVEDgrfstTDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1030-1249 |
5.16e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 70.11 E-value: 5.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYP-------------------SRPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVM 1090
Cdd:COG1134 5 IEVENVSKSYRlyhepsrslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1091 IEGKDIKKLDLKAlrkhiGLvqqEPALfatTIYENI-----LYGnegASQSE-------VVESAMLANahsFItSLPEG- 1157
Cdd:COG1134 85 VNGRVSALLELGA-----GF---HPEL---TGRENIylngrLLG---LSRKEidekfdeIVEFAELGD---FI-DQPVKt 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1158 YSTkvgergvqmsgGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVV-VAHRLSTIKN-ADT 1235
Cdd:COG1134 147 YSS-----------GMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIfVSHSMGAVRRlCDR 215
|
250
....*....|....
gi 79487035 1236 ISVLHGGKIVEQGS 1249
Cdd:COG1134 216 AIWLEKGRLVMDGD 229
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
401-619 |
5.31e-13 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 68.81 E-value: 5.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPS-RPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEP--ISGAVLLDGnniSELDIKWLRg 477
Cdd:cd03232 4 LTWKNLNYTVPVkGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILING---RPLDKNFQR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 478 QIGLVNQEPALFAT-TIRENILYgkddataeeitrAAKLseaisfinnlpegfetqvgeRGiqLSGGQKQRIAISRAIVK 556
Cdd:cd03232 80 STGYVEQQDVHSPNlTVREALRF------------SALL--------------------RG--LSVEQRKRLTIGVELAA 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79487035 557 NPSILLLDEATSALDAESEKSVQEALDRV-MVGRTTVVVAHRLSTV--RNADIIAVVHE-GKIVEFG 619
Cdd:cd03232 126 KPSILFLDEPTSGLDSQAAYNIVRFLKKLaDSGQAILCTIHQPSASifEKFDRLLLLKRgGKTVYFG 192
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
414-574 |
7.54e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 72.84 E-value: 7.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 414 PDVVIFDRLNLA-IPAGKIvALVGGSGSGKSTVISLIERFYEPISG-AVLLDGnniseldIKwlrgqIGLVNQEPALFAT 491
Cdd:PRK11819 18 PKKQILKDISLSfFPGAKI-GVLGLNGAGKSTLLRIMAGVDKEFEGeARPAPG-------IK-----VGYLPQEPQLDPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 492 -TIRENI-------------------LYGKDDATAEE-ITRAAKLSEAISFIN---------------NLPEGfETQVGe 535
Cdd:PRK11819 85 kTVRENVeegvaevkaaldrfneiyaAYAEPDADFDAlAAEQGELQEIIDAADawdldsqleiamdalRCPPW-DAKVT- 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 79487035 536 rgiQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAES 574
Cdd:PRK11819 163 ---KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
75-300 |
7.79e-13 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 70.51 E-value: 7.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 75 VLMTLGSVGAcihGASVPIFFiffGKLINIIGLAYLFPKQAS-HRVAKYSLDFVYLSVAILFSSWLEVACWMHTGERQAA 153
Cdd:cd18547 5 IILAIISTLL---SVLGPYLL---GKAIDLIIEGLGGGGGVDfSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 154 KMRRAYLRSMLSQDISLFDTEaSTGEVISAITSDILVVQDALSEKVGNFLHYISRFIAGFAIGFTSVWQISLVTLSIVPL 233
Cdd:cd18547 79 DLRKDLFEKLQRLPLSYFDTH-SHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79487035 234 IalaggiyAFVAIGLIARVRKSYIK----AGEI---AEEVIGNVRTVQAFTGEERAVRLYREALENTYKYGRKA 300
Cdd:cd18547 158 S-------LLVTKFIAKRSQKYFRKqqkaLGELngyIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKA 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1001-1245 |
8.42e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 72.37 E-value: 8.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1001 MV-ASVFEILDRKTQIVGETseelnnvegTIELKGVhfSYPSRPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLIL 1079
Cdd:COG3845 237 MVgREVLLRVEKAPAEPGEV---------VLEVENL--SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1080 RFYDPTAGKVMIEGKDIKKLDLKALRKH-IGLVQQEP---ALFAT-TIYENIL---YGNEGASQSEVV-ESAMLANAHSF 1150
Cdd:COG3845 306 GLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPEDRlgrGLVPDmSVAENLIlgrYRRPPFSRGGFLdRKAIRAFAEEL 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1151 ITSL---PEGYSTKVGergvQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVVVahrL 1227
Cdd:COG3845 386 IEEFdvrTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLL---I 458
|
250 260
....*....|....*....|...
gi 79487035 1228 ST-----IKNADTISVLHGGKIV 1245
Cdd:COG3845 459 SEdldeiLALSDRIAVMYEGRIV 481
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
413-636 |
1.01e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.58 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 413 RPDVVIFDRLNLAIPAGKIVALVGGSGSGKS-TVISLIeRFYEPISGAV-------------LLDGNNISELDIKWLRG- 477
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALM-RLLEQAGGLVqcdkmllrrrsrqVIELSEQSAAQMRHVRGa 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 478 QIGLVNQEPAL-----------FATTIRENILYGKDDATAEeitrAAKLSEAIsfinNLPEGfETQVGERGIQLSGGQKQ 546
Cdd:PRK10261 105 DMAMIFQEPMTslnpvftvgeqIAESIRLHQGASREEAMVE----AKRMLDQV----RIPEA-QTILSRYPHQLSGGMRQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 547 RIAISRAIVKNPSILLLDEATSALDAESEKSVQEaLDRVM---VGRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFGNHE 622
Cdd:PRK10261 176 RVMIAMALSCRPAVLIADEPTTALDVTIQAQILQ-LIKVLqkeMSMGVIFITHDMGVVAEiADRVLVMYQGEAVETGSVE 254
|
250
....*....|....
gi 79487035 623 NLISNPDGAYSSLL 636
Cdd:PRK10261 255 QIFHAPQHPYTRAL 268
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1048-1245 |
1.11e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.97 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1048 FRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLD-LKALRKHIGLV----QQEpALFAT-T 1121
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSpRDAIRAGIAYVpedrKGE-GLVLDlS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1122 IYENILYgnegASQSEVV------ESAMLANAHSFITSL---PEGYSTKVGergvQMSGGQRQRIAIARAILKNPAILLL 1192
Cdd:COG1129 347 IRENITL----ASLDRLSrgglldRRRERALAEEYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLIL 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 1193 DEATSALDVESERVVQQALDRLMANRTTVVVAhrlST-----IKNADTISVLHGGKIV 1245
Cdd:COG1129 419 DEPTRGIDVGAKAEIYRLIRELAAEGKAVIVI---SSelpelLGLSDRILVMREGRIV 473
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
398-637 |
1.17e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.91 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 398 DGHIQFKDATFSypsrpdvvifdrlnlaIPAGKIVALVGGSGSGKSTVislierfYEPISGAVLLDGNNISELDI---KW 474
Cdd:PRK15056 18 NGHTALRDASFT----------------VPGGSIAALVGVNGSGKSTL-------FKALMGFVRLASGKISILGQptrQA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 475 LRGQ-IGLVNQEPAL---FATTIRENILYGK-------DDATAEEitrAAKLSEAISFINNLpEGFETQVGErgiqLSGG 543
Cdd:PRK15056 75 LQKNlVAYVPQSEEVdwsFPVLVEDVVMMGRyghmgwlRRAKKRD---RQIVTAALARVDMV-EFRHRQIGE----LSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 544 QKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRVM-VGRTTVVVAHRLSTVRNADIIAVVHEGKIVEFGNHE 622
Cdd:PRK15056 147 QKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTE 226
|
250
....*....|....*..
gi 79487035 623 NLIS--NPDGAYSSLLR 637
Cdd:PRK15056 227 TTFTaeNLELAFSGVLR 243
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1025-1248 |
1.78e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 71.35 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1025 NVEGTIELKGVHFSYPSrpdVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLK-A 1103
Cdd:PRK09700 1 MATPYISMAGIGKSFGP---VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1104 LRKHIGLVQQEPALF-ATTIYENILYGNE------GASQSEVVESAMLANAHSFITSLPEGYSTKVGErgvqMSGGQRQR 1176
Cdd:PRK09700 78 AQLGIGIIYQELSVIdELTVLENLYIGRHltkkvcGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79487035 1177 IAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVV-VAHRLSTIKN-ADTISVLHGGKIVEQG 1248
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
401-618 |
1.81e-12 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 71.81 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPdvVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAV---------LLDGNNISELD 471
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmaVFSQHHVDGLD 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 472 IkwlrgqiglvNQEPALFATTIRENILygkddataEEITRAAKLSEAISfinnlpegfetqvGERGIQ----LSGGQKQR 547
Cdd:PLN03073 587 L----------SSNPLLYMMRCFPGVP--------EQKLRAHLGSFGVT-------------GNLALQpmytLSGGQKSR 635
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79487035 548 IAISRAIVKNPSILLLDEATSALDAESEKSVQEALdrVMVGRTTVVVAHRLSTVRNA-DIIAVVHEGKIVEF 618
Cdd:PLN03073 636 VAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGL--VLFQGGVLMVSHDEHLISGSvDELWVVSEGKVTPF 705
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1030-1247 |
1.83e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.19 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSrpdVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKH-I 1108
Cdd:PRK10762 5 LQLKGIDKAFPG---VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1109 GLVQQEPALFAT-TIYENILYGNEGASQSEVVE-SAMLANAHSFITSLPEGYSTK--VGErgvqMSGGQRQRIAIARAIL 1184
Cdd:PRK10762 82 GIIHQELNLIPQlTIAENIFLGREFVNRFGRIDwKKMYAEADKLLARLNLRFSSDklVGE----LSIGEQQMVEIAKVLS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 1185 KNPAILLLDEATSAL-DVESE---RVVQQALDRlmaNRTTVVVAHRLSTI-KNADTISVLHGGK-IVEQ 1247
Cdd:PRK10762 158 FESKVIIMDEPTDALtDTETEslfRVIRELKSQ---GRGIVYISHRLKEIfEICDDVTVFRDGQfIAER 223
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
409-574 |
1.83e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 71.50 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 409 SYPsrPDVVIFDRLNLA-IPAGKIvALVGGSGSGKSTVISLIERFYEPISG-AVLLDGnniseldIKwlrgqIGLVNQEP 486
Cdd:TIGR03719 13 VVP--PKKEILKDISLSfFPGAKI-GVLGLNGAGKSTLLRIMAGVDKDFNGeARPQPG-------IK-----VGYLPQEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 487 ALFAT-TIRENI-------------------LYGKDDATAEE-ITRAAKLSEAISFIN---------------NLPEGfE 530
Cdd:TIGR03719 78 QLDPTkTVRENVeegvaeikdaldrfneisaKYAEPDADFDKlAAEQAELQEIIDAADawdldsqleiamdalRCPPW-D 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 79487035 531 TQVGErgiqLSGGQKQRIAISRAIVKNPSILLLDEATSALDAES 574
Cdd:TIGR03719 157 ADVTK----LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1053-1258 |
2.45e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 67.98 E-value: 2.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1053 LIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDL-KALRKHIGLVQQEPALFA-TTIYENILYGN 1130
Cdd:PRK11614 26 LHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTaKIMREAVAIVPEGRRVFSrMTVEENLAMGG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1131 EGASQSEVVESamLANAHSFITSLPEGYSTKVGergvQMSGGQRQRIAIARAILKNPAILLLDEATSALdveSERVVQQA 1210
Cdd:PRK11614 106 FFAERDQFQER--IKWVYELFPRLHERRIQRAG----TMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL---APIIIQQI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 79487035 1211 LDRLMANR----TTVVVAHRLS-TIKNADTISVLHGGKIVEQGSHRKLVLNKS 1258
Cdd:PRK11614 177 FDTIEQLReqgmTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLANEA 229
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1043-1246 |
2.65e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 70.97 E-value: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1043 PDVVIFRDFDLIVRAGKSMALVGQSGSGKSS---VISLILRF--YDptaGKVMIEGKDIKKLDLKALRKH-IGLVQQEPA 1116
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTlmkVLSGVYPHgsYE---GEILFDGEVCRFKDIRDSEALgIVIIHQELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1117 LFA-TTIYENILYGNEGASQ-----SEVVESA--MLANAhsfitSLPEGYSTKVGERGVqmsgGQRQRIAIARAILKNPA 1188
Cdd:NF040905 89 LIPyLSIAENIFLGNERAKRgvidwNETNRRAreLLAKV-----GLDESPDTLVTDIGV----GKQQLVEIAKALSKDVK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79487035 1189 ILLLDEATSAL-DVESERVvqqaLDRLMANR----TTVVVAHRLSTI-KNADTISVLHGGKIVE 1246
Cdd:NF040905 160 LLILDEPTAALnEEDSAAL----LDLLLELKaqgiTSIIISHKLNEIrRVADSITVLRDGRTIE 219
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
747-958 |
2.82e-12 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 68.95 E-value: 2.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 747 KEIKKIAILFCCASVITLIVYTIEHICFGTMGERLTLRVRENMFRAILKNEIGWFDEvdNTSSMLASRLESD----ATLL 822
Cdd:cd18544 38 QGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDR--TPVGRLVTRVTNDtealNELF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 823 KTIVVDrstiLLQNLGLVVTSFIIAFILNWRLTLVVLATYPLVIsghisekLFMQGYGGDLNKAYLK-----ANMLA--G 895
Cdd:cd18544 116 TSGLVT----LIGDLLLLIGILIAMFLLNWRLALISLLVLPLLL-------LATYLFRKKSRKAYREvreklSRLNAflQ 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79487035 896 ESVSNIRTVAAFCAEEKILELYSRELLEPSKSSFRRGQIAGLFYGVSQFFIFSSYGLALWYGS 958
Cdd:cd18544 185 ESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGG 247
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
422-628 |
3.81e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 67.65 E-value: 3.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 422 LNLAIPAGKIVALVGGSGSGKSTVISLIERFYePISGAVLLDGNNISELDIKWL---RGQigLVNQEPALFATTIRENI- 497
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELarhRAY--LSQQQTPPFAMPVFQYLt 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 498 LYGKDDATAEEITRAakLSEAISFINnLPEGFETQVGergiQLSGGQKQRIAISRAIVK-----NPS--ILLLDEATSAL 570
Cdd:PRK03695 92 LHQPDKTRTEAVASA--LNEVAEALG-LDDKLGRSVN----QLSGGEWQRVRLAAVVLQvwpdiNPAgqLLLLDEPMNSL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79487035 571 D-AEseksvQEALDRVMV-----GRTTVVVAHRLS-TVRNADIIAVVHEGKIVEFGNHENLISNP 628
Cdd:PRK03695 165 DvAQ-----QAALDRLLSelcqqGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1044-1249 |
4.14e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 70.22 E-value: 4.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1044 DVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLI--LRFYDPTAGKVM-----------IE------------GKDIKK 1098
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIyhvalcekcgyVErpskvgepcpvcGGTLEP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1099 LDL----------KALRKHIGLVQQEPalFAttiyeniLYGNEgasqsEVVESAMlanahsfiTSLPE-GYStkvGERGV 1167
Cdd:TIGR03269 92 EEVdfwnlsdklrRRIRKRIAIMLQRT--FA-------LYGDD-----TVLDNVL--------EALEEiGYE---GKEAV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1168 QM---------------------SGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANR--TTVVVA 1224
Cdd:TIGR03269 147 GRavdliemvqlshrithiardlSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTS 226
|
250 260
....*....|....*....|....*.
