|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
40-1221 |
6.41e-162 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 521.13 E-value: 6.41e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 40 LMALGSIGACIHGASVPVFFIFFGKLINIIGLAylfpqeasHKVAKYSLDFVYLSVVILFSSWLEVACWMHTGERQAAKI 119
Cdd:PTZ00265 61 LLGVSFVCATISGGTLPFFVSVFGVIMKNMNLG--------ENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 120 RKAYLRSMLSQDISLFDTEIStgeviSAITSEILVVQDAISEKVGNfmHFISRFIAGFAIGFASVW------QISLVTLS 193
Cdd:PTZ00265 133 KLEFLKSVFYQDGQFHDNNPG-----SKLTSDLDFYLEQVNAGIGT--KFITIFTYASAFLGLYIWslfknaRLTLCITC 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 194 IVPFIALAGGIyafVSSGLIVRVRKSYVKAN---EIAEEVIGNVRTVQAFTGEEKAVSSYQGALRNTYNYGRKAGLAKGL 270
Cdd:PTZ00265 206 VFPLIYICGVI---CNKKVKINKKTSLLYNNntmSIIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 271 GLGSLHFVLFLSWALLIWFTSIVVHKGIAN--------GGESFTTMLNVVIAGLSLGQAAPDISTFMRASAAAYPIFQMI 342
Cdd:PTZ00265 283 HIGMINGFILASYAFGFWYGTRIIISDLSNqqpnndfhGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEII 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 343 ER-----NTEDktGRKLGNVNgDILFKDVTFTYPSRPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTD 417
Cdd:PTZ00265 363 NRkplveNNDD--GKKLKDIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTE 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 418 GAVML-DGNDIRYLDLKWLRGHIGLVNQEPVLFATTIRENIMYG----KD------------------------------ 462
Cdd:PTZ00265 440 GDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslKDlealsnyynedgndsqenknkrnscrakca 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 463 --------DATSEEITNAAKLSEAIS---------------FINNLPEGFETQVGERGIQLSGGQKQRISISRAIVKNPS 519
Cdd:PTZ00265 520 gdlndmsnTTDSNELIEMRKNYQTIKdsevvdvskkvlihdFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPK 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 520 ILLLDEATSALDAESEKIVQEALDRVM--VGRTTVVVAHRLSTVRNADIIAVVG-------------------------- 571
Cdd:PTZ00265 600 ILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLSnrergstvdvdiigedptkdnkennn 679
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 572 ---------------------GGKIIESGSHDELISNPDGAYSSLLRIQEAASPNLNHT--------------------- 609
Cdd:PTZ00265 680 knnkddnnnnnnnnnnkinnaGSYIIEQGTHDALMKNKNGIYYTMINNQKVSSKKSSNNdndkdsdmkssaykdsergyd 759
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 610 PSLPVSTKPLPELPITETTSSIHQSVNQPDTTKQAKVTVGR---------------LYSMIRPDWKYGLCGTLGSFIAGS 674
Cdd:PTZ00265 760 PDEMNGNSKHENESASNKKSCKMSDENASENNAGGKLPFLRnlfkrkpkapnnlriVYREIFSYKKDVTIIALSILVAGG 839
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 675 QMPLFALGIAQaLVSYYMDWETTQNEVKRISILFCCGSVITVIVHTIEHTTFGIMGERLTLRVRQKMFSAILRNEIGWFD 754
Cdd:PTZ00265 840 LYPVFALLYAK-YVSTLFDFANLEANSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFD 918
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 755 KVDNTSSMLASRLESDATLLRTIVVDRSTILLENLGLVVTAFIISFILNWRLTLVVLATYPLI-----ISGHISEKIFMQ 829
Cdd:PTZ00265 919 QDKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYFCPIVAAVLTGTYFIFmrvfaIRARLTANKDVE 998
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 830 GYGGNLSKAYLKAN----------MLAGESISNIRTVVAFCAEEKVLDLYSKELLEPSERSFRRGQMAGILYGVSQ---F 896
Cdd:PTZ00265 999 KKEINQPGTVFAYNsddeifkdpsFLIQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQsaqL 1078
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 897 FIFSsygLALWYGSILMEKGLSSFESVMKTFMVLIVTALVMGEVLALAPDLLKGNQMVVSVFELLDRRTQV-VGDTG--- 972
Cdd:PTZ00265 1079 FINS---FAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRKSNIdVRDNGgir 1155
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 973 -EELSNVEGTIELKGVHFSYPSRPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYD---------------- 1035
Cdd:PTZ00265 1156 iKNKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtnd 1235
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1036 --------------------------------------PTAGIIMIDGQDIKKLKLKSLRRHIGLVQQEPALFATTIYEN 1077
Cdd:PTZ00265 1236 mtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYEN 1315
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1078 ILYGKEGASESEVMEAAKLANAHSFISSLPEGYSTKVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESER 1157
Cdd:PTZ00265 1316 IKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEK 1395
|
1370 1380 1390 1400 1410 1420 1430
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15220188 1158 VVQQALDRL--MRDRTTVVVAHRLSTIKNSDMISVIQD----GKIIE-QGSHNILVENKNGPYSKLISLQQ 1221
Cdd:PTZ00265 1396 LIEKTIVDIkdKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLSVQDGVYKKYVKLAK 1466
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
641-1224 |
1.32e-160 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 491.22 E-value: 1.32e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 641 TKQAKVTVGRLYSMIRPDWKYGLCGTLGSFIAGSQMPLFALGIAQALVSYYMDWETTQneVKRISILFCCGSVITVIVHT 720
Cdd:COG1132 2 SKSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSA--LLLLLLLLLGLALLRALLSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 721 IEHTTFGIMGERLTLRVRQKMFSAILRNEIGWFDKvdNTSSMLASRLESDATLLRTIVVDRSTILLENLGLVVTAFIISF 800
Cdd:COG1132 80 LQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDR--RRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 801 ILNWRLTLVVLATYPLIIsghisekIFMQGYGGNLSKAYLKA-------NMLAGESISNIRTVVAFCAEEKVLDLYSKEL 873
Cdd:COG1132 158 VIDWRLALIVLLVLPLLL-------LVLRLFGRRLRKLFRRVqealaelNGRLQESLSGIRVVKAFGREERELERFREAN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 874 LEPSERSFRRGQMAGILYGVSQFFIFSSYGLALWYGSILMEKGLSSFESVMkTFMVLIVTALV-MGEVLALAPDLLKGNQ 952
Cdd:COG1132 231 EELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLV-AFILYLLRLFGpLRQLANVLNQLQRALA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 953 MVVSVFELLDRRTQVV-GDTGEELSNVEGTIELKGVHFSYPsrPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVL 1031
Cdd:COG1132 310 SAERIFELLDEPPEIPdPPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1032 RFYDPTAGIIMIDGQDIKKLKLKSLRRHIGLVQQEPALFATTIYENILYGKEGASESEVMEAAKLANAHSFISSLPEGYS 1111
Cdd:COG1132 388 RFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYD 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1112 TKVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVVVAHRLSTIKNSDMISVI 1191
Cdd:COG1132 468 TVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVL 547
|
570 580 590
....*....|....*....|....*....|...
gi 15220188 1192 QDGKIIEQGSHNILVEnKNGPYSKLISLQQRQR 1224
Cdd:COG1132 548 DDGRIVEQGTHEELLA-RGGLYARLYRLQFGEE 579
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
40-603 |
4.87e-155 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 476.58 E-value: 4.87e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 40 LMALGSIGACIHGASVPVFFIFFGKLINIIglaylFPQEASHKVAKYSLDFVYLSVVILFSSWLEVACWMHTGERQAAKI 119
Cdd:COG1132 22 LLILALLLLLLSALLELLLPLLLGRIIDAL-----LAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 120 RKAYLRSMLSQDISLFDTEiSTGEVISAITSEILVVQDAISEKVGNFMHFISRFIAGFAIGFASVWQISLVTLSIVPFIA 199
Cdd:COG1132 97 RRDLFEHLLRLPLSFFDRR-RTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 200 LAGGIYAFVSSGLIVRVRKSYVKANEIAEEVIGNVRTVQAFTGEEKAVSSYQGALRNTYNYGRKAGLAKGLGLGSLHFVL 279
Cdd:COG1132 176 LVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 280 FLSWALLIWFTSIVVHKGIANGGE--SFTTMLNVVIAGLS-LGQAapdISTFMRASAAAYPIFQMIERNTE--DKTG-RK 353
Cdd:COG1132 256 NLGLALVLLVGGLLVLSGSLTVGDlvAFILYLLRLFGPLRqLANV---LNQLQRALASAERIFELLDEPPEipDPPGaVP 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 354 LGNVNGDILFKDVTFTYPSRPDVVifDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLK 433
Cdd:COG1132 333 LPPVRGEIEFENVSFSYPGDRPVL--KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLE 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 434 WLRGHIGLVNQEPVLFATTIRENIMYGKDDATSEEITNAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRISISRA 513
Cdd:COG1132 411 SLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARA 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 514 IVKNPSILLLDEATSALDAESEKIVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVGGGKIIESGSHDELISNpDGAYS 593
Cdd:COG1132 491 LLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLAR-GGLYA 569
|
570
....*....|
gi 15220188 594 SLLRIQEAAS 603
Cdd:COG1132 570 RLYRLQFGEE 579
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
361-599 |
4.56e-137 |
|
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: 416.17 E-value: 4.56e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSRPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHIG 440
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 441 LVNQEPVLFATTIRENIMYGKDDATSEEITNAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRISISRAIVKNPSI 520
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15220188 521 LLLDEATSALDAESEKIVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVGGGKIIESGSHDELISNpDGAYSSLLRIQ 599
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQ-KGVYAKLVKAQ 238
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
982-1220 |
5.46e-137 |
|
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: 416.17 E-value: 5.46e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIG 1061
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEPALFATTIYENILYGKEGASESEVMEAAKLANAHSFISSLPEGYSTKVGERGIQMSGGQRQRIAIARAVLKNPEI 1141
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15220188 1142 LLLDEATSALDVESERVVQQALDRLMRDRTTVVVAHRLSTIKNSDMISVIQDGKIIEQGSHNILVENKnGPYSKLISLQ 1220
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQK-GVYAKLVKAQ 238
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
75-599 |
3.46e-124 |
|
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: 395.22 E-value: 3.46e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 75 FPQEASHKVAKYSLDFVYLSVVILFSSWLEVACWMHTGERQAAKIRKAYLRSMLSQDISLFDTeISTGEVISAITSEILV 154
Cdd:TIGR02204 49 FSKDSSGLLNRYFAFLLVVALVLALGTAARFYLVTWLGERVVADIRRAVFAHLISLSPSFFDK-NRSGEVVSRLTTDTTL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 155 VQDAISEKVGNFMHFISRFIAGFAIGFASVWQISLVTLSIVPFIALAggIYAFvssGLIVRVRK-----SYVKANEIAEE 229
Cdd:TIGR02204 128 LQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLP--ILLF---GRRVRKLSresqdRIADAGSYAGE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 230 VIGNVRTVQAFTGEEKAVSSYQGALRNTYNYGRKAGLAKGLGLGSLHFVLFLSWALLIWFTSIVVHKGIANGGESFTTML 309
Cdd:TIGR02204 203 TLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVF 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 310 NVVIAGLSLGQAAPDISTFMRASAAAYPIFQMIERN---TEDKTGRKLG-NVNGDILFKDVTFTYPSRPDVVIFDKLNFV 385
Cdd:TIGR02204 283 YAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEpdiKAPAHPKTLPvPLRGEIEFEQVNFAYPARPDQPALDGLNLT 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 386 IPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHIGLVNQEPVLFATTIRENIMYGKDDAT 465
Cdd:TIGR02204 363 VRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDAT 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 466 SEEITNAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRISISRAIVKNPSILLLDEATSALDAESEKIVQEALDRV 545
Cdd:TIGR02204 443 DEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETL 522
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 15220188 546 MVGRTTVVVAHRLSTVRNADIIAVVGGGKIIESGSHDELISNpDGAYSSLLRIQ 599
Cdd:TIGR02204 523 MKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAK-GGLYARLARLQ 575
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
48-596 |
9.30e-124 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 398.71 E-value: 9.30e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 48 ACIHGASVPvFFIffGKLINIIGLAYLFPQEAShkvAKYSLDFvyLSVVILFSSWLEVACWMHTGERQAAKIRKAYLRSM 127
Cdd:TIGR00958 173 SSLGEMFIP-FYT--GRVIDTLGGDKGPPALAS---AIFFMCL--LSIASSVSAGLRGGSFNYTMARINLRIREDLFRSL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 128 LSQDISLFDTEiSTGEVISAITSEILVVQDAISEKVGNFMHFISRFIAGFAIGFASVWQISLVTLSIVPFIALAGGIYAF 207
Cdd:TIGR00958 245 LRQDLGFFDEN-KTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 208 VSSGLIVRVRKSYVKANEIAEEVIGNVRTVQAFTGEEKAVSSYQGALRNTYNYGRKAGLAKGLGLGSLHFVLFLSWALLI 287
Cdd:TIGR00958 324 RYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVL 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 288 WFTSIVVHKGIANGGEsfttMLNVVIAGLSLGQAAPDISTF----MRASAAAYPIFQMIER--NTEDKTGRKLGNVNGDI 361
Cdd:TIGR00958 404 YYGGQLVLTGKVSSGN----LVSFLLYQEQLGEAVRVLSYVysgmMQAVGASEKVFEYLDRkpNIPLTGTLAPLNLEGLI 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 362 LFKDVTFTYPSRPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHIGL 441
Cdd:TIGR00958 480 EFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVAL 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 442 VNQEPVLFATTIRENIMYGKDDATSEEITNAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRISISRAIVKNPSIL 521
Cdd:TIGR00958 560 VGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVL 639
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15220188 522 LLDEATSALDAESEKIVQEalDRVMVGRTTVVVAHRLSTVRNADIIAVVGGGKIIESGSHDELISNPDgAYSSLL 596
Cdd:TIGR00958 640 ILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQG-CYKHLV 711
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
639-1221 |
3.34e-121 |
|
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: 391.50 E-value: 3.34e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 639 DTTKQAKVTVGRLYSMIRPDWKYGLCGTLGSFIAGsqmpLFALGIA---QALVSYY-----MDWETTqnevkrISILFCC 710
Cdd:COG2274 135 DKRGEKPFGLRWFLRLLRRYRRLLLQVLLASLLIN----LLALATPlftQVVIDRVlpnqdLSTLWV------LAIGLLL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 711 GSVITVIVHTIEHTTFGIMGERLTLRVRQKMFSAILRNEIGWFDKvdNTSSMLASRLeSDATLLRTIVVDRSTILLENLG 790
Cdd:COG2274 205 ALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFES--RSVGDLASRF-RDVESIREFLTGSLLTALLDLL 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 791 LVVTAFIISFILNWRLTLVVLATYPLIISghISekIFMQGYGGNLSKAYLKAN-MLAG---ESISNIRTVVAFCAEEKVL 866
Cdd:COG2274 282 FVLIFLIVLFFYSPPLALVVLLLIPLYVL--LG--LLFQPRLRRLSREESEASaKRQSllvETLRGIETIKALGAESRFR 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 867 DLYSKELLEPSERSFRRGQMAGILYGVSQFFIFSSYGLALWYGSIL-MEKGLSsfesvMKTFM-VLIVTALVMGEVLALA 944
Cdd:COG2274 358 RRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLvIDGQLT-----LGQLIaFNILSGRFLAPVAQLI 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 945 PDLLKGNQMVVSV---FELLDRRT-QVVGDTGEELSNVEGTIELKGVHFSYPSRpDVTIFSDFNLLVPSGKSMALVGQSG 1020
Cdd:COG2274 433 GLLQRFQDAKIALerlDDILDLPPeREEGRSKLSLPRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSG 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1021 SGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIGLVQQEPALFATTIYENILYGKEGASESEVMEAAKLANAH 1100
Cdd:COG2274 512 SGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLH 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1101 SFISSLPEGYSTKVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVVVAHRLS 1180
Cdd:COG2274 592 DFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLS 671
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 15220188 1181 TIKNSDMISVIQDGKIIEQGSHNILVEnKNGPYSKLISLQQ 1221
Cdd:COG2274 672 TIRLADRIIVLDKGRIVEDGTHEELLA-RKGLYAELVQQQL 711
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
650-1217 |
6.76e-120 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 388.31 E-value: 6.76e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 650 RLYSMIRPDWKYglcgtLGSFIagsqMPLFALGIAQALVSYY----MDW---ETTQNEVKRISILFCCGSVITVIVHTIE 722
Cdd:TIGR00958 151 RLLGLSGRDWPW-----LISAF----VFLTLSSLGEMFIPFYtgrvIDTlggDKGPPALASAIFFMCLLSIASSVSAGLR 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 723 HTTFGIMGERLTLRVRQKMFSAILRNEIGWFDKvdNTSSMLASRLESDATLLRTIVVDRSTILLENLGLVVTAFIISFIL 802
Cdd:TIGR00958 222 GGSFNYTMARINLRIREDLFRSLLRQDLGFFDE--NKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWL 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 803 NWRLTLVVLATYPLIIsghISEKIFMQGYGgNLSK----AYLKANMLAGESISNIRTVVAFCAEEKVLDLYsKELLEPSE 878
Cdd:TIGR00958 300 SPRLTMVTLINLPLVF---LAEKVFGKRYQ-LLSEelqeAVAKANQVAEEALSGMRTVRSFAAEEGEASRF-KEALEETL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 879 RSFRRGQMAGILY----GVSQFFIFSsygLALWYGSILMEKGLSSFESVMkTFMV--LIVTALV--MGEVLalaPDLLKG 950
Cdd:TIGR00958 375 QLNKRKALAYAGYlwttSVLGMLIQV---LVLYYGGQLVLTGKVSSGNLV-SFLLyqEQLGEAVrvLSYVY---SGMMQA 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 951 NQMVVSVFELLDRRTQVVGDTGEELSNVEGTIELKGVHFSYPSRPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLV 1030
Cdd:TIGR00958 448 VGASEKVFEYLDRKPNIPLTGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALL 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1031 LRFYDPTAGIIMIDGQDIKKLKLKSLRRHIGLVQQEPALFATTIYENILYGKEGASESEVMEAAKLANAHSFISSLPEGY 1110
Cdd:TIGR00958 528 QNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGY 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1111 STKVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQalDRLMRDRTTVVVAHRLSTIKNSDMISV 1190
Cdd:TIGR00958 608 DTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILV 685
|
570 580
....*....|....*....|....*..
gi 15220188 1191 IQDGKIIEQGSHNILVENKnGPYSKLI 1217
Cdd:TIGR00958 686 LKKGSVVEMGTHKQLMEDQ-GCYKHLV 711
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
729-1220 |
9.46e-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: 383.28 E-value: 9.46e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 729 MGERLTLRVRQKMFSAILRNEIGWFDKvdNTSSMLASRLESDATLLRTIVVDRSTILLENLGLVVTAFIISFILNWRLTL 808
Cdd:TIGR02204 85 LGERVVADIRRAVFAHLISLSPSFFDK--NRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 809 VVLATYPLIISGhisekifMQGYGGNLSKA-------YLKANMLAGESISNIRTVVAFCAEEKVLDLYSKELLEPSERSF 881
Cdd:TIGR02204 163 LVLLAVPLVLLP-------ILLFGRRVRKLsresqdrIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAAR 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 882 RRGQMAGILYGVSQFFIFSSYGLALWYGSILMEKG------LSSFesVMKTFMVLIVTAlVMGEVLAlapDLLKGNQMVV 955
Cdd:TIGR02204 236 QRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGkmsagtLGQF--VFYAVMVAGSIG-TLSEVWG---ELQRAAGAAE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 956 SVFELLdrrtQVVGDTGEELS------NVEGTIELKGVHFSYPSRPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSL 1029
Cdd:TIGR02204 310 RLIELL----QAEPDIKAPAHpktlpvPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQL 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1030 VLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIGLVQQEPALFATTIYENILYGKEGASESEVMEAAKLANAHSFISSLPEG 1109
Cdd:TIGR02204 386 LLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEG 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1110 YSTKVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVVVAHRLSTIKNSDMIS 1189
Cdd:TIGR02204 466 YDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIV 545
|
490 500 510
....*....|....*....|....*....|.