gi 79487035 1225 HRLSTIKN-ADTISVLHGGKIVEQGS 1249
Cdd:TIGR03269 227 HWPEVIEDlSDKAIWLENGEIKEEGT 252
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
760-964 |
5.19e-12 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 68.27 E-value: 5.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 760 SVITLIVYTIEHIC----FGTMGeRLTLRVRENMFRAILKNEIGWFDEvdNTSSMLASRLESDATLLKTIVVDRSTILLQ 835
Cdd:cd18589 43 SLLTIASAVSEFVCdliyNITMS-RIHSRLQGLVFAAVLRQEIAFFDS--NQTGDIVSRVTTDTEDMSESLSENLSLLMW 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 836 NLGLVVTSFIIAFILNWRLTLVVLATYPLV-----ISGHiseklFMQGYGGDLNKAYLKANMLAGESVSNIRTVAAFCAE 910
Cdd:cd18589 120 YLARGLFLFIFMLWLSPKLALLTALGLPLLllvpkFVGK-----FQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANE 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 911 EKILELYSRELlepsKSSFRRGQIAGLFYGVSQFFI-FSSYGLA---LWYGSTLMDKG 964
Cdd:cd18589 195 EGEAQRYRQRL----QKTYRLNKKEAAAYAVSMWTSsFSGLALKvgiLYYGGQLVTAG 248
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
401-565 |
7.04e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 69.62 E-value: 7.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRPDVVifDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIG 480
Cdd:PRK10522 323 LELRNVTFAYQDNGFSV--GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 LVNQEPALFATTIrENILYGKDDATAEEITRAAKLSEAISFINNlpegfetQVgeRGIQLSGGQKQRIAISRAIVKNPSI 560
Cdd:PRK10522 401 AVFTDFHLFDQLL-GPEGKPANPALVEKWLERLKMAHKLELEDG-------RI--SNLKLSKGQKKRLALLLALAEERDI 470
|
....*
gi 79487035 561 LLLDE 565
Cdd:PRK10522 471 LLLDE 475
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
752-956 |
7.85e-12 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 67.53 E-value: 7.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 752 IAILFCCASVITLIVYTIEHICfGTMGERLTLRVRENMFRAILKNEIGWFDevDNTSSMLASRLESDATLLKTIVVDRST 831
Cdd:cd18563 46 VLGLAGAYVLSALLGILRGRLL-ARLGERITADLRRDLYEHLQRLSLSFFD--KRQTGSLMSRVTSDTDRLQDFLSDGLP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 832 ILLQNLGLVVTSFIIAFILNWRLTLVVLATYPLVIsghisekLFMQGYGGDLNKAYLKA-------NMLAGESVSNIRTV 904
Cdd:cd18563 123 DFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVV-------WGSYFFWKKIRRLFHRQwrrwsrlNSVLNDTLPGIRVV 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 79487035 905 AAFCAEEKILELYSRELLEPSKSSFRRGQIAGLFYGVSQfFIFSSYGLALWY 956
Cdd:cd18563 196 KAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLT-FLTSLGTLIVWY 246
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1048-1244 |
8.95e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 69.31 E-value: 8.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1048 FRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKAlRKHIGLV-----QQEPALFA-TT 1121
Cdd:PRK15439 279 FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-RLARGLVylpedRQSSGLYLdAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1122 IYENI---LYGNEGASQSEVVESAMLanahsfitslpEGYSTKVG------ERGVQ-MSGGQRQRIAIARAILKNPAILL 1191
Cdd:PRK15439 358 LAWNVcalTHNRRGFWIKPARENAVL-----------ERYRRALNikfnhaEQAARtLSGGNQQKVLIAKCLEASPQLLI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 79487035 1192 LDEATSALDVESERVVQQALDRLMANRTTVV-VAHRLSTI-KNADTISVLHGGKI 1244
Cdd:PRK15439 427 VDEPTRGVDVSARNDIYQLIRSIAAQNVAVLfISSDLEEIeQMADRVLVMHQGEI 481
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
418-621 |
1.19e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 66.35 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 418 IFDRLNLAIPAGKIVALVGGSGSGKSTVISLI--ERFYEPISGAVLLDGNNISELDIKWLRGQ-IGLVNQEPA------- 487
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPEDRAGEgIFMAFQYPVeipgvsn 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 488 -LFATTIRENILYGKDDATAEEITRAAKLSEAISFINnLPEGFETQVGERGiqLSGGQKQRIAISRAIVKNPSILLLDEA 566
Cdd:PRK09580 96 qFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLK-MPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPELCILDES 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 567 TSALDAESEKSVQEALDRVMVG-RTTVVVAH--RLSTVRNADIIAVVHEGKIVEFGNH 621
Cdd:PRK09580 173 DSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDF 230
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
147-325 |
1.50e-11 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 66.77 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 147 TGERQAAKMRRAYLRSMlsQDISL-FDTEASTGEVISAITSDILVVQDALSEKVGNFLHYISRFIAGFAIGFTSVWQISL 225
Cdd:cd18564 81 VGQRVVLDLRRDLFAHL--QRLSLsFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLAL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 226 VTLSIVPLIALAggiyAFVAIGLI-ARVRKSYIKAGEIA---EEVIGNVRTVQAFTGEERAVRLYREALENTYKYGRKAG 301
Cdd:cd18564 159 IALAVAPLLLLA----ARRFSRRIkEASREQRRREGALAsvaQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAA 234
|
170 180
....*....|....*....|....
gi 79487035 302 LTKGLGLGSMHCVLFLSWALLVWF 325
Cdd:cd18564 235 RLQALLSPVVDVLVAVGTALVLWF 258
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
147-325 |
1.59e-11 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 66.69 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 147 TGERQAAKMRRAYLRSMLSQDISLFDTeASTGEVISAITSDILVVQDALSEKVGNFLHYISRFIAGFAIGFTSVWQISLV 226
Cdd:cd18542 66 ASQKVAYDLRNDLYDHLQRLSFSFHDK-ARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 227 TLSIVPLIalaggiyAFVAIGLIARVRKSYIKAGE-------IAEEVIGNVRTVQAFTGEERAVRLYREALENTYKYGRK 299
Cdd:cd18542 145 SLAIIPFI-------ALFSYVFFKKVRPAFEEIREqegelntVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIK 217
|
170 180
....*....|....*....|....*.
gi 79487035 300 AGLTKGLGLGSMHCVLFLSWALLVWF 325
Cdd:cd18542 218 LAKLLAKYWPLMDFLSGLQIVLVLWV 243
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
417-619 |
1.70e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 66.39 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 417 VIFDRLNLAIPAGKIVALVGGSGSGKSTVI-SLIERFYEP-------ISGAVLLDGNNISELDIKWLRGQIGLVNQ--EP 486
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLkALAGDLTGGgaprgarVTGDVTLNGEPLAAIDAPRLARLRAVLPQaaQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 487 AlFATTIRENILYGK----------DDATAEEITRAAKLSEAisfinnlpegfETQVGERGIQLSGGQKQRIAISRAIVK 556
Cdd:PRK13547 95 A-FAFSAREIVLLGRypharragalTHRDGEIAWQALALAGA-----------TALVGRDVTTLSGGELARVQFARVLAQ 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79487035 557 ---------NPSILLLDEATSALDAESEKSVQEALDRVM----VGRTTVVVAHRLSTvRNADIIAVVHEGKIVEFG 619
Cdd:PRK13547 163 lwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLArdwnLGVLAIVHDPNLAA-RHADRIAMLADGAIVAHG 237
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1052-1260 |
1.71e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 65.78 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1052 DLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKL-DLKALRKhiGLVQ--QEPALFAT-TIYENIL 1127
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpGHQIARM--GVVRtfQHVRLFREmTVIENLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1128 ygnegASQSEVVESAMLA---NAHSFITSLPEG------YSTKVGERGV------QMSGGQRQRIAIARAILKNPAILLL 1192
Cdd:PRK11300 103 -----VAQHQQLKTGLFSgllKTPAFRRAESEAldraatWLERVGLLEHanrqagNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79487035 1193 DEATSALDVESERVVQQALDRLmanrttvvvahrlstiKNADTISVL---HGGKIVEQGSHRKLVLNKSGP 1260
Cdd:PRK11300 178 DEPAAGLNPKETKELDELIAEL----------------RNEHNVTVLlieHDMKLVMGISDRIYVVNQGTP 232
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
421-570 |
2.26e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 65.29 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 421 RLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDI-KWLRGQIGLVNQEPALFA-TTIRENIL 498
Cdd:PRK11614 23 EVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTaKIMREAVAIVPEGRRVFSrMTVEENLA 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79487035 499 YG----KDDATAEEITRAAKLseaisfinnLPEGFETQVgERGIQLSGGQKQRIAISRAIVKNPSILLLDEATSAL 570
Cdd:PRK11614 103 MGgffaERDQFQERIKWVYEL---------FPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
408-589 |
2.84e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 64.20 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 408 FSYPSRPdvvIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISElDIKWLRGQIGLVNQEPA 487
Cdd:PRK13540 9 FDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHRSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 488 LFAT-TIRENILYG-KDDATAEEITRAAKLSEAISFInNLPEGFetqvgergiqLSGGQKQRIAISRAIVKNPSILLLDE 565
Cdd:PRK13540 85 INPYlTLRENCLYDiHFSPGAVGITELCRLFSLEHLI-DYPCGL----------LSSGQKRQVALLRLWMSKAKLWLLDE 153
|
170 180
....*....|....*....|....
gi 79487035 566 ATSALDaesEKSVQEALDRVMVGR 589
Cdd:PRK13540 154 PLVALD---ELSLLTIITKIQEHR 174
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1044-1249 |
3.39e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 65.05 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1044 DVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRF--YDPTAGKVMIEGKDIKKLD--------------------- 1100
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEpeerahlgiflafqypieipg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1101 ----------LKALRKHIGLVQQEPALFATTIYENIlygnegasqsEVVEsaMLAnahSFIT-SLPEGYStkvgergvqm 1169
Cdd:CHL00131 99 vsnadflrlaYNSKRKFQGLPELDPLEFLEIINEKL----------KLVG--MDP---SFLSrNVNEGFS---------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1170 sGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLM-ANRTTVVVAH--RLSTIKNADTISVLHGGKIVE 1246
Cdd:CHL00131 154 -GGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIK 232
|
...
gi 79487035 1247 QGS 1249
Cdd:CHL00131 233 TGD 235
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1051-1261 |
3.41e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 66.08 E-value: 3.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1051 FDLIVRAGKSMALVGQSGSGKSSVISLILRFYDP----TAGKVMIEGKDIKKLDLKALRK----HIGLVQQEP------- 1115
Cdd:COG4170 26 VSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERRKiigrEIAMIFQEPsscldps 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1116 ---------ALFATTiYENILYGNEGASQSEVVEsaMLANA----HSFI-TSLPEgystkvgergvQMSGGQRQRIAIAR 1181
Cdd:COG4170 106 akigdqlieAIPSWT-FKGKWWQRFKWRKKRAIE--LLHRVgikdHKDImNSYPH-----------ELTEGECQKVMIAM 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1182 AILKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVV--VAHRLSTIKN-ADTISVLHGGKIVEQGSHRKLVLNKS 1258
Cdd:COG4170 172 AIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSIllISHDLESISQwADTITVLYCGQTVESGPTEQILKSPH 251
|
...
gi 79487035 1259 GPY 1261
Cdd:COG4170 252 HPY 254
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1029-1254 |
3.50e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 67.30 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1029 TIELKGVHFSYPSRPDVVifRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHI 1108
Cdd:PRK10522 322 TLELRNVTFAYQDNGFSV--GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1109 GLVQQEPALFATtiyeniLYGNEG-ASQSEVVES--AMLANAHSfiTSLPEGYSTKvgergVQMSGGQRQRIAIARAILK 1185
Cdd:PRK10522 400 SAVFTDFHLFDQ------LLGPEGkPANPALVEKwlERLKMAHK--LELEDGRISN-----LKLSKGQKKRLALLLALAE 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79487035 1186 NPAILLLDEATSALDVESERVVQQALDRLM--ANRTTVVVAHRLSTIKNADTISVLHGGKIVE-QGSHRKLV 1254
Cdd:PRK10522 467 ERDILLLDEWAADQDPHFRREFYQVLLPLLqeMGKTIFAISHDDHYFIHADRLLEMRNGQLSElTGEERDAA 538
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
126-289 |
4.07e-11 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 65.67 E-value: 4.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 126 FVYLSVAILFS-------SWLEVACWMHTGERQAAKMRRAYLRSMLSQDISLFDTEaSTGEVISAITSDILVVQDALSEK 198
Cdd:cd18565 53 LWLLGGLTVAAflleslfQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDR-QTGDLMSVLNNDVNQLERFLDDG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 199 VGNFLHYISRFIAGFAIGFTSVWQISLVTLSIVPLIALAGGIYAFVAIGLIARVRKSyikAGEIA---EEVIGNVRTVQA 275
Cdd:cd18565 132 ANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREA---VGDLNarlENNLSGIAVIKA 208
|
170 180
....*....|....*....|.
gi 79487035 276 FTGE-------ERAVRLYREA 289
Cdd:cd18565 209 FTAEdferervADASEEYRDA 229
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
414-617 |
4.39e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.86 E-value: 4.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 414 PDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIK-WLRGQIGLVNQE----PAL 488
Cdd:PRK11288 15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGVAIIYQElhlvPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 489 fatTIRENILYGKDDATAEEITRAAKLSEAISFINNLPEGF--ETQVGErgiqLSGGQKQRIAISRAIVKNPSILLLDEA 566
Cdd:PRK11288 95 ---TVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIdpDTPLKY----LSIGQRQMVEIAKALARNARVIAFDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 567 TSALDA-ESEKsvqeaLDRVMV-----GRTTVVVAHRLSTV-RNADIIAVVHEGKIVE 617
Cdd:PRK11288 168 TSSLSArEIEQ-----LFRVIRelraeGRVILYVSHRMEEIfALCDAITVFKDGRYVA 220
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1036-1248 |
4.69e-11 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 64.28 E-value: 4.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1036 HFSYPSRPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKlDLKALRKHIGLV--QQ 1113
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWK-RRKKFLRRIGVVfgQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1114 E------PAL----FATTIYeNILYGNEGASQSEVVEsaMLANAHSFITSLpegystkvgeRgvQMSGGQRQRIAIARAI 1183
Cdd:cd03267 104 TqlwwdlPVIdsfyLLAAIY-DLPPARFKKRLDELSE--LLDLEELLDTPV----------R--QLSLGQRMRAEIAAAL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 1184 LKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVVV--AHRLSTI-KNADTISVLHGGKIVEQG 1248
Cdd:cd03267 169 LHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLltSHYMKDIeALARRVLVIDKGRLLYDG 236
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
415-616 |
5.63e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 66.77 E-value: 5.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 415 DVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYE--PISGAVLLDGNNISELDIKWL-RGQIGLVNQEPALFAT 491
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 492 -TIRENILYGKD-------DATAEEITRAAKLSEAISfINNLPEgfETQVGERGiqlsGGQKQRIAISRAIVKNPSILLL 563
Cdd:TIGR02633 93 lSVAENIFLGNEitlpggrMAYNAMYLRAKNLLRELQ-LDADNV--TRPVGDYG----GGQQQLVEIAKALNKQARLLIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 564 DEATSALdaeSEKSVQEALDRV----MVGRTTVVVAHRLSTVRN-ADIIAVVHEGKIV 616
Cdd:TIGR02633 166 DEPSSSL---TEKETEILLDIIrdlkAHGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1041-1224 |
5.66e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 63.28 E-value: 5.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1041 SRPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKL------DLKALRKHIGLvqqE 1114
Cdd:PRK13538 10 ERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrdeyhqDLLYLGHQPGI---K 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1115 PALfatTIYENILYGnegASQSEVVESAMLANAhsfitsLpegysTKVGERGV------QMSGGQRQRIAIARAILKNPA 1188
Cdd:PRK13538 87 TEL---TALENLRFY---QRLHGPGDDEALWEA------L-----AQVGLAGFedvpvrQLSAGQQRRVALARLWLTRAP 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 79487035 1189 ILLLDEATSALDVESERVVQQALDRLMANRTTVVVA 1224
Cdd:PRK13538 150 LWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILT 185
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
391-664 |
6.34e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 66.50 E-value: 6.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 391 GRKLG-KVdghIQFKDATFSYPSRpdvVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLdGNNIse 469
Cdd:TIGR03719 315 GPRLGdKV---IEAENLTKAFGDK---LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV-- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 470 ldikwlrgQIGLVNQE-PALFAT-TIRENILYGKD--DATAEEITRAAKLSeAISFinnlpEGFETQ--VGergiQLSGG 543
Cdd:TIGR03719 386 --------KLAYVDQSrDALDPNkTVWEEISGGLDiiKLGKREIPSRAYVG-RFNF-----KGSDQQkkVG----QLSGG 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 544 QKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRvmVGRTTVVVAH------RLSTvrnaDIIAVVHEGKIVE 617
Cdd:TIGR03719 448 ERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLN--FAGCAVVISHdrwfldRIAT----HILAFEGDSHVEW 521
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 79487035 618 F-GNHENLISNpdgaysSLLRLQETAslqrnpslnrtlSRPHSIKYSR 664
Cdd:TIGR03719 522 FeGNFSEYEED------KKRRLGEDA------------DQPHRIKYKK 551
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1055-1245 |
7.43e-11 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 62.65 E-value: 7.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1055 VRAGKSMALVGQSGSGKSSVIS-LILRFYDPT-AGKVMIEGKDIKkldlKALRKHIGLVQQEPALFAT-TIYENILYgne 1131
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDvLAGRKTAGViTGEILINGRPLD----KNFQRSTGYVEQQDVHSPNlTVREALRF--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1132 gasqsevveSAMLanahsfitslpegystkvgeRGvqMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQAL 1211
Cdd:cd03232 103 ---------SALL--------------------RG--LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFL 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 79487035 1212 DRL-MANRTTVVVAHRLS--TIKNADTISVLH-GGKIV 1245
Cdd:cd03232 152 KKLaDSGQAILCTIHQPSasIFEKFDRLLLLKrGGKTV 189
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1048-1248 |
9.16e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.13 E-value: 9.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1048 FRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKldlkALRKH-IGLVQQEPAL---FATTIY 1123
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ----ALQKNlVAYVPQSEEVdwsFPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1124 ENILYGNEG---------ASQSEVVESAMLAnahsfiTSLPEGYSTKVGErgvqMSGGQRQRIAIARAILKNPAILLLDE 1194
Cdd:PRK15056 99 DVVMMGRYGhmgwlrrakKRDRQIVTAALAR------VDMVEFRHRQIGE----LSGGQKKRVFLARAIAQQGQVILLDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 79487035 1195 ATSALDVESERVVQQALDRLMAN-RTTVVVAHRLSTIKNADTISVLHGGKIVEQG 1248
Cdd:PRK15056 169 PFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
93-296 |
1.01e-10 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 64.39 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 93 IFFIFFGKLINIIGLAY----------LFPKQASHRVAKYSLDFVYLSVAILFSSWLeVACWMHT-GERQAAKMRRAYLR 161
Cdd:cd18549 5 FLDLFCAVLIAALDLVFplivryiiddLLPSKNLRLILIIGAILLALYILRTLLNYF-VTYWGHVmGARIETDMRRDLFE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 162 SMLSQDISLFDtEASTGEVISAITSDILvvqdalseKVGNFLHY--------ISRFIAGFAIGFTSVWQISLVTLSIVPL 233
Cdd:cd18549 84 HLQKLSFSFFD-NNKTGQLMSRITNDLF--------DISELAHHgpedlfisIITIIGSFIILLTINVPLTLIVFALLPL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79487035 234 IAlaggIYAFVAIG-LIARVRKSYIKAGEI---AEEVIGNVRTVQAFTGEE-------RAVRLYREALENTYKY 296
Cdd:cd18549 155 MI----IFTIYFNKkMKKAFRRVREKIGEInaqLEDSLSGIRVVKAFANEEyeiekfdEGNDRFLESKKKAYKA 224
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1041-1212 |
1.05e-10 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 62.38 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1041 SRPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRkHIGLVQQEPALFAT 1120
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHE-NILYLGHLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1121 -TIYENILYGNE-GASQSEVVESAMLANAHSFITSLPEGystkvgergvQMSGGQRQRIAIARAILKNPAILLLDEATSA 1198
Cdd:TIGR01189 88 lSALENLHFWAAiHGGAQRTIEDALAAVGLTGFEDLPAA----------QLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170
....*....|....
gi 79487035 1199 LDVESERVVQQALD 1212
Cdd:TIGR01189 158 LDKAGVALLAGLLR 171
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
420-693 |
1.15e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 64.38 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 420 DRLNLAIPAGKIVALVGGSGSGKS----TVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIG----LVNQEPAlfaT 491
Cdd:PRK11022 24 DRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLVGaevaMIFQDPM---T 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 492 TIRENILYGKDDATAEEI----TRAAKLSEAISFInnlpegfeTQVGergI------------QLSGGQKQRIAISRAIV 555
Cdd:PRK11022 101 SLNPCYTVGFQIMEAIKVhqggNKKTRRQRAIDLL--------NQVG---IpdpasrldvyphQLSGGMSQRVMIAMAIA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 556 KNPSILLLDEATSALDAESEKSVQEALDRVMVGRTT--VVVAHRLSTV-RNADIIAVVHEGKIVEFGNHENLISNPDGAY 632
Cdd:PRK11022 170 CRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMalVLITHDLALVaEAAHKIIVMYAGQVVETGKAHDIFRAPRHPY 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 633 S-SLLR-LQETASLQrnpslNRTLSRPHSI--KYSRE---LSRTRSSFCSERESVTRPD-GADPSKKVK 693
Cdd:PRK11022 250 TqALLRaLPEFAQDK-----ARLASLPGVVpgKYDRPngcLLNPRCPYATDRCRAEEPAlNMLAGRQSK 313
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1047-1226 |
1.17e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 62.67 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1047 IFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIGLVQQEPALFattiyeni 1126
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASLIDAIGRKGDFKDAV-------- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1127 lygnegasqsEVVESAMLANAHSFITSLPEgystkvgergvqMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERV 1206
Cdd:COG2401 117 ----------ELLNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKR 174
|
170 180
....*....|....*....|..
gi 79487035 1207 VQQALDRLM--ANRTTVVVAHR 1226
Cdd:COG2401 175 VARNLQKLArrAGITLVVATHH 196
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
414-617 |
1.36e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 65.20 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 414 PDVVIFDRLNLAIPAGKIVALVGGSGSGKST---VISLIERF--YEpisGAVLLDGNNISELDIK--WLRGqIGLVNQEP 486
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTlmkVLSGVYPHgsYE---GEILFDGEVCRFKDIRdsEALG-IVIIHQEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 487 ALFA-TTIRENILYGKDDAT------AEEITRAAKLSEAIsfinNLPEGFETQVGERGIqlsgGQKQRIAISRAIVKNPS 559
Cdd:NF040905 88 ALIPyLSIAENIFLGNERAKrgvidwNETNRRARELLAKV----GLDESPDTLVTDIGV----GKQQLVEIAKALSKDVK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79487035 560 ILLLDEATSAL-DAESEKsvqeALDRVM----VGRTTVVVAHRLSTVRN-ADIIAVVHEGKIVE 617
Cdd:NF040905 160 LLILDEPTAALnEEDSAA----LLDLLLelkaQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
401-656 |
1.38e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.19 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSrpdVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKwLRGQ-- 478
Cdd:PRK09700 6 ISMAGIGKSFGP---VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK-LAAQlg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 479 IGLVNQEPALF-ATTIRENILYGKDDAT----------AEEITRAAKLSEAISFINNLpegfETQVGErgiqLSGGQKQR 547
Cdd:PRK09700 82 IGIIYQELSVIdELTVLENLYIGRHLTKkvcgvniidwREMRVRAAMMLLRVGLKVDL----DEKVAN----LSISHKQM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 548 IAISRAIVKNPSILLLDEATSAL-DAESEKsvqeaLDRVM-----VGRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFGN 620
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSLtNKEVDY-----LFLIMnqlrkEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGM 228
|
250 260 270
....*....|....*....|....*....|....*..
gi 79487035 621 HENlISNPDgayssLLRLQETASLQ-RNPSLNRTLSR 656
Cdd:PRK09700 229 VSD-VSNDD-----IVRLMVGRELQnRFNAMKENVSN 259
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
412-584 |
1.56e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 62.13 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 412 SRPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRgqiglvnqepalfat 491
Cdd:PRK13538 10 ERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQ--------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 492 tireNILY-G-----KDDATAEEITR-AAKLS-----EAIsfINNLpegfeTQVGERGI------QLSGGQKQRIAISRA 553
Cdd:PRK13538 75 ----DLLYlGhqpgiKTELTALENLRfYQRLHgpgddEAL--WEAL-----AQVGLAGFedvpvrQLSAGQQRRVALARL 143
|
170 180 190
....*....|....*....|....*....|.
gi 79487035 554 IVKNPSILLLDEATSALDAESEKSVQEALDR 584
Cdd:PRK13538 144 WLTRAPLWILDEPFTAIDKQGVARLEALLAQ 174
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
753-960 |
2.61e-10 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 63.30 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 753 AILFCCASVITLIVYT-----IEHICFGTMGERLTLRVRENMFRAILKNEIGWFDEvdNTSSMLASRLESDATLLKTIVV 827
Cdd:cd18564 52 LLLLAAAALVGIALLRglasyAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDR--RRTGDLLSRLTGDVGAIQDLLV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 828 DRSTILLQNLGLVVTSFIIAFILNWRLTLVVLATYPLVIsghisekLFMQGYGGDLNKAYLKANM-------LAGESVSN 900
Cdd:cd18564 130 SGVLPLLTNLLTLVGMLGVMFWLDWQLALIALAVAPLLL-------LAARRFSRRIKEASREQRRregalasVAQESLSA 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79487035 901 IRTVAAFCAEEKILELYSREllepSKSSFRRG----QIAGLFYGVSQFFIFSSYGLALWYGSTL 960
Cdd:cd18564 203 IRVVQAFGREEHEERRFARE----NRKSLRAGlraaRLQALLSPVVDVLVAVGTALVLWFGAWL 262
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1050-1225 |
3.08e-10 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 62.04 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1050 DFDLIVRAG---KS--MALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDI--KKLDLKAlrKHIGLVQQepalFATTI 1122
Cdd:cd03237 12 EFTLEVEGGsisESevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVsyKPQYIKA--DYEGTVRD----LLSSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1123 YENilYGNEGASQSEVVESAMLanahsfitslpegysTKVGERGV-QMSGGQRQRIAIARAILKNPAILLLDEATSALDV 1201
Cdd:cd03237 86 TKD--FYTHPYFKTEIAKPLQI---------------EQILDREVpELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
170 180
....*....|....*....|....*.
gi 79487035 1202 ESERVVQQALDRLM--ANRTTVVVAH 1225
Cdd:cd03237 149 EQRLMASKVIRRFAenNEKTAFVVEH 174
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
1049-1249 |
3.19e-10 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 62.25 E-value: 3.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1049 RDFDLIVRAGKSMALVGQSGSGKSSVISLILrfYDPTAGKVMIEGKDIKKLD----LKALRKHIgLVQQEP--------- 1115
Cdd:cd03271 12 KNIDVDIPLGVLTCVTGVSGSGKSSLINDTL--YPALARRLHLKKEQPGNHDriegLEHIDKVI-VIDQSPigrtprsnp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1116 ----ALFaTTIYE----------------NILYgnEGASQSEVVEsaMLAN-AHSFITSLPE-------------GYsTK 1161
Cdd:cd03271 89 atytGVF-DEIRElfcevckgkrynretlEVRY--KGKSIADVLD--MTVEeALEFFENIPKiarklqtlcdvglGY-IK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1162 VGERGVQMSGGQRQRIAIARAILK---NPAILLLDEATSALDVESERVVQQALDRLMANRTTVVVA-HRLSTIKNADTIS 1237
Cdd:cd03271 163 LGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIeHNLDVIKCADWII 242
|
250
....*....|....*...
gi 79487035 1238 VL------HGGKIVEQGS 1249
Cdd:cd03271 243 DLgpeggdGGGQVVASGT 260
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1058-1243 |
3.79e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.13 E-value: 3.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1058 GKSMALVGQSGSGKSSVISLIL-RFYDPT-AGKVMIEGKDIKKLDLKalrkHIGLVQQEPALFA-TTIYENILYGNEGAS 1134
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANNRKPTKQILK----RTGFVTQDDILYPhLTVRETLVFCSLLRL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1135 QSEVVESAMLANAHSFITSL--PEGYSTKVGE---RGVqmSGGQRQRIAIARAILKNPAILLLDEATSALDVESE-RVVQ 1208
Cdd:PLN03211 170 PKSLTKQEKILVAESVISELglTKCENTIIGNsfiRGI--SGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAyRLVL 247
|
170 180 190
....*....|....*....|....*....|....*..
gi 79487035 1209 QALDRLMANRTTVVVAHRLST--IKNADTISVLHGGK 1243
Cdd:PLN03211 248 TLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGR 284
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
752-964 |
4.03e-10 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 62.49 E-value: 4.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 752 IAILFCCASVITLIVYTIEHICFGTMGERLTLRVRENMFRAILKNEIGWFDEVDNTSSMlaSRLESDATLLKTIVVDRST 831
Cdd:cd18545 42 IALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKIL--SRVINDVNSLSDLLSNGLI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 832 ILLQNLGLVVTSFIIAFILNWRLTLVVLATYPLVIsghisekLFMQGYGGDLNKAYLK-----ANMLAG--ESVSNIRTV 904
Cdd:cd18545 120 NLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLV-------LVVFLLRRRARKAWQRvrkkiSNLNAYlhESISGIRVI 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 905 AAFCAEEKILELYSRELLEPSKSSFRRGQIAGLFYGVSQFFIFSSYGLALWYGSTLMDKG 964
Cdd:cd18545 193 QSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTALVYWYGGKLVLGG 252
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1018-1249 |
4.96e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 61.73 E-value: 4.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1018 ETSEELNNVEGTIELKGVHFSypsRPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIK 1097
Cdd:PRK15112 2 ETLLEVRNLSKTFRYRTGWFR---RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1098 KLDLKALRKHIGLVQQEPAlfaTTIyenilygNEGASQSEVVESAMLANahsfiTSL-PEGYSTKVGE--RGV------- 1167
Cdd:PRK15112 79 FGDYSYRSQRIRMIFQDPS---TSL-------NPRQRISQILDFPLRLN-----TDLePEQREKQIIEtlRQVgllpdha 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1168 -----QMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANR--TTVVVAHRLSTIKN-ADTISVL 1239
Cdd:PRK15112 144 syyphMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQgiSYIYVTQHLGMMKHiSDQVLVM 223
|
250
....*....|
gi 79487035 1240 HGGKIVEQGS 1249
Cdd:PRK15112 224 HQGEVVERGS 233
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1035-1258 |
5.46e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 60.35 E-value: 5.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1035 VHFSYPSRPdvvIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKlDLKALRKHIGLVQQE 1114
Cdd:PRK13540 7 LDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1115 PALFAT-TIYENILYGNEGASQS-EVVESAMLANAHSFItSLPEGYstkvgergvqMSGGQRQRIAIARAILKNPAILLL 1192
Cdd:PRK13540 83 SGINPYlTLRENCLYDIHFSPGAvGITELCRLFSLEHLI-DYPCGL----------LSSGQKRQVALLRLWMSKAKLWLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79487035 1193 DEATSALDvesERVVQQALDRLMANRTtvvvahrlstiknadtisvlHGGKIVEQgSHRKLVLNKS 1258
Cdd:PRK13540 152 DEPLVALD---ELSLLTIITKIQEHRA--------------------KGGAVLLT-SHQDLPLNKA 193
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1041-1211 |
5.71e-10 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 60.20 E-value: 5.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1041 SRPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDlKALRKHIGLVQQEPALFAT 1120
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQR-DSIARGLLYLGHAPGIKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1121 -TIYENILYGNEGASQSEVVESamLAnahsfitslpegystKVGERGV------QMSGGQRQRIAIARAILKNPAILLLD 1193
Cdd:cd03231 88 lSVLENLRFWHADHSDEQVEEA--LA---------------RVGLNGFedrpvaQLSAGQQRRVALARLLLSGRPLWILD 150
|
170
....*....|....*...
gi 79487035 1194 EATSALDVESERVVQQAL 1211
Cdd:cd03231 151 EPTTALDKAGVARFAEAM 168
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1040-1248 |
6.27e-10 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 60.35 E-value: 6.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1040 PSRPDVVIFRDFDLIVRAGKSMALVGQSGSGKSS---VISLILRFYDPTAGKVMIEGKDIKKLDLKAlRKHIGLVQQEPA 1116
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkALANRTEGNVSVEGDIHYNGIPYKEFAEKY-PGEIIYVSEEDV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1117 LFATTIYEnilygnegasqsEVVESAMLANAHSFItslpegystkvgeRGVqmSGGQRQRIAIARAILKNPAILLLDEAT 1196
Cdd:cd03233 94 HFPTLTVR------------ETLDFALRCKGNEFV-------------RGI--SGGERKRVSIAEALVSRASVLCWDNST 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79487035 1197 SALDVEServvqqALD-----RLMAN--RTTVVVAhrLS-----TIKNADTISVLHGGKIVEQG 1248
Cdd:cd03233 147 RGLDSST------ALEilkciRTMADvlKTTTFVS--LYqasdeIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
745-960 |
6.67e-10 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 61.66 E-value: 6.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 745 TQKEIKKIAILFCCASVITLIVYTIEHICFGTMGERLTLRVRENMFRAILKNEIGWFDEvdNTSSMLASRLESDatlLKT 824
Cdd:cd18541 35 TASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQK--NRTGDLMARATND---LNA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 825 IvvdRSTI------LLQNLGLVVTSFIIAFILNWRLTLVVLATYPLVIsghisekLFMQGYGGDLNKAYLKA-------N 891
Cdd:cd18541 110 V---RMALgpgilyLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLA-------LLVYRLGKKIHKRFRKVqeafsdlS 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 892 MLAGESVSNIRTVAAFCAEEKILELYSRELLEPSKSSFRRGQIAGLFYGVSQFFIFSSYGLALWYGSTL 960
Cdd:cd18541 180 DRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRL 248
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1049-1268 |
7.01e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 62.03 E-value: 7.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1049 RDFDLIVRAGKSMALVGQSGSGKSSVISL---ILRfydPTAGKVMIEGKDIKKlDLKALRKHIGLV----QQ-------- 1113
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMltgILV---PTSGEVRVLGYVPFK-RRKEFARRIGVVfgqrSQlwwdlpai 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1114 ------------EPALFATTIyenilygnegasqSEVVEsaMLaNAHSFITslpegysTKVgeRgvQMSGGQRQRIAIAR 1181
Cdd:COG4586 115 dsfrllkaiyriPDAEYKKRL-------------DELVE--LL-DLGELLD-------TPV--R--QLSLGQRMRCELAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1182 AILKNPAILLLDEATSALDVESERVVQQALDRLMANR-TTVVVA-HRLSTIKN-ADTISVLHGGKIVEQGSHRKLVlNKS 1258
Cdd:COG4586 168 ALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgTTILLTsHDMDDIEAlCDRVIVIDHGRIIYDGSLEELK-ERF 246
|
250
....*....|
gi 79487035 1259 GPYfKLISLQ 1268
Cdd:COG4586 247 GPY-KTIVLE 255
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1046-1251 |
8.11e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.38 E-value: 8.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1046 VIFRDFDLIVRAGKSMALVGQSGSGKSSVI-SLILRFYDPTA-------GKVMIEGKDIKKLDLKAL-RKHIGLVQQEPA 1116
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLkALAGDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLaRLRAVLPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1117 LFATTIYENILYG--------NEGASQSEVVESAMLANAhsfitslpeGYSTKVGERGVQMSGGQRQRIAIARAILK--- 1185
Cdd:PRK13547 95 AFAFSAREIVLLGrypharraGALTHRDGEIAWQALALA---------GATALVGRDVTTLSGGELARVQFARVLAQlwp 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1186 ------NPAILLLDEATSALDVESERvvqqaldRLMANRTTVVVAHRLSTI----------KNADTISVLHGGKIVEQGS 1249
Cdd:PRK13547 166 phdaaqPPRYLLLDEPTAALDLAHQH-------RLLDTVRRLARDWNLGVLaivhdpnlaaRHADRIAMLADGAIVAHGA 238
|
..
gi 79487035 1250 HR 1251
Cdd:PRK13547 239 PA 240
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
429-608 |
1.06e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 58.15 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 429 GKIVALVGGSGSGKSTVISLIERFYEPISGAVL-LDGNNISELDIKWLRGQIglvnqepalfattirenilygkddatae 507
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIyIDGEDILEEVLDQLLLII---------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 508 eitraaklseaisfinnlpegfetqVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRVMV 587
Cdd:smart00382 54 -------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLL 108
|
170 180
....*....|....*....|....*..