gi 15220188 1190 VIQDGKIIEQGSHNILVEnKNGPYSKLISLQ 1220
Cdd:TIGR02204 546 VMDQGRIVAQGTHAELIA-KGGLYARLARLQ 575
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
93-599 |
2.92e-116 |
|
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: 378.41 E-value: 2.92e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 93 LSVVILFSSWLEVA---CWMHTGERQAAKIRKAYLRSMLSQDISLFDTEiSTGEVISAItSEILVVQDAISekvGNFMHF 169
Cdd:COG2274 202 LLLALLFEGLLRLLrsyLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESR-SVGDLASRF-RDVESIREFLT---GSLLTA 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 170 ISRFIagFAIGFASV-----WQISLVTLSIVPFIALaggIYAFVSSGLIVRVRKSYVKANEIA---EEVIGNVRTVQAFT 241
Cdd:COG2274 277 LLDLL--FVLIFLIVlffysPPLALVVLLLIPLYVL---LGLLFQPRLRRLSREESEASAKRQsllVETLRGIETIKALG 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 242 GEEKAVSSYQGALRNTYNYGRKAG-LAKGLGLGSlHFVLFLSWALLIWFTSIVVHKGIANGGE--SFTTMLNVVIAGL-S 317
Cdd:COG2274 352 AESRFRRRWENLLAKYLNARFKLRrLSNLLSTLS-GLLQQLATVALLWLGAYLVIDGQLTLGQliAFNILSGRFLAPVaQ 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 318 LGQAAPDISTFMRASAAAYPIFQMIERNTEDKTGRKLGNVNGDILFKDVTFTYPSRPDVVIfDKLNFVIPAGKVVALVGG 397
Cdd:COG2274 431 LIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPRLKGDIELENVSFRYPGDSPPVL-DNISLTIKPGERVAIVGR 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 398 SGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHIGLVNQEPVLFATTIRENIMYGKDDATSEEITNAAKLSE 477
Cdd:COG2274 510 SGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAG 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 478 AISFINNLPEGFETQVGERGIQLSGGQKQRISISRAIVKNPSILLLDEATSALDAESEKIVQEALDRVMVGRTTVVVAHR 557
Cdd:COG2274 590 LHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHR 669
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 15220188 558 LSTVRNADIIAVVGGGKIIESGSHDELISNpDGAYSSLLRIQ 599
Cdd:COG2274 670 LSTIRLADRIIVLDKGRIVEDGTHEELLAR-KGLYAELVQQQ 710
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
982-1216 |
4.61e-116 |
|
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: 360.39 E-value: 4.61e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRPDvTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIG 1061
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEPALFATTIYENILYGKEGASESEVMEAAKLANAHSFISSLPEGYSTKVGERGIQMSGGQRQRIAIARAVLKNPEI 1141
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15220188 1142 LLLDEATSALDVESERVVQQALDRLMRDRTTVVVAHRLSTIKNSDMISVIQDGKIIEQGSHNILVEnKNGPYSKL 1216
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLA-QGGVYAKL 233
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
772-1225 |
5.78e-112 |
|
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: 363.37 E-value: 5.78e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 772 TLLRTIVVDRSTILLEnLGLVVTAFIISFilNWRLTLVVLAT---YpLIISGHISEKIFmqGYGGNLSKAYLKANMLAGE 848
Cdd:COG5265 150 FLLRFLLFNILPTLLE-IALVAGILLVKY--DWWFALITLVTvvlY-IAFTVVVTEWRT--KFRREMNEADSEANTRAVD 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 849 SISNIRTVVAFCAEEKVLDLYSKELLEpSERSFRRGQMAGILYGVSQFFIFSSyGLA--LWYGSILMEKG---LSSFesV 923
Cdd:COG5265 224 SLLNYETVKYFGNEAREARRYDEALAR-YERAAVKSQTSLALLNFGQALIIAL-GLTamMLMAAQGVVAGtmtVGDF--V 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 924 M-KTFMVLIVTAL-VMGEV-----LALApDLlkgNQMvvsvFELLDRRTQVVGDTG-EELSNVEGTIELKGVHFSY-PSR 994
Cdd:COG5265 300 LvNAYLIQLYIPLnFLGFVyreirQALA-DM---ERM----FDLLDQPPEVADAPDaPPLVVGGGEVRFENVSFGYdPER 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 995 PdvtIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIGLVQQEPALFATTI 1074
Cdd:COG5265 372 P---ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTI 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1075 YENILYGKEGASESEVMEAAKLANAHSFISSLPEGYSTKVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVE 1154
Cdd:COG5265 449 AYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSR 528
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15220188 1155 SERVVQQALDRLMRDRTTVVVAHRLSTIKNSDMISVIQDGKIIEQGSHNILVEnKNGPYSKLISLQQRQRH 1225
Cdd:COG5265 529 TERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLA-QGGLYAQMWARQQEEEE 598
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
650-1223 |
4.43e-110 |
|
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: 357.10 E-value: 4.43e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 650 RLYSMIRPDWKYGLCGTLGSFIAGSQMPLFAlgiaqALVSYYMD---WETTQNEVKRISILFCCGSVITVIVHTIEHTTF 726
Cdd:TIGR02203 4 RLWSYVRPYKAGLVLAGVAMILVAATESTLA-----ALLKPLLDdgfGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 727 GIMGERLTLRVRQKMFSAILRNEIGWFDKvdNTSSMLASRLESDATLLRTIVVDRSTILLENLGLVVTAFIISFILNWRL 806
Cdd:TIGR02203 79 SWVSNKVVRDIRVRMFEKLLGLPVSFFDR--QPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 807 TLVVLATYPLI--ISGHISEKIFMQGYggNLSKAYLKANMLAGESISNIRTVVAFCAEEkvldlYSKELLEPSERSFRRG 884
Cdd:TIGR02203 157 TLIVVVMLPVLsiLMRRVSKRLRRISK--EIQNSMGQVTTVAEETLQGYRVVKLFGGQA-----YETRRFDAVSNRNRRL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 885 QM-----AGILYGVSQFFIFSSYGLALWygsilmekgLSSFESVMKTFMVLIVTALVMGEVLALAP---------DLLKG 950
Cdd:TIGR02203 230 AMkmtsaGSISSPITQLIASLALAVVLF---------IALFQAQAGSLTAGDFTAFITAMIALIRPlksltnvnaPMQRG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 951 NQMVVSVFELLDRRTQVvgDTGE-ELSNVEGTIELKGVHFSYPSRpDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSL 1029
Cdd:TIGR02203 301 LAAAESLFTLLDSPPEK--DTGTrAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1030 VLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIGLVQQEPALFATTIYENILYGK-EGASESEVMEAAKLANAHSFISSLPE 1108
Cdd:TIGR02203 378 IPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPL 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1109 GYSTKVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVVVAHRLSTIKNSDMI 1188
Cdd:TIGR02203 458 GLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRI 537
|
570 580 590
....*....|....*....|....*....|....*
gi 15220188 1189 SVIQDGKIIEQGSHNILVEnKNGPYSKLISLQQRQ 1223
Cdd:TIGR02203 538 VVMDDGRIVERGTHNELLA-RNGLYAQLHNMQFRE 571
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
361-595 |
7.47e-109 |
|
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: 341.13 E-value: 7.47e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSRPDVVIfDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHIG 440
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVL-RDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 441 LVNQEPVLFATTIRENIMYGKDDATSEEITNAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRISISRAIVKNPSI 520
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15220188 521 LLLDEATSALDAESEKIVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVGGGKIIESGSHDELISNpDGAYSSL 595
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQ-GGVYAKL 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
982-1220 |
3.18e-107 |
|
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: 336.89 E-value: 3.18e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPsrPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIG 1061
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEPALFATTIYENILYGKEGASESEVMEAAKLANAHSFISSLPEGYSTKVGERGIQMSGGQRQRIAIARAVLKNPEI 1141
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15220188 1142 LLLDEATSALDVESERVVQQALDRLMRDRTTVVVAHRLSTIKNSDMISVIQDGKIIEQGSHNILVeNKNGPYSKLISLQ 1220
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELL-AKGGLYAEMWKAQ 236
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
118-599 |
5.95e-107 |
|
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: 348.63 E-value: 5.95e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 118 KIRKAYLRSMLSQDISLFDTEiSTGEVISAITSEILVVQDAISEKVGNFMHFISRFIAGFAIGFASVWQISLVTLSIVPF 197
Cdd:TIGR02203 88 DIRVRMFEKLLGLPVSFFDRQ-PTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 198 IALAGGIYAFVSSGLIVRVRKSYVKANEIAEEVIGNVRTVQAFTGEEKAVSSYQGALRNTYNYGRKAGLAKGLGLGSLHF 277
Cdd:TIGR02203 167 LSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 278 VLFLSWALLIWFTSIVVHKGIANGGE--SFTTMLNVVIAGL-SLGQAApdiSTFMRASAAAYPIFQMIERNTE-DKTGRK 353
Cdd:TIGR02203 247 IASLALAVVLFIALFQAQAGSLTAGDftAFITAMIALIRPLkSLTNVN---APMQRGLAAAESLFTLLDSPPEkDTGTRA 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 354 LGNVNGDILFKDVTFTYPSRpDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLK 433
Cdd:TIGR02203 324 IERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLA 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 434 WLRGHIGLVNQEPVLFATTIRENIMYGK-DDATSEEITNAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRISISR 512
Cdd:TIGR02203 403 SLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIAR 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 513 AIVKNPSILLLDEATSALDAESEKIVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVGGGKIIESGSHDELISNpDGAY 592
Cdd:TIGR02203 483 ALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLAR-NGLY 561
|
....*..
gi 15220188 593 SSLLRIQ 599
Cdd:TIGR02203 562 AQLHNMQ 568
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
41-338 |
1.05e-102 |
|
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: 327.12 E-value: 1.05e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 41 MALGSIGACIHGASVPVFFIFFGKLINII---GLAYLFPQEASHKVAKYSLDFVYLSVVILFSSWLEVACWMHTGERQAA 117
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFtdfGSGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 118 KIRKAYLRSMLSQDISLFDTeISTGEVISAITSEILVVQDAISEKVGNFMHFISRFIAGFAIGFASVWQISLVTLSIVPF 197
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDK-NGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 198 IALAGGIYAFVSSGLIVRVRKSYVKANEIAEEVIGNVRTVQAFTGEEKAVSSYQGALRNTYNYGRKAGLAKGLGLGSLHF 277
Cdd:cd18577 160 IAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFF 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15220188 278 VLFLSWALLIWFTSIVVHKGIANGGESFTTMLNVVIAGLSLGQAAPDISTFMRASAAAYPI 338
Cdd:cd18577 240 IIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
361-599 |
1.09e-101 |
|
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: 321.87 E-value: 1.09e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTY-PSRPdvvIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHI 439
Cdd:cd03253 1 IEFENVTFAYdPGRP---VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 440 GLVNQEPVLFATTIRENIMYGKDDATSEEITNAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRISISRAIVKNPS 519
Cdd:cd03253 78 GVVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 520 ILLLDEATSALDAESEKIVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVGGGKIIESGSHDELIsNPDGAYSSLLRIQ 599
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELL-AKGGLYAEMWKAQ 236
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
339-603 |
4.90e-100 |
|
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: 331.01 E-value: 4.90e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 339 FQMIERNTE--DKTGRK-LGNVNGDILFKDVTFTY-PSRPdvvIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYE 414
Cdd:COG5265 333 FDLLDQPPEvaDAPDAPpLVVGGGEVRFENVSFGYdPERP---ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYD 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 415 PTDGAVMLDGNDIRYLDLKWLRGHIGLVNQEPVLFATTIRENIMYGKDDATSEEITNAAKLSEAISFINNLPEGFETQVG 494
Cdd:COG5265 410 VTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVG 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 495 ERGIQLSGGQKQRISISRAIVKNPSILLLDEATSALDAESEKIVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVGGGK 574
Cdd:COG5265 490 ERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGR 569
|
250 260
....*....|....*....|....*....
gi 15220188 575 IIESGSHDELISNpDGAYSSLLRIQEAAS 603
Cdd:COG5265 570 IVERGTHAELLAQ-GGLYAQMWARQQEEE 597
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
652-967 |
3.85e-99 |
|
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: 318.24 E-value: 3.85e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 652 YSMIRPDWKYGLCGTLGSFIAGSQMPLFALGIAQALVSYYM-DWETTQNEVKRISILFCCGSVITVIVHTIEHTTFGIMG 730
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLpDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 731 ERLTLRVRQKMFSAILRNEIGWFDKVDNTSSMLASRLESDATLLRTIVVDRSTILLENLGLVVTAFIISFILNWRLTLVV 810
Cdd:cd18578 81 ERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 811 LATYPLIISGHISEKIFMQGYGGNLSKAYLKANMLAGESISNIRTVVAFCAEEKVLDLYSKELLEPSERSFRRGQMAGIL 890
Cdd:cd18578 161 LATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLG 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15220188 891 YGVSQFFIFSSYGLALWYGSILMEKGLSSFESVMKTFMVLIVTALVMGEVLALAPDLLKGNQMVVSVFELLDRRTQV 967
Cdd:cd18578 241 FGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
980-1211 |
2.59e-96 |
|
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: 306.84 E-value: 2.59e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 980 GTIELKGVHFSYpsRPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRH 1059
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1060 IGLVQQEPALFATTIYENILYGKEGASESEVMEAAKLANAHSFISSLPEGYSTKVGERGIQMSGGQRQRIAIARAVLKNP 1139
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220188 1140 EILLLDEATSALDVESERVVQQALDRLMRDRTTVVVAHRLSTIKNSDMISVIQDGKIIEQGSHNILVEnKNG 1211
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLA-KKG 229
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
650-1209 |
7.56e-96 |
|
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: 318.24 E-value: 7.56e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 650 RLYSMIRPDWKYGLCGTLGSFIAGSQMPLFALGIAQALVSYYMDWETTQNEVKRISILFCCGSVITVIVHTIEHTTFgIM 729
Cdd:COG4988 7 RLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAF-RA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 730 GERLTLRVRQKMFSAILRNEIGWfdkvdntssmlaSRLESDATLLrTIVVDRstilLENL--------------GLV-VT 794
Cdd:COG4988 86 AARVKRRLRRRLLEKLLALGPAW------------LRGKSTGELA-TLLTEG----VEALdgyfarylpqlflaALVpLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 795 AFIISFILNWRLTLVVLATYPLIIsghisekIFMQ--GYG-GNLSKAYLKA-NMLAG---ESISNIRTVVAFCAEEKvld 867
Cdd:COG4988 149 ILVAVFPLDWLSGLILLVTAPLIP-------LFMIlvGKGaAKASRRQWRAlARLSGhflDRLRGLTTLKLFGRAKA--- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 868 lYSKELLEPSERsFRRGQMAgILY------GVSQFFIFSSYGLALWY-GSILMEKGLSSFEsvmkTFMVLIvtalvmgev 940
Cdd:COG4988 219 -EAERIAEASED-FRKRTMK-VLRvaflssAVLEFFASLSIALVAVYiGFRLLGGSLTLFA----ALFVLL--------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 941 laLAPDL--------------LKGNQMVVSVFELLDRRTQVVGDTGEELSNVEG-TIELKGVHFSYPSRPdvTIFSDFNL 1005
Cdd:COG4988 283 --LAPEFflplrdlgsfyharANGIAAAEKIFALLDAPEPAAPAGTAPLPAAGPpSIELEDVSFSYPGGR--PALDGLSL 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1006 LVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIGLVQQEPALFATTIYENILYGKEGA 1085
Cdd:COG4988 359 TIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDA 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1086 SESEVMEAAKLANAHSFISSLPEGYSTKVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDR 1165
Cdd:COG4988 439 SDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRR 518
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 15220188 1166 LMRDRTTVVVAHRLSTIKNSDMISVIQDGKIIEQGSHNILVENK 1209
Cdd:COG4988 519 LAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
359-585 |
1.06e-94 |
|
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: 302.61 E-value: 1.06e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 359 GDILFKDVTFTYpsRPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGH 438
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 439 IGLVNQEPVLFATTIRENIMYGKDDATSEEITNAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRISISRAIVKNP 518
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15220188 519 SILLLDEATSALDAESEKIVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVGGGKIIESGSHDELI 585
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
119-599 |
5.23e-94 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 313.88 E-value: 5.23e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 119 IRKAYLRSMLSQDISLFDTEiSTGEVISAITSEILVVQDAISEKVGNFMHFISRFIAGFAIGFASVWQISLVTLSIVPFI 198
Cdd:PRK11176 100 MRRRLFGHMMGMPVSFFDKQ-STGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVIAPIV 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 199 ALAGGIyafVSSglivRVRK-------SYVKANEIAEEVIGNVRTVQAFTGEEKAVSSYQGALRNTYNYGRKAGLAKGLG 271
Cdd:PRK11176 179 SIAIRV---VSK----RFRNisknmqnTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASSIS 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 272 LGSLHFVLFLSWALLIWFTSIVVHKGIANGGeSFTTMLNVVIAGLSLGQAAPDI-STFMRASAAAYPIFQMIERNTEDKT 350
Cdd:PRK11176 252 DPIIQLIASLALAFVLYAASFPSVMDTLTAG-TITVVFSSMIALMRPLKSLTNVnAQFQRGMAACQTLFAILDLEQEKDE 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 351 G-RKLGNVNGDILFKDVTFTYPSRpDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRY 429
Cdd:PRK11176 331 GkRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRD 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 430 LDLKWLRGHIGLVNQEPVLFATTIRENIMYGKDDATS-EEITNAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRI 508
Cdd:PRK11176 410 YTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQYSrEQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRI 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 509 SISRAIVKNPSILLLDEATSALDAESEKIVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVGGGKIIESGSHDELISNp 588
Cdd:PRK11176 490 AIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQ- 568
|
490
....*....|.
gi 15220188 589 DGAYSSLLRIQ 599
Cdd:PRK11176 569 NGVYAQLHKMQ 579
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
185-599 |
8.07e-94 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 313.44 E-value: 8.07e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 185 WQIS--LVTLSIVpFIALAggiyAFV---SSGLIVRVRKSYVKANEIAEEVIGNVRTVQAFTGEEKAVSsyqgALRNTYN 259
Cdd:PRK13657 156 WRLSlvLVVLGIV-YTLIT----TLVmrkTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNRIEAETQ----ALRDIAD 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 260 YGRKA--------GLAKGLGLGSLHFVLFLSWALLIWFtsivVHKGIANGGE-----SFTTMLnvvIAGL--------SL 318
Cdd:PRK13657 227 NLLAAqmpvlswwALASVLNRAASTITMLAILVLGAAL----VQKGQLRVGEvvafvGFATLL---IGRLdqvvafinQV 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 319 GQAAPDISTFmrasaaaypiFQMIE--RNTEDKTG-RKLGNVNGDILFKDVTFTYPSRPDVVifDKLNFVIPAGKVVALV 395
Cdd:PRK13657 300 FMAAPKLEEF----------FEVEDavPDVRDPPGaIDLGRVKGAVEFDDVSFSYDNSRQGV--EDVSFEAKPGQTVAIV 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 396 GGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHIGLVNQEPVLFATTIRENIMYGKDDATSEEITNAAKL 475
Cdd:PRK13657 368 GPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAER 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 476 SEAISFINNLPEGFETQVGERGIQLSGGQKQRISISRAIVKNPSILLLDEATSALDAESEKIVQEALDRVMVGRTTVVVA 555
Cdd:PRK13657 448 AQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIA 527
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 15220188 556 HRLSTVRNADIIAVVGGGKIIESGSHDELISNpDGAYSSLLRIQ 599
Cdd:PRK13657 528 HRLSTVRNADRILVFDNGRVVESGSFDELVAR-GGRFAALLRAQ 570
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
735-1220 |
2.80e-92 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 308.87 E-value: 2.80e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 735 LRVRQKMFSAILRNEIGWFDKvdNTSSMLASRLESDATL--------LRTIVVDRSTILlenlGLvvtaFIISFILNWRL 806
Cdd:PRK11176 98 MTMRRRLFGHMMGMPVSFFDK--QSTGTLLSRITYDSEQvassssgaLITVVREGASII----GL----FIMMFYYSWQL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 807 TLVVLATYPlIISGHIS--EKIF------MQGYGGNLSKAylKANMLAGEsisniRTVVAFCA---EEKVLDLYSKELle 875
Cdd:PRK11176 168 SLILIVIAP-IVSIAIRvvSKRFrnisknMQNTMGQVTTS--AEQMLKGH-----KEVLIFGGqevETKRFDKVSNRM-- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 876 psersfRRGQM-----AGILYGVSQFFifSSYGLALwygsILMekgLSSFESVMKTFMVLIVTaLVMGEVLALAPDL--- 947
Cdd:PRK11176 238 ------RQQGMkmvsaSSISDPIIQLI--ASLALAF----VLY---AASFPSVMDTLTAGTIT-VVFSSMIALMRPLksl 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 948 -------LKGNQMVVSVFELLDRRTQVvgDTGE-ELSNVEGTIELKGVHFSYPSRpDVTIFSDFNLLVPSGKSMALVGQS 1019
Cdd:PRK11176 302 tnvnaqfQRGMAACQTLFAILDLEQEK--DEGKrVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRS 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1020 GSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIGLVQQEPALFATTIYENILYGKEGA-SESEVMEAAKLAN 1098
Cdd:PRK11176 379 GSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAY 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1099 AHSFISSLPEGYSTKVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVVVAHR 1178
Cdd:PRK11176 459 AMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHR 538
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 15220188 1179 LSTIKNSDMISVIQDGKIIEQGSHNILVEnKNGPYSKLISLQ 1220
Cdd:PRK11176 539 LSTIEKADEILVVEDGEIVERGTHAELLA-QNGVYAQLHKMQ 579
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
798-1216 |
1.88e-91 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 306.89 E-value: 1.88e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 798 ISFILNWRLT--LVVLATYPLIISGHISEKIF-MQG----YGGNLSKAylkanmlAGESISNIRTVVAFC---AEEKVLD 867
Cdd:PRK13657 150 LALFMNWRLSlvLVVLGIVYTLITTLVMRKTKdGQAaveeHYHDLFAH-------VSDAIGNVSVVQSYNrieAETQALR 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 868 LYSKELLEpsersfrrgqmagilygvSQFFIFSSYGLA---------------LWYGSILMEKGLSSFESVMkTFM---- 928
Cdd:PRK13657 223 DIADNLLA------------------AQMPVLSWWALAsvlnraastitmlaiLVLGAALVQKGQLRVGEVV-AFVgfat 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 929 VLI-----VTALVMGEVLAlAPDLLKGNQMVVSVFELLDRrtqvvgDTGEELSNVEGTIELKGVHFSYP-SRPDVtifSD 1002
Cdd:PRK13657 284 LLIgrldqVVAFINQVFMA-APKLEEFFEVEDAVPDVRDP------PGAIDLGRVKGAVEFDDVSFSYDnSRQGV---ED 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1003 FNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIGLVQQEPALFATTIYENILYGK 1082
Cdd:PRK13657 354 VSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGR 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1083 EGASESEVMEAAKLANAHSFISSLPEGYSTKVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQA 1162
Cdd:PRK13657 434 PDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAA 513
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 15220188 1163 LDRLMRDRTTVVVAHRLSTIKNSDMISVIQDGKIIEQGSHNILVEnKNGPYSKL 1216
Cdd:PRK13657 514 LDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVA-RGGRFAAL 566
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
280-587 |
2.96e-89 |
|
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: 299.75 E-value: 2.96e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 280 FLSWALLIWFTSIvvhkGIANGGesFTTMLNVVIAGLSLGQA------AP-------DISTF----MRASAAAYPIFQMI 342
Cdd:COG4988 242 FLSSAVLEFFASL----SIALVA--VYIGFRLLGGSLTLFAAlfvlllAPefflplrDLGSFyharANGIAAAEKIFALL 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 343 ERN---TEDKTGRKLGNVNGDILFKDVTFTYPSRPDVVifDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGA 419
Cdd:COG4988 316 DAPepaAPAGTAPLPAAGPPSIELEDVSFSYPGGRPAL--DGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGS 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 420 VMLDGNDIRYLDLKWLRGHIGLVNQEPVLFATTIRENIMYGKDDATSEEITNAAKLSEAISFINNLPEGFETQVGERGIQ 499
Cdd:COG4988 394 ILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRG 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 500 LSGGQKQRISISRAIVKNPSILLLDEATSALDAESEKIVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVGGGKIIESG 579
Cdd:COG4988 474 LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQG 553
|
....*...