gi 79487035 588 ------GRTTVVVAHRLSTVRNADIIA 608
Cdd:smart00382 109 lllkseKNLTVILTTNDEKDLGPALLR 135
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
397-599 |
1.21e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 62.46 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 397 VDGHIQFKDATFSYPSRpDVVIfDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYePISGAVLldgnniseldIKWLR 476
Cdd:TIGR00954 448 QDNGIKFENIPLVTPNG-DVLI-ESLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGRL----------TKPAK 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 477 GQIGLVNQEPALFATTIRENILYgkDDATAEEITRAAKLSEAISFINNLPEG--FETQVGERGIQ-----LSGGQKQRIA 549
Cdd:TIGR00954 515 GKLFYVPQRPYMTLGTLRDQIIY--PDSSEDMKRRGLSDKDLEQILDNVQLThiLEREGGWSAVQdwmdvLSGGEKQRIA 592
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 79487035 550 ISRAIVKNPSILLLDEATSALDAESEKSVQEALDRvmVGRTTVVVAHRLS 599
Cdd:TIGR00954 593 MARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHRKS 640
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
749-915 |
1.24e-09 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 60.88 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 749 IKKIAILFCCASVITLIVYTIEHICFGTMGERLTLRVRENMFRAILKNEIGWFDEvdNTSSMLASRLESDA-----TLLK 823
Cdd:cd18547 44 LLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDT--HSHGDIMSRVTNDVdnisqALSQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 824 TIvvdrsTILLQNLGLVVTSFIIAFILNWRLTLVVLATYPL------VISGHiSEKLFM--QGYGGDLNkAYLKanmlag 895
Cdd:cd18547 122 SL-----TQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLsllvtkFIAKR-SQKYFRkqQKALGELN-GYIE------ 188
|
170 180
....*....|....*....|
gi 79487035 896 ESVSNIRTVAAFCAEEKILE 915
Cdd:cd18547 189 EMISGQKVVKAFNREEEAIE 208
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1048-1241 |
1.32e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.52 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1048 FRDFDL-IVRAGKSMALVGQSGSGKSSVISL--------------------ILRFYdptAGKVMIEG-KDIKKLDLKALR 1105
Cdd:PRK13409 88 FKLYGLpIPKEGKVTGILGPNGIGKTTAVKIlsgelipnlgdyeeepswdeVLKRF---RGTELQNYfKKLYNGEIKVVH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1106 KhIGLVQQEPALFATTIYENILYGNEGASQSEVVESAMLANahsfitslpegystkVGERGV-QMSGGQRQRIAIARAIL 1184
Cdd:PRK13409 165 K-PQYVDLIPKVFKGKVRELLKKVDERGKLDEVVERLGLEN---------------ILDRDIsELSGGELQRVAIAAALL 228
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 1185 KNPAILLLDEATSALDVEsERV-VQQALDRLMANRTTVVVAHRLSTIKN-ADTISVLHG 1241
Cdd:PRK13409 229 RDADFYFFDEPTSYLDIR-QRLnVARLIRELAEGKYVLVVEHDLAVLDYlADNVHIAYG 286
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1054-1241 |
1.41e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 60.07 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1054 IVRAGKSMALVGQSGSGKSSVISL--------------------ILRFYDPTAGKVMIEgkDIKKLDLKALRKhIGLVQQ 1113
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKIlagklkpnlgkfddppdwdeILDEFRGSELQNYFT--KLLEGDVKVIVK-PQYVDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1114 EPALFATTIYENILYGNEGASQSEVVESAMLanahsfitslpegysTKVGERGV-QMSGGQRQRIAIARAILKNPAILLL 1192
Cdd:cd03236 99 IPKAVKGKVGELLKKKDERGKLDELVDQLEL---------------RHVLDRNIdQLSGGELQRVAIAAALARDADFYFF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 79487035 1193 DEATSALDVESERVVQQALDRLMA-NRTTVVVAHRLSTIKN-ADTISVLHG 1241
Cdd:cd03236 164 DEPSSYLDIKQRLNAARLIRELAEdDNYVLVVEHDLAVLDYlSDYIHCLYG 214
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
127-295 |
2.05e-09 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 60.17 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 127 VYLSVAIL--FSSWLEVACWMHTGERQAAKMRRAYLRSMLSQDISLFDTEaSTGEVISAITSDILVVQDALSEKVGNFLH 204
Cdd:cd18545 45 LFLALNLVnwVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSR-PVGKILSRVINDVNSLSDLLSNGLINLIP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 205 YISRFIAGFAIGFTSVWQISLVTLSIVPLIALaggiyafVAIGLIARVRKSYIKA--------GEIAEEVIGnVRTVQAF 276
Cdd:cd18545 124 DLLTLVGIVIIMFSLNVRLALVTLAVLPLLVL-------VVFLLRRRARKAWQRVrkkisnlnAYLHESISG-IRVIQSF 195
|
170
....*....|....*....
gi 79487035 277 TGEERAVRLYREALENTYK 295
Cdd:cd18545 196 AREDENEEIFDELNRENRK 214
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1030-1227 |
2.18e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 59.74 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRpdvVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKdikkldlkaLRkhIG 1109
Cdd:PRK09544 5 VSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1110 LVQQEPALFAT---TIyENILYGNEGASQSEVVESAMLANAHSFItslpegystkvgERGVQ-MSGGQRQRIAIARAILK 1185
Cdd:PRK09544 71 YVPQKLYLDTTlplTV-NRFLRLRPGTKKEDILPALKRVQAGHLI------------DAPMQkLSGGETQRVLLARALLN 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 79487035 1186 NPAILLLDEATSALDVESERVVQQALDRLMA--NRTTVVVAHRL 1227
Cdd:PRK09544 138 RPQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDL 181
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
752-964 |
2.54e-09 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 59.91 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 752 IAILFCCASVITLIVYTIEHICFGTMGERLTLRVRENMFRAILKNEIGWFDEvdNTSSMLASRLeSDATLLKTIVVDRST 831
Cdd:cd18782 44 IGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDK--RPVGELSTRI-SELDTIRGFLTGTAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 832 ILLQNLGLVVTSFIIAFILNWRLTLVVLATYPLVIsghiseklFMQGYGGDLNKAYLKANMLAG--------ESVSNIRT 903
Cdd:cd18782 121 TTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQL--------LLTFLFGPILRRQIRRRAEASaktqsylvESLTGIQT 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79487035 904 VAAFCAEEKILELYSRELLEPSKSSFRRGQIAGLFYGVSQFFIFSSYGLALWYGSTLMDKG 964
Cdd:cd18782 193 VKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSLLVLWVGAYLVLRG 253
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
422-607 |
3.32e-09 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 59.17 E-value: 3.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 422 LNLAIPAGKIVALVGGSGSGKSTVIslIERFYEPISGAVLLDGNNISELDIKWLRGQIG---LVNQEP------------ 486
Cdd:cd03271 14 IDVDIPLGVLTCVTGVSGSGKSSLI--NDTLYPALARRLHLKKEQPGNHDRIEGLEHIDkviVIDQSPigrtprsnpaty 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 487 -ALFaTTIRE----------------NILY-GKD-----DATAEEitrAAKLSEAISFINNLPEGFET------QVGERG 537
Cdd:cd03271 92 tGVF-DEIRElfcevckgkrynretlEVRYkGKSiadvlDMTVEE---ALEFFENIPKIARKLQTLCDvglgyiKLGQPA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79487035 538 IQLSGGQKQRIAISRAIVK---NPSILLLDEATSALDAESEKSVQEALDR-VMVGRTTVVVAHRLSTVRNADII 607
Cdd:cd03271 168 TTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRlVDKGNTVVVIEHNLDVIKCADWI 241
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1030-1250 |
4.63e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 58.65 E-value: 4.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRPdvvIFRDFDLIVRAGKSMALVGQSGSGKSSVISLIL--RFYDPTAGKVMIEGKDIKKLDLKALR-K 1106
Cdd:PRK09580 2 LSIKDLHVSVEDKA---ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPEDRAgE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1107 HIGLVQQEPA--------LFATTIYeNILYGNEGASQSEVVESAMLANAHSFITSLPEGYSTKvgERGVQMSGGQRQRIA 1178
Cdd:PRK09580 79 GIFMAFQYPVeipgvsnqFFLQTAL-NAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTR--SVNVGFSGGEKKRND 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79487035 1179 IARAILKNPAILLLDEATSALDVESERVVQQALDRLM-ANRTTVVVAHR---LSTIKnADTISVLHGGKIVEQGSH 1250
Cdd:PRK09580 156 ILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRdGKRSFIIVTHYqriLDYIK-PDYVHVLYQGRIVKSGDF 230
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
752-965 |
9.19e-09 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 58.26 E-value: 9.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 752 IAILFCCASVITLIVYTIEHICfGTMGERLTLRVRENMFRAI--L------KNEIGWfdevdntssmLASRLESDATLLK 823
Cdd:cd18540 45 ILLYLGLILIQALSVFLFIRLA-GKIEMGVSYDLRKKAFEHLqtLsfsyfdKTPVGW----------IMARVTSDTQRLG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 824 TIV----VDrstiLLQNLGLVVTSFIIAFILNWRLTLVVLATYPL--VISghisekLFMQgyggdlnKAYLKAN------ 891
Cdd:cd18540 114 EIIswglVD----LVWGITYMIGILIVMLILNWKLALIVLAVVPVlaVVS------IYFQ-------KKILKAYrkvrki 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 892 --MLAG---ESVSNIRTVAAFCAEEKILELYSRELLEPSKSSFRRGQIAGLFYGVSQFFIFSSYGLALWYGSTLMDKGL 965
Cdd:cd18540 177 nsRITGafnEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIATALVLWYGGILVLAGA 255
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
382-616 |
9.19e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 59.66 E-value: 9.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 382 TVTKTSAKSGRKLGKVDGhiqfkdatFSYPSRPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLI--ERfyEPISGA 459
Cdd:COG3845 245 RVEKAPAEPGEVVLEVEN--------LSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGS 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 460 VLLDGNNISELDIKWLRGQ-IGLVNQEP---ALFAT-TIRENIL--------YGK----DDATAEEitRAAKLSEA--IS 520
Cdd:COG3845 315 IRLDGEDITGLSPRERRRLgVAYIPEDRlgrGLVPDmSVAENLIlgryrrppFSRggflDRKAIRA--FAEELIEEfdVR 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 521 finnlPEGFETQVGergiQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEAL----DRvmvGRTTVVVAH 596
Cdd:COG3845 393 -----TPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLlelrDA---GAAVLLISE 460
|
250 260
....*....|....*....|.
gi 79487035 597 RLSTVRN-ADIIAVVHEGKIV 616
Cdd:COG3845 461 DLDEILAlSDRIAVMYEGRIV 481
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
411-619 |
1.03e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 56.50 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 411 PSRPDVVIFDRLNLAIPAGKIVALVGGSGSGKST---VISLIERFYEPISGAVLLDGNNISELDIKWlRGQIGLVNQEPA 487
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkALANRTEGNVSVEGDIHYNGIPYKEFAEKY-PGEIIYVSEEDV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 488 LFAT-TIRENIlygkddataeEITRAAKLSEAIsfinnlpegfetqvgeRGIqlSGGQKQRIAISRAIVKNPSILLLDEA 566
Cdd:cd03233 94 HFPTlTVRETL----------DFALRCKGNEFV----------------RGI--SGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79487035 567 TSALDAESeksvqeALDRVMVGRTtvvVAHRLSTVRNA-------------DIIAVVHEGKIVEFG 619
Cdd:cd03233 146 TRGLDSST------ALEILKCIRT---MADVLKTTTFVslyqasdeiydlfDKVLVLYEGRQIYYG 202
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
404-578 |
1.07e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.12 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 404 KDATFSYP-SRPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVIS-LIERfyepISGAVLLDGNNIS---ELDIKWLRgQ 478
Cdd:TIGR00956 763 RNLTYEVKiKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNvLAER----VTTGVITGGDRLVngrPLDSSFQR-S 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 479 IGLVNQEPALFAT-TIRENILYGKDDATAEEITRAAKLS--EAISFINNLPEGFETQVGERGIQLSGGQKQRIAISRAIV 555
Cdd:TIGR00956 838 IGYVQQQDLHLPTsTVRESLRFSAYLRQPKSVSKSEKMEyvEEVIKLLEMESYADAVVGVPGEGLNVEQRKRLTIGVELV 917
|
170 180
....*....|....*....|....
gi 79487035 556 KNPSILL-LDEATSALDAESEKSV 578
Cdd:TIGR00956 918 AKPKLLLfLDEPTSGLDSQTAWSI 941
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1032-1225 |
1.90e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 58.41 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1032 LKGVHFSYPsrPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVIslilrfydptagKVM------IEGKDIKKLDLKalr 1105
Cdd:TIGR03719 7 MNRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLL------------RIMagvdkdFNGEARPQPGIK--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1106 khIGLVQQEPALFAT-TIYENI-------------------LYGNEGAS-------QSEVVESAMLANAHSFITSL---- 1154
Cdd:TIGR03719 70 --VGYLPQEPQLDPTkTVRENVeegvaeikdaldrfneisaKYAEPDADfdklaaeQAELQEIIDAADAWDLDSQLeiam 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79487035 1155 -----PEGySTKVGErgvqMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMAnrTTVVVAH 1225
Cdd:TIGR03719 148 dalrcPPW-DADVTK----LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG--TVVAVTH 216
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
415-618 |
2.01e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 58.64 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 415 DVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGavlldgnniselDIKWLRG-QIGLVNQEPALFattI 493
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSG------------EIGLAKGiKLGYFAQHQLEF---L 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 494 RenilygKDDATAEEITRAAKlSEAISFINNLPEGFETQ---VGERGIQLSGGQKQRIAISRAIVKNPSILLLDEATSAL 570
Cdd:PRK10636 389 R------ADESPLQHLARLAP-QELEQKLRDYLGGFGFQgdkVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHL 461
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 79487035 571 DAESEKSVQEALdrVMVGRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEF 618
Cdd:PRK10636 462 DLDMRQALTEAL--IDFEGALVVVSHDRHLLRStTDDLYLVHDGKVEPF 508
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
429-619 |
2.08e-08 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 56.65 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 429 GKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNIS----ELDIKwlrgqiglvnqepalFATTIREnILYGKDDA 504
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqYIKAD---------------YEGTVRD-LLSSITKD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 505 TAE------EITRAAKLSEAISfiNNLPEgfetqvgergiqLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSV 578
Cdd:cd03237 89 FYThpyfktEIAKPLQIEQILD--REVPE------------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 79487035 579 QEALDRVMVG--RTTVVVAHrlsTVRNADIIA---VVHEGKIVEFG 619
Cdd:cd03237 155 SKVIRRFAENneKTAFVVEH---DIIMIDYLAdrlIVFEGEPSVNG 197
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
147-325 |
2.36e-08 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 57.01 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 147 TGERQAAKMRRAYLRSMLSQDISLFDTEaSTGEVISAITSDILVVQDALSEKVGNFLHYISRFIAGFAIGFTSVWQISLV 226
Cdd:cd18544 68 LGQRIIYDLRRDLFSHIQRLPLSFFDRT-PVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 227 TLSIVPLIALAGGIYAFVAIGLIARVRKSyikageIAE------EVIGNVRTVQAFTGEERAVRLYREALENTYKYGRKA 300
Cdd:cd18544 147 SLLVLPLLLLATYLFRKKSRKAYREVREK------LSRlnaflqESISGMSVIQLFNREKREFEEFDEINQEYRKANLKS 220
|
170 180
....*....|....*....|....*
gi 79487035 301 GLTKGLGLGSMHCVLFLSWALLVWF 325
Cdd:cd18544 221 IKLFALFRPLVELLSSLALALVLWY 245
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1058-1239 |
2.49e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 54.30 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1058 GKSMALVGQSGSGKSSVISLILRFYDPTAGKV-MIEGKDIKKLDLKALRKHIglvqqepalfattiyenilygnegasqs 1136
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGViYIDGEDILEEVLDQLLLII---------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1137 evvesamlanahsfitslpegystkVGERGVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLM- 1215
Cdd:smart00382 54 -------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLl 108
|
170 180 190
....*....|....*....|....*....|
gi 79487035 1216 ------ANRTTVVVAHRLSTIKNADTISVL 1239
Cdd:smart00382 109 lllkseKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1047-1263 |
2.99e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.58 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1047 IFRDFDLIVRAGKSMALVGQSGSGKS----SVISLILRFYDPTAGKVMIEGkdikkLDLKALRKH-----IGLVQQEPAL 1117
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCStllkTIASNTDGFHIGVEGVITYDG-----ITPEEIKKHyrgdvVYNAETDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1118 FATTIYENILY-------GNEGASQSEVVESAMLANAHSFITSLPEGYSTKVGE---RGVqmSGGQRQRIAIARAILKNP 1187
Cdd:TIGR00956 151 PHLTVGETLDFaarcktpQNRPDGVSREEYAKHIADVYMATYGLSHTRNTKVGNdfvRGV--SGGERKRVSIAEASLGGA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1188 AILLLDEATSALDVEServvqqALDRLMANRTTVVVAHRLSTI------KNA----DTISVLHGGKIVEQGShrklvLNK 1257
Cdd:TIGR00956 229 KIQCWDNATRGLDSAT------ALEFIRALKTSANILDTTPLVaiyqcsQDAyelfDKVIVLYEGYQIYFGP-----ADK 297
|
....*.
gi 79487035 1258 SGPYFK 1263
Cdd:TIGR00956 298 AKQYFE 303
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
752-960 |
3.13e-08 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 56.69 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 752 IAILFCCASVITLIVYTIEHICFGTMGERLTLRVRENMFRAILKNEIGWFDevdntsSM----LASRLeSDATLLKTIVV 827
Cdd:cd18570 44 ISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFE------TRktgeIISRF-NDANKIREAIS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 828 DRSTILLQNLGLVVTSFIIAFILNWRLTLVVLATYPL-VISGHISEKLF-------MQGYggdlnkAYLKANMLagESVS 899
Cdd:cd18570 117 STTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLyILIILLFNKPFkkknrevMESN------AELNSYLI--ESLK 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79487035 900 NIRTVAAFCAEEKILELYSRELLEPSKSSFRRGQIaGLFYGVSQFFIFSSYGLA-LWYGSTL 960
Cdd:cd18570 189 GIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKL-SNLQSSIKGLISLIGSLLiLWIGSYL 249
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
412-598 |
3.63e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.71 E-value: 3.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 412 SRPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKwlRGQ---IGLVNQEPAL 488
Cdd:PRK10762 13 AFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPK--SSQeagIGIIHQELNL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 489 FAT-TIRENILYGKDDATA-------EEITRAAKLSEAIsfinNLPEGFETQVGErgiqLSGGQKQRIAISRAIVKNPSI 560
Cdd:PRK10762 91 IPQlTIAENIFLGREFVNRfgridwkKMYAEADKLLARL----NLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 79487035 561 LLLDEATSAL-DAESeksvqEALDRVM-----VGRTTVVVAHRL 598
Cdd:PRK10762 163 IIMDEPTDALtDTET-----ESLFRVIrelksQGRGIVYISHRL 201
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
126-288 |
3.89e-08 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 56.34 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 126 FVYLSVAILFSSWLEVACWMHTGERQAAKMRRAYLRSMLSQDISLFDTEAStGEVISAITSDIlvvqDALSEKVGNFLhy 205
Cdd:cd18546 45 YLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHERETS-GRIMTRMTSDI----DALSELLQTGL-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 206 ISRFIAGFAIGFTSV------WQISLVTLSIVPLIALAGGIYAFVAIGLIARVRKsyikagEIAE------EVIGNVRTV 273
Cdd:cd18546 118 VQLVVSLLTLVGIAVvllvldPRLALVALAALPPLALATRWFRRRSSRAYRRARE------RIAAvnadlqETLAGIRVV 191
|
170
....*....|....*
gi 79487035 274 QAFTGEERAVRLYRE 288
Cdd:cd18546 192 QAFRRERRNAERFAE 206
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1167-1241 |
4.77e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 54.12 E-value: 4.77e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 1167 VQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLM--ANRTTVVVAHRLSTIKN-ADTISVLHG 1241
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSeeGKKTALVVEHDLAVLDYlSDRIHVFEG 147
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
745-964 |
4.90e-08 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 55.92 E-value: 4.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 745 TQKEIKKIAILfccaSVITLIVYTIEHIC------FG-TMGERLTLRVRENMFRAILKNEIGWFDEvdNTSSMLASRLES 817
Cdd:cd18549 34 PSKNLRLILII----GAILLALYILRTLLnyfvtyWGhVMGARIETDMRRDLFEHLQKLSFSFFDN--NKTGQLMSRITN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 818 DatLLK----------TIVVdrSTILLqnlglvVTSFIIAFILNWRLTLVVLATYPLVIsghisekLFMQGYGGDLNKAY 887
Cdd:cd18549 108 D--LFDiselahhgpeDLFI--SIITI------IGSFIILLTINVPLTLIVFALLPLMI-------IFTIYFNKKMKKAF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 888 LKA-------NMLAGESVSNIRTVAAFCAEEKILELYSR---ELLEPSKSSFRrgqIAGLFYGVSQFFIFSSYGLALWYG 957
Cdd:cd18549 171 RRVrekigeiNAQLEDSLSGIRVVKAFANEEYEIEKFDEgndRFLESKKKAYK---AMAYFFSGMNFFTNLLNLVVLVAG 247
|
....*..
gi 79487035 958 STLMDKG 964
Cdd:cd18549 248 GYFIIKG 254
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1041-1245 |
5.78e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.05 E-value: 5.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1041 SRPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIK-KLDLKALRKHIGLVQQEPALF- 1118
Cdd:PRK10982 7 SFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQELNLVl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1119 ATTIYENILYGNEGASQSEVVESAMLANAHSFITSLPEGYSTKvgERGVQMSGGQRQRIAIARAILKNPAILLLDEATSA 1198
Cdd:PRK10982 87 QRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPR--AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 79487035 1199 LdveSERVVQ---QALDRLMANRTTVV-VAHRLSTI-KNADTISVLHGGKIV 1245
Cdd:PRK10982 165 L---TEKEVNhlfTIIRKLKERGCGIVyISHKMEEIfQLCDEITILRDGQWI 213
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1030-1211 |
6.98e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 57.18 E-value: 6.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRPdvVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGK---------DIKKLD 1100
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKvrmavfsqhHVDGLD 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1101 LKAlrkhiglvqqEPALFATTIYENilygnegasqseVVESAMLANAHSFITSlpegystkvGERGVQ----MSGGQRQR 1176
Cdd:PLN03073 587 LSS----------NPLLYMMRCFPG------------VPEQKLRAHLGSFGVT---------GNLALQpmytLSGGQKSR 635
|
170 180 190
....*....|....*....|....*....|....*
gi 79487035 1177 IAIARAILKNPAILLLDEATSALDVESERVVQQAL 1211
Cdd:PLN03073 636 VAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGL 670
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1157-1249 |
7.72e-08 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 56.95 E-value: 7.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1157 GYsTKVGERGVQMSGGQRQRIAIARAILK---NPAILLLDEATSALDVESERVVQQALDRLMANRTTVVV-AHRLSTIKN 1232
Cdd:TIGR00630 819 GY-IRLGQPATTLSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVViEHNLDVIKT 897
|
90 100
....*....|....*....|...
gi 79487035 1233 ADTISVL------HGGKIVEQGS 1249
Cdd:TIGR00630 898 ADYIIDLgpeggdGGGTVVASGT 920
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
752-964 |
8.61e-08 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 55.19 E-value: 8.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 752 IAILFCCASVITLIVYTIEHICFGTMGERLTLRVRENMFRAILKNEIGWFDEvdNTSSMLASRLESD----ATLLKTIVV 827
Cdd:cd18546 41 AAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHER--ETSGRIMTRMTSDidalSELLQTGLV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 828 DrstiLLQNLGLVVTSFIIAFILNWRLTLVVLATYPL-----VISGHISeklfmqgyggdlNKAYLKANMLAG------- 895
Cdd:cd18546 119 Q----LVVSLLTLVGIAVVLLVLDPRLALVALAALPPlalatRWFRRRS------------SRAYRRARERIAavnadlq 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 896 ESVSNIRTVAAFCAEEKILELYSRELLEPSKSSFRRGQIAGLFYGVSQFFIFSSYGLALWYGSTLMDKG 964
Cdd:cd18546 183 ETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWRVAAG 251
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
155-289 |
9.22e-08 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 55.18 E-value: 9.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 155 MRRAYLRSMLSQDISLFDtEASTGEVISAITSDILVVQDALS---EKVGNFLHyisrFIAGFAIGFTSVWQISLVTLSIV 231
Cdd:cd18543 74 LRTDLFAHLQRLDGAFHD-RWQSGQLLSRATSDLSLVQRFLAfgpFLLGNLLT----LVVGLVVMLVLSPPLALVALASL 148
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 232 PLIALAGgiyafvaigliARVRKSYI--------KAGEIA---EEVIGNVRTVQAFTGEERAVRLYREA 289
Cdd:cd18543 149 PPLVLVA-----------RRFRRRYFpasrraqdQAGDLAtvvEESVTGIRVVKAFGRERRELDRFEAA 206
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
424-611 |
9.50e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 54.68 E-value: 9.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 424 LAIPA-GKIVALVGGSGSGKSTVISLIE--------RFYEPISGAVLLDGNNISELDI---KWLRGQIGL------VNQE 485
Cdd:cd03236 20 LPVPReGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDEFRGSELQNyftKLLEGDVKVivkpqyVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 486 PALFATTIREnILYGKDD-ATAEEITRAAKLseaisfinnlpegfeTQVGERGI-QLSGGQKQRIAISRAIVKNPSILLL 563
Cdd:cd03236 100 PKAVKGKVGE-LLKKKDErGKLDELVDQLEL---------------RHVLDRNIdQLSGGELQRVAIAAALARDADFYFF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 79487035 564 DEATSALDAESEKSVQEAL-DRVMVGRTTVVVAHRLSTVRN-ADIIAVVH 611
Cdd:cd03236 164 DEPSSYLDIKQRLNAARLIrELAEDDNYVLVVEHDLAVLDYlSDYIHCLY 213
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1030-1225 |
1.10e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.18 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRPdvvIFRDFDLIVRAGKSMALVGQSGSGKSSVISLIL----RFYdptAGKVMIEGK---------DI 1096
Cdd:PRK10938 261 IVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpQGY---SNDLTLFGRrrgsgetiwDI 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1097 KKldlkalrkHIGLVQQEPAL---FATTIYENILYG---NEGASQSevVESAMLANAHSFITSLpeGYSTKVGERGVQ-M 1169
Cdd:PRK10938 335 KK--------HIGYVSSSLHLdyrVSTSVRNVILSGffdSIGIYQA--VSDRQQKLAQQWLDIL--GIDKRTADAPFHsL 402
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 1170 SGGQrQRIA-IARAILKNPAILLLDEATSALDVESERVVQQALDRLMANRTT--VVVAH 1225
Cdd:PRK10938 403 SWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqlLFVSH 460
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
426-619 |
1.18e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.66 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 426 IPAGKIVALVGGSGSGKST----VISLIERFYEPISGAVLLDGnnISELDI-KWLRGQI-----------GLVNQEPALF 489
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTllktIASNTDGFHIGVEGVITYDG--ITPEEIkKHYRGDVvynaetdvhfpHLTVGETLDF 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 490 ATTIR--ENILYGKDdataeEITRAAKLSEAISFINNLPEGFETQVGE---RGIqlSGGQKQRIAISRAIVKNPSILLLD 564
Cdd:TIGR00956 162 AARCKtpQNRPDGVS-----REEYAKHIADVYMATYGLSHTRNTKVGNdfvRGV--SGGERKRVSIAEASLGGAKIQCWD 234
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79487035 565 EATSALDAESeksvqeALDRVMVGRTTVVVAHRLSTV------RNA----DIIAVVHEGKIVEFG 619
Cdd:TIGR00956 235 NATRGLDSAT------ALEFIRALKTSANILDTTPLVaiyqcsQDAyelfDKVIVLYEGYQIYFG 293
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1041-1202 |
1.22e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 53.70 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1041 SRPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKalrKHIGLVQQEPALFAT 1120
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS---RFMAYLGHLPGLKAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1121 -TIYENI--LYGNEGASQSEVVESAMLanahsfITSLPEGYSTKVGergvQMSGGQRQRIAIARAILKNPAILLLDEATS 1197
Cdd:PRK13543 97 lSTLENLhfLCGLHGRRAKQMPGSALA------IVGLAGYEDTLVR----QLSAGQKKRLALARLWLSPAPLWLLDEPYA 166
|
....*
gi 79487035 1198 ALDVE 1202
Cdd:PRK13543 167 NLDLE 171
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
400-606 |
1.24e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.79 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 400 HIQFKDATFSYPSRPdvvIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIE----RFYepiSGAVLL------DGNNIse 469
Cdd:PRK10938 260 RIVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpQGY---SNDLTLfgrrrgSGETI-- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 470 LDIKwlrGQIGLVNQEPAL---FATTIRENILYGKDDATAeeITRA---AKLSEAISFINNLpeGFETQVGERGIQ-LSG 542
Cdd:PRK10938 332 WDIK---KHIGYVSSSLHLdyrVSTSVRNVILSGFFDSIG--IYQAvsdRQQKLAQQWLDIL--GIDKRTADAPFHsLSW 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 543 GQkQRIA-ISRAIVKNPSILLLDEATSALDAESEKSVQEALDrVMV--GRTTVV------------VAHRLSTVRNADI 606
Cdd:PRK10938 405 GQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVD-VLIseGETQLLfvshhaedapacITHRLEFVPDGDI 481
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1048-1241 |
1.33e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.95 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1048 FRDFDL-IVRAGKSMALVGQSGSGKSSVISL--------------------ILRFYdptAGKVMIEG-KDIKKLDLKALR 1105
Cdd:COG1245 88 FRLYGLpVPKKGKVTGILGPNGIGKSTALKIlsgelkpnlgdydeepswdeVLKRF---RGTELQDYfKKLANGEIKVAH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1106 KhIGLVQQEPALFATTIYENILYGNEGASQSEVVESAMLANahsfitslpegystkVGERGV-QMSGGQRQRIAIARAIL 1184
Cdd:COG1245 165 K-PQYVDLIPKVFKGTVRELLEKVDERGKLDELAEKLGLEN---------------ILDRDIsELSGGELQRVAIAAALL 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1185 KNPAILLLDEATSALDVeSERV-VQQALDRLM-ANRTTVVVAHRLSTI-KNADTISVLHG 1241
Cdd:COG1245 229 RDADFYFFDEPSSYLDI-YQRLnVARLIRELAeEGKYVLVVEHDLAILdYLADYVHILYG 287
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
419-622 |
1.36e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 55.79 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 419 FDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGnniSELDIK----WLRGQIGLVN---QEPALFAT 491
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDG---KPVRIRsprdAIRAGIAYVPedrKGEGLVLD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 492 -TIRENILYG--KDDATAEEITRAAKLSEAISFINNL---PEGFETQVGergiQLSGGQKQRIAISRAIVKNPSILLLDE 565
Cdd:COG1129 345 lSIRENITLAslDRLSRGGLLDRRRERALAEEYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDE 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79487035 566 ATSALD--AESE--KSVQEALDRvmvGRTTVVVahrlST-----VRNADIIAVVHEGKIV-EFGNHE 622
Cdd:COG1129 421 PTRGIDvgAKAEiyRLIRELAAE---GKAVIVI----SSelpelLGLSDRILVMREGRIVgELDREE 480
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
391-668 |
2.15e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.12 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 391 GRKLG-KVdghIQFKDATFSYPSRpdvVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLdGNNIse 469
Cdd:PRK11819 317 GPRLGdKV---IEAENLSKSFGDR---LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV-- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 470 ldikwlrgQIGLVNQEpalfattiRENIlygKDDATaeeitraakLSEAISfinnlpEGFET-QVGERGI---------- 538
Cdd:PRK11819 388 --------KLAYVDQS--------RDAL---DPNKT---------VWEEIS------GGLDIiKVGNREIpsrayvgrfn 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 539 -----------QLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRvmVGRTTVVVAH------RLSTv 601
Cdd:PRK11819 434 fkggdqqkkvgVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLE--FPGCAVVISHdrwfldRIAT- 510
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79487035 602 rnaDIIAVVHEGKIVEF-GN----HENLISnpdgayssllRLQETAslqrnpslnrtlSRPHSIKYsRELSR 668
Cdd:PRK11819 511 ---HILAFEGDSQVEWFeGNfqeyEEDKKR----------RLGADA------------ARPHRIKY-KKLTR 556
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
780-920 |
2.17e-07 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 54.03 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 780 RLTLRV----RENMFRAILKNEIGWFDEVDntSSMLASRLESDATLLKTIVVdRSTILLQNLGLVVTSFIIAFILNWRLT 855
Cdd:cd18543 65 RLSLGVehdlRTDLFAHLQRLDGAFHDRWQ--SGQLLSRATSDLSLVQRFLA-FGPFLLGNLLTLVVGLVVMLVLSPPLA 141
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79487035 856 LVVLATYP-LVISGHISEKLFM------QGYGGDLnkaylkaNMLAGESVSNIRTVAAFCAEEKILELYSRE 920
Cdd:cd18543 142 LVALASLPpLVLVARRFRRRYFpasrraQDQAGDL-------ATVVEESVTGIRVVKAFGRERRELDRFEAA 206
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1031-1235 |
2.36e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.34 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1031 ELKGVHFSYPsrpDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIeGKdikKLDLKALRKHIGL 1110
Cdd:PRK11147 321 EMENVNYQID---GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GT---KLEVAYFDQHRAE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1111 VQQEpalfaTTIYENIlygNEGASQSEV--VESAMLANAHSFITSlPEGYSTKVGergvQMSGGQRQRIAIARAILKNPA 1188
Cdd:PRK11147 394 LDPE-----KTVMDNL---AEGKQEVMVngRPRHVLGYLQDFLFH-PKRAMTPVK----ALSGGERNRLLLARLFLKPSN 460
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 79487035 1189 ILLLDEATSALDVEServvQQALDRLMANR--TTVVVAHRLSTIKNADT 1235
Cdd:PRK11147 461 LLILDEPTNDLDVET----LELLEELLDSYqgTVLLVSHDRQFVDNTVT 505
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
401-601 |
2.76e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 53.19 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 401 IQFKDATFSYPSRpdvVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNniseldikwLRgqIG 480
Cdd:PRK09544 5 VSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 481 LVNQEPALFAT---TIrENILYGKDDATAEEITRAAKLSEAISFINnlpegFETQvgergiQLSGGQKQRIAISRAIVKN 557
Cdd:PRK09544 71 YVPQKLYLDTTlplTV-NRFLRLRPGTKKEDILPALKRVQAGHLID-----APMQ------KLSGGETQRVLLARALLNR 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 79487035 558 PSILLLDEATSALDAESEKSVQEALD--RVMVGRTTVVVAHRLSTV 601
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDqlRRELDCAVLMVSHDLHLV 184
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
420-599 |
3.00e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 55.24 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 420 DRLNL------AIPAGKIVALVGGSGSGKSTVISLIerfyepisgAVLLDGNNIsELDIKwlrgqIGLVNQEPALFA--- 490
Cdd:PLN03140 891 DRLQLlrevtgAFRPGVLTALMGVSGAGKTTLMDVL---------AGRKTGGYI-EGDIR-----ISGFPKKQETFAris 955
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 491 ------------TTIRENILYGKDDATAEEITRAAKLSeaisFINNLPEGFETQ------VGERGIQ-LSGGQKQRIAIS 551
Cdd:PLN03140 956 gyceqndihspqVTVRESLIYSAFLRLPKEVSKEEKMM----FVDEVMELVELDnlkdaiVGLPGVTgLSTEQRKRLTIA 1031
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 79487035 552 RAIVKNPSILLLDEATSALDAESEKSVQEAL-DRVMVGRTTVVVAHRLS 599
Cdd:PLN03140 1032 VELVANPSIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPS 1080
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1170-1237 |
3.54e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.43 E-value: 3.54e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1170 SGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANR--TTVVVAHRLSTIknaDTIS 1237
Cdd:PRK13409 455 SGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEReaTALVVDHDIYMI---DYIS 521
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
148-325 |
3.86e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 53.28 E-value: 3.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 148 GERQAAKMRRAYLRSMLSQDISLFDtEASTGEVISAITSDILVVQDALSEKVGNFLHYISRFIAGFAIGFTSVWQISLVT 227
Cdd:cd18563 71 GERITADLRRDLYEHLQRLSLSFFD-KRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 228 LSIVPLIALagGIYAFvaiglIARVRKSYIKAGEIAE-------EVIGNVRTVQAFTGEERAVRLYREALENTYKYGRKA 300
Cdd:cd18563 150 LIPVPLVVW--GSYFF-----WKKIRRLFHRQWRRWSrlnsvlnDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRA 222
|
170 180
....*....|....*....|....*
gi 79487035 301 GLTKGLGLGSMHCVLFLSwALLVWF 325
Cdd:cd18563 223 EKLWATFFPLLTFLTSLG-TLIVWY 246
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1018-1231 |
4.80e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 54.37 E-value: 4.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1018 ETSEELNNVEGTIELKGVHFSYPSRpDVVIfRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYdPTAGKVMIegkdik 1097
Cdd:TIGR00954 440 PGRGIVEYQDNGIKFENIPLVTPNG-DVLI-ESLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGRLT------ 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1098 kldlKALRKHIGLVQQEPALFATTIYENILYGN-------EGASQSEVVEsaMLANAHsfITSLPEgysTKVGERGVQ-- 1168
Cdd:TIGR00954 511 ----KPAKGKLFYVPQRPYMTLGTLRDQIIYPDssedmkrRGLSDKDLEQ--ILDNVQ--LTHILE---REGGWSAVQdw 579
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79487035 1169 ---MSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRlmANRTTVVVAHRLSTIK 1231
Cdd:TIGR00954 580 mdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHRKSLWK 643
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
412-578 |
5.02e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.97 E-value: 5.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 412 SRPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIK-WLRGQIGLVNQEPALF- 489
Cdd:PRK10982 7 SFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKeALENGISMVHQELNLVl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 490 ATTIRENILYGKDDATAEEITRAAKLSEAISFINNLpeGFETQVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEATSA 569
Cdd:PRK10982 87 QRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDEL--DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
....*....