gi 15220188 580 SHDELISN 587
Cdd:COG4988 554 THEELLAK 561
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
725-1219 |
1.96e-88 |
|
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: 297.83 E-value: 1.96e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 725 TFGIM------GERL-----TLRV----RQKMFSAILRNEIGWFDKVDntSSMLASRLESDatllrtivVDRstilLENL 789
Cdd:COG4987 63 AFAIGrtvfryLERLvshdaTLRLladlRVRLYRRLEPLAPAGLARLR--SGDLLNRLVAD--------VDA----LDNL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 790 ----------GLVVTAFIISFI--LNWRLTLVVLATY-------PLI---ISGHISEKIfmqgyggnlskAYLKANM--L 845
Cdd:COG4987 129 ylrvllpllvALLVILAAVAFLafFSPALALVLALGLllaglllPLLaarLGRRAGRRL-----------AAARAALraR 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 846 AGESISNIRTVVAFCAEEKVLDLY---SKELLEPSERSFR-RGQMAGILYGVSQFFIFssygLALWYGSILMEKGLSSFe 921
Cdd:COG4987 198 LTDLLQGAAELAAYGALDRALARLdaaEARLAAAQRRLARlSALAQALLQLAAGLAVV----AVLWLAAPLVAAGALSG- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 922 svmkTFMVLIV-TALVMGEVLALAPD-LLKGNQMVVS---VFELLDRRTQVVGDTGEELSNVEGTIELKGVHFSYPSRPD 996
Cdd:COG4987 273 ----PLLALLVlAALALFEALAPLPAaAQHLGRVRAAarrLNELLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGR 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 997 vTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIGLVQQEPALFATTIYE 1076
Cdd:COG4987 349 -PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRE 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1077 NILYGKEGASESEVMEAAKLANAHSFISSLPEGYSTKVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESE 1156
Cdd:COG4987 428 NLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATE 507
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15220188 1157 RVVQQALDRLMRDRTTVVVAHRLSTIKNSDMISVIQDGKIIEQGSHNILVEnKNGPYSKLISL 1219
Cdd:COG4987 508 QALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLA-QNGRYRQLYQR 569
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
361-599 |
1.00e-82 |
|
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: 270.13 E-value: 1.00e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYpsRPD-VVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHI 439
Cdd:cd03252 1 ITFEHVRFRY--KPDgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 440 GLVNQEPVLFATTIRENIMYGKDDATSEEITNAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRISISRAIVKNPS 519
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 520 ILLLDEATSALDAESEKIVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVGGGKIIESGSHDELISNpDGAYSSLLRIQ 599
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE-NGLYAYLYQLQ 237
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
982-1220 |
7.14e-81 |
|
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: 264.73 E-value: 7.14e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYpsRPDVT-IFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHI 1060
Cdd:cd03252 1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1061 GLVQQEPALFATTIYENILYGKEGASESEVMEAAKLANAHSFISSLPEGYSTKVGERGIQMSGGQRQRIAIARAVLKNPE 1140
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1141 ILLLDEATSALDVESERVVQQALDRLMRDRTTVVVAHRLSTIKNSDMISVIQDGKIIEQGSHNILVEnKNGPYSKLISLQ 1220
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLA-ENGLYAYLYQLQ 237
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
977-1196 |
6.97e-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: 261.64 E-value: 6.97e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 977 NVEGTIELKGVHFSYPSRPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSL 1056
Cdd:cd03248 7 HLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1057 RRHIGLVQQEPALFATTIYENILYGKEGASESEVMEAAKLANAHSFISSLPEGYSTKVGERGIQMSGGQRQRIAIARAVL 1136
Cdd:cd03248 87 HSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1137 KNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVVVAHRLSTIKNSDMISVIQDGKI 1196
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
140-598 |
1.74e-79 |
|
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: 272.80 E-value: 1.74e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 140 STGEVISAITSEILVVQDAisekvgnFMHFISRFIAGFAIGFASVWQISLVTLSIVPFIALAGGIYAFVSSGLIVRVRKs 219
Cdd:COG4987 110 RSGDLLNRLVADVDALDNL-------YLRVLLPLLVALLVILAAVAFLAFFSPALALVLALGLLLAGLLLPLLAARLGR- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 220 yvKANEIAEEVIGNVRT-----------VQAFTGEEKAVSSYQGALRNTYNYGRKAGLAKGLGLGSLHFVLFLSWALLIW 288
Cdd:COG4987 182 --RAGRRLAAARAALRArltdllqgaaeLAAYGALDRALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLW 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 289 FTSIVVHKGIANGGE----------SFTTMLNVVIAGLSLGQaapdistfMRASAAAypIFQMIER--NTEDKTGRKLGN 356
Cdd:COG4987 260 LAAPLVAAGALSGPLlallvlaalaLFEALAPLPAAAQHLGR--------VRAAARR--LNELLDAppAVTEPAEPAPAP 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 357 VNGDILFKDVTFTYPSRPDVViFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLR 436
Cdd:COG4987 330 GGPSLELEDVSFRYPGAGRPV-LDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLR 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 437 GHIGLVNQEPVLFATTIRENIMYGKDDATSEEITNAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRISISRAIVK 516
Cdd:COG4987 409 RRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLR 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 517 NPSILLLDEATSALDAESEKIVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVGGGKIIESGSHDELISNPdGAYSSLL 596
Cdd:COG4987 489 DAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQN-GRYRQLY 567
|
..
gi 15220188 597 RI 598
Cdd:COG4987 568 QR 569
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
356-575 |
1.28e-78 |
|
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: 258.17 E-value: 1.28e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 356 NVNGDILFKDVTFTYPSRPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWL 435
Cdd:cd03248 7 HLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 436 RGHIGLVNQEPVLFATTIRENIMYGKDDATSEEITNAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRISISRAIV 515
Cdd:cd03248 87 HSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 516 KNPSILLLDEATSALDAESEKIVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVGGGKI 575
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
982-1195 |
1.68e-76 |
|
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: 249.99 E-value: 1.68e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRPdVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIG 1061
Cdd:cd03228 1 IEFKNVSFSYPGRP-KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEPALFATTIYENILygkegasesevmeaaklanahsfisslpegystkvgergiqmSGGQRQRIAIARAVLKNPEI 1141
Cdd:cd03228 80 YVPQDPFLFSGTIRENIL------------------------------------------SGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15220188 1142 LLLDEATSALDVESERVVQQALDRLMRDRTTVVVAHRLSTIKNSDMISVIQDGK 1195
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 ... |
774-1220 |
2.19e-76 |
|
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: 267.38 E-value: 2.19e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 774 LRTIVVDRSTILLENLGLVVTAFIISFILNWRLTLVVLATYP------LIISGHISEKIFMQGYGGNLSKAYLKanmlag 847
Cdd:TIGR01846 248 IRNFLTGSALTVVLDLLFVVVFLAVMFFYSPTLTGVVIGSLVcyallsVFVGPILRKRVEDKFERSAAATSFLV------ 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 848 ESISNIRTVVAFCAEEKVLDLYSKELLEPSERSFRRGQMAGILYGVSQFFIFSSYGLALWYGSILMEKGLSSFESVMKTF 927
Cdd:TIGR01846 322 ESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALSPGQLVAFN 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 928 MVlivTALVMGEVLALAPDLLKGNQMVVSVFEL---LDRRTQVVGDTGEELSNVEGTIELKGVHFSY-PSRPDVtiFSDF 1003
Cdd:TIGR01846 402 ML---AGRVTQPVLRLAQLWQDFQQTGIALERLgdiLNSPTEPRSAGLAALPELRGAITFENIRFRYaPDSPEV--LSNL 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1004 NLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIGLVQQEPALFATTIYENILYGKE 1083
Cdd:TIGR01846 477 NLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNP 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1084 GASESEVMEAAKLANAHSFISSLPEGYSTKVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQAL 1163
Cdd:TIGR01846 557 GAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNM 636
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 15220188 1164 DRLMRDRTTVVVAHRLSTIKNSDMISVIQDGKIIEQGSHNILVEnKNGPYSKLISLQ 1220
Cdd:TIGR01846 637 REICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLA-LQGLYARLWQQQ 692
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
189-599 |
2.20e-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: 264.68 E-value: 2.20e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 189 LVTLSIVPFIALaggiYAFVSSGLIVRVRKSYVK---ANEIAEEVIGNVRTVQAFTGEEKAVSSYQGALRNTYNYGRKAG 265
Cdd:TIGR01846 283 VVIGSLVCYALL----SVFVGPILRKRVEDKFERsaaATSFLVESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVT 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 266 LAKGLGLGSLHFVLFLSWALLIWFTSIVVHKGIANGGESFT-TMLNVVIAG--LSLGQAAPDistFMRASAAAYPIFQMI 342
Cdd:TIGR01846 359 NLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALSPGQLVAfNMLAGRVTQpvLRLAQLWQD---FQQTGIALERLGDIL 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 343 ERNTEDKTGRK--LGNVNGDILFKDVTFTYpsRPDV-VIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGA 419
Cdd:TIGR01846 436 NSPTEPRSAGLaaLPELRGAITFENIRFRY--APDSpEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQ 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 420 VMLDGNDIRYLDLKWLRGHIGLVNQEPVLFATTIRENIMYGKDDATSEEITNAAKLSEAISFINNLPEGFETQVGERGIQ 499
Cdd:TIGR01846 514 VLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGAN 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 500 LSGGQKQRISISRAIVKNPSILLLDEATSALDAESEKIVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVGGGKIIESG 579
Cdd:TIGR01846 594 LSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESG 673
|
410 420
....*....|....*....|
gi 15220188 580 SHDELISNpDGAYSSLLRIQ 599
Cdd:TIGR01846 674 RHEELLAL-QGLYARLWQQQ 692
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
361-574 |
2.69e-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: 246.53 E-value: 2.69e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSRPDVViFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHIG 440
Cdd:cd03228 1 IEFKNVSFSYPGRPKPV-LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 441 LVNQEPVLFATTIRENImygkddatseeitnaaklseaisfinnlpegfetqvgergiqLSGGQKQRISISRAIVKNPSI 520
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15220188 521 LLLDEATSALDAESEKIVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVGGGK 574
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
359-579 |
1.69e-72 |
|
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: 240.57 E-value: 1.69e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 359 GDILFKDVTFTYPSRPDVVIfDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGH 438
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPAL-DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 439 IGLVNQEPVLFATTIRENIMYGKDDATSEEITNAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRISISRAIVKNP 518
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15220188 519 SILLLDEATSALDAESEKIVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVGGGKIIESG 579
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
678-1217 |
8.59e-71 |
|
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: 248.65 E-value: 8.59e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 678 LFALGIAQA-LVSYYMDWETTQNEVKRISILFCCGSVITVIVHTIEHTTFGIMGERLTLRVRQKMFSAILRNEIGWFDKv 756
Cdd:TIGR01192 31 LAAITIAEPiLFGRIIDAISSKSDVLPTLALWAGFGVFNTIAYVLVAREADRLAHGRRATLLTEAFGRIISMPLSWHQQ- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 757 DNTSSMLASRLESDATLlrtivvdrSTILLE----NLGLVVTAFII---SFILNWRLT--LVVLATYPLIISghiseKIF 827
Cdd:TIGR01192 110 RGTSNALHTLLRATETL--------FGLWLEfmrqHLATFVALFLLiptAFAMDWRLSivLMVLGILYILIA-----KLV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 828 MQ-GYGGNLSKAYLKANMLA--GESISNIRTVVAF---CAEEKVLDLYSKELLEpsersfrrgqmagilygvSQFFIFSS 901
Cdd:TIGR01192 177 MQrTKNGQAAVEHHYHNVFKhvSDSISNVSVVHSYnriEAETSALKQFTNNLLS------------------AQYPVLDW 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 902 YGLAlwygsilmeKGLSSFESVMKTFMVLIVTA-------LVMGEVLALA--PDLLKG--NQMVVSVFELLDRRTQV--- 967
Cdd:TIGR01192 239 WALA---------SGLNRMASTISMMCILVIGTvlvikgeLSVGEVIAFIgfANLLIGrlDQMSGFITQIFEARAKLedf 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 968 ------VGDTGE-----ELSNVEGTIELKGVHFSYPSRPDVTifSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDP 1036
Cdd:TIGR01192 310 fdledsVFQREEpadapELPNVKGAVEFRHITFEFANSSQGV--FDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1037 TAGIIMIDGQDIKKLKLKSLRRHIGLVQQEPALFATTIYENILYGKEGASESEVMEAAKLANAHSFISSLPEGYSTKVGE 1116
Cdd:TIGR01192 388 TVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGE 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1117 RGIQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVVVAHRLSTIKNSDMISVIQDGKI 1196
Cdd:TIGR01192 468 RGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRL 547
|
570 580
....*....|....*....|.
gi 15220188 1197 IEQGSHNILVeNKNGPYSKLI 1217
Cdd:TIGR01192 548 IEKGSFQELI-QKDGRFYKLL 567
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
980-1200 |
8.58e-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: 8.58e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 980 GTIELKGVHFSYPSRPDVTIfSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRH 1059
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPAL-DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1060 IGLVQQEPALFATTIYENILYGKEGASESEVMEAAKLANAHSFISSLPEGYSTKVGERGIQMSGGQRQRIAIARAVLKNP 1139
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15220188 1140 EILLLDEATSALDVESERVVQQALDRLMRDRTTVVVAHRLSTIKNSDMISVIQDGKIIEQG 1200
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
732-1218 |
8.36e-69 |
|
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: 246.01 E-value: 8.36e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 732 RLTLRVRQKMFSAILRNEIGWFDKvdNTSSMLASRLESDATLLRTIVVDRSTILLeNLGLVVTAFIISFILNWRLTLVVL 811
Cdd:TIGR03796 224 KLAVGMSARFLWHILRLPVRFFAQ--RHAGDIASRVQLNDQVAEFLSGQLATTAL-DAVMLVFYALLMLLYDPVLTLIGI 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 812 AT------YPLIISGHI--SEKIFMQGYGgnlskaylkanMLAGESIS---NIRTVVAFCAEE----KVLDLYSKELLEP 876
Cdd:TIGR03796 301 AFaainvlALQLVSRRRvdANRRLQQDAG-----------KLTGVAISglqSIETLKASGLESdffsRWAGYQAKLLNAQ 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 877 SERsfrrGQMAGILYGVSQFFIFSSYGLALWYGSILMEKG------LSSFESVMKTFMvLIVTALV--MGEVLALAPDLL 948
Cdd:TIGR03796 370 QEL----GVLTQILGVLPTLLTSLNSALILVVGGLRVMEGqltigmLVAFQSLMSSFL-EPVNNLVgfGGTLQELEGDLN 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 949 KGNQMVVSVFELLDRRTQVVGDTGEELSNVEGTIELKGVHFSYpSRPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLS 1028
Cdd:TIGR03796 445 RLDDVLRNPVDPLLEEPEGSAATSEPPRRLSGYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAK 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1029 LVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIGLVQQEPALFATTIYENILYGKEGASESEVMEAAKLANAHSFISSLPE 1108
Cdd:TIGR03796 524 LVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPG 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1109 GYSTKVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRlmRDRTTVVVAHRLSTIKNSDMI 1188
Cdd:TIGR03796 604 GYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRR--RGCTCIIVAHRLSTIRDCDEI 681
|
490 500 510
....*....|....*....|....*....|
gi 15220188 1189 SVIQDGKIIEQGSHNILVEnKNGPYSKLIS 1218
Cdd:TIGR03796 682 IVLERGKVVQRGTHEELWA-VGGAYARLIR 710
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
789-1191 |
1.31e-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: 237.57 E-value: 1.31e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 789 LGLVVTAFIISFIL--NWRLTLVVLATYPLIIsghisekIFMQ--GYGG-NLSKAYLKA-NMLAG---ESISNIRTVVAF 859
Cdd:TIGR02857 127 LAVIVPLAILAAVFpqDWISGLILLLTAPLIP-------IFMIliGWAAqAAARKQWAAlSRLSGhflDRLRGLPTLKLF 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 860 CAEEKvldlYSKELLEPSERsFRRGQMA----GILYG-VSQFFifSSYGLALwygsILMEKGLSSFESVMktfmvLIVTA 934
Cdd:TIGR02857 200 GRAKA----QAAAIRRSSEE-YRERTMRvlriAFLSSaVLELF--ATLSVAL----VAVYIGFRLLAGDL-----DLATG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 935 LVmgeVLALAPDL--------------LKGNQMVVSVFELLDRRTQVVGDTGEELSNVEGTIELKGVHFSYPSRPDVtiF 1000
Cdd:TIGR02857 264 LF---VLLLAPEFylplrqlgaqyharADGVAAAEALFAVLDAAPRPLAGKAPVTAAPASSLEFSGVSVAYPGRRPA--L 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1001 SDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIGLVQQEPALFATTIYENILY 1080
Cdd:TIGR02857 339 RPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRL 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1081 GKEGASESEVMEAAKLANAHSFISSLPEGYSTKVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQ 1160
Cdd:TIGR02857 419 ARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVL 498
|
410 420 430
....*....|....*....|....*....|.
gi 15220188 1161 QALDRLMRDRTTVVVAHRLSTIKNSDMISVI 1191
Cdd:TIGR02857 499 EALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
687-1221 |
1.88e-66 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 236.15 E-value: 1.88e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 687 LVSYYMDWETTQNE-----VKRISILFCCGSVITVIVHTIEHTTFGIMGERLTLRVRQKMFSAILRNEIGWFDKvdNTSS 761
Cdd:PRK10790 45 LISYFIDNMVAKGNlplglVAGLAAAYVGLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDT--QPVG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 762 MLASRLESDATLLRTIVVDRSTILLENLGLVVTAFIISFILNWRLTLVVLATYP-----LIISGHISEKIFMQgyggnlS 836
Cdd:PRK10790 123 QLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAIMIFPavlvvMVIYQRYSTPIVRR------V 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 837 KAYLkANMLAG--ESISNIRTVVAFCAEEKvldlYSKELLEPSeRSFRRGQM------------------AGILYGVSQF 896
Cdd:PRK10790 197 RAYL-ADINDGfnEVINGMSVIQQFRQQAR----FGERMGEAS-RSHYMARMqtlrldgfllrpllslfsALILCGLLML 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 897 FIFSSYG---LALWYGSI---------LMEkgLSSFESVMKTfmvlivtALVMGEvlalapdllkgnqmvvSVFELLDRR 964
Cdd:PRK10790 271 FGFSASGtieVGVLYAFIsylgrlnepLIE--LTTQQSMLQQ-------AVVAGE----------------RVFELMDGP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 965 TQVVGDTGEELSNveGTIELKGVHFSYpsRPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMID 1044
Cdd:PRK10790 326 RQQYGNDDRPLQS--GRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1045 GQDIKKLKLKSLRRHIGLVQQEPALFATTIYENILYGKEGASES--EVMEAAKLAnahSFISSLPEGYSTKVGERGIQMS 1122
Cdd:PRK10790 402 GRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQvwQALETVQLA---ELARSLPDGLYTPLGEQGNNLS 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1123 GGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALdRLMRDRTT-VVVAHRLSTIKNSDMISVIQDGKIIEQGS 1201
Cdd:PRK10790 479 VGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQAL-AAVREHTTlVVIAHRLSTIVEADTILVLHRGQAVEQGT 557
|
570 580
....*....|....*....|
gi 15220188 1202 HNILVEnKNGPYSKLISLQQ 1221
Cdd:PRK10790 558 HQQLLA-AQGRYWQMYQLQL 576
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
340-1214 |
4.20e-65 |
|
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: 242.93 E-value: 4.20e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 340 QMIERNTedktgRKLGNVNGdILFKDVTFTYpSRPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGA 419
Cdd:TIGR00957 622 DSIERRT-----IKPGEGNS-ITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGH 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 420 VMLdgndiryldlkwlRGHIGLVNQEPVLFATTIRENIMYGK--DDATSEEITNAAKLseaISFINNLPEGFETQVGERG 497
Cdd:TIGR00957 695 VHM-------------KGSVAYVPQQAWIQNDSLRENILFGKalNEKYYQQVLEACAL---LPDLEILPSGDRTEIGEKG 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 498 IQLSGGQKQRISISRAIVKNPSILLLDEATSALDAESEKIVQEAL---DRVMVGRTTVVVAHRLSTVRNADIIAVVGGGK 574
Cdd:TIGR00957 759 VNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGK 838
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 575 IIESGSHDELISNpDGAYSSLLRIQEAASPNLNHTPSLPVS-TKPLPELPITETTSSIHQSVNQP-------------DT 640
Cdd:TIGR00957 839 ISEMGSYQELLQR-DGAFAEFLRTYAPDEQQGHLEDSWTALvSGEGKEAKLIENGMLVTDVVGKQlqrqlsasssdsgDQ 917
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 641 TKQ-----------AKVTVGRLYSMIRPD---------WKY----GLCGTLGSFIagsqmpLFALGIAQALVSYYmdW-- 694
Cdd:TIGR00957 918 SRHhgssaelqkaeAKEETWKLMEADKAQtgqvelsvyWDYmkaiGLFITFLSIF------LFVCNHVSALASNY--Wls 989
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 695 --------ETTQNEVK-RISILFCCGSV--ITVIVHTIEHTTFGIMGERltlRVRQKMFSAILRNEIGWFDKvdNTSSML 763
Cdd:TIGR00957 990 lwtddpmvNGTQNNTSlRLSVYGALGILqgFAVFGYSMAVSIGGIQASR---VLHQDLLHNKLRSPMSFFER--TPSGNL 1064
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 764 ASRLESDATLLRTIVVDRSTILLENLGLVVTAFIIsFILNWRLTLVVLATYPLIISghisekiFMQGYGGNLSKAYLKAN 843
Cdd:TIGR00957 1065 VNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIV-ILLATPIAAVIIPPLGLLYF-------FVQRFYVASSRQLKRLE 1136
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 844 MLA--------GESISNIRTVVAFcAEEKVLDLYSKELLEPSERSFRRGQMAGILYGVSQFFIFSSYGLALWYGSILMEK 915
Cdd:TIGR00957 1137 SVSrspvyshfNETLLGVSVIRAF-EEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRH 1215
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 916 GLSSFESVMKTFMVLIVTAlVMGEVLALAPDLLKGNQMVVSVFELLDRRT----QVVGDTGEELSNVEGTIELKGVHFSY 991
Cdd:TIGR00957 1216 SLSAGLVGLSVSYSLQVTF-YLNWLVRMSSEMETNIVAVERLKEYSETEKeapwQIQETAPPSGWPPRGRVEFRNYCLRY 1294
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 992 psRPDVT-IFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIGLVQQEPALF 1070
Cdd:TIGR00957 1295 --REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLF 1372
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1071 ATTIYENI-LYGKegASESEVMEAAKLANAHSFISSLPEGYSTKVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEATS 1149
Cdd:TIGR00957 1373 SGSLRMNLdPFSQ--YSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15220188 1150 ALDVESERVVQQALDRLMRDRTTVVVAHRLSTIKNSDMISVIQDGKIIEQGSHNILVENKNGPYS 1214
Cdd:TIGR00957 1451 AVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYS 1515
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
40-347 |
1.29e-64 |
|
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: 221.94 E-value: 1.29e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 40 LMALGSIGACIHGASVPVFFIFFGKLINIigLAYLFPQEASHKVAKYSLDFVYLSVVILFSSWLEVACWMHTGERQAAKI 119
Cdd:cd18578 10 LLLLGLIGAIIAGAVFPVFAILFSKLISV--FSLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAGERLTRRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 120 RKAYLRSMLSQDISLFDTEI-STGEVISAITSEILVVQDAISEKVGNFMHFISRFIAGFAIGFASVWQISLVTLSIVPFI 198
Cdd:cd18578 88 RKLAFRAILRQDIAWFDDPEnSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVGLATVPLL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 199 ALAGGIYAFVSSGLIVRVRKSYVKANEIAEEVIGNVRTVQAFTGEEKAVSSYQGALRNTYNYGRKAGLAKGLGLGSLHFV 278
Cdd:cd18578 168 LLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGFGLSQSL 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220188 279 LFLSWALLIWFTSIVVHKGIANGGESFTTMLNVVIAGLSLGQA---APDIStfmRASAAAYPIFQMIERNTE 347
Cdd:cd18578 248 TFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAfsfAPDIA---KAKAAAARIFRLLDRKPE 316
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
112-570 |
5.73e-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: 5.73e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 112 GERQAAKIRKAyLRSMLSQDISLFDT----EISTGEVISAITSEIlvvqDAISEkvgnfmhFISRF--------IAGFAI 179
Cdd:TIGR02857 68 AARAAAAVKSQ-LRERLLEAVAALGPrwlqGRPSGELATLALEGV----EALDG-------YFARYlpqlvlavIVPLAI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 180 GFASVWQ------ISLVTLSIVP-FIALAGgiyafvsSGLIVRVRKSYVKANEIAEEVIGNVR---TVQAFtgeeKAVSS 249
Cdd:TIGR02857 136 LAAVFPQdwisglILLLTAPLIPiFMILIG-------WAAQAAARKQWAALSRLSGHFLDRLRglpTLKLF----GRAKA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 250 YQGALRNTYNYGRKAGLAkglglgslhfVL---FLSWALLIWFTSIVVhKGIA--------NGGESFTTMLNVVI----A 314
Cdd:TIGR02857 205 QAAAIRRSSEEYRERTMR----------VLriaFLSSAVLELFATLSV-ALVAvyigfrllAGDLDLATGLFVLLlapeF 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 315 GLSLGQAAPDISTFMRASAAAYPIFQMIERNTEDKTGRK--LGNVNGDILFKDVTFTYPSRPDVVifDKLNFVIPAGKVV 392
Cdd:TIGR02857 274 YLPLRQLGAQYHARADGVAAAEALFAVLDAAPRPLAGKApvTAAPASSLEFSGVSVAYPGRRPAL--RPVSFTVPPGERV 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 393 ALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHIGLVNQEPVLFATTIRENIMYGKDDATSEEITNA 472
Cdd:TIGR02857 352 ALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREA 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 473 AKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRISISRAIVKNPSILLLDEATSALDAESEKIVQEALDRVMVGRTTV 552
Cdd:TIGR02857 432 LERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVL 511
|
490
....*....|....*...