gi 79487035 570 LdaeSEKSV 578
Cdd:PRK10982 165 L---TEKEV 170
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
415-574 |
5.04e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.19 E-value: 5.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 415 DVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIerfyepiSGAVLLD-GNNISELDIKWLRGQiglvnQEP------- 486
Cdd:PRK11147 15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDdGRIIYEQDLIVARLQ-----QDPprnvegt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 487 --ALFATTIRENILYGKD----------DATAEEITRAAKLSEAISfINNLPEgFETQVGERGIQ-----------LSGG 543
Cdd:PRK11147 83 vyDFVAEGIEEQAEYLKRyhdishlvetDPSEKNLNELAKLQEQLD-HHNLWQ-LENRINEVLAQlgldpdaalssLSGG 160
|
170 180 190
....*....|....*....|....*....|.
gi 79487035 544 QKQRIAISRAIVKNPSILLLDEATSALDAES 574
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1030-1225 |
5.05e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.13 E-value: 5.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRPdvvIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVmiegkdikKLDLKAlrkHIG 1109
Cdd:PRK15064 320 LEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--------KWSENA---NIG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1110 LVQQEPAL-FAT--TIYENILYGNEGASQSEVVESA---MLANAHSFitslpeGYSTKVgergvqMSGGQRQRIAIARAI 1183
Cdd:PRK15064 386 YYAQDHAYdFENdlTLFDWMSQWRQEGDDEQAVRGTlgrLLFSQDDI------KKSVKV------LSGGEKGRMLFGKLM 453
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 79487035 1184 LKNPAILLLDEATSALDVESERVVQQALDrlMANRTTVVVAH 1225
Cdd:PRK15064 454 MQKPNVLVMDEPTNHMDMESIESLNMALE--KYEGTLIFVSH 493
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
749-985 |
6.46e-07 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 52.40 E-value: 6.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 749 IKKIAILFCCASVITLIVYTIEHICFGTMGERLTLRVRENMFRAILK---NEIGWFdevdNTSSMLaSRLESDATLLKTI 825
Cdd:cd18548 38 ILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSfsfAEIDKF----GTSSLI-TRLTNDVTQVQNF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 826 VVDRSTILLQNLGLVVTSFIIAFILNWRLTLVVLATYPLVISG-----HISEKLFMQgyggdLNKAYLKANMLAGESVSN 900
Cdd:cd18548 113 VMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVvflimKKAIPLFKK-----VQKKLDRLNRVVRENLTG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 901 IRTVAAFCAEEKILELY---SRELLEPSKSSFRrgqIAGLFYGVSQFFIFSSYGLALWYGSTLMDKGLAGFKSVMK--TF 975
Cdd:cd18548 188 IRVIRAFNREDYEEERFdkaNDDLTDTSLKAGR---LMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLVAfiNY 264
|
250
....*....|
gi 79487035 976 MVLIVTALAM 985
Cdd:cd18548 265 LMQILMSLMM 274
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
761-957 |
7.73e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 52.57 E-value: 7.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 761 VITLIVYTIEHI-------CFGTMGERLTLRVRENMFRAILKNEIGWFDevDNTSSMLASRLESDATLLKTIVVDRSTIL 833
Cdd:cd18565 58 GLTVAAFLLESLfqylsgvLWRRFAQRVQHDLRTDTYDHVQRLDMAFFE--DRQTGDLMSVLNNDVNQLERFLDDGANSI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 834 LQNLGLVVTSFIIAFILNWRLTLVVLATYPLVI------SGHISEKlfmqgYG------GDLNkAYLKANmlagesVSNI 901
Cdd:cd18565 136 IRVVVTVLGIGAILFYLNWQLALVALLPVPLIIagtywfQRRIEPR-----YRavreavGDLN-ARLENN------LSGI 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79487035 902 RTVAAFCAEEkilelYSRELLEPSKSSFRRGQIA-----GLFYGVSQFFIFSSYGLALWYG 957
Cdd:cd18565 204 AVIKAFTAED-----FERERVADASEEYRDANWRairlrAAFFPVIRLVAGAGFVATFVVG 259
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1170-1237 |
1.06e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.86 E-value: 1.06e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1170 SGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANR--TTVVVAHRLSTIknaDTIS 1237
Cdd:COG1245 457 SGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRgkTAMVVDHDIYLI---DYIS 523
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
404-622 |
1.07e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.97 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 404 KDATFSYPSRPdvvIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVlldgnniseldiKWL-RGQIGLV 482
Cdd:PRK15064 323 ENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------KWSeNANIGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 483 NQEPA--------LF------------ATTIRE---NILYGKDDataeeITRAAKLseaisfinnlpegfetqvgergiq 539
Cdd:PRK15064 388 AQDHAydfendltLFdwmsqwrqegddEQAVRGtlgRLLFSQDD-----IKKSVKV------------------------ 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 540 LSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDrvMVGRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEF 618
Cdd:PRK15064 439 LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALE--KYEGTLIFVSHDREFVSSlATRIIEITPDGVVDF 516
|
....*
gi 79487035 619 -GNHE 622
Cdd:PRK15064 517 sGTYE 521
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
402-625 |
1.19e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 51.36 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 402 QFKDATFSYPSRPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNnISELDIK-WLRGQI- 479
Cdd:PRK13546 23 RMKDALIPKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-VSVIAISaGLSGQLt 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 480 GLVNQE-PALFATTIRENIlygkdDATAEEITRAAKLSEaisFINNLPEGFetqvgergiqlSGGQKQRIAISRAIVKNP 558
Cdd:PRK13546 102 GIENIEfKMLCMGFKRKEI-----KAMTPKIIEFSELGE---FIYQPVKKY-----------SSGMRAKLGFSINITVNP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79487035 559 SILLLDEATSALDaesEKSVQEALDRVM----VGRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFGNHENLI 625
Cdd:PRK13546 163 DILVIDEALSVGD---QTFAQKCLDKIYefkeQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVL 231
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1058-1261 |
1.62e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 51.73 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1058 GKSMALVGQSGSGKSSVISLILRF----YDPTAGKVMIEGKDIKKLDLKALRKHIG----LVQQEPalfattiyenilyg 1129
Cdd:PRK15093 33 GEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRLSPRERRKLVGhnvsMIFQEP-------------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1130 negasQSEVVESAMLAnaHSFITSLPeGYSTK--------------------VGERG---------VQMSGGQRQRIAIA 1180
Cdd:PRK15093 99 -----QSCLDPSERVG--RQLMQNIP-GWTYKgrwwqrfgwrkrraiellhrVGIKDhkdamrsfpYELTEGECQKVMIA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1181 RAILKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVV--VAHRLSTI-KNADTISVLHGGKIVEQGSHRKLVLNK 1257
Cdd:PRK15093 171 IALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTIllISHDLQMLsQWADKINVLYCGQTVETAPSKELVTTP 250
|
....
gi 79487035 1258 SGPY 1261
Cdd:PRK15093 251 HHPY 254
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1032-1203 |
1.73e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.43 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1032 LKGVHFSYPsrPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVIslilrfydptagKVM------IEGKDIKKLDLKalr 1105
Cdd:PRK11819 9 MNRVSKVVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLL------------RIMagvdkeFEGEARPAPGIK--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1106 khIGLVQQEPALFAT-TIYENI-------------------LYGNEGAS-------QSEV---------------VESAM 1143
Cdd:PRK11819 72 --VGYLPQEPQLDPEkTVRENVeegvaevkaaldrfneiyaAYAEPDADfdalaaeQGELqeiidaadawdldsqLEIAM 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1144 LAnahsfiTSLPEGySTKVGergvQMSGGQRQRIAIARAILKNPAILLLDEATSALDVES 1203
Cdd:PRK11819 150 DA------LRCPPW-DAKVT----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
426-627 |
1.87e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 52.20 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 426 IPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQI-GLVNQEpalfattiRENILYGKDDA 504
Cdd:PRK13545 47 VPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLtGIENIE--------LKGLMMGLTKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 505 TAEEIT-RAAKLSEAISFINNLPEGFetqvgergiqlSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALD 583
Cdd:PRK13545 119 KIKEIIpEIIEFADIGKFIYQPVKTY-----------SSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMN 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 79487035 584 RVM-VGRTTVVVAHRLSTVRNADIIAV-VHEGKIVEFGNHENLISN 627
Cdd:PRK13545 188 EFKeQGKTIFFISHSLSQVKSFCTKALwLHYGQVKEYGDIKEVVDH 233
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
415-595 |
2.60e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.05 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 415 DVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLierfyepISGA---------VLldGNNISelDIKWLR---GQI--- 479
Cdd:NF033858 13 KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSL-------IAGArkiqqgrveVL--GGDMA--DARHRRavcPRIaym 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 480 --GL-VNQEPALfatTIRENI-----LYGKD----DATAEEITRAAKLSeaiSFINNlPEGfetqvgergiQLSGGQKQR 547
Cdd:NF033858 82 pqGLgKNLYPTL---SVFENLdffgrLFGQDaaerRRRIDELLRATGLA---PFADR-PAG----------KLSGGMKQK 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 79487035 548 IAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRVMVGRT--TVVVA 595
Cdd:NF033858 145 LGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPgmSVLVA 194
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
777-866 |
2.94e-06 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 50.56 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 777 MGERLTLRVRENMFRAILKNEIGWFDEVdNTSSmLASRLESDATLLKTIVVDRSTILLQNLGLVVTSFIIAFILNWRLTL 856
Cdd:cd18550 66 IGQGVMYDLRVQLYAHLQRMSLAFFTRT-RTGE-IQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLAL 143
|
90
....*....|
gi 79487035 857 VVLATYPLVI 866
Cdd:cd18550 144 LSLVLLPLFV 153
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1030-1229 |
3.23e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 51.47 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1030 IELKGVHFSYPSRpdvVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIeGKDIKkldlkalrkhIG 1109
Cdd:TIGR03719 323 IEAENLTKAFGDK---LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK----------LA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1110 LV-QQEPALFAT-TIYENILYGNE----GASQsevVESAMLANAHSFITSLPEgysTKVGergvQMSGGQRQRIAIARaI 1183
Cdd:TIGR03719 389 YVdQSRDALDPNkTVWEEISGGLDiiklGKRE---IPSRAYVGRFNFKGSDQQ---KKVG----QLSGGERNRVHLAK-T 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 79487035 1184 LKNPA-ILLLDEATSALDVESERVVQQALDRLMAnrTTVVVAH------RLST 1229
Cdd:TIGR03719 458 LKSGGnVLLLDEPTNDLDVETLRALEEALLNFAG--CAVVISHdrwfldRIAT 508
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
411-622 |
3.42e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 51.36 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 411 PSRPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYE-PISGAVLLDGNnisELDIK----WLRGQIGLVNQE 485
Cdd:TIGR02633 268 VINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGK---PVDIRnpaqAIRAGIAMVPED 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 486 PAlfattiRENILygKDDATAEEITRAAKlsEAISFINNLPEGFETQVGERGIQ---------------LSGGQKQRIAI 550
Cdd:TIGR02633 345 RK------RHGIV--PILGVGKNITLSVL--KSFCFKMRIDAAAELQIIGSAIQrlkvktaspflpigrLSGGNQQKAVL 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79487035 551 SRAIVKNPSILLLDEATSALDAESEKSVQEALDR-VMVGRTTVVVAHRLSTVRN-ADIIAVVHEGKI-VEFGNHE 622
Cdd:TIGR02633 415 AKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKLkGDFVNHA 489
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1169-1248 |
3.96e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.47 E-value: 3.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1169 MSGGQRQRIAIARAILKNP--AILLLDEATSALDVESERVVQQALDRLMANRTTV-VVAHRLSTIKNADTI------SVL 1239
Cdd:cd03238 88 LSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTViLIEHNLDVLSSADWIidfgpgSGK 167
|
....*....
gi 79487035 1240 HGGKIVEQG 1248
Cdd:cd03238 168 SGGKVVFSG 176
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
538-611 |
4.25e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 48.34 E-value: 4.25e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79487035 538 IQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRVMV--GRTTVVVAHRLSTVRN-ADIIAVVH 611
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYlSDRIHVFE 146
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
408-598 |
4.36e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 51.55 E-value: 4.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 408 FSYPSRPDVvifDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISElDIKWLRGQIGLVNQEPA 487
Cdd:TIGR01257 1947 YSGTSSPAV---DRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQFDA 2022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 488 L-FATTIRENI-LYGK-DDATAEEITRAAKLSeaisfINNLpeGFETQVGERGIQLSGGQKQRIAISRAIVKNPSILLLD 564
Cdd:TIGR01257 2023 IdDLLTGREHLyLYARlRGVPAEEIEKVANWS-----IQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLD 2095
|
170 180 190
....*....|....*....|....*....|....*
gi 79487035 565 EATSALDAESEKSVQEALDRVM-VGRTTVVVAHRL 598
Cdd:TIGR01257 2096 EPTTGMDPQARRMLWNTIVSIIrEGRAVVLTSHSM 2130
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1012-1201 |
4.59e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.88 E-value: 4.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1012 KTQIVGETSEELNNVEGtielkgvhFSYPSRPDVvifrDFDLivRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMI 1091
Cdd:PRK10982 242 KENKPGEVILEVRNLTS--------LRQPSIRDV----SFDL--HKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1092 EGKDIKKLD-LKALRKHIGLVQQEPAlfATTIYENIlygnegasqsEVVESAMLANAHSFITSL---------------- 1154
Cdd:PRK10982 308 HGKKINNHNaNEAINHGFALVTEERR--STGIYAYL----------DIGFNSLISNIRNYKNKVglldnsrmksdtqwvi 375
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 79487035 1155 ------PEGYSTKVGergvQMSGGQRQRIAIARAILKNPAILLLDEATSALDV 1201
Cdd:PRK10982 376 dsmrvkTPGHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDV 424
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
778-964 |
6.02e-06 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 49.46 E-value: 6.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 778 GERLTLRVRENMFRAILKNEIGWFDevDNTSSMLASRLESDATLLKTIVVDRSTILLQNLGLVVTSFIIAFILNWRLTLV 857
Cdd:cd18778 68 EQKVVADLRSDLYDKLQRLSLRYFD--DRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 858 VLATYPLVIsghisekLFMQGYGGDLNKAYLKANMLAGE-------SVSNIRTVAAFCAEEKILELYSRELLEPSKSSFR 930
Cdd:cd18778 146 TLIPIPFLA-------LGAWLYSKKVRPRYRKVREALGElnallqdNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLR 218
|
170 180 190
....*....|....*....|....*....|....