gi 15220188 553 VVAHRLSTVRNADIIAVV 570
Cdd:TIGR02857 512 LVTHRLALAALADRIVVL 529
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
789-1221 |
3.00e-62 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 223.44 E-value: 3.00e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 789 LGLVVTaFIISFILNWRLTLVVLATYPLIisghiseKIFMQGYGGNLSK-------AYLKANMLAGESISNIRTVVAFCA 861
Cdd:PRK10789 123 MGCAVL-IVMSTQISWQLTLLALLPMPVM-------AIMIKRYGDQLHErfklaqaAFSSLNDRTQESLTSIRMIKAFGL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 862 EEKVLDLYSKELLEPSERSFRRGQMAG-------ILYGVSQFFIFSSYGLALWYGSILMEKgLSSFesvmktFMVLivtA 934
Cdd:PRK10789 195 EDRQSALFAADAEDTGKKNMRVARIDArfdptiyIAIGMANLLAIGGGSWMVVNGSLTLGQ-LTSF------VMYL---G 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 935 LVMGEVLALA---PDLLKGNQMVVSVFELLDRRTqVVGDTGEELSNVEGTIELKGVHFSYPSRpDVTIFSDFNLLVPSGK 1011
Cdd:PRK10789 265 LMIWPMLALAwmfNIVERGSAAYSRIRAMLAEAP-VVKDGSEPVPEGRGELDVNIRQFTYPQT-DHPALENVNFTLKPGQ 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1012 SMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIGLVQQEPALFATTIYENILYGKEGASESEVM 1091
Cdd:PRK10789 343 MLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIE 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1092 EAAKLANAHSFISSLPEGYSTKVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRT 1171
Cdd:PRK10789 423 HVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRT 502
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 15220188 1172 TVVVAHRLSTIKNSDMISVIQDGKIIEQGSHNILVEnKNGPYSKLISLQQ 1221
Cdd:PRK10789 503 VIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQ-QSGWYRDMYRYQQ 551
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
663-950 |
4.60e-62 |
|
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: 214.26 E-value: 4.60e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 663 LCGTLGSFIAGSQMPLFAL---GIAQALVSY---YMDWETTQNEVKRISILFCCGSVITVIVHTIEHTTFGIMGERLTLR 736
Cdd:cd18577 2 IIGLLAAIAAGAALPLMTIvfgDLFDAFTDFgsgESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQARR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 737 VRQKMFSAILRNEIGWFDKvdNTSSMLASRLESDATLLRTIVVDRSTILLENLGLVVTAFIISFILNWRLTLVVLATYPL 816
Cdd:cd18577 82 IRKRYLKALLRQDIAWFDK--NGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 817 I-ISGHISEKiFMQGYGGNLSKAYLKANMLAGESISNIRTVVAFCAEEKVLDLYSKELLEPSERSFRRGQMAGILYGVSQ 895
Cdd:cd18577 160 IaIVGGIMGK-LLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLF 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 15220188 896 FFIFSSYGLALWYGSILMEKGLSSFESVMKTFMVLIVTALVMGEVLALAPDLLKG 950
Cdd:cd18577 239 FIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKA 293
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
980-1201 |
3.20e-61 |
|
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: 208.50 E-value: 3.20e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 980 GTIELKGVHFSYpsRPD-VTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRR 1058
Cdd:cd03244 1 GDIEFKNVSLRY--RPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1059 HIGLVQQEPALFATTIYENI-LYGKegASESEVMEAAKLANAHSFISSLPEGYSTKVGERGIQMSGGQRQRIAIARAVLK 1137
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLdPFGE--YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220188 1138 NPEILLLDEATSALDVESERVVQQALDRLMRDRTTVVVAHRLSTIKNSDMISVIQDGKIIEQGS 1201
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
16-598 |
3.66e-61 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 230.30 E-value: 3.66e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 16 EKEKKRPS---VSFLKLFSFADfyDCVLMALGSIGAcihGASVPVFFIFFGKLIN-IIGLAYLfpqEASHKvaKYSLDFV 91
Cdd:PTZ00265 804 KRKPKAPNnlrIVYREIFSYKK--DVTIIALSILVA---GGLYPVFALLYAKYVStLFDFANL---EANSN--KYSLYIL 873
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 92 YLSVVILFSSWLEVACWMHTGERQAAKIRKAYLRSMLSQDISLFDTEISTGEVISA-ITSEILVVQDAISEKVGNFMHFI 170
Cdd:PTZ00265 874 VIAIAMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQDKHAPGLLSAhINRDVHLLKTGLVNNIVIFTHFI 953
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 171 SRFIAGFAIGFasvwqislvtlSIVPFIA-LAGGIYAFVSSGLIVRVRKSyvKANEIAEEVIGNVRTVQAFTGEEKAVSS 249
Cdd:PTZ00265 954 VLFLVSMVMSF-----------YFCPIVAaVLTGTYFIFMRVFAIRARLT--ANKDVEKKEINQPGTVFAYNSDDEIFKD 1020
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 250 ----YQGALRNTY---NYG---------------RKAGLAKGLGLGSLHFVLFLSWALLI-----WFTSIVVHKGIANGG 302
Cdd:PTZ00265 1021 psflIQEAFYNMNtviIYGledyfcnliekaidySNKGQKRKTLVNSMLWGFSQSAQLFInsfayWFGSFLIRRGTILVD 1100
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 303 ESFTTMLNVVIAGLSLGQAAPDISTFMRASAAAYPIFQMIER----NTEDKTGRKLGNVN---GDILFKDVTFTYPSRPD 375
Cdd:PTZ00265 1101 DFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRksniDVRDNGGIRIKNKNdikGKIEIMDVNFRYISRPN 1180
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 376 VVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFY------------EPTD-------------------------- 417
Cdd:PTZ00265 1181 VPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknEHTNdmtneqdyqgdeeqnvgmknvnefsl 1260
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 418 ----------------GAVMLDGNDIRYLDLKWLRGHIGLVNQEPVLFATTIRENIMYGKDDATSEEITNAAKLSEAISF 481
Cdd:PTZ00265 1261 tkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEF 1340
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 482 INNLPEGFETQVGERGIQLSGGQKQRISISRAIVKNPSILLLDEATSALDAESEKIVQEALDRV--MVGRTTVVVAHRLS 559
Cdd:PTZ00265 1341 IESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRIA 1420
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 15220188 560 TVRNADIIAVVGG----GKIIES-GSHDELISNPDGAYSSLLRI 598
Cdd:PTZ00265 1421 SIKRSDKIVVFNNpdrtGSFVQAhGTHEELLSVQDGVYKKYVKL 1464
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
956-1223 |
5.56e-61 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 220.10 E-value: 5.56e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 956 SVFELLDRRTQVVGDTGEELSNVEG-TIELKgvhfsypsrpDVTIFS----------DFNLlvPSGKSMALVGQSGSGKS 1024
Cdd:PRK11174 323 SLVTFLETPLAHPQQGEKELASNDPvTIEAE----------DLEILSpdgktlagplNFTL--PAGQRIALVGPSGAGKT 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1025 SVLSLVLRFYdPTAGIIMIDGQDIKKLKLKSLRRHIGLVQQEPALFATTIYENILYGKEGASESEVMEAAKLANAHSFIS 1104
Cdd:PRK11174 391 SLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLP 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1105 SLPEGYSTKVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVVVAHRLSTIKN 1184
Cdd:PRK11174 470 LLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQ 549
|
250 260 270
....*....|....*....|....*....|....*....
gi 15220188 1185 SDMISVIQDGKIIEQGSHNILVeNKNGPYSKLisLQQRQ 1223
Cdd:PRK11174 550 WDQIWVMQDGQIVQQGDYAELS-QAGGLFATL--LAHRQ 585
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
90-1217 |
7.12e-61 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 229.48 E-value: 7.12e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 90 FVYLSVV---ILFSSWLEVACWMHTGeRQAAKIRKAYLRSMLSQDISLFD---TEISTGEVISAITSEILVVQdAISEKV 163
Cdd:PLN03232 341 YVYAFLIffgVTFGVLCESQYFQNVG-RVGFRLRSTLVAAIFHKSLRLTHearKNFASGKVTNMITTDANALQ-QIAEQL 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 164 -----GNFMHFISRFIAGFAIGFASVWQiSLVTLSIVPFIALaggiyafvssgLIVRVRKSYV-------KANEIAEEVI 231
Cdd:PLN03232 419 hglwsAPFRIIVSMVLLYQQLGVASLFG-SLILFLLIPLQTL-----------IVRKMRKLTKeglqwtdKRVGIINEIL 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 232 GNVRTVQAFTGEEKAVSSYQGALRNTYNYGRKAGLAKGLG---LGSLHFVLflswaLLIWFTSIVVHKGIANGGESFTTM 308
Cdd:PLN03232 487 ASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNsfiLNSIPVVV-----TLVSFGVFVLLGGDLTPARAFTSL 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 309 LNVVIAGLSLGQAAPDISTFMRASAAAYPIFQMI---ERNTEDKTGRKLGNVNgdILFKDVTFTYPSRPDVVIFDKLNFV 385
Cdd:PLN03232 562 SLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLlseERILAQNPPLQPGAPA--ISIKNGYFSWDSKTSKPTLSDINLE 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 386 IPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLdgndiryldlkwLRGHIGLVNQEPVLFATTIRENIMYGKDdAT 465
Cdd:PLN03232 640 IPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV------------IRGSVAYVPQVSWIFNATVRENILFGSD-FE 706
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 466 SEEITNAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRISISRAIVKNPSILLLDEATSALDAE-SEKIVQEALDR 544
Cdd:PLN03232 707 SERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCMKD 786
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 545 VMVGRTTVVVAHRLSTVRNADIIAVVGGGKIIESGSHDELISNpdgaySSLLRIQEAASPNLNHTPSLPVSTKPLPELPI 624
Cdd:PLN03232 787 ELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKS-----GSLFKKLMENAGKMDATQEVNTNDENILKLGP 861
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 625 TETTSSIHQSVNQPDTTKQAKVTVGRLYSMIRPDWKYGLCGTLGSFIAG--SQMPLFALGIA----QALVSYYMDWETTQ 698
Cdd:PLN03232 862 TVTIDVSERNLGSTKQGKRGRSVLVKQEERETGIISWNVLMRYNKAVGGlwVVMILLVCYLTtevlRVSSSTWLSIWTDQ 941
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 699 NEVKRIS--------ILFCCGSVITVIVHTIEHTTFGIMGERltlRVRQKMFSAILRNEIGWFDKvdNTSSMLASRLESD 770
Cdd:PLN03232 942 STPKSYSpgfyivvyALLGFGQVAVTFTNSFWLISSSLHAAK---RLHDAMLNSILRAPMLFFHT--NPTGRVINRFSKD 1016
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 771 ATLLRTIVVDRSTILLENLGLVVTAFIISFILNwrlTLVVLATYPLIISGHiSEKIFMQGYGGNLSK--AYLKANMLA-- 846
Cdd:PLN03232 1017 IGDIDRNVANLMNMFMNQLWQLLSTFALIGTVS---TISLWAIMPLLILFY-AAYLYYQSTSREVRRldSVTRSPIYAqf 1092
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 847 GESISNIRTVVAFCAEEKVLDLYSKEL---------LEPSER--SFRRGQMAGILYGVSQFFIfssyglALWYGSILMEK 915
Cdd:PLN03232 1093 GEALNGLSSIRAYKAYDRMAKINGKSMdnnirftlaNTSSNRwlTIRLETLGGVMIWLTATFA------VLRNGNAENQA 1166
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 916 GLSSFESVMKTFmVLIVTALVMGeVL---ALAPDLLKGNQMVVSVFELLDRRTQVVGDTGEELS-NVEGTIELKGVHFSY 991
Cdd:PLN03232 1167 GFASTMGLLLSY-TLNITTLLSG-VLrqaSKAENSLNSVERVGNYIDLPSEATAIIENNRPVSGwPSRGSIKFEDVHLRY 1244
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 992 -PSRPDVtiFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIGLVQQEPALF 1070
Cdd:PLN03232 1245 rPGLPPV--LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLF 1322
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1071 ATTIYENILYGKEgASESEVMEAAKLANAHSFISSLPEGYSTKVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEATSA 1150
Cdd:PLN03232 1323 SGTVRFNIDPFSE-HNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15220188 1151 LDVESERVVQQALDRLMRDRTTVVVAHRLSTIKNSDMISVIQDGKIIEQGSHNILVENKNGPYSKLI 1217
Cdd:PLN03232 1402 VDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMV 1468
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
359-580 |
3.41e-60 |
|
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: 205.81 E-value: 3.41e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 359 GDILFKDVTFTYPSRPDVVIfDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGH 438
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVL-KNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 439 IGLVNQEPVLFATTIRENImygkdD----ATSEEITNAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRISISRAI 514
Cdd:cd03244 80 ISIIPQDPVLFSGTIRSNL-----DpfgeYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15220188 515 VKNPSILLLDEATSALDAESEKIVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVGGGKIIESGS 580
Cdd:cd03244 155 LRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
118-601 |
2.73e-59 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 215.35 E-value: 2.73e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 118 KIRKAYLRSMLSQDISLFDTEiSTGEVISAITSEILVVQDAISEKVGNFMHFISRFIAGFAIGFASVWQISLVTLSIVPF 197
Cdd:PRK10790 99 QLRTDVMDAALRQPLSAFDTQ-PVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAIMIFPA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 198 IALAGGIYAFVSSGLIVRVRKSYVKANEIAEEVIGNVRTVQAFTGEEKAVSSYQGALRNTYNYGRKAGLAKGL---GLGS 274
Cdd:PRK10790 178 VLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFllrPLLS 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 275 LHFVLFLSWALLIW-FTSI-VVHKGIANGGESFTTMLNVVIAGLSLGQaapdiSTFMRASAAAYPIFQMIERNTED--KT 350
Cdd:PRK10790 258 LFSALILCGLLMLFgFSASgTIEVGVLYAFISYLGRLNEPLIELTTQQ-----SMLQQAVVAGERVFELMDGPRQQygND 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 351 GRKLGNvnGDILFKDVTFTYpsRPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYL 430
Cdd:PRK10790 333 DRPLQS--GRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSL 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 431 DLKWLRGHIGLVNQEPVLFATTIRENIMYGKDdATSEEITNAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRISI 510
Cdd:PRK10790 409 SHSVLRQGVAMVQQDPVVLADTFLANVTLGRD-ISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLAL 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 511 SRAIVKNPSILLLDEATSALDAESEKIVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVGGGKIIESGSHDELISNpDG 590
Cdd:PRK10790 488 ARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAA-QG 566
|
490
....*....|.
gi 15220188 591 AYSSLLRIQEA 601
Cdd:PRK10790 567 RYWQMYQLQLA 577
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
361-1217 |
1.69e-57 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 218.84 E-value: 1.69e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSRPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLdgndiryldlkwLRGHIG 440
Cdd:PLN03130 615 ISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 441 LVNQEPVLFATTIRENIMYGK--DDATSEEITNAAKLSEAISFinnLPEGFETQVGERGIQLSGGQKQRISISRAIVKNP 518
Cdd:PLN03130 683 YVPQVSWIFNATVRDNILFGSpfDPERYERAIDVTALQHDLDL---LPGGDLTEIGERGVNISGGQKQRVSMARAVYSNS 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 519 SILLLDEATSALDAE-SEKIVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVGGGKIIESGSHDELISNP-------DG 590
Cdd:PLN03130 760 DVYIFDDPLSALDAHvGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGplfqklmEN 839
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 591 AYSSLLRIQEAASPNLNHTPSLPVSTKPLPELPiTETTSSIHQSVNQPDTTKQAKVTVGRLYSMIRPDWKYGLCGtlgsf 670
Cdd:PLN03130 840 AGKMEEYVEENGEEEDDQTSSKPVANGNANNLK-KDSSSKKKSKEGKSVLIKQEERETGVVSWKVLERYKNALGG----- 913
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 671 iAGSQMPLFALGIAQALV----SYYMDWETTQNEVKRISILFCCG-----SVITVIVhTIEHTTFGIMGE-RLTLRVRQK 740
Cdd:PLN03130 914 -AWVVMILFLCYVLTEVFrvssSTWLSEWTDQGTPKTHGPLFYNLiyallSFGQVLV-TLLNSYWLIMSSlYAAKRLHDA 991
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 741 MFSAILRNEIGWFDKvdNTSSMLASRLESDatllrTIVVDRSTILLENL------GLVVTAFIISFILnwrlTLVVLATY 814
Cdd:PLN03130 992 MLGSILRAPMSFFHT--NPLGRIINRFAKD-----LGDIDRNVAVFVNMflgqifQLLSTFVLIGIVS----TISLWAIM 1060
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 815 PLIISGHiSEKIFMQGYG------GNLSKAYLKANMlaGESISNIRTVVAFCAEEKVLDLYSKELlePSERSFRRGQMAG 888
Cdd:PLN03130 1061 PLLVLFY-GAYLYYQSTArevkrlDSITRSPVYAQF--GEALNGLSTIRAYKAYDRMAEINGRSM--DNNIRFTLVNMSS 1135
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 889 ILY-GVSQFFIfssYGLALWYGSIL--MEKGLSS----FESVMKTFM--VLIVTALVMGeVL---ALAPDLLKGNQMVVS 956
Cdd:PLN03130 1136 NRWlAIRLETL---GGLMIWLTASFavMQNGRAEnqaaFASTMGLLLsyALNITSLLTA-VLrlaSLAENSLNAVERVGT 1211
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 957 VFELLDRRTQVVGDT----GEELSnveGTIELKGVHFSYpsRPDVT-IFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVL 1031
Cdd:PLN03130 1212 YIDLPSEAPLVIENNrpppGWPSS---GSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALF 1286
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1032 RFYDPTAGIIMIDGQDIKKLKLKSLRRHIGLVQQEPALFATTIYENILYGKEgASESEVMEAAKLANAHSFISSLPEGYS 1111
Cdd:PLN03130 1287 RIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNE-HNDADLWESLERAHLKDVIRRNSLGLD 1365
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1112 TKVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVVVAHRLSTIKNSDMISVI 1191
Cdd:PLN03130 1366 AEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVL 1445
|
890 900
....*....|....*....|....*.
gi 15220188 1192 QDGKIIEQGSHNILVENKNGPYSKLI 1217
Cdd:PLN03130 1446 DAGRVVEFDTPENLLSNEGSAFSKMV 1471
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
959-1223 |
3.64e-57 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 208.53 E-value: 3.64e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 959 ELLDRRTQVVGDTGEELSNVEGTIELKGVHFSYPSRPDvTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTA 1038
Cdd:PRK11160 316 EITEQKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1039 GIIMIDGQDIKKLKLKSLRRHIGLVQQEPALFATTIYENILYGKEGASESEVMEAAKLANAHSFISSlPEGYSTKVGERG 1118
Cdd:PRK11160 395 GEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGG 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1119 IQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVVVAHRLSTIKNSDMISVIQDGKIIE 1198
Cdd:PRK11160 474 RQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIE 553
|
250 260
....*....|....*....|....*
gi 15220188 1199 QGSHNILVENKNGPYskliSLQQRQ 1223
Cdd:PRK11160 554 QGTHQELLAQQGRYY----QLKQRL 574
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
169-599 |
2.06e-56 |
|
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: 208.66 E-value: 2.06e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 169 FISRFIAGFAIG--FASVWQISLVTLSIvpfIALAGGIYAFVSSGLIVRVRKSYVKANEIAEEvignvrTVQAFTG---- 242
Cdd:TIGR03797 257 LLSGIFALLNLGlmFYYSWKLALVAVAL---ALVAIAVTLVLGLLQVRKERRLLELSGKISGL------TVQLINGiskl 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 243 -----EEKAVSSYQGalrntyNYGRKAGLAK-----GLGLGSLHFVL-FLSWALLIWFTSIVVHKGIANGGE--SFTTML 309
Cdd:TIGR03797 328 rvagaENRAFARWAK------LFSRQRKLELsaqriENLLTVFNAVLpVLTSAALFAAAISLLGGAGLSLGSflAFNTAF 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 310 NVVIAG-LSLGQAAPDISTFMRASAAAYPIFQMIERNTEDKTgrKLGNVNGDILFKDVTFTYpsRPD-VVIFDKLNFVIP 387
Cdd:TIGR03797 402 GSFSGAvTQLSNTLISILAVIPLWERAKPILEALPEVDEAKT--DPGKLSGAIEVDRVTFRY--RPDgPLILDDVSLQIE 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 388 AGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHIGLVNQEPVLFATTIRENIMyGKDDATSE 467
Cdd:TIGR03797 478 PGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIA-GGAPLTLD 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 468 EITNAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRISISRAIVKNPSILLLDEATSALDAESEKIVQEALDRVMV 547
Cdd:TIGR03797 557 EAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKV 636
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 15220188 548 GRttVVVAHRLSTVRNADIIAVVGGGKIIESGSHDELISNPdGAYSSLLRIQ 599
Cdd:TIGR03797 637 TR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMARE-GLFAQLARRQ 685
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
788-1220 |
5.61e-56 |
|
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: 207.50 E-value: 5.61e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 788 NLGLVvtafiisFILNWRLTLVVLATYPLIISGHISEKIF-------MQGYGGNLSKayLKANMLAGesISNIRtvVAfC 860
Cdd:TIGR03797 266 NLGLM-------FYYSWKLALVAVALALVAIAVTLVLGLLqvrkerrLLELSGKISG--LTVQLING--ISKLR--VA-G 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 861 AEEKVLDLYSKELLEPSERSFRRGQMAGILYGVSQFF-IFSSygLALWY--GSILMEKGLSSFESVmkTFMVLIVTalVM 937
Cdd:TIGR03797 332 AENRAFARWAKLFSRQRKLELSAQRIENLLTVFNAVLpVLTS--AALFAaaISLLGGAGLSLGSFL--AFNTAFGS--FS 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 938 GEVLALAPDLLKGNQmVVSVFE----LLDRRTQVVGDTGE--ELSnveGTIELKGVHFSYpsRPD-VTIFSDFNLLVPSG 1010
Cdd:TIGR03797 406 GAVTQLSNTLISILA-VIPLWErakpILEALPEVDEAKTDpgKLS---GAIEVDRVTFRY--RPDgPLILDDVSLQIEPG 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1011 KSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIGLVQQEPALFATTIYENILyGKEGASESEV 1090
Cdd:TIGR03797 480 EFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIA-GGAPLTLDEA 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1091 MEAAKLANAHSFISSLPEGYSTKVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLmrDR 1170
Cdd:TIGR03797 559 WEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERL--KV 636
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 15220188 1171 TTVVVAHRLSTIKNSDMISVIQDGKIIEQGSHNILVEnKNGPYSKLISLQ 1220
Cdd:TIGR03797 637 TRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMA-REGLFAQLARRQ 685
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
382-597 |
1.18e-54 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 201.61 E-value: 1.18e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 382 LNFVIPAGKVVALVGGSGSGKSTMISLIERFYePTDGAVMLDGNDIRYLDLKWLRGHIGLVNQEPVLFATTIRENIMYGK 461
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 462 DDATSEEITNAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRISISRAIVKNPSILLLDEATSALDAESEKIVQEA 541
Cdd:PRK11174 448 PDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQA 527
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15220188 542 LDRVMVGRTTVVVAHRLSTVRNADIIAVVGGGKIIESGSHDELiSNPDGAYSSLLR 597
Cdd:PRK11174 528 LNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAEL-SQAGGLFATLLA 582
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
330-602 |
2.36e-54 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 199.94 E-value: 2.36e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 330 RASAAAYPIFQMIERNTEDKTGRK-LGNVNGDILFKDVTFTYPSRpDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISL 408
Cdd:PRK10789 282 RGSAAYSRIRAMLAEAPVVKDGSEpVPEGRGELDVNIRQFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 409 IERFYEPTDGAVMLDGNDIRYLDLKWLRGHIGLVNQEPVLFATTIRENIMYGKDDATSEEITNAAKLSEAISFINNLPEG 488
Cdd:PRK10789 361 IQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQG 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 489 FETQVGERGIQLSGGQKQRISISRAIVKNPSILLLDEATSALDAESEKIVQEALDRVMVGRTTVVVAHRLSTVRNADIIA 568
Cdd:PRK10789 441 YDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEIL 520
|
250 260 270
....*....|....*....|....*....|....*.
gi 15220188 569 VVGGGKIIESGSHDELISNPdGAYSSLLRIQ--EAA 602
Cdd:PRK10789 521 VMQHGHIAQRGNHDQLAQQS-GWYRDMYRYQqlEAA 555
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
782-1217 |
2.60e-53 |
|
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: 199.97 E-value: 2.60e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 782 STIL--LENLGLVVTAFIISFILNWRLTLVVLATYPLIISGHIsekIFMQGYGGNLSKAYLKANMLAG---ESISNIRTV 856
Cdd:TIGR01193 271 STILslFLDMWILVIVGLFLVRQNMLLFLLSLLSIPVYAVIII---LFKRTFNKLNHDAMQANAVLNSsiiEDLNGIETI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 857 VAFCAEE----KVLDLYSkELLEPSERSFRRGQMAGILYGVSQFFIFSsygLALWYGSILMEKGLSSFESVMkTFMVLIV 932
Cdd:TIGR01193 348 KSLTSEAerysKIDSEFG-DYLNKSFKYQKADQGQQAIKAVTKLILNV---VILWTGAYLVMRGKLTLGQLI-TFNALLS 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 933 TALV-MGEVLALAPDLLKG-------NQ--MVVSVFELLDRRTqvvgdtgeELSNVEGTIELKGVHFSYPSRPDvtIFSD 1002
Cdd:TIGR01193 423 YFLTpLENIINLQPKLQAArvannrlNEvyLVDSEFINKKKRT--------ELNNLNGDIVINDVSYSYGYGSN--ILSD 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1003 FNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIGLVQQEPALFATTIYENILYG- 1081
Cdd:TIGR01193 493 ISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGa 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1082 KEGASESEVMEAAKLANAHSFISSLPEGYSTKVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQ 1161
Cdd:TIGR01193 573 KENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVN 652
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 15220188 1162 ALDRlMRDRTTVVVAHRLSTIKNSDMISVIQDGKIIEQGSHNILVeNKNGPYSKLI 1217
Cdd:TIGR01193 653 NLLN-LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELL-DRNGFYASLI 706
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
358-597 |
4.27e-53 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 196.58 E-value: 4.27e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 358 NGDILFKDVTFTYPSRPDVVIfDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRG 437
Cdd:PRK11160 336 QVSLTLNNVSFTYPDQPQPVL-KGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 438 HIGLVNQEPVLFATTIRENIMYGKDDATSEEITNA------AKLSEAisfinnlPEGFETQVGERGIQLSGGQKQRISIS 511
Cdd:PRK11160 415 AISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVlqqvglEKLLED-------DKGLNAWLGEGGRQLSGGEQRRLGIA 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 512 RAIVKNPSILLLDEATSALDAESEKIVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVGGGKIIESGSHDELISNpDGA 591
Cdd:PRK11160 488 RALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQ-QGR 566
|
....*.
gi 15220188 592 YSSLLR 597
Cdd:PRK11160 567 YYQLKQ 572
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
929-1200 |
6.68e-53 |
|
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: 195.74 E-value: 6.68e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 929 VLIVTALVMGevLALAP-DLLKGN-QMVVSVFELLDRRTQVVGDTGEE-----LSNVEGTIELKGVHFSYPSRpDVTIFS 1001
Cdd:COG4618 273 AMIAASILMG--RALAPiEQAIGGwKQFVSARQAYRRLNELLAAVPAEpermpLPRPKGRLSVENLTVVPPGS-KRPILR 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1002 DFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIGLVQQEPALFATTIYENI--L 1079
Cdd:COG4618 350 GVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIarF 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1080 ygkEGASESEVMEAAKLANAHSFISSLPEGYSTKVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVV 1159
Cdd:COG4618 430 ---GDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAAL 506
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 15220188 1160 QQALDRLmRDR--TTVVVAHRLSTIKNSDMISVIQDGKIIEQG 1200
Cdd:COG4618 507 AAAIRAL-KARgaTVVVITHRPSLLAAVDKLLVLRDGRVQAFG 548
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
728-1196 |
1.23e-52 |
|
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: 194.49 E-value: 1.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 728 IMGERLTLRVRQKMFSAILRNEIgwfdkvdNTSSMLASRLESDATLLRTIVVDRSTILLENLGLVVTAFIISFILNWRLT 807
Cdd:TIGR01842 72 RIGEKLDGALNQPIFAASFSATL-------RRGSGDGLQALRDLDQLRQFLTGPGLFAFFDAPWMPIYLLVCFLLHPWIG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 808 LVVLATYPLIISGHISEKIFMQGYGGNLSKAYLKANMLAGESISNIRTVVAFC----AEEKVLDLYSKELLEPSERSFRr 883
Cdd:TIGR01842 145 ILALGGAVVLVGLALLNNRATKKPLKEATEASIRANNLADSALRNAEVIEAMGmmgnLTKRWGRFHSKYLSAQSAASDR- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 884 gqmAGILYGVSQFFIFSSYGLALWYGSILmekglsSFESVMKTFMVlIVTALVMGEvlALAP-DLLKGN--QMVVS---- 956
Cdd:TIGR01842 224 ---AGMLSNLSKYFRIVLQSLVLGLGAYL------AIDGEITPGMM-IAGSILVGR--ALAPiDGAIGGwkQFSGArqay 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 957 -----VFELLDRRTQVVgdtgeELSNVEGTIELKGVHFSYPSrPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVL 1031
Cdd:TIGR01842 292 krlneLLANYPSRDPAM-----PLPEPEGHLSVENVTIVPPG-GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIV 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1032 RFYDPTAGIIMIDGQDIKKLKLKSLRRHIGLVQQEPALFATTIYENILYGKEGASESEVMEAAKLANAHSFISSLPEGYS 1111
Cdd:TIGR01842 366 GIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYD 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1112 TKVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRL-MRDRTTVVVAHRLSTIKNSDMISV 1190
Cdd:TIGR01842 446 TVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGCVDKILV 525
|
....*.
gi 15220188 1191 IQDGKI 1196
Cdd:TIGR01842 526 LQDGRI 531
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
328-586 |
1.15e-51 |
|
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: 191.89 E-value: 1.15e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 328 FMRASAAAYPIFQMIERNTEDKTGRKLGNVNGDILFKDVTFTYPSRpDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMIS 407
Cdd:COG4618 298 FVSARQAYRRLNELLAAVPAEPERMPLPRPKGRLSVENLTVVPPGS-KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLAR 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 408 LIERFYEPTDGAVMLDGNDIRYLDLKWLRGHIGLVNQEPVLFATTIRENI--MygkDDATSEEITNAAKLSEAISFINNL 485
Cdd:COG4618 377 LLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIarF---GDADPEKVVAAAKLAGVHEMILRL 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 486 PEGFETQVGERGIQLSGGQKQRISISRAIVKNPSILLLDEATSALDAESEKIVQEALDRV-MVGRTTVVVAHRLSTVRNA 564
Cdd:COG4618 454 PDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAV 533
|
250 260
....*....|....*....|..
gi 15220188 565 DIIAVVGGGKIIESGSHDELIS 586
Cdd:COG4618 534 DKLLVLRDGRVQAFGPRDEVLA 555
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
112-595 |
4.70e-51 |
|
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: 193.03 E-value: 4.70e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 112 GERQAAKIRKAYLRSMLSQDISLFDTEiSTGEVISAIT--SEILvvqDAISEKVGN-FMHFISRFIAGFAIGFASVwQIS 188
Cdd:TIGR01193 224 GQRLSIDIILSYIKHLFELPMSFFSTR-RTGEIVSRFTdaSSII---DALASTILSlFLDMWILVIVGLFLVRQNM-LLF 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 189 LVTLSIVPFIALAggIYAFVS--SGLIVRVRKSYVKANEIAEEVIGNVRTVQAFTGEEKAVSSYQGALRNTYNYGRKAGL 266
Cdd:TIGR01193 299 LLSLLSIPVYAVI--IILFKRtfNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQK 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 267 AKGlGLGSLHFVLFLSWALLI-WFTSIVVHKGIANGGE---------SFTTMLNVVIaglslgqaapDISTFMRASAAAY 336
Cdd:TIGR01193 377 ADQ-GQQAIKAVTKLILNVVIlWTGAYLVMRGKLTLGQlitfnallsYFLTPLENII----------NLQPKLQAARVAN 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 337 P-IFQMIERNTEDKTGRK---LGNVNGDILFKDVTFTYPSRPDVVifDKLNFVIPAGKVVALVGGSGSGKSTMISLIERF 412
Cdd:TIGR01193 446 NrLNEVYLVDSEFINKKKrteLNNLNGDIVINDVSYSYGYGSNIL--SDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGF 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 413 YEPTDGAVMLDGNDIRYLDLKWLRGHIGLVNQEPVLFATTIRENIMYG-KDDATSEEITNAAKLSEAISFINNLPEGFET 491
Cdd:TIGR01193 524 FQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDDIENMPLGYQT 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 492 QVGERGIQLSGGQKQRISISRAIVKNPSILLLDEATSALDAESE-KIVQEALDrvMVGRTTVVVAHRLSTVRNADIIAVV 570
Cdd:TIGR01193 604 ELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEkKIVNNLLN--LQDKTIIFVAHRLSVAKQSDKIIVL 681
|
490 500
....*....|....*....|....*
gi 15220188 571 GGGKIIESGSHDELIsNPDGAYSSL 595
Cdd:TIGR01193 682 DHGKIIEQGSHDELL-DRNGFYASL 705
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
370-1226 |
3.51e-50 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 195.00 E-value: 3.51e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 370 YPSRPDVVIFDkLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVmldgndiryldlkWLRGHIGLVNQEPVLF 449
Cdd:PTZ00243 668 FELEPKVLLRD-VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIM 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 450 ATTIRENIMYgKDDATSEEITNAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRISISRAIVKNPSILLLDEATSA 529
Cdd:PTZ00243 734 NATVRGNILF-FDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 530 LDAE-SEKIVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVGGGKIIESGSHDELISNPdgAYSSlLRIQEAASPNLNH 608
Cdd:PTZ00243 813 LDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS--LYAT-LAAELKENKDSKE 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 609 --TPSLPVSTKPLPELPIT-ETTSSIHQSVNQPDTTKQAKVTVGRLysMIRPD-------WK-----YGLCGtlGSFIAG 673
Cdd:PTZ00243 890 gdADAEVAEVDAAPGGAVDhEPPVAKQEGNAEGGDGAALDAAAGRL--MTREEkasgsvpWStyvayLRFCG--GLHAAG 965
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 674 SQMPLFALG--IAQALVSYYMDWETtqNEVKRISILFCCGSVITVIVHTIE-----HTTFGIMgERLTLRVRQKMFSAIL 746
Cdd:PTZ00243 966 FVLATFAVTelVTVSSGVWLSMWST--RSFKLSAATYLYVYLGIVLLGTFSvplrfFLSYEAM-RRGSRNMHRDLLRSVS 1042
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 747 RNEIGWFDkvdnTSSM--LASRLESDATLLRTIVVDrSTILLenlgLVVTAFIISFIlnwrltLVVLATYPLII-----S 819
Cdd:PTZ00243 1043 RGTMSFFD----TTPLgrILNRFSRDIDILDNTLPM-SYLYL----LQCLFSICSSI------LVTSASQPFVLvalvpC 1107
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 820 GHISEKIfMQGYG---------GNLSKAYLKAnmLAGESISNIRTVVAFCAEEKV-------LDL-YSKELLEpsersfr 882
Cdd:PTZ00243 1108 GYLYYRL-MQFYNsanreirriKSVAKSPVFT--LLEEALQGSATITAYGKAHLVmqealrrLDVvYSCSYLE------- 1177
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 883 rgQMAGILYGVSQFF----IFSSYGLALWYGSILMEK----GLSSFESVMKTFMVLIVTALVMgEVLALAPDLLKGNQMV 954
Cdd:PTZ00243 1178 --NVANRWLGVRVEFlsniVVTVIALIGVIGTMLRATsqeiGLVSLSLTMAMQTTATLNWLVR-QVATVEADMNSVERLL 1254
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 955 VSVFEL--------------LDRRTQVVGDtgeelsnVEGTIELKGVHFS----YPSRPDVTIFSDFNL-------LVPS 1009
Cdd:PTZ00243 1255 YYTDEVphedmpeldeevdaLERRTGMAAD-------VTGTVVIEPASPTsaapHPVQAGSLVFEGVQMryreglpLVLR 1327
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1010 GKS--------MALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIGLVQQEPALFATTIYENILYG 1081
Cdd:PTZ00243 1328 GVSfriaprekVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPF 1407
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1082 KEgASESEVMEAAKLANAHSFISSLPEGYSTKVGERGIQMSGGQRQRIAIARAVLKNPE-ILLLDEATSALDVESERVVQ 1160
Cdd:PTZ00243 1408 LE-ASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSgFILMDEATANIDPALDRQIQ 1486
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15220188 1161 QALDRLMRDRTTVVVAHRLSTIKNSDMISVIQDGKIIEQGSHNILVENKNGPYSKLI-SLQQRQRHH 1226
Cdd:PTZ00243 1487 ATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMVeALGRSEAKR 1553
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
723-1179 |
3.70e-50 |
|
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: 186.80 E-value: 3.70e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 723 HTTFGIMGerltlRVRQKMFSAILRNEIGWFDKVdNTSSMLAsRLESD-----ATLLRTIVVDRSTILLenlGLVVTAFI 797
Cdd:TIGR02868 79 DAALRSLG-----ALRVRVYERLARQALAGRRRL-RRGDLLG-RLGADvdalqDLYVRVIVPAGVALVV---GAAAVAAI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 798 isFILNWRLTLVVLATypLIISGHISEKIFmqGYGGNLSKAYLKAnmLAGESISNIRTVVAFCAEEKV---LDLYSKELL 874
Cdd:TIGR02868 149 --AVLSVPAALILAAG--LLLAGFVAPLVS--LRAARAAEQALAR--LRGELAAQLTDALDGAAELVAsgaLPAALAQVE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 875 EPSERSFRRGQMAGILYGVSQFFIFSSYGLALWyGSILMEKGLSSFESVMKTFM-VLIVTALVMGEVLALAPDLLkgnQM 953
Cdd:TIGR02868 221 EADRELTRAERRAAAATALGAALTLLAAGLAVL-GALWAGGPAVADGRLAPVTLaVLVLLPLAAFEAFAALPAAA---QQ 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 954 VVSVFELLDRRTQVVGDTG----------EELSNVEGTIELKGVHFSYPSRPDVtiFSDFNLLVPSGKSMALVGQSGSGK 1023
Cdd:TIGR02868 297 LTRVRAAAERIVEVLDAAGpvaegsapaaGAVGLGKPTLELRDLSAGYPGAPPV--LDGVSLDLPPGERVAILGPSGSGK 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1024 SSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIGLVQQEPALFATTIYENILYGKEGASESEVMEAAKLANAHSFI 1103
Cdd:TIGR02868 375 STLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWL 454
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15220188 1104 SSLPEGYSTKVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVVVAHRL 1179
Cdd:TIGR02868 455 RALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
114-558 |
6.62e-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: 182.95 E-value: 6.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 114 RQAAKIRkAYLRSMLSQDISLFDTEISTGEVISAITSEILVVQDAISEKV----------GNFMHFISRFIAGFAIGFAS 183