gi 79487035 931 RGQIAGLFYGVSQFFIFSSYGLALWYGSTLMDKG 964
Cdd:cd18778 219 AMKLWAIFHPLMEFLTSLGTVLVLGFGGRLVLAG 252
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
155-325 |
6.16e-06 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 49.72 E-value: 6.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 155 MRRAYLRSMLSQDISLFDtEASTGEVISAITSDILVVQDALSEKVGNFLHYISRFIAGFAIGFTSVWQISLVTLSIVPLI 234
Cdd:cd18541 75 LRNDLFAHLLTLSPSFYQ-KNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 235 AlaggiyaFVAIGLIARVRKSYIKAGE-------IAEEVIGNVRTVQAFTGEERAVRLYREALENTYKYGRKAGLTKGLG 307
Cdd:cd18541 154 A-------LLVYRLGKKIHKRFRKVQEafsdlsdRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALF 226
|
170
....*....|....*...
gi 79487035 308 LGSMHCVLFLSWALLVWF 325
Cdd:cd18541 227 FPLIGLLIGLSFLIVLWY 244
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1050-1244 |
8.64e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 49.82 E-value: 8.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1050 DFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPT-AGKVMIEGKDIK-KLDLKALRKHIGLVQQEP------------ 1115
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDiRNPAQAIRAGIAMVPEDRkrhgivpilgvg 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1116 ---ALFATTIYENILYGNEGASQSEVVESAMLANAHSFITSLPEGystkvgergvQMSGGQRQRIAIARAILKNPAILLL 1192
Cdd:TIGR02633 358 kniTLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIG----------RLSGGNQQKAVLAKMLLTNPRVLIL 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 79487035 1193 DEATSALDVESERVVQQALDRLMANRTT-VVVAHRLSTIKN-ADTISVLHGGKI 1244
Cdd:TIGR02633 428 DEPTRGVDVGAKYEIYKLINQLAQEGVAiIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
146-236 |
9.65e-06 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 49.02 E-value: 9.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 146 HTGERQAAKMRRAYLRSMLSQDISLFdTEASTGEVISAITSDILVVQDALSEKVGNFLHYISRFIAGFAIGFTSVWQISL 225
Cdd:cd18550 65 RIGQGVMYDLRVQLYAHLQRMSLAFF-TRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLAL 143
|
90
....*....|.
gi 79487035 226 VTLSIVPLIAL 236
Cdd:cd18550 144 LSLVLLPLFVL 154
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
152-325 |
1.10e-05 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 48.93 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 152 AAKMRRAYLRSMLSQDISLFDtEASTGEVISAITSDILVVQDAlsekVGNFLHYISR----FIAGFAIGFTSVWQISLVT 227
Cdd:cd18548 71 GRDLRKDLFEKIQSFSFAEID-KFGTSSLITRLTNDVTQVQNF----VMMLLRMLVRapimLIGAIIMAFRINPKLALIL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 228 LSIVPLIALAGGIYAFVAIGLIARVRKSYIKAGEIAEEVIGNVRTVQAFTGEERAVRLYREALENTYKYGRKAGLTKGLG 307
Cdd:cd18548 146 LVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALL 225
|
170
....*....|....*...
gi 79487035 308 LGSMHCVLFLSWALLVWF 325
Cdd:cd18548 226 NPLMMLIMNLAIVAILWF 243
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1065-1238 |
1.16e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.56 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1065 GQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDlKALRKHIGlvQQEPALFATTIYENILYGNEGASQSEVVESAMl 1144
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA-KPYCTYIG--HNLGLKLEMTVFENLKFWSEIYNSAETLYAAI- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1145 anaHSF-ITSLpegystkVGERGVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQaLDRLMANRTTVVV 1223
Cdd:PRK13541 109 ---HYFkLHDL-------LDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNN-LIVMKANSGGIVL 177
|
170
....*....|....*..
gi 79487035 1224 --AHRLSTIKNADTISV 1238
Cdd:PRK13541 178 lsSHLESSIKSAQILQL 194
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1052-1245 |
1.37e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.47 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1052 DLIVRA------GKSMALVGQSGSGKSSVIS-LILRFYD--PTAGKVM-----IEGKDIKKLD---------LKALRKHI 1108
Cdd:PLN03073 191 DLIVDAsvtlafGRHYGLVGRNGTGKTTFLRyMAMHAIDgiPKNCQILhveqeVVGDDTTALQcvlntdierTQLLEEEA 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1109 GLVQQEPALFATTIYENILYGNEGASQSEVVeSAMLA------------NAHSFITSLPEG--YSTKVGERGV-QMSGGQ 1173
Cdd:PLN03073 271 QLVAQQRELEFETETGKGKGANKDGVDKDAV-SQRLEeiykrlelidayTAEARAASILAGlsFTPEMQVKATkTFSGGW 349
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79487035 1174 RQRIAIARAILKNPAILLLDEATSALDVESERVVQQALdrLMANRTTVVVAHRLSTIKNADT-ISVLHGGKIV 1245
Cdd:PLN03073 350 RMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSHAREFLNTVVTdILHLHGQKLV 420
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1055-1227 |
1.71e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 49.63 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1055 VRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKlDLKALRKHIGLVQQEPAL--FATTIYENILYGNEG 1132
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQFDAIddLLTGREHLYLYARLR 2040
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1133 ASQSEVVESAmlanAHSFITSLpeGYSTKVGERGVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALD 1212
Cdd:TIGR01257 2041 GVPAEEIEKV----ANWSIQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIV 2114
|
170
....*....|....*.
gi 79487035 1213 RLM-ANRTTVVVAHRL 1227
Cdd:TIGR01257 2115 SIIrEGRAVVLTSHSM 2130
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
423-650 |
1.72e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.86 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 423 NLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIK---------WLRGQIGLVNQEPALFATTI 493
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEqlqklvsdeWQRNNTDMLSPGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 494 RENILYGKDDATaeeitRAAKLSEAIsfinnlpeGFETQVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAE 573
Cdd:PRK10938 103 AEIIQDEVKDPA-----RCEQLAQQF--------GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 574 SEKSVQEALDRVMV-GRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFGNHENLISnpDGAYSSL--------LRLQETAS 643
Cdd:PRK10938 170 SRQQLAELLASLHQsGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQ--QALVAQLahseqlegVQLPEPDE 247
|
....*..
gi 79487035 644 LQRNPSL 650
Cdd:PRK10938 248 PSARHAL 254
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
423-611 |
3.16e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 48.24 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 423 NLAIP-AGKIVALVGGSGSGKSTVISL---------------------IERFyepiSGAVLLDG-NNISELDIKWLRgQI 479
Cdd:COG1245 92 GLPVPkKGKVTGILGPNGIGKSTALKIlsgelkpnlgdydeepswdevLKRF----RGTELQDYfKKLANGEIKVAH-KP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 480 GLVNQEPALFATTIREnILYGKDD-ATAEEITRAAKLSEAIsfinnlpegfetqvgERGI-QLSGGQKQRIAISRAIVKN 557
Cdd:COG1245 167 QYVDLIPKVFKGTVRE-LLEKVDErGKLDELAEKLGLENIL---------------DRDIsELSGGELQRVAIAAALLRD 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 558 PSILLLDEATSALD----AESEKSVQEALDRvmvGRTTVVVAHRLSTVrnaDIIA-VVH 611
Cdd:COG1245 231 ADFYFFDEPSSYLDiyqrLNVARLIRELAEE---GKYVLVVEHDLAIL---DYLAdYVH 283
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
844-965 |
3.17e-05 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 47.49 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 844 FIIAFILNWRLTLVVLATYP------LVISGHISEKLFMQGYGGDLNKAYLKanmlagESVSNIRTVAAFCAEEKILELY 917
Cdd:cd18588 133 LAVMFYYSPTLTLIVLASLPlyallsLLVTPILRRRLEEKFQRGAENQSFLV------ETVTGIETVKSLAVEPQFQRRW 206
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 79487035 918 SRELLEPSKSSFRRGQIAGLFYGVSQFFIFSSYGLALWYGSTL-MDKGL 965
Cdd:cd18588 207 EELLARYVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLvMDGEL 255
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
426-596 |
3.41e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.27 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 426 IPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLldgnniSELDIKWlrgqiglvnqEPAlfattirenilYGKDD-- 503
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD------PELKISY----------KPQ-----------YIKPDyd 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 504 ATAEEITRAAKLSEAISFIN-------NLPEGFETQVGErgiqLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEK 576
Cdd:PRK13409 415 GTVEDLLRSITDDLGSSYYKseiikplQLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRL 490
|
170 180
....*....|....*....|..
gi 79487035 577 SVQEALDRVMVGR--TTVVVAH 596
Cdd:PRK13409 491 AVAKAIRRIAEEReaTALVVDH 512
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1016-1253 |
3.41e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.08 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1016 VGETSEE----LNNVEGTIELKGVHFSYPSRPDVvifrDFDLivRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMI 1091
Cdd:PRK10762 238 VGRKLEDqyprLDKAPGEVRLKVDNLSGPGVNDV----SFTL--RKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1092 EGKDIK-KLDLKAL----------RKHIGL-----VQQEPALFATTIYENILYGNEGASQSEVVESamlanahsFITSlp 1155
Cdd:PRK10762 312 DGHEVVtRSPQDGLangivyisedRKRDGLvlgmsVKENMSLTALRYFSRAGGSLKHADEQQAVSD--------FIRL-- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1156 egYSTKVGERGVQ---MSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANRTTV--VVAHRLSTI 1230
Cdd:PRK10762 382 --FNIKTPSMEQAiglLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIilVSSEMPEVL 459
|
250 260
....*....|....*....|....*...
gi 79487035 1231 KNADTISVLHGGKI-----VEQGSHRKL 1253
Cdd:PRK10762 460 GMSDRILVMHEGRIsgeftREQATQEKL 487
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
423-611 |
3.62e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.88 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 423 NLAIP-AGKIVALVGGSGSGKSTVISL---------------------IERFyepiSGAVLLDG-NNISELDIKWLRgQI 479
Cdd:PRK13409 92 GLPIPkEGKVTGILGPNGIGKTTAVKIlsgelipnlgdyeeepswdevLKRF----RGTELQNYfKKLYNGEIKVVH-KP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 480 GLVNQEPALFATTIREnILYGKDDAtaeeitraAKLSEAISFINnlpegfETQVGERGI-QLSGGQKQRIAISRAIVKNP 558
Cdd:PRK13409 167 QYVDLIPKVFKGKVRE-LLKKVDER--------GKLDEVVERLG------LENILDRDIsELSGGELQRVAIAAALLRDA 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 79487035 559 SILLLDEATSALDAESEKSVQEALDRVMVGRTTVVVAHRLSTVrnaDIIA-VVH 611
Cdd:PRK13409 232 DFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDLAVL---DYLAdNVH 282
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
153-295 |
7.49e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 46.38 E-value: 7.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 153 AKMRRAYLRSMLSQDISLFDTeASTGEVISAITSDILVVQDALSEKVGNFLHYISRFIAGFAIGFTSVWQISLVTLSIVP 232
Cdd:cd18778 73 ADLRSDLYDKLQRLSLRYFDD-RQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIP 151
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79487035 233 LIALAGGIYAFVAIGLIARVRKSyikAGEIA---EEVIGNVRTVQAFTGEERAVRLYREALENTYK 295
Cdd:cd18778 152 FLALGAWLYSKKVRPRYRKVREA---LGELNallQDNLSGIREIQAFGREEEEAKRFEALSRRYRK 214
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1040-1244 |
8.81e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.85 E-value: 8.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1040 PSRPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYdPTA--GKVMIEGKDIK-KLDLKALRKHIGLVQQE-- 1114
Cdd:PRK13549 270 PVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY-PGRweGEIFIDGKPVKiRNPQQAIAQGIAMVPEDrk 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1115 -----PALfatTIYENILYGNEG--ASQSEVVESAMLANAHSFI------TSLPEgysTKVGergvQMSGGQRQRIAIAR 1181
Cdd:PRK13549 349 rdgivPVM---GVGKNITLAALDrfTGGSRIDDAAELKTILESIqrlkvkTASPE---LAIA----RLSGGNQQKAVLAK 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 1182 AILKNPAILLLDEATSALDV----ESERVVQQALDRLMAnrtTVVVAHRLSTIKN-ADTISVLHGGKI 1244
Cdd:PRK13549 419 CLLLNPKILILDEPTRGIDVgakyEIYKLINQLVQQGVA---IIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
830-976 |
8.92e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 46.01 E-value: 8.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 830 STILlqNLGLVVTSFIIAFILNWRLTLVVLATYPLVISGHISEKLFMQGYGGDLNKAYLKANMLAGESVSNIRTVAAFCA 909
Cdd:cd18568 121 TTIL--DLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAA 198
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79487035 910 EEKIL----ELYSRELlepsKSSFRRGQIAGLFYGVSQFFIFSSYGLALWYGSTLMDKG------LAGFKSVMKTFM 976
Cdd:cd18568 199 ERPIRwrweNKFAKAL----NTRFRGQKLSIVLQLISSLINHLGTIAVLWYGAYLVISGqltigqLVAFNMLFGSVI 271
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
539-636 |
8.99e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 46.33 E-value: 8.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 539 QLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRVMVGRTTVV--VAHRLSTVRN-ADIIAVVHEGKI 615
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTIllISHDLQMLSQwADKINVLYCGQT 237
|
90 100
....*....|....*....|.
gi 79487035 616 VEFGNHENLISNPDGAYSSLL 636
Cdd:PRK15093 238 VETAPSKELVTTPHHPYTQAL 258
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1052-1245 |
1.03e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.48 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1052 DLIVRAGKSMALVGQSGSGKSSVISLIlrfydptAGKVMI-EGKDIKKLDLKALRkhiglVQQEPALFAT-TIYEnilYG 1129
Cdd:PRK11147 23 ELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLdDGRIIYEQDLIVAR-----LQQDPPRNVEgTVYD---FV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1130 NEG-ASQSEVVESAmlanaHSFITSLPEGYSTKVGER--GVQ--------------------------------MSGGQR 1174
Cdd:PRK11147 88 AEGiEEQAEYLKRY-----HDISHLVETDPSEKNLNElaKLQeqldhhnlwqlenrinevlaqlgldpdaalssLSGGWL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79487035 1175 QRIAIARAILKNPAILLLDEATSALDVESERVVQQALdrLMANRTTVVVAHRLSTIKNADT-ISVLHGGKIV 1245
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL--KTFQGSIIFISHDRSFIRNMATrIVDLDRGKLV 232
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
422-616 |
1.38e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 44.94 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 422 LNLAIPAGKIVALVGGSGSGKST-VISLI-----ERFYEPISGAVLLDGNNISELDIKWLRG-------QIGLVNQEPAL 488
Cdd:cd03270 14 VDVDIPRNKLVVITGVSGSGKSSlAFDTIyaegqRRYVESLSAYARQFLGQMDKPDVDSIEGlspaiaiDQKTTSRNPRS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 489 FATTIRE-----NILYGKddataeeitraAKLSEAISFINNLPEGFETqVGERGIQLSGGQKQRIAISRAIVKNPS--IL 561
Cdd:cd03270 94 TVGTVTEiydylRLLFAR-----------VGIRERLGFLVDVGLGYLT-LSRSAPTLSGGEAQRIRLATQIGSGLTgvLY 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79487035 562 LLDEATSALDAESEKSVQEALDRVM-VGRTTVVVAHRLSTVRNADII------AVVHEGKIV 616
Cdd:cd03270 162 VLDEPSIGLHPRDNDRLIETLKRLRdLGNTVLVVEHDEDTIRAADHVidigpgAGVHGGEIV 223
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1050-1248 |
1.46e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.19 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1050 DFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGkdikklDLKALRKHIGLVQQepalfaTTIYENILYG 1129
Cdd:PRK13546 42 DISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG------EVSVIAISAGLSGQ------LTGIENIEFK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1130 N--EGASQSE-------VVESAMLANahsFITSLPEGYSTkvgergvqmsgGQRQRIAIARAILKNPAILLLDEatsALD 1200
Cdd:PRK13546 110 MlcMGFKRKEikamtpkIIEFSELGE---FIYQPVKKYSS-----------GMRAKLGFSINITVNPDILVIDE---ALS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 79487035 1201 VESERVVQQALDRLM----ANRTTVVVAHRLSTIKNADT-ISVLHGGKIVEQG 1248
Cdd:PRK13546 173 VGDQTFAQKCLDKIYefkeQNKTIFFVSHNLGQVRQFCTkIAWIEGGKLKDYG 225
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
1169-1248 |
2.05e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 44.17 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1169 MSGGQRQRIAIARAILKN--PAILLLDEATSALDVESERVVQQALDRLM-ANRTTVVVAHRLSTIKNADTISVL------ 1239
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGltGVLYVLDEPSIGLHPRDNDRLIETLKRLRdLGNTVLVVEHDEDTIRAADHVIDIgpgagv 217
|
....*....