Cdd:TIGR02868 83 RSLGALR-VRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIvpagvalvvgAAAVAAIAVLSVPAALILAA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 184 vwqISLVTLSIVPFIALAGGIYAFVSsglIVRVRKSYVKAneiAEEVIGNVRTVQAFTGEEKAVSSYQGALRNTYNYGRK 263
Cdd:TIGR02868 162 ---GLLLAGFVAPLVSLRAARAAEQA---LARLRGELAAQ---LTDALDGAAELVASGALPAALAQVEEADRELTRAERR 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 264 AGLAKGLGLGSLHFVLFLSWALLIWFTSivvhKGIANGGESFTTMLNVVIAGLSLGQA----APDISTFMRASAAAYPIF 339
Cdd:TIGR02868 233 AAAATALGAALTLLAAGLAVLGALWAGG----PAVADGRLAPVTLAVLVLLPLAAFEAfaalPAAAQQLTRVRAAAERIV 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 340 QMiernTEDKTGRKLGNVNGD---------ILFKDVTFTYPSRPDVviFDKLNFVIPAGKVVALVGGSGSGKSTMISLIE 410
Cdd:TIGR02868 309 EV----LDAAGPVAEGSAPAAgavglgkptLELRDLSAGYPGAPPV--LDGVSLDLPPGERVAILGPSGSGKSTLLATLA 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 411 RFYEPTDGAVMLDGNDIRYLDLKWLRGHIGLVNQEPVLFATTIRENIMYGKDDATSEEITNAAKLSEAISFINNLPEGFE 490
Cdd:TIGR02868 383 GLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLD 462
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15220188 491 TQVGERGIQLSGGQKQRISISRAIVKNPSILLLDEATSALDAESEKIVQEALDRVMVGRTTVVVAHRL 558
Cdd:TIGR02868 463 TVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
41-338 |
1.70e-48 |
|
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: 175.54 E-value: 1.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 41 MALGSIGACIHGASVPVFFIFFGKLI-------------NIIGLAYLF--PQEASHKVAKYSLDFVYLSVVILFSSWLEV 105
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTdsftnggmtnitgNSSGLNSSAgpFEKLEEEMTLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 106 ACWMHTGERQAAKIRKAYLRSMLSQDISLFDTEiSTGEVISAITSEILVVQDAISEKVGNFMHFISRFIAGFAIGFASVW 185
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVN-DTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 186 QISLVTLSIVPFIALAGGIYAFVSSGLIVRVRKSYVKANEIAEEVIGNVRTVQAFTGEEKAVSSYQGALRNTYNYGRKAG 265
Cdd:cd18558 160 KLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKA 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15220188 266 LAKGLGLGSLHFVLFLSWALLIWFTSIVVHKGIANGGESFTTMLNVVIAGLSLGQAAPDISTFMRASAAAYPI 338
Cdd:cd18558 240 ITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAAYHI 312
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
982-1196 |
1.99e-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: 170.09 E-value: 1.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRpDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIG 1061
Cdd:cd03246 1 LEVENVSFRYPGA-EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEPALFATTIYENILygkegasesevmeaaklanahsfisslpegystkvgergiqmSGGQRQRIAIARAVLKNPEI 1141
Cdd:cd03246 80 YLPQDDELFSGSIAENIL------------------------------------------SGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15220188 1142 LLLDEATSALDVESERVVQQALDRL-MRDRTTVVVAHRLSTIKNSDMISVIQDGKI 1196
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
353-586 |
1.95e-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: 179.08 E-value: 1.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 353 KLGNVNGDILFKDVTFTYPSrPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDL 432
Cdd:TIGR01842 309 PLPEPEGHLSVENVTIVPPG-GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDR 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 433 KWLRGHIGLVNQEPVLFATTIRENIMYGKDDATSEEITNAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRISISR 512
Cdd:TIGR01842 388 ETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALAR 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15220188 513 AIVKNPSILLLDEATSALDAESEKIVQEALDRVMV-GRTTVVVAHRLSTVRNADIIAVVGGGKIIESGSHDELIS 586
Cdd:TIGR01842 468 ALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKArGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLA 542
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
982-1177 |
5.55e-46 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 164.60 E-value: 5.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRPdvtIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIG 1061
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEPALFATTIYENILYGKEGASESEVMEAAK--LANAHsfissLPEGY-STKVGErgiqMSGGQRQRIAIARAVLKN 1138
Cdd:COG4619 78 YVPQEPALWGGTVRDNLPFPFQLRERKFDRERALelLERLG-----LPPDIlDKPVER----LSGGERQRLALIRALLLQ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15220188 1139 PEILLLDEATSALDVESERVVQQALDRLMR--DRTTVVVAH 1177
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYLAeeGRAVLWVSH 189
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
364-575 |
3.52e-45 |
|
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: 160.84 E-value: 3.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 364 KDVTFTYPSRPDVVIFDkLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHIGLVN 443
Cdd:cd03246 4 ENVSFRYPGAEPPVLRN-VSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 444 QEPVLFATTIRENImygkddatseeitnaaklseaisfinnlpegfetqvgergiqLSGGQKQRISISRAIVKNPSILLL 523
Cdd:cd03246 83 QDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15220188 524 DEATSALDAESEKIVQEALDRV-MVGRTTVVVAHRLSTVRNADIIAVVGGGKI 575
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
982-1201 |
4.93e-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: 162.50 E-value: 4.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPsrPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIG 1061
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEPA--LFATTIYENILYGKE--GASESE----VMEAAKLAN----AHSFISSLpegystkvgergiqmSGGQRQRI 1129
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPEnlGLPREEirerVEEALELVGlehlADRPPHEL---------------SGGQKQRV 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220188 1130 AIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVVVA-HRLSTI-KNSDMISVIQDGKIIEQGS 1201
Cdd:COG1122 144 AIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVaELADRVIVLDDGRIVADGT 217
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
982-1200 |
6.94e-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: 160.17 E-value: 6.94e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRpDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKlKSLRRHIG 1061
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEPALFATTIYENIlygkegasesevmeaaklanahsfisslpegystkvgerGIQMSGGQRQRIAIARAVLKNPEI 1141
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15220188 1142 LLLDEATSALDVESERVVQQALDRLMRDRTTVVVAHRLSTIKNSDMISVIQDGKIIEQG 1200
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
663-945 |
3.43e-44 |
|
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: 163.22 E-value: 3.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 663 LCGTLGSFIAGSQMPLFAL------------------GIAQALVSYYMDWETTQNEVKRISILFCCGSVITVIVHTIEHT 724
Cdd:cd18558 2 VVGILCAIIHGGLLPAFMVifgdmtdsftnggmtnitGNSSGLNSSAGPFEKLEEEMTLYAYYYLIIGAIVLITAYIQGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 725 TFGIMGERLTLRVRQKMFSAILRNEIGWFDKvdNTSSMLASRLESDATLLRTIVVDRSTILLENLGLVVTAFIISFILNW 804
Cdd:cd18558 82 FWGLAAGRQTKKIRYKFFHAIMRQEIGWFDV--NDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 805 RLTLVVLATYPLI-ISGHISEKIfMQGYGGNLSKAYLKANMLAGESISNIRTVVAFCAEEKVLDLYSKELLEPSERSFRR 883
Cdd:cd18558 160 KLTLVILAISPVLgLSAVVWAKI-LSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKK 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15220188 884 GQMAGILYGVSQFFIFSSYGLALWYG-SILMEKGLSSFESVMKTFMVLIVTALVMGEVLALAP 945
Cdd:cd18558 239 AITFNISMGAAFLLIYASYALAFWYGtYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEA 301
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
982-1218 |
4.53e-44 |
|
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: 168.16 E-value: 4.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRP--DVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLK---LKSL 1056
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1057 RRHIGLVQQEP--ALFAT-TIYENI-----LYGKEGASE-----SEVMEA----AKLANAHSFisslpegystkvgergi 1119
Cdd:COG1123 341 RRRVQMVFQDPysSLNPRmTVGDIIaeplrLHGLLSRAErrervAELLERvglpPDLADRYPH----------------- 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1120 QMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDR--TTVVVAHRLSTIKN-SDMISVIQDGKI 1196
Cdd:COG1123 404 ELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELglTYLFISHDLAVVRYiADRVAVMYDGRI 483
|
250 260
....*....|....*....|...
gi 15220188 1197 IEQGSHNILVENKNGPYSK-LIS 1218
Cdd:COG1123 484 VEDGPTEEVFANPQHPYTRaLLA 506
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
982-1201 |
1.94e-43 |
|
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: 157.73 E-value: 1.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPsrpDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYD-----PTAGIIMIDGQDIKKLKLK-- 1054
Cdd:cd03260 1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1055 SLRRHIGLVQQEPALFATTIYENILYG-------KEGASESEVMEAAKLANahsfissLPEgystKVGER--GIQMSGGQ 1125
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgikLKEELDERVEEALRKAA-------LWD----EVKDRlhALGLSGGQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15220188 1126 RQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVVVAHRLSTIKN-SDMISVIQDGKIIEQGS 1201
Cdd:cd03260 147 QQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGP 223
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
982-1200 |
2.16e-43 |
|
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: 157.30 E-value: 2.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSrpdVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKslRRHIG 1061
Cdd:cd03259 1 LELKGLSKTYGS---VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEPALFAT-TIYENILYG------KEGASESEVMEAAKLANAHSFISSLPEgystkvgergiQMSGGQRQRIAIARA 1134
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGlklrgvPKAEIRARVRELLELVGLEGLLNRYPH-----------ELSGGQQQRVALARA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15220188 1135 VLKNPEILLLDEATSALDVESERVVQQALDRLMRDR--TTVVVAHRLS-TIKNSDMISVIQDGKIIEQG 1200
Cdd:cd03259 145 LAREPSLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
363-584 |
2.24e-43 |
|
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: 157.73 E-value: 2.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 363 FKDVTFTYPsrpDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYE-----PTDGAVMLDGNDIRYLDLK--WL 435
Cdd:cd03260 3 LRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvlEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 436 RGHIGLVNQEPVLFATTIRENIMYG------KDDATSEEITNAAkLSEAisfinNLPEGFETQVGERGiqLSGGQKQRIS 509
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDERVEEA-LRKA-----ALWDEVKDRLHALG--LSGGQQQRLC 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15220188 510 ISRAIVKNPSILLLDEATSALDAESEKIVQEALDRVMVGRTTVVVAHRLSTV-RNADIIAVVGGGKIIESGSHDEL 584
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAaRVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
982-1195 |
5.33e-43 |
|
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: 155.71 E-value: 5.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRPDVT--IFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIImidgqdikklklkSLRRH 1059
Cdd:cd03250 1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-------------SVPGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1060 IGLVQQEPALFATTIYENILYGKEGASE--SEVMEAAKLanaHSFISSLPEGYSTKVGERGIQMSGGQRQRIAIARAVLK 1137
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPFDEEryEKVIKACAL---EPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1138 NPEILLLDEATSALDVE-SERVVQQAL-DRLMRDRTTVVVAHRLSTIKNSDMISVIQDGK 1195
Cdd:cd03250 145 DADIYLLDDPLSAVDAHvGRHIFENCIlGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
361-574 |
6.16e-43 |
|
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: 155.71 E-value: 6.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSRPDV--VIFDKLNFVIPAGKVVALVGGSGSGKSTMISLI--ErfYEPTDGAVmldgndiryldlkWLR 436
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSV-------------SVP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 437 GHIGLVNQEPVLFATTIRENIMYGK--DDATSEEITNAAKLSEAISfinNLPEGFETQVGERGIQLSGGQKQRISISRAI 514
Cdd:cd03250 66 GSIAYVSQEPWIQNGTIRENILFGKpfDEERYEKVIKACALEPDLE---ILPDGDLTEIGEKGINLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220188 515 VKNPSILLLDEATSALDAE-SEKIVQEALDRVMV-GRTTVVVAHRLSTVRNADIIAVVGGGK 574
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHvGRHIFENCILGLLLnNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
361-589 |
9.15e-43 |
|
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: 155.95 E-value: 9.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPsrPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHIG 440
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 441 LVNQEPV--LFATTIRENIMYG------KDDATSEEITNAAKLSEAisfinnlpEGFEtqvgERGI-QLSGGQKQRISIS 511
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGpenlglPREEIRERVEEALELVGL--------EHLA----DRPPhELSGGQKQRVAIA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 512 RAIVKNPSILLLDEATSALDAESEKIVQEALDRVMVGRTTVVVA-HRLSTV-RNADIIAVVGGGKIIESGSHDELISNPD 589
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVaELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
980-1201 |
1.03e-42 |
|
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: 154.88 E-value: 1.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 980 GTIELKGVHFSYpsRPDV-TIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRR 1058
Cdd:cd03369 5 GEIEVENLSVRY--APDLpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1059 HIGLVQQEPALFATTIYENI-LYGKEgaSESEVMEAaklanahsfisslpegysTKVGERGIQMSGGQRQRIAIARAVLK 1137
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdPFDEY--SDEEIYGA------------------LRVSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220188 1138 NPEILLLDEATSALDVESERVVQQALDRLMRDRTTVVVAHRLSTIKNSDMISVIQDGKIIEQGS 1201
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
361-588 |
1.41e-42 |
|
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: 155.92 E-value: 1.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSRPDVVifDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHIG 440
Cdd:cd03295 1 IEFENVTKRYGGGKKAV--NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 441 LVNQEPVLFA-TTIRENI-MYGKDDATSEEiTNAAKLSEAISFINNLPEGFetqvGER-GIQLSGGQKQRISISRAIVKN 517
Cdd:cd03295 79 YVIQQIGLFPhMTVEENIaLVPKLLKWPKE-KIRERADELLALVGLDPAEF----ADRyPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220188 518 PSILLLDEATSALDAESEKIVQEALDRV--MVGRTTVVVAHRL-STVRNADIIAVVGGGKIIESGSHDELISNP 588
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLqqELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
982-1201 |
1.43e-42 |
|
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: 155.91 E-value: 1.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRpdvTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKL---KLKSLRR 1058
Cdd:COG1127 6 IEVRNLTKSFGDR---VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLsekELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1059 HIGLVQQEPALF-ATTIYENILYG-KE--GASESEVMEAA--KLAnahsfisslpegystKVGERGI------QMSGGQR 1126
Cdd:COG1127 83 RIGMLFQGGALFdSLTVFENVAFPlREhtDLSEAEIRELVleKLE---------------LVGLPGAadkmpsELSGGMR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1127 QRIAIARAVLKNPEILLLDEATSALDVESERVvqqaLDRLMRDR------TTVVVAHRLSTIKN-SDMISVIQDGKIIEQ 1199
Cdd:COG1127 148 KRVALARALALDPEILLYDEPTAGLDPITSAV----IDELIRELrdelglTSVVVTHDLDSAFAiADRVAVLADGKIIAE 223
|
..
gi 15220188 1200 GS 1201
Cdd:COG1127 224 GT 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
363-606 |
2.14e-42 |
|
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: 163.15 E-value: 2.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 363 FKDVTFTYPSRP--DVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYL---DLKWLRG 437
Cdd:COG1123 263 VRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLsrrSLRELRR 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 438 HIGLVNQEPV--LFAT-TIRENIMYG---KDDATSEEItnAAKLSEAISFInNLPEGFEtqvgERGI-QLSGGQKQRISI 510
Cdd:COG1123 343 RVQMVFQDPYssLNPRmTVGDIIAEPlrlHGLLSRAER--RERVAELLERV-GLPPDLA----DRYPhELSGGQRQRVAI 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 511 SRAIVKNPSILLLDEATSALDAESEKIVQEALDRV--MVGRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESGSHDELISN 587
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRDLqrELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFAN 495
|
250 260
....*....|....*....|
gi 15220188 588 PDGAYS-SLLriqeAASPNL 606
Cdd:COG1123 496 PQHPYTrALL----AAVPSL 511
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
982-1199 |
3.55e-42 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 154.05 E-value: 3.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPS-RPDVTIFSDFNLLVPSGKSMALVGQSGSGKS---SVLSLVLRfydPTAGIIMIDGQDIKKLKLKSL- 1056
Cdd:COG1136 5 LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKStllNILGGLDR---PTSGEVLIDGQDISSLSERELa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1057 ---RRHIGLVQQEPALFAT-TIYENI----LYGKEGASES-----EVMEAAKLAN-AHSFISslpegystkvgergiQMS 1122
Cdd:COG1136 82 rlrRRHIGFVFQFFNLLPElTALENValplLLAGVSRKERrerarELLERVGLGDrLDHRPS---------------QLS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15220188 1123 GGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRD--RTTVVVAHRLSTIKNSDMISVIQDGKIIEQ 1199
Cdd:COG1136 147 GGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElgTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
982-1201 |
4.15e-42 |
|
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: 154.20 E-value: 4.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRpdvTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLK---LKSLRR 1058
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1059 HIGLVQQEPALF-ATTIYENI---LYGKEGASESE----VMEAAKLANAHSFISSLPEgystkvgergiQMSGGQRQRIA 1130
Cdd:cd03261 78 RMGMLFQSGALFdSLTVFENVafpLREHTRLSEEEireiVLEKLEAVGLRGAEDLYPA-----------ELSGGMKKRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15220188 1131 IARAVLKNPEILLLDEATSALDVESERVVQQaLDRLMRDR---TTVVVAHRLSTI-KNSDMISVIQDGKIIEQGS 1201
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDD-LIRSLKKElglTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGT 220
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
982-1215 |
5.77e-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: 154.19 E-value: 5.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRP-DVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHI 1060
Cdd:COG1124 2 LEVRNLSVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1061 GLVQQEPAL-------FATTIYENILYGKEGASESEVMEAAKLANahsfissLPEGYSTKvgeRGIQMSGGQRQRIAIAR 1133
Cdd:COG1124 82 QMVFQDPYAslhprhtVDRILAEPLRIHGLPDREERIAELLEQVG-------LPPSFLDR---YPHQLSGGQRQRVAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1134 AVLKNPEILLLDEATSALDVeserVVQ----QALDRLMRDR--TTVVVAHRLSTIKN-SDMISVIQDGKIIEQGSHNILV 1206
Cdd:COG1124 152 ALILEPELLLLDEPTSALDV----SVQaeilNLLKDLREERglTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLL 227
|
....*....
gi 15220188 1207 ENKNGPYSK 1215
Cdd:COG1124 228 AGPKHPYTR 236
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
363-556 |
9.00e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 152.28 E-value: 9.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 363 FKDVTFTYPSRPdvvIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHIGLV 442
Cdd:COG4619 3 LEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 443 NQEPVLFATTIRENIMYG---KDDATSEEItnAAKLSEAIsfinNLPEGF-ETQVGErgiqLSGGQKQRISISRAIVKNP 518
Cdd:COG4619 80 PQEPALWGGTVRDNLPFPfqlRERKFDRER--ALELLERL----GLPPDIlDKPVER----LSGGERQRLALIRALLLQP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15220188 519 SILLLDEATSALDAESEKIVQEALDRVM--VGRTTVVVAH 556
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLaeEGRAVLWVSH 189
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
382-528 |
1.66e-41 |
|
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: 149.34 E-value: 1.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 382 LNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHIGLVNQEPVLF-ATTIRENIMYG 460
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENLRLG 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 461 kddATSEEITNAAKLSEAISFINNLPEGF--ETQVGERGIQLSGGQKQRISISRAIVKNPSILLLDEATS 528
Cdd:pfam00005 84 ---LLLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
361-588 |
1.70e-41 |
|
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: 152.35 E-value: 1.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSRP-DVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYL---DLKWLR 436
Cdd:cd03258 2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLsgkELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 437 GHIGLVNQEPVLFAT-TIRENIMYgkddatSEEITNAAKlSEAISFINNLPE--GFETQVGERGIQLSGGQKQRISISRA 513
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVAL------PLEIAGVPK-AEIEERVLELLElvGLEDKADAYPAQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15220188 514 IVKNPSILLLDEATSALDAESEKIVQEALDRV--MVGRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESGSHDELISNP 588
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLRDInrELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
363-574 |
1.88e-41 |
|
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: 151.47 E-value: 1.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 363 FKDVTFTYPSRpDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHIGLV 442
Cdd:cd03225 2 LKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 443 NQEP--VLFATTIRENIMYG------KDDATSEEITNAAKLSEAISFINNLPEgfetqvgergiQLSGGQKQRISISRAI 514
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAFGlenlglPEEEIEERVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220188 515 VKNPSILLLDEATSALDAESEKIVQEALDRVM-VGRTTVVVAHRLSTVRN-ADIIAVVGGGK 574
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKaEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
983-1195 |
6.03e-41 |
|
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: 149.92 E-value: 6.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 983 ELKGVHFSYPSRpDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIGL 1062
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1063 VQQEPA--LFATTIYENILYGKE--GASESEVMEAAKLANAHSFISSLPegystkvgERGI-QMSGGQRQRIAIARAVLK 1137
Cdd:cd03225 80 VFQNPDdqFFGPTVEEEVAFGLEnlGLPEEEIEERVEEALELVGLEGLR--------DRSPfTLSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1138 NPEILLLDEATSALDVESERVVQQALDRLMRDRTTVVVA-HRLSTIKN-SDMISVIQDGK 1195
Cdd:cd03225 152 DPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLEDGK 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
982-1201 |
1.91e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 149.44 E-value: 1.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPsrpDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKlKLKSLRRHIG 1061
Cdd:COG1131 1 IEVRGLTKRYG---DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEPALFAT-TIYENI-----LYGKEGA-SESEVMEAAKLANahsfissLPEGYSTKVGergiQMSGGQRQRIAIARA 1134
Cdd:COG1131 77 YVPQEPALYPDlTVRENLrffarLYGLPRKeARERIDELLELFG-------LTDAADRKVG----TLSGGMKQRLGLALA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15220188 1135 VLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVVVA-HRLSTI-KNSDMISVIQDGKIIEQGS 1201
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAeRLCDRVAIIDKGRIVADGT 214
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
982-1201 |
3.28e-40 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 152.56 E-value: 3.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPsrpDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIkkLKLKSLRRHIG 1061
Cdd:COG3842 6 LELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV--TGLPPEKRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEPALFA-TTIYENILYG--KEGASESE----VMEAAKLANahsfissLpEGYstkvGERGI-QMSGGQRQRIAIAR 1133
Cdd:COG3842 81 MVFQDYALFPhLTVAENVAFGlrMRGVPKAEirarVAELLELVG-------L-EGL----ADRYPhQLSGGQQQRVALAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15220188 1134 AVLKNPEILLLDEATSALDVESERVVQQALDRLMRDR--TTVVVAHRLS---TIknSDMISVIQDGKIIEQGS 1201
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELgiTFIYVTHDQEealAL--ADRIAVMNDGRIEQVGT 219
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
982-1200 |
3.98e-40 |
|
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: 148.42 E-value: 3.98e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRPD-VTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLK---LKSLR 1057
Cdd:cd03257 2 LEVKNLSVSFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1058 RHIGLVQQEP--ALFAT-TIYENI---LYGKEGASESEVMEAAKLANAHSFisSLPEGYSTKvgeRGIQMSGGQRQRIAI 1131
Cdd:cd03257 82 KEIQMVFQDPmsSLNPRmTIGEQIaepLRIHGKLSKKEARKEAVLLLLVGV--GLPEEVLNR---YPHELSGGQRQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220188 1132 ARAVLKNPEILLLDEATSALDVESERVVQQALDRL--MRDRTTVVVAHRLSTIKN-SDMISVIQDGKIIEQG 1200
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLqeELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
361-579 |
4.14e-40 |
|
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: 146.30 E-value: 4.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSRpDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDlKWLRGHIG 440
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 441 LVNQEPVLFATTIRENImygkddatseeitnaaklseaisfinnlpegfetqvgerGIQLSGGQKQRISISRAIVKNPSI 520
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15220188 521 LLLDEATSALDAESEKIVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVGGGKIIESG 579
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
359-580 |
5.55e-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: 147.17 E-value: 5.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 359 GDILFKDVTFTY-PSRPDVVifDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRG 437
Cdd:cd03369 5 GEIEVENLSVRYaPDLPPVL--KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 438 HIGLVNQEPVLFATTIRENI-MYgkDDATSEEITNAAKLSEAisfinnlpegfetqvgerGIQLSGGQKQRISISRAIVK 516
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdPF--DEYSDEEIYGALRVSEG------------------GLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220188 517 NPSILLLDEATSALDAESEKIVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVGGGKIIESGS 580
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
982-1201 |
6.60e-40 |
|
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: 147.73 E-value: 6.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRP-DVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSL---R 1057
Cdd:cd03258 2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1058 RHIGLVQQEPALFAT-TIYENILYGKEGASESEVMEAAKLANAHSFIsslpeGYSTKVGERGIQMSGGQRQRIAIARAVL 1136
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALPLEIAGVPKAEIEERVLELLELV-----GLEDKADAYPAQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15220188 1137 KNPEILLLDEATSALDVESERVVQQALDRLMRDR--TTVVVAHRLSTIKN-SDMISVIQDGKIIEQGS 1201
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGT 224
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
375-588 |
9.15e-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: 147.83 E-value: 9.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 375 DVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDI--RYLDLKWLRGHIGLVNQEPVLFA-T 451
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKVGMVFQQFNLFPhL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 452 TIRENIMYG--------KDDAtsEEItnAAKLSEaisfinnlpegfetQVG--ERG----IQLSGGQKQRISISRAIVKN 517
Cdd:COG1126 93 TVLENVTLApikvkkmsKAEA--EER--AMELLE--------------RVGlaDKAdaypAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15220188 518 PSILLLDEATSALDAEsekIVQEALDrVMV-----GRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESGSHDELISNP 588
Cdd:COG1126 155 PKVMLFDEPTSALDPE---LVGEVLD-VMRdlakeGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEFFENP 227
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
361-586 |
1.65e-39 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 146.75 E-value: 1.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPsrpDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRyLDLKWLRGHIG 440
Cdd:COG1131 1 IEVRGLTKRYG---DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA-RDPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 441 LVNQEPVLFAT-TIRENI-----MYGKDDATSEEitnaaKLSEAISFINnLPEGFETQVGergiQLSGGQKQRISISRAI 514
Cdd:COG1131 77 YVPQEPALYPDlTVRENLrffarLYGLPRKEARE-----RIDELLELFG-LTDAADRKVG----TLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220188 515 VKNPSILLLDEATSALDAESEKIVQEALDRVMVGRTTVVVA-HRLSTV-RNADIIAVVGGGKIIESGSHDELIS 586
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAeRLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
982-1196 |
2.07e-39 |
|
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: 146.10 E-value: 2.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRPD-VTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSL---- 1056
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1057 RRHIGLVQQEPALFAT-TIYENILYGKE--GASESEVMEAAK--LANAHsfissLPEGYSTKVGergiQMSGGQRQRIAI 1131
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELPLLlaGVPKKERRERAEelLERVG-----LGDRLNHYPS----ELSGGQQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15220188 1132 ARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDR--TTVVVAHRLSTIKNSDMISVIQDGKI 1196
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1000-1149 |
3.53e-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: 142.79 E-value: 3.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1000 FSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIGLVQQEPALF-ATTIYENI 1078
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15220188 1079 LYgkeGASESEVMEAAKLANAHSFISSLPEGY--STKVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEATS 1149
Cdd:pfam00005 81 RL---GLLLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
363-579 |
4.78e-39 |
|
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: 145.34 E-value: 4.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 363 FKDVTFTYPSRPDVV-IFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLD---LKWLRGH 438
Cdd:cd03257 4 VKNLSVSFPTGGGSVkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 439 IGLVNQEPvlFAT-----TIRENIM-----YGKDDATSEEITNAAKLSEAIsfinNLPEGFETQvgeRGIQLSGGQKQRI 508
Cdd:cd03257 84 IQMVFQDP--MSSlnprmTIGEQIAeplriHGKLSKKEARKEAVLLLLVGV----GLPEEVLNR---YPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220188 509 SISRAIVKNPSILLLDEATSALDAESEKIVQEALD--RVMVGRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESG 579
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKklQEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
982-1198 |
6.24e-39 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 144.81 E-value: 6.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPsrPDVTIFSDFNLLVPSGkSMA-LVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKS---LR 1057
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKG-EFVfLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1058 RHIGLVQQEPALFAT-TIYENILYGKE--GASESE----VMEAAKLANAHSFISSLPegystkvgergIQMSGGQRQRIA 1130
Cdd:COG2884 79 RRIGVVFQDFRLLPDrTVYENVALPLRvtGKSRKEirrrVREVLDLVGLSDKAKALP-----------HELSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15220188 1131 IARAVLKNPEILLLDEATSALDVE-SERVVqQALDRLMRDRTTVVVA-HRLSTIKNSDM-ISVIQDGKIIE 1198
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPEtSWEIM-ELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
663-935 |
7.69e-39 |
|
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: 146.25 E-value: 7.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 663 LCGTLGSFIAGSQMPLFALGIAQALVSYYMDWETTQNEVKRIS---ILFCCGSVITVIVHTiehTTFGIMGERLTLRVRQ 739
Cdd:pfam00664 2 ILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSlalLLLGLAQFILSFLQS---YLLNHTGERLSRRLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 740 KMFSAILRNEIGWFDKvdNTSSMLASRLESDATLLRTIVVDRSTILLENLGLVVTAFIISFILNWRLTLVVLATYPLIIS 819
Cdd:pfam00664 79 KLFKKILRQPMSFFDT--NSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 820 GHISEKIFMQGYGGNLSKAYLKANMLAGESISNIRTVVAFCAEEKVLDLYSKELLEPSERSFRRGQMAGILYGVSQFFIF 899
Cdd:pfam00664 157 VSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGY 236
|
250 260 270
....*....|....*....|....*....|....*...
gi 15220188 900 SSYGLALWYGSILMEKGLSSFES--VMKTFMVLIVTAL 935
Cdd:pfam00664 237 LSYALALWFGAYLVISGELSVGDlvAFLSLFAQLFGPL 274
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
982-1201 |
9.38e-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: 145.19 E-value: 9.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRPdvtIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIG 1061
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LV-QQEPALFATTIYENILYG-----KEGASESE-----VMEAAKLANAHSFIsslpegystkvgERGI-QMSGGQRQRI 1129
Cdd:COG1120 79 YVpQEPPAPFGLTVRELVALGryphlGLFGRPSAedreaVEEALERTGLEHLA------------DRPVdELSGGERQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15220188 1130 AIARAVLKNPEILLLDEATSALDVESERVVQQALDRL--MRDRTTVVVAHRLS-TIKNSDMISVIQDGKIIEQGS 1201
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGP 221
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
41-313 |
1.24e-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: 145.48 E-value: 1.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 41 MALGSIGACIHGASVPVFFIFFGKLINIIglaylFPQ--EASHKVAKYSLDFVYLSVVILFSSWLEVACWMHTGERQAAK 118
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVL-----LPDgdPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 119 IRKAYLRSMLSQDISLFDTeISTGEVISAITSEILVVQDAISEKVGNFMHFISRFIAGFAIGFASVWQISLVTLSIVPFI 198
Cdd:pfam00664 76 LRRKLFKKILRQPMSFFDT-NSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 199 ALAGGIYAFVSSGLIVRVRKSYVKANEIAEEVIGNVRTVQAFTGEEKAVSSYQGALRNTYNYGRKAGLAKGLGLGSLHFV 278
Cdd:pfam00664 155 ILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFI 234
|
250 260 270
....*....|....*....|....*....|....*
gi 15220188 279 LFLSWALLIWFTSIVVHKGIANGGESFTTMLNVVI 313
Cdd:pfam00664 235 GYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQ 269
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
88-597 |
1.83e-38 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 157.06 E-value: 1.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 88 LDFVYLSVVILFSSWLeVACWMHTGERqaakIRKAYLRSMLSQDISLFDTEiSTGEVISAITSEILVVQDAISEKVGNFM 167
Cdd:PLN03232 959 LGFGQVAVTFTNSFWL-ISSSLHAAKR----LHDAMLNSILRAPMLFFHTN-PTGRVINRFSKDIGDIDRNVANLMNMFM 1032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 168 HFISRFIAGFAIgFASVWQISLvtLSIVPFIALAGGIYAFV-SSGLIVRVRKSYVKANEIAE--EVIGNVRTVQAFTGEE 244
Cdd:PLN03232 1033 NQLWQLLSTFAL-IGTVSTISL--WAIMPLLILFYAAYLYYqSTSREVRRLDSVTRSPIYAQfgEALNGLSSIRAYKAYD 1109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 245 KAVSSYQGALRNTYNYGrkagLAKGLGLGSLHFVLFLSWALLIWFTSI--VVHKGIANGGESFTTMLNVVIAGLSlgQAA 322
Cdd:PLN03232 1110 RMAKINGKSMDNNIRFT----LANTSSNRWLTIRLETLGGVMIWLTATfaVLRNGNAENQAGFASTMGLLLSYTL--NIT 1183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 323 PDISTFMRASAAAYPIFQMIERNTE-----------DKTGRKLGN--VNGDILFKDVTFTY-PSRPDVVifDKLNFVIPA 388
Cdd:PLN03232 1184 TLLSGVLRQASKAENSLNSVERVGNyidlpseataiIENNRPVSGwpSRGSIKFEDVHLRYrPGLPPVL--HGLSFFVSP 1261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 389 GKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHIGLVNQEPVLFATTIRENImygkdDATSEE 468
Cdd:PLN03232 1262 SEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI-----DPFSEH 1336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 469 itNAAKLSEAI------SFINNLPEGFETQVGERGIQLSGGQKQRISISRAIVKNPSILLLDEATSALDAESEKIVQEAL 542
Cdd:PLN03232 1337 --NDADLWEALerahikDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTI 1414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 15220188 543 DRVMVGRTTVVVAHRLSTVRNADIIAVVGGGKIIESGSHDELISNPDGAYSSLLR 597
Cdd:PLN03232 1415 REEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVH 1469
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
361-589 |
2.95e-38 |
|
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: 143.58 E-value: 2.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSRpdvVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLD---LKWLRG 437
Cdd:COG1127 6 IEVRNLTKSFGDR---VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 438 HIGLVNQEPVLF-ATTIRENIMY------GKDDATSEEITNaAKLSeaisfinnlpegfetQVGERGI------QLSGGQ 504
Cdd:COG1127 83 RIGMLFQGGALFdSLTVFENVAFplrehtDLSEAEIRELVL-EKLE---------------LVGLPGAadkmpsELSGGM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 505 KQRISISRAIVKNPSILLLDEATSALDAE-SEKIV------QEALdrvmvGRTTVVVAHRLSTVRN-ADIIAVVGGGKII 576
Cdd:COG1127 147 RKRVALARALALDPEILLYDEPTAGLDPItSAVIDelirelRDEL-----GLTSVVVTHDLDSAFAiADRVAVLADGKII 221
|
250
....*....|...
gi 15220188 577 ESGSHDELISNPD 589
Cdd:COG1127 222 AEGTPEELLASDD 234
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
361-589 |
5.01e-38 |
|
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: 142.64 E-value: 5.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSRpdvVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYL---DLKWLRG 437
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLseaELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 438 HIGLVNQEPVLF-ATTIRENIMY------GKDDATSEEITnAAKLSEAisfinnlpeGFETQVGERGIQLSGGQKQRISI 510
Cdd:cd03261 78 RMGMLFQSGALFdSLTVFENVAFplrehtRLSEEEIREIV-LEKLEAV---------GLRGAEDLYPAELSGGMKKRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 511 SRAIVKNPSILLLDEATSALD-AESEKIVQEALD-RVMVGRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESGSHDELISN 587
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDpIASGVIDDLIRSlKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRAS 227
|
..
gi 15220188 588 PD 589
Cdd:cd03261 228 DD 229
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
982-1201 |
6.99e-38 |
|
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: 142.30 E-value: 6.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRPdvtIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKsLRRHIG 1061
Cdd:COG4555 2 IEVENLSKKYGKVP---ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEPALFAT-TIYENI-----LYGKEGASESEVMEAAklanAHSFIssLPEGYSTKVGErgiqMSGGQRQRIAIARAV 1135
Cdd:COG4555 78 VLPDERGLYDRlTVRENIryfaeLYGLFDEELKKRIEEL----IELLG--LEEFLDRRVGE----LSTGMKKKVALARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15220188 1136 LKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVVVA-HRLSTIKN-SDMISVIQDGKIIEQGS 1201
Cdd:COG4555 148 VHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGS 215
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
361-579 |
8.55e-38 |
|
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: 141.12 E-value: 8.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSrpdVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIryLDLKWLRGHIG 440
Cdd:cd03259 1 LELKGLSKTYGS---VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV--TGVPPERRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 441 LVNQEPVLFAT-TIRENIMYGKDDATSEEITNAAKLSEAISFInnlpeGFETQVGERGIQLSGGQKQRISISRAIVKNPS 519
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGLKLRGVPKAEIRARVRELLELV-----GLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15220188 520 ILLLDEATSALDAESEKIVQEALDRVM--VGRTTVVVAHRLS-TVRNADIIAVVGGGKIIESG 579
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQreLGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
982-1177 |
9.09e-38 |
|
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: 141.46 E-value: 9.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPS-RPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKklklkSLRRHI 1060
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT-----GPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1061 GLVQQEPALFA-TTIYENILYGKE--GASESEVMEAAklanahsfisslpEGYSTKVGERGI------QMSGGQRQRIAI 1131
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLElqGVPKAEARERA-------------EELLELVGLSGFenayphQLSGGMRQRVAL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15220188 1132 ARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDR--TTVVVAH 1177
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTH 190
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
361-577 |
1.14e-37 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 141.33 E-value: 1.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPS-RPDVVIFDKLNFVIPAGKVVALVGGSGSGKST---MISLIERfyePTDGAVMLDGNDIRYLD---LK 433
Cdd:COG1136 5 LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDISSLSereLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 434 WLRG-HIGLVNQEPVLFAT-TIRENIMY-----GKDDATSEEItnAAKLSEAI---SFINNLPEgfetqvgergiQLSGG 503
Cdd:COG1136 82 RLRRrHIGFVFQFFNLLPElTALENVALplllaGVSRKERRER--ARELLERVglgDRLDHRPS-----------QLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15220188 504 QKQRISISRAIVKNPSILLLDEATSALDAESEKIVQEALDRV--MVGRTTVVVAHRLSTVRNADIIAVVGGGKIIE 577
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
61-336 |
1.35e-37 |
|
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: 143.08 E-value: 1.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 61 FFGKLINIIGLAylfpqEASHKVAKYSLDFVYLSVVILFSSWLEVACWMHTGERQAAKIRKAYLRSMLSQDISLFDTEiS 140
Cdd:cd18557 18 LIGRLIDTIIKG-----GDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKH-K 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 141 TGEVISAITSEILVVQDAISEKVGNFMHFISRFIAGFAIGFASVWQISLVTLSIVPFIALAGGIYAFVSSGLIVRVRKSY 220
Cdd:cd18557 92 TGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDAL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 221 VKANEIAEEVIGNVRTVQAFTGEEKAVSSYQGALRNTYNYGRKAGLAKGLGLGSLHFVLFLSWALLIWFTSIVVHKGIAN 300
Cdd:cd18557 172 AKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQLT 251
|
250 260 270
....*....|....*....|....*....|....*.
gi 15220188 301 GGESFTTMLNVVIAGLSLGQAAPDISTFMRASAAAY 336
Cdd:cd18557 252 VGELTSFILYTIMVASSVGGLSSLLADIMKALGASE 287
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
983-1195 |
2.99e-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: 137.38 E-value: 2.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 983 ELKGVHFSYPSRPdvtIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIGL 1062
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1063 VqqepalfattiyenilygkegasesevmeaaklanahsfisslpegystkvgergIQMSGGQRQRIAIARAVLKNPEIL 1142
Cdd:cd00267 78 V-------------------------------------------------------PQLSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15220188 1143 LLDEATSALDVESERVVQQALDRLMRD-RTTVVVAHRLSTIKN-SDMISVIQDGK 1195
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1004-1217 |
3.43e-37 |
|
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: 140.81 E-value: 3.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1004 NLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIGLVQQEPALFATTIYENiLYGKE 1083
Cdd:cd03288 41 KAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFN-LDPEC 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1084 GASESEVMEAAKLANAHSFISSLPEGYSTKVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQAL 1163
Cdd:cd03288 120 KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVV 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15220188 1164 DRLMRDRTTVVVAHRLSTIKNSDMISVIQDGKIIEQGSHNILVENKNGPYSKLI 1217
Cdd:cd03288 200 MTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLV 253
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
976-1177 |
6.09e-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: 140.22 E-value: 6.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 976 SNVEGTIELKGVHFSYPSRP-DVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLklk 1054
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1055 slRRHIGLVQQEPALFA-TTIYENILYG--KEGASESE----VMEAAKLANAHSFISSLPEgystkvgergiQMSGGQRQ 1127
Cdd:COG1116 79 --GPDRGVVFQEPALLPwLTVLDNVALGleLRGVPKAErrerARELLELVGLAGFEDAYPH-----------QLSGGMRQ 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15220188 1128 RIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRL-MRDRTTVV-VAH 1177
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLfVTH 197
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
361-574 |
6.25e-37 |
|
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: 137.32 E-value: 6.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPsrpDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLD--LKWLRGH 438
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 439 IGLVNQEPVLFAT-TIRENIMYGkddatseeitnaaklseaisfinnlpegfetqvgergiqLSGGQKQRISISRAIVKN 517
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 518 PSILLLDEATSALDAESEKIVQEALDRV--MVGRTTVVVAHRLSTVRN-ADIIAVVGGGK 574
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
982-1197 |
7.06e-37 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 139.81 E-value: 7.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSrpDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLK---LKSLRR 1058
Cdd:COG3638 3 LELRNLSKRYPG--GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1059 HIGLVQQEPALFA-TTIYENILYGkegasesevmeaakLANAHSFISSLPEGYST-----------KVG------ERGIQ 1120
Cdd:COG3638 81 RIGMIFQQFNLVPrLSVLTNVLAG--------------RLGRTSTWRSLLGLFPPedreralealeRVGladkayQRADQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1121 MSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDR--TTVVVAHRLSTIKN-SDMISVIQDGKII 1197
Cdd:COG3638 147 LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDgiTVVVNLHQVDLARRyADRIIGLRDGRVV 226
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
983-1200 |
7.16e-37 |
|
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: 137.18 E-value: 7.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 983 ELKGVHFSYPSRpdvTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIGL 1062
Cdd:cd03214 1 EVENLSVGYGGR---TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1063 VQQepalfattiyenilygkegaseseVMEAAKLAN-AHSFISSLpegystkvgergiqmSGGQRQRIAIARAVLKNPEI 1141
Cdd:cd03214 78 VPQ------------------------ALELLGLAHlADRPFNEL---------------SGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15220188 1142 LLLDEATSALDVEServvQQALDRLMRD------RTTVVVAHRLS-TIKNSDMISVIQDGKIIEQG 1200
Cdd:cd03214 119 LLLDEPTSHLDIAH----QIELLELLRRlarergKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
982-1201 |
7.77e-37 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 143.55 E-value: 7.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRpdvTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKslRRHIG 1061
Cdd:PRK09452 15 VELRGISKSFDGK---EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEPALFA-TTIYENILYG----KEGASESE--VMEAAKLANAHSFISSLPEgystkvgergiQMSGGQRQRIAIARA 1134
Cdd:PRK09452 90 TVFQSYALFPhMTVFENVAFGlrmqKTPAAEITprVMEALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1135 VLKNPEILLLDEATSALDVESERVVQQALDRLMRDR--TTVVVAH-RLSTIKNSDMISVIQDGKIIEQGS 1201
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLgiTFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
361-588 |
9.44e-37 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 142.14 E-value: 9.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSRP-DVVIFDKLNFVIPAGKVVALVGGSGSGKST---MISLIERfyePTDGAVMLDGNDIRYLDLKWLR 436
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLER---PTSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 437 G---HIGLVNQEPVLFAT-TIRENIMY-----GKDDAtseEItnAAKLSEAISFI------NNLPEgfetqvgergiQLS 501
Cdd:COG1135 79 AarrKIGMIFQHFNLLSSrTVAENVALpleiaGVPKA---EI--RKRVAELLELVglsdkaDAYPS-----------QLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 502 GGQKQRISISRAIVKNPSILLLDEATSALDAESEKIVQEALDRV---MvGRTTVVVAHRLSTVRN-ADIIAVVGGGKIIE 577
Cdd:COG1135 143 GGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDInreL-GLTIVLITHEMDVVRRiCDRVAVLENGRIVE 221
|
250
....*....|.