gi 79487035 1240 HGGKIVEQG 1248
Cdd:cd03270 218 HGGEIVAQG 226
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1044-1244 |
2.39e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.55 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1044 DVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVmiegkdikkldlkALRKHIGLvqqepALFATTIY 1123
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI-------------GLAKGIKL-----GYFAQHQL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1124 EnILYGNEGASQ--SEVVESAMLANAHSFITSLpeGYS-TKVGERGVQMSGGQRQRIAIARAILKNPAILLLDEATSALD 1200
Cdd:PRK10636 386 E-FLRADESPLQhlARLAPQELEQKLRDYLGGF--GFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 79487035 1201 VESERVVQQALdrLMANRTTVVVAHRLSTIKN-ADTISVLHGGKI 1244
Cdd:PRK10636 463 LDMRQALTEAL--IDFEGALVVVSHDRHLLRStTDDLYLVHDGKV 505
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1052-1253 |
2.51e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.01 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1052 DLIVRAGKSMALVGQSGSGKSSVI-----SLILrfydpTAGKVMIEGKDIKKLDLKALRKhigLVQQE------------ 1114
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALAralagELPL-----LSGERQSQFSHITRLSFEQLQK---LVSDEwqrnntdmlspg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1115 PALFATTIYENIlygnegasQSEVVESAMLAN-AHSF-ITSLpegystkVGERGVQMSGGQRQRIAIARAILKNPAILLL 1192
Cdd:PRK10938 95 EDDTGRTTAEII--------QDEVKDPARCEQlAQQFgITAL-------LDRRFKYLSTGETRKTLLCQALMSEPDLLIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79487035 1193 DEATSALDVESERVVQQALDRLMANRTTVV-VAHRLSTIKN-ADTISVLHGGKIVEQGSHRKL 1253
Cdd:PRK10938 160 DEPFDGLDVASRQQLAELLASLHQSGITLVlVLNRFDEIPDfVQFAGVLADCTLAETGEREEI 222
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
540-615 |
2.81e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.99 E-value: 2.81e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79487035 540 LSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRVMV-GRTTVVVAHRLSTVRN-ADIIAVVHEGKI 615
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAeGLSIILVSSEMPEVLGmSDRILVMHEGRI 473
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1137-1228 |
3.65e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.22 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1137 EVVESAMLANAHSFITSLP--EGYSTKvgergvqmsggQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQAL-DR 1213
Cdd:PLN03140 997 EVMELVELDNLKDAIVGLPgvTGLSTE-----------QRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVrNT 1065
|
90
....*....|....*
gi 79487035 1214 LMANRTTVVVAHRLS 1228
Cdd:PLN03140 1066 VDTGRTVVCTIHQPS 1080
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
422-619 |
4.46e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 42.70 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 422 LNLAIPAGKIVALVGGSGSGKSTVISliERFYEpisgavlldgnniseldikwlRGQIGLVNQEPALFATTIrenILYGK 501
Cdd:cd03238 14 LDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYA---------------------SGKARLISFLPKFSRNKL---IFIDQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 502 ddataeeitraaklseaISFINNLPEGFETqVGERGIQLSGGQKQRIAISRAIVKNP--SILLLDEATSALDAESEKSVQ 579
Cdd:cd03238 68 -----------------LQFLIDVGLGYLT-LGQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLL 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 79487035 580 EALDR-VMVGRTTVVVAHRLSTVRNAD-IIAVVHE-----GKIVEFG 619
Cdd:cd03238 130 EVIKGlIDLGNTVILIEHNLDVLSSADwIIDFGPGsgksgGKVVFSG 176
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
404-571 |
5.74e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.01 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 404 KDATFSYPSRPDVVIFDRLNLAIPAGKIVALVGGSGSGKS-TVISLIERFY-EPISGAVLLDGNnisELDIKWL------ 475
Cdd:NF040905 261 KNWTVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYgRNISGTVFKDGK---EVDVSTVsdaida 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 476 --------RGQIGLVNQEpalfatTIRENIlygkddataeeiTRAA--KLSEAiSFINnlpEGFETQVGER--------- 536
Cdd:NF040905 338 glayvtedRKGYGLNLID------DIKRNI------------TLANlgKVSRR-GVID---ENEEIKVAEEyrkkmnikt 395
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 79487035 537 -GI-----QLSGGQKQRIAISRAIVKNPSILLLDEATSALD 571
Cdd:NF040905 396 pSVfqkvgNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
423-616 |
6.54e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 43.75 E-value: 6.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 423 NLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGnniseldikwlrgqiglvnqEPALFATT---IRENILY 499
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG--------------------KPIDIRSPrdaIRAGIML 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 500 GKDDATAEEITRAAKLSE--AIS----------FINNlpeGFETQVGERGIQ---------------LSGGQKQRIAISR 552
Cdd:PRK11288 333 CPEDRKAEGIIPVHSVADniNISarrhhlragcLINN---RWEAENADRFIRslniktpsreqlimnLSGGNQQKAILGR 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79487035 553 AIVKNPSILLLDEATSALD--AESE--KSVQEALDRvmvGRTTVVVAHRLSTVRN-ADIIAVVHEGKIV 616
Cdd:PRK11288 410 WLSEDMKVILLDEPTRGIDvgAKHEiyNVIYELAAQ---GVAVLFVSSDLPEVLGvADRIVVMREGRIA 475
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
540-625 |
7.57e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.85 E-value: 7.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 540 LSGGQKQRIAISRAIVK---NPSILLLDEATSALDAESEKSVQEALDR-VMVGRTTVVVAHRLSTVRNAD-IIAV----- 609
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHFDDIKKLLEVLQRlVDKGNTVVVIEHNLDVIKTADyIIDLgpegg 909
|
90
....*....|....*.
gi 79487035 610 VHEGKIVEFGNHENLI 625
Cdd:TIGR00630 910 DGGGTVVASGTPEEVA 925
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
539-622 |
7.58e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 43.76 E-value: 7.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 539 QLSGGQKQRIAISRAIVKNPSILLLDEATSALD----AESEKSVQEALDRvmvGRTTVVVAHRLSTVRN-ADIIAVVHEG 613
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDvgakYEIYKLINQLVQQ---GVAIIVISSELPEVLGlSDRVLVMHEG 481
|
90
....*....|
gi 79487035 614 KI-VEFGNHE 622
Cdd:PRK13549 482 KLkGDLINHN 491
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
503-596 |
7.59e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.70 E-value: 7.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 503 DATAEEiTRAAKLSEAISFINnlpegfETQVgERGIQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEAL 582
Cdd:PLN03073 316 DAYTAE-ARAASILAGLSFTP------EMQV-KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL 387
|
90
....*....|....
gi 79487035 583 drVMVGRTTVVVAH 596
Cdd:PLN03073 388 --LKWPKTFIVVSH 399
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1163-1248 |
9.33e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.19 E-value: 9.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1163 GERGVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVVVAHRL--STIKNADTISVLH 1240
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYmeEAEQLAHELTVID 218
|
....*...
gi 79487035 1241 GGKIVEQG 1248
Cdd:NF000106 219 RGRVIADG 226
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
540-614 |
1.07e-03 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 43.23 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 540 LSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRVMVGR--TTVVVAHRLSTVrnaDIIA---VVHEGK 614
Cdd:COG1245 456 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRgkTAMVVDHDIYLI---DYISdrlMVFEGE 532
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
176-348 |
1.23e-03 |
|
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 1 (TMD1) of the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), which belongs to the ABCC subfamily. CFTR functions as a chloride channel, in contrast to other ABC transporters, and controls ion and water secretion and absorption in epithelial tissues. ABC proteins are formed from two homologous halves each containing a transmembrane domain (TMD) and a cytosolic nucleotide binding domain (NBD). In CFTR, these two TMD-NBD halves are linked by the unique regulatory (R) domain, which is not present in other ABC transporters. The ion channel only opens when its R-domain is phosphorylated by cyclic AMP-dependent protein kinase (PKA) and ATP is bound at the NBDs. Mutations in CFTR cause cystic fibrosis, the most common lethal genetic disorder in populations of Northern European descent.
Pssm-ID: 350038 [Multi-domain] Cd Length: 291 Bit Score: 42.24 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 176 STGEVISAITSDILVVQDALSekvgnFLHYIsrFIAGFAIGFTSV--W-QISLVTLSIVPLIALAGGIYAFVAiGLIARV 252
Cdd:cd18594 94 TTGHIVNLLSNDVQKFDEVLV-----YLHFL--WIAPLQVIVLTGllWrEIGPSSLAGLGVLLLLLPLQAYLG-KLFAKY 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 253 RKSYIK-AGE---IAEEVIGNVRTVQAFTGEERAVRLYREALENTYKYGRKAGLTKGLglgsmHCVLFLSWALLVWFTSV 328
Cdd:cd18594 166 RRKTAGlTDErvkIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAF-----NMAFFFFSPTLVSFATF 240
|
170 180
....*....|....*....|....*
gi 79487035 329 VVH---KDIADGGKSFTT--MLNVV 348
Cdd:cd18594 241 VPYvltGNTLTARKVFTVisLLNAL 265
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
417-619 |
1.33e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.81 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 417 VIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIerfyepisgavlldgnniseldikwlrgqiglvnqepaLFATTIREN 496
Cdd:cd03227 9 SYFVPNDVTFGEGSLTIITGPNGSGKSTILDAI--------------------------------------GLALGGAQS 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 497 ILYGKDDATAEEITRAAKLsEAISFInnlpegfetqvgergIQLSGGQKQRIAISRAI----VKNPSILLLDEATSALDA 572
Cdd:cd03227 51 ATRRRSGVKAGCIVAAVSA-ELIFTR---------------LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDP 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 79487035 573 ESEKSVQEALDRVMVGRTTVVVA-HRLSTVRNADiiAVVHEGKIVEFG 619
Cdd:cd03227 115 RDGQALAEAILEHLVKGAQVIVItHLPELAELAD--KLIHIKKVITGV 160
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
774-964 |
1.36e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 42.18 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 774 FGTMGERLTLRVRENMFRAILKNEIGWFDEvdNTSSMLASRLEsDATLLKTIVVDRSTILLQNLGLVVTSFIIAFILNWR 853
Cdd:cd18566 66 LAWIGARFDHRLSNAAFEHLLSLPLSFFER--EPSGAHLERLN-SLEQIREFLTGQALLALLDLPFVLIFLGLIWYLGGK 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 854 LTLVVLATYPL-----VISGHISEKLFMQGYGGDLNKAylkaNMLAgESVSNIRTVAAFCAEEKILELYSRELLEPSKSS 928
Cdd:cd18566 143 LVLVPLVLLGLfvlvaILLGPILRRALKERSRADERRQ----NFLI-ETLTGIHTIKAMAMEPQMLRRYERLQANAAYAG 217
|
170 180 190
....*....|....*....|....*....|....*.
gi 79487035 929 FRRGQIAGLFYGVSQFFIFSSYGLALWYGSTLMDKG 964
Cdd:cd18566 218 FKVAKINAVAQTLGQLFSQVSMVAVVAFGALLVING 253
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1161-1212 |
1.37e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.80 E-value: 1.37e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 79487035 1161 KVGergvQMSGGQRQRIAIARaILKNPA-ILLLDEATSALDVESERVVQQALD 1212
Cdd:PRK11819 442 KVG----VLSGGERNRLHLAK-TLKQGGnVLLLDEPTNDLDVETLRALEEALL 489
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
429-617 |
1.88e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 42.46 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 429 GKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNI---SELDIkwLRGQIGLVNQ---EPALFAT-TIRENIlygk 501
Cdd:PRK09700 289 GEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIsprSPLDA--VKKGMAYITEsrrDNGFFPNfSIAQNM---- 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 502 ddataeEITRAAKLSEAISFINNLPEGFETQVGERG---------------IQLSGGQKQRIAISRAIVKNPSILLLDEA 566
Cdd:PRK09700 363 ------AISRSLKDGGYKGAMGLFHEVDEQRTAENQrellalkchsvnqniTELSGGNQQKVLISKWLCCCPEVIIFDEP 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 79487035 567 TSALD----AESEKSVQEALDRvmvGRTTVVVAHRLSTVRNA-DIIAVVHEGKIVE 617
Cdd:PRK09700 437 TRGIDvgakAEIYKVMRQLADD---GKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
504-646 |
1.92e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 42.03 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 504 ATAEEITRAAKLSEAisfinnlpegfetqVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALd 583
Cdd:NF000106 123 ARADELLERFSLTEA--------------AGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEV- 187
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79487035 584 RVMV--GRTTVVVAHRLSTVRN-ADIIAVVHEGKIVEFGNHENLISNPdGAYSSLLRLQETASLQR 646
Cdd:NF000106 188 RSMVrdGATVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDELKTKV-GGRTLQIRPAHAAELDR 252
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
453-661 |
2.46e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.31 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 453 YEPISGAVLLDGNNISELdikwlrgqIGLVNQEPALFATTIReniLYGKDDATAEEITRAAKlsEAISFINNLpeGFETQ 532
Cdd:TIGR00630 416 LKPEALAVTVGGKSIADV--------SELSIREAHEFFNQLT---LTPEEKKIAEEVLKEIR--ERLGFLIDV--GLDYL 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 533 VGERGIQ-LSGGQKQRIAISRAI------VknpsILLLDEATSALDAESEKSVQEALDRVM-VGRTTVVVAHRLSTVRNA 604
Cdd:TIGR00630 481 SLSRAAGtLSGGEAQRIRLATQIgsgltgV----LYVLDEPSIGLHQRDNRRLINTLKRLRdLGNTLIVVEHDEDTIRAA 556
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79487035 605 DII------AVVHEGKIVEFGNHENLISNPD---GAYsslLRLQETASL--QRNPSLNRTL----SRPHSIK 661
Cdd:TIGR00630 557 DYVidigpgAGEHGGEVVASGTPEEILANPDsltGQY---LSGRKKIEVpaERRPGNGKFLtlkgARENNLK 625
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1168-1248 |
3.59e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1168 QMSGGQRQRIAIAR--AILK-NPA-ILLLDEATSALD-VESERVVQqaLDRLMANRTT-VVVAHRLSTIKNADtisVLHG 1241
Cdd:TIGR02168 1089 LLSGGEKALTALALlfAIFKvKPApFCILDEVDAPLDdANVERFAN--LLKEFSKNTQfIVITHNKGTMEVAD---QLYG 1163
|
....*..
gi 79487035 1242 GKIVEQG 1248
Cdd:TIGR02168 1164 VTMQEKG 1170
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
1157-1249 |
4.06e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.60 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1157 GYsTKVGERGVQMSGGQRQRIAIARAILKNP---AILLLDEATSALDVESERVVQQALDRLMANRTTVVV-AHRLSTIKN 1232
Cdd:PRK00349 820 GY-IKLGQPATTLSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVViEHNLDVIKT 898
|
90 100
....*....|....*....|...
gi 79487035 1233 ADTISVL------HGGKIVEQGS 1249
Cdd:PRK00349 899 ADWIIDLgpeggdGGGEIVATGT 921
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1040-1201 |
4.80e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.93 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1040 PSRPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSV-ISLILRFYDP-TAGKVMIEGKDIkklDLKAL------------- 1104
Cdd:NF040905 268 PLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYGRnISGTVFKDGKEV---DVSTVsdaidaglayvte 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1105 -RKHIGLVQQEpalfatTIYENILYGN-EGASQSEVV-ESAMLANAHSFITSLpegySTK---VGERGVQMSGGQRQRIA 1178
Cdd:NF040905 345 dRKGYGLNLID------DIKRNITLANlGKVSRRGVIdENEEIKVAEEYRKKM----NIKtpsVFQKVGNLSGGNQQKVV 414
|
170 180
....*....|....*....|...
gi 79487035 1179 IARAILKNPAILLLDEATSALDV 1201
Cdd:NF040905 415 LSKWLFTDPDVLILDEPTRGIDV 437
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
777-964 |
5.05e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 40.52 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 777 MGERLTLRVRENMFRAILKNEIGWF------DevdntssmLASRLESDATLLKTIVVDRSTILLqNLGLVVTSFIIAFIL 850
Cdd:cd18567 69 LSTSLNLQWTSNLFRHLLRLPLSYFekrhlgD--------IVSRFGSLDEIQQTLTTGFVEALL-DGLMAILTLVMMFLY 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 851 NWRLTLVVLATypLVISGHIseKLFMQGYGGDLNKAYL----KANMLAGESVSNIRTVAAFCAEEKILELYSRELLEPSK 926
Cdd:cd18567 140 SPKLALIVLAA--VALYALL--RLALYPPLRRATEEQIvasaKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAIN 215
|
170 180 190
....*....|....*....|....*....|....*...
gi 79487035 927 SSFRRGQIAGLFYGVSQFFIFSSYGLALWYGSTLMDKG 964
Cdd:cd18567 216 ADIRLQRLQILFSAANGLLFGLENILVIYLGALLVLDG 253
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1167-1250 |
6.53e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 38.88 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1167 VQMSGGQRQRIAIARAI---LKNPAIL-LLDEATSALDVESERVVQQALDRLMANRTTVVVA-HRLSTIKNADTIsvLHG 1241
Cdd:cd03227 76 LQLSGGEKELSALALILalaSLKPRPLyILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVItHLPELAELADKL--IHI 153
|
....*....
gi 79487035 1242 GKIVEQGSH 1250
Cdd:cd03227 154 KKVITGVYK 162
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
1169-1248 |
6.73e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.78 E-value: 6.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487035 1169 MSGGQRQRIAIARAILK---NPAILLLDEATSAL---DVeseRVVQQALDRLMANRTTVVV-AHRLSTIKNADTISVL-- 1239
Cdd:COG0178 827 LSGGEAQRVKLASELSKrstGKTLYILDEPTTGLhfhDI---RKLLEVLHRLVDKGNTVVViEHNLDVIKTADWIIDLgp 903
|
90
....*....|...
gi 79487035 1240 ----HGGKIVEQG 1248
Cdd:COG0178 904 eggdGGGEIVAEG 916
|
|
| |