gi 15220188 578 SGSHDELISNP 588
Cdd:COG1135 222 QGPVLDVFANP 232
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
60-334 |
9.60e-37 |
|
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: 140.85 E-value: 9.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 60 IFFGKLIN-IIGLAYLFPQEASHKVAKYSLDFVYLSVVILFSSWLEVACWMHTGERQAAKIRKAYLRSMLSQDISLFDTe 138
Cdd:cd18780 17 YFFGQVIDaVTNHSGSGGEEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDV- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 139 ISTGEVISAITSEILVVQDAISEKVGNFMHFISRFIAGFAIGFASVWQISLVTLSIVPFIALAGGIYAFVSSGLIVRVRK 218
Cdd:cd18780 96 TRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 219 SYVKANEIAEEVIGNVRTVQAFTGEEKAVSSYQGALRNTYNYGRKAGLAKGLGLGSLHFVLFLSWALLIWFTSIVVHKGI 298
Cdd:cd18780 176 ALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGE 255
|
250 260 270
....*....|....*....|....*....|....*.
gi 15220188 299 ANGGESFTTMLNVVIAGLSLGQAAPDISTFMRASAA 334
Cdd:cd18780 256 LTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGA 291
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
982-1201 |
1.00e-36 |
|
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: 138.85 E-value: 1.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSrpDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLK---LKSLRR 1058
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1059 HIGLVQQEPALFA-TTIYENILYGKegasesevmeaaklANAHSFISSLPEGYS-----------TKVG------ERGIQ 1120
Cdd:cd03256 79 QIGMIFQQFNLIErLSVLENVLSGR--------------LGRRSTWRSLFGLFPkeekqralaalERVGlldkayQRADQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1121 MSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDR--TTVVVAHRLSTIK-NSDMISVIQDGKII 1197
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDLAReYADRIVGLKDGRIV 224
|
....
gi 15220188 1198 EQGS 1201
Cdd:cd03256 225 FDGP 228
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
982-1201 |
1.24e-36 |
|
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: 138.97 E-value: 1.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRPdvTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIG 1061
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEPALFA-TTIYENI-----LYG-KEGASESEVMEAAKLANahsfissLPEGystKVGER-GIQMSGGQRQRIAIAR 1133
Cdd:cd03295 79 YVIQQIGLFPhMTVEENIalvpkLLKwPKEKIRERADELLALVG-------LDPA---EFADRyPHELSGGQQQRVGVAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15220188 1134 AVLKNPEILLLDEATSALDVESERVVQQALDRLMRD--RTTVVVAHRL-STIKNSDMISVIQDGKIIEQGS 1201
Cdd:cd03295 149 ALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElgKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGT 219
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
363-574 |
1.30e-36 |
|
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: 135.45 E-value: 1.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 363 FKDVTFTYPSRPdvvIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHIGLV 442
Cdd:cd00267 2 IENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 443 nqepvlfattirenimygkddatseeitnaaklseaisfinnlpegfetqvgergIQLSGGQKQRISISRAIVKNPSILL 522
Cdd:cd00267 79 -------------------------------------------------------PQLSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15220188 523 LDEATSALDAESEKIVQEALDRVMV-GRTTVVVAHRLSTVRNA-DIIAVVGGGK 574
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
361-577 |
1.49e-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: 137.60 E-value: 1.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPS-RPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLdlkwlRGHI 439
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP-----GPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 440 GLVNQEPVLFA-TTIRENIMYG---KDDATSEEITNAAKLSEAI---SFINNLPEgfetqvgergiQLSGGQKQRISISR 512
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGlelQGVPKAEARERAEELLELVglsGFENAYPH-----------QLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 513 AIVKNPSILLLDEATSALDAESEKIVQEALDRVMV--GRTTVVVAHRLS-TVRNADIIAVVGG--GKIIE 577
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
363-621 |
1.88e-36 |
|
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: 145.43 E-value: 1.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 363 FKDVTFTYPSRPDVVIfDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPT---DGAVMLDGNDIRYLDLKWLRGHI 439
Cdd:COG1123 7 VRDLSVRYPGGDVPAV-DGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRRI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 440 GLVNQEP--VLFATTIRENIMYG--KDDATSEEItnAAKLSEAISFInnlpeGFETQVGERGIQLSGGQKQRISISRAIV 515
Cdd:COG1123 86 GMVFQDPmtQLNPVTVGDQIAEAleNLGLSRAEA--RARVLELLEAV-----GLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 516 KNPSILLLDEATSALDAESEKIVQEALDRVMV--GRTTVVVAHRLSTV-RNADIIAVVGGGKIIESGSHDELISNPDgay 592
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAAPQ--- 235
|
250 260
....*....|....*....|....*....
gi 15220188 593 ssllriQEAASPNLNHTPSLPVSTKPLPE 621
Cdd:COG1123 236 ------ALAAVPRLGAARGRAAPAAAAAE 258
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
982-1196 |
2.67e-36 |
|
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: 135.22 E-value: 2.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRPdvtIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKlKLKSLRRHIG 1061
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEPALFAT-TIYENILYgkegasesevmeaaklanahsfisslpegystkvgergiqmSGGQRQRIAIARAVLKNPE 1140
Cdd:cd03230 77 YLPEEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15220188 1141 ILLLDEATSALDVESERVVQQALDRLMRDRTTVVVA-HRLSTIKN-SDMISVIQDGKI 1196
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKEGKTILLSsHILEEAERlCDRVAILNNGRI 173
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
982-1201 |
5.12e-36 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 140.21 E-value: 5.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRP-DVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLK---LKSLR 1057
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSereLRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1058 RHIGLVQQEPALFAT-TIYENILYGKE--GASESE----VME-------AAKlanAHSFISslpegystkvgergiQMSG 1123
Cdd:COG1135 82 RKIGMIFQHFNLLSSrTVAENVALPLEiaGVPKAEirkrVAEllelvglSDK---ADAYPS---------------QLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1124 GQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLmRDR---TTVVVAHRLSTIKN-SDMISVIQDGKIIEQ 1199
Cdd:COG1135 144 GQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDI-NRElglTIVLITHEMDVVRRiCDRVAVLENGRIVEQ 222
|
..
gi 15220188 1200 GS 1201
Cdd:COG1135 223 GP 224
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
364-586 |
5.90e-36 |
|
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: 137.10 E-value: 5.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 364 KDVTFTYPSRPdvvIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHIGLVN 443
Cdd:COG1120 5 ENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 444 QEPVL-FATTIRENIMYG---------KDDATSEEITNAAkLSeaisfinnlpegfetQVG-----ERGI-QLSGGQKQR 507
Cdd:COG1120 82 QEPPApFGLTVRELVALGryphlglfgRPSAEDREAVEEA-LE---------------RTGlehlaDRPVdELSGGERQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 508 ISISRAIVKNPSILLLDEATSALD----AESEKIVQE-ALDRvmvGRTTVVVAHRLS-TVRNADIIAVVGGGKIIESGSH 581
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDlahqLEVLELLRRlARER---GRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPP 222
|
....*
gi 15220188 582 DELIS 586
Cdd:COG1120 223 EEVLT 227
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
383-592 |
8.75e-36 |
|
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: 137.39 E-value: 8.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 383 NFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYL---DLKWLRGH-IGLVNQEPVLFA-TTIRENI 457
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMsrkELRELRRKkISMVFQSFALLPhRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 458 MYGKDDATSEEITNAAKLSEAISFINnlPEGFETQVGErgiQLSGGQKQRISISRAIVKNPSILLLDEATSALDAESEKI 537
Cdd:cd03294 124 AFGLEVQGVPRAEREERAAEALELVG--LEGWEHKYPD---ELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRRE 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15220188 538 VQEALDRV--MVGRTTVVVAHRLS-TVRNADIIAVVGGGKIIESGSHDELISNPDGAY 592
Cdd:cd03294 199 MQDELLRLqaELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTNPANDY 256
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
982-1195 |
8.76e-36 |
|
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: 134.24 E-value: 8.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPsrpDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKL--KLKSLRRH 1059
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLedELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1060 IGLVQQEPALFAT-TIYENILYGkegasesevmeaaklanahsfisslpegystkvgergiqMSGGQRQRIAIARAVLKN 1138
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1139 PEILLLDEATSALDVESERVVQQALDRL--MRDRTTVVVAHRLS-TIKNSDMISVIQDGK 1195
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDeAARLADRVVVLRDGK 178
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
360-588 |
9.26e-36 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 139.85 E-value: 9.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 360 DILFKDVTFTYPsrpDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIryLDLK-WLRGh 438
Cdd:COG3842 5 ALELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV--TGLPpEKRN- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 439 IGLVNQEPVLFA-TTIRENIMYG--KDDATSEEItnAAKLSEAISFINnLpEGFEtqvgERGI-QLSGGQKQRISISRAI 514
Cdd:COG3842 79 VGMVFQDYALFPhLTVAENVAFGlrMRGVPKAEI--RARVAELLELVG-L-EGLA----DRYPhQLSGGQQQRVALARAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15220188 515 VKNPSILLLDEATSALDAESEKIVQEALDRVM--VGRTTVVVAHRLS---TVrnADIIAVVGGGKIIESGSHDELISNP 588
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLREEMREELRRLQreLGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEEIYERP 227
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
982-1201 |
1.11e-35 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 135.89 E-value: 1.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPsrpDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDI--KKLKLKSLRRH 1059
Cdd:COG1126 2 IEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1060 IGLVQQEPALFA-TTIYENILYGKE---GASESEVMEAAK--LAnahsfisslpegystKVG--ERG----IQMSGGQRQ 1127
Cdd:COG1126 79 VGMVFQQFNLFPhLTVLENVTLAPIkvkKMSKAEAEERAMelLE---------------RVGlaDKAdaypAQLSGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1128 RIAIARAVLKNPEILLLDEATSALDVESERVVqqaLDrLMRD-----RTTVVVAHRLSTIKN-SDMISVIQDGKIIEQGS 1201
Cdd:COG1126 144 RVAIARALAMEPKVMLFDEPTSALDPELVGEV---LD-VMRDlakegMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGP 219
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
338-1196 |
2.11e-35 |
|
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: 147.36 E-value: 2.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 338 IFQMIERNTEDKTGRKLGNVNGDILFKDvtFTYPSRPdvvIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTD 417
Cdd:TIGR01271 406 IGELFEKIKQNNKARKQPNGDDGLFFSN--FSLYVTP---VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSE 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 418 GavmldgnDIRYldlkwlRGHIGLVNQEPVLFATTIRENIMYG--KDDATSEEITNAAKLSEAISFinnLPEGFETQVGE 495
Cdd:TIGR01271 481 G-------KIKH------SGRISFSPQTSWIMPGTIKDNIIFGlsYDEYRYTSVIKACQLEEDIAL---FPEKDKTVLGE 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 496 RGIQLSGGQKQRISISRAIVKNPSILLLDEATSALDAESEK-IVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVGGGK 574
Cdd:TIGR01271 545 GGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKeIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGV 624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 575 IIESGSHDELIS-NPDgaYSSLLRIQEAASpNLNHTPSLPVSTKPL------PELPITETTSSIHQSVNQPDTTKQAKVT 647
Cdd:TIGR01271 625 CYFYGTFSELQAkRPD--FSSLLLGLEAFD-NFSAERRNSILTETLrrvsidGDSTVFSGPETIKQSFKQPPPEFAEKRK 701
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 648 VGRLYSMIRPDWKYGLCGTLGSFIAGSQMPLFALGIAQALVSYYMDWETTQNEVKRISIlFCCG---------SVITVIV 718
Cdd:TIGR01271 702 QSIILNPIASARKFSFVQMGPQKAQATTIEDAVREPSERKFSLVPEDEQGEESLPRGNQ-YHHGlqhqaqrrqSVLQLMT 780
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 719 HTieHTTFGIMgERLTLRVRqKMFSAILRNEIGwfDKVDntssMLASRLESDA--------------------------- 771
Cdd:TIGR01271 781 HS--NRGENRR-EQLQTSFR-KKSSITQQNELA--SELD----IYSRRLSKDSvyeiseeineedlkecfaderenvfet 850
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 772 ----TLLRTIVVDRSTILLENLGLVVTAFII--SFILNWRLT----------------LVVLATYPLIISGH-------- 821
Cdd:TIGR01271 851 ttwnTYLRYITTNRNLVFVLIFCLVIFLAEVaaSLLGLWLITdnpsapnyvdqqhanaSSPDVQKPVIITPTsayyifyi 930
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 822 ---ISEKIFMQGYGGNL---------SK--------AYLKANMLAGESISNIRTVVAFCAEEKVLD-------------- 867
Cdd:TIGR01271 931 yvgTADSVLALGFFRGLplvhtlltvSKrlheqmlhSVLQAPMAVLNTMKAGRILNRFTKDMAIIDdmlpltlfdfiqlt 1010
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 868 ------LYSKELLEPSE--------------RSF--RRGQMAGILYGVSQFFIFSSYGLA---LW---------YGSILM 913
Cdd:TIGR01271 1011 livlgaIFVVSVLQPYIfiaaipvavifimlRAYflRTSQQLKQLESEARSPIFSHLITSlkgLWtirafgrqsYFETLF 1090
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 914 EKGLSS-------FESVMKTFM-------VLIVTALV-------------MGEVLALAPDLLKGNQMVVS---------- 956
Cdd:TIGR01271 1091 HKALNLhtanwflYLSTLRWFQmridiifVFFFIAVTfiaigtnqdgegeVGIILTLAMNILSTLQWAVNssidvdglmr 1170
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 957 ----VFELLDRRTQVVGDTGEELSNVEGT---IELKGVHFSYPSRPDVT--------------IFSDFNLLVPSGKSMAL 1015
Cdd:TIGR01271 1171 svsrVFKFIDLPQEEPRPSGGGGKYQLSTvlvIENPHAQKCWPSGGQMDvqgltakyteagraVLQDLSFSVEGGQRVGL 1250
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1016 VGQSGSGKSSVLSLVLRFYDpTAGIIMIDGQDIKKLKLKSLRRHIGLVQQEPALFATTIYENiLYGKEGASESEVMEAAK 1095
Cdd:TIGR01271 1251 LGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKN-LDPYEQWSDEEIWKVAE 1328
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1096 LANAHSFISSLPEGYSTKVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVVV 1175
Cdd:TIGR01271 1329 EVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILS 1408
|
1050 1060
....*....|....*....|.
gi 15220188 1176 AHRLSTIKNSDMISVIQDGKI 1196
Cdd:TIGR01271 1409 EHRVEALLECQQFLVIEGSSV 1429
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
361-575 |
2.62e-35 |
|
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: 134.15 E-value: 2.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSRPD-VVIFDKLNFVIPAGKVVALVGGSGSGKST---MISLIERfyePTDGAVMLDGNDIRYLDLKWL- 435
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVRVDGTDISKLSEKELa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 436 ---RGHIGLVNQEPVLFAT-TIRENIMY-----GKDDATSEEitNAAKLSEAIsfinNLPEGFETQVGergiQLSGGQKQ 506
Cdd:cd03255 78 afrRRHIGFVFQSFNLLPDlTALENVELplllaGVPKKERRE--RAEELLERV----GLGDRLNHYPS----ELSGGQQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15220188 507 RISISRAIVKNPSILLLDEATSALDAESEKIVQEALDRV--MVGRTTVVVAHRLSTVRNADIIAVVGGGKI 575
Cdd:cd03255 148 RVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
359-602 |
4.10e-35 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 146.42 E-value: 4.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 359 GDILFKDVTFTYpsRPDVV-IFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRG 437
Cdd:PLN03130 1236 GSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRK 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 438 HIGLVNQEPVLFATTIRENImygkdDATSEEitNAAKLSEAIS------FINNLPEGFETQVGERGIQLSGGQKQRISIS 511
Cdd:PLN03130 1314 VLGIIPQAPVLFSGTVRFNL-----DPFNEH--NDADLWESLErahlkdVIRRNSLGLDAEVSEAGENFSVGQRQLLSLA 1386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 512 RAIVKNPSILLLDEATSALDAESEKIVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVGGGKIIESGSHDELISNPDGA 591
Cdd:PLN03130 1387 RALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSA 1466
|
250
....*....|.
gi 15220188 592 YSSLLRIQEAA 602
Cdd:PLN03130 1467 FSKMVQSTGAA 1477
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
982-1201 |
4.36e-35 |
|
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: 141.58 E-value: 4.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRpDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTA---GIIMIDGQDIKKLKLKSLRR 1058
Cdd:COG1123 5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1059 HIGLVQQEP--ALFATTIYENILYGKE--GASESEVMEAAKLANAHSFISSLPEGYSTkvgergiQMSGGQRQRIAIARA 1134
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEALEnlGLSRAEARARVLELLEAVGLERRLDRYPH-------QLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1135 VLKNPEILLLDEATSALDVESERVVQQALDRLMRDR--TTVVVAHRLSTIKN-SDMISVIQDGKIIEQGS 1201
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEiADRVVVMDDGRIVEDGP 226
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1002-1213 |
5.94e-35 |
|
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: 134.69 E-value: 5.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1002 DFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKL---KLKSLRRH-IGLVQQEPALFA-TTIYE 1076
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMsrkELRELRRKkISMVFQSFALLPhRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1077 NILYGKE--GASESE----VMEAAKLANAHSFISSLPEgystkvgergiQMSGGQRQRIAIARAVLKNPEILLLDEATSA 1150
Cdd:cd03294 122 NVAFGLEvqGVPRAEreerAAEALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSA 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15220188 1151 LDVESERVVQQALDRLMRD--RTTVVVAHRLS-TIKNSDMISVIQDGKIIEQGSHNILVENKNGPY 1213
Cdd:cd03294 191 LDPLIRREMQDELLRLQAElqKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTNPANDY 256
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
361-584 |
7.50e-35 |
|
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: 133.83 E-value: 7.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSrpdVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRgHIG 440
Cdd:COG4555 2 IEVENLSKKYGK---VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARR-QIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 441 LVNQEPVLFAT-TIRENIMY------GKDDATSEEITNAAKLseaisfiNNLPEGFETQVGErgiqLSGGQKQRISISRA 513
Cdd:COG4555 78 VLPDERGLYDRlTVRENIRYfaelygLFDEELKKRIEELIEL-------LGLEEFLDRRVGE----LSTGMKKKVALARA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15220188 514 IVKNPSILLLDEATSALDAESEKIVQEALDRVM-VGRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESGSHDEL 584
Cdd:COG4555 147 LVHDPKVLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
359-597 |
9.56e-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: 133.88 E-value: 9.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 359 GDILFKDVTFTYPSRPDVVIfDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGH 438
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVL-KHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 439 IGLVNQEPVLFATTIRENIMYGKDdATSEEITNAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRISISRAIVKNP 518
Cdd:cd03288 97 LSIILQDPILFSGSIRFNLDPECK-CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKS 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15220188 519 SILLLDEATSALDAESEKIVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVGGGKIIESGSHDELISNPDGAYSSLLR 597
Cdd:cd03288 176 SILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLVR 254
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
364-604 |
1.23e-34 |
|
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: 133.39 E-value: 1.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 364 KDVTFTYPSRP-DVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHIGLV 442
Cdd:COG1124 5 RNLSVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 443 NQEPvlFAT-----TIRENIM-----YGKDDATSEeitnAAKLSEAIsfinNLPEGFETQvgeRGIQLSGGQKQRISISR 512
Cdd:COG1124 85 FQDP--YASlhprhTVDRILAeplriHGLPDREER----IAELLEQV----GLPPSFLDR---YPHQLSGGQRQRVAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 513 AIVKNPSILLLDEATSALDAesekIVQ-EALD-----RVMVGRTTVVVAHRLSTV-RNADIIAVVGGGKIIESGSHDELI 585
Cdd:COG1124 152 ALILEPELLLLDEPTSALDV----SVQaEILNllkdlREERGLTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTVADLL 227
|
250
....*....|....*....
gi 15220188 586 SNPDGAYSSLLRiqeAASP 604
Cdd:COG1124 228 AGPKHPYTRELL---AASL 243
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1007-1218 |
1.57e-34 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 135.24 E-value: 1.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1007 VPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLK---LKSLRRHIGLVQQEPalFAT-----TIYEnI 1078
Cdd:COG4608 41 IRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP--YASlnprmTVGD-I 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1079 LygkegaseSEVMEAAKLANAHS---FISSLPEgystKVGERGIQM-------SGGQRQRIAIARAVLKNPEILLLDEAT 1148
Cdd:COG4608 118 I--------AEPLRIHGLASKAErreRVAELLE----LVGLRPEHAdryphefSGGQRQRIGIARALALNPKLIVCDEPV 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15220188 1149 SALDVeServVQ-QALDRLM--RDR---TTVVVAHRLSTIKN-SDMISVIQDGKIIEQGSHNILVENKNGPYSK-LIS 1218
Cdd:COG4608 186 SALDV-S---IQaQVLNLLEdlQDElglTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYARPLHPYTQaLLS 259
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
361-556 |
2.93e-34 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 132.52 E-value: 2.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSRP-DVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDlkwlrGHI 439
Cdd:COG1116 8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG-----PDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 440 GLVNQEPVLFA-TTIRENIMYG-----KDDATSEEITNAA----KLSEaisFINNLPEgfetqvgergiQLSGGQKQRIS 509
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGlelrgVPKAERRERARELlelvGLAG---FEDAYPH-----------QLSGGMRQRVA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15220188 510 ISRAIVKNPSILLLDEATSALDA--------ESEKIVQEAldrvmvGRTTVVVAH 556
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDAltrerlqdELLRLWQET------GKTVLFVTH 197
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
982-1218 |
2.99e-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: 134.41 E-value: 2.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRP-DVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDP---TAGIIMIDGQDIKKLKLKSLR 1057
Cdd:COG0444 2 LEVRNLKVYFPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1058 ----RHIGLVQQEP--AL---------FATTIYENILYGKEGASE--SEVMEAAKLANAHSFISSLPEgystkvgergiQ 1120
Cdd:COG0444 82 kirgREIQMIFQDPmtSLnpvmtvgdqIAEPLRIHGGLSKAEAREraIELLERVGLPDPERRLDRYPH-----------E 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1121 MSGGQRQRIAIARAVLKNPEILLLDEATSALDVeserVVQ-QALDrLMRD-----RTTVV-VAHRLSTIKN-SDMISVIQ 1192
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQaQILN-LLKDlqrelGLAILfITHDLGVVAEiADRVAVMY 225
|
250 260
....*....|....*....|....*..
gi 15220188 1193 DGKIIEQGSHNILVENKNGPYSK-LIS 1218
Cdd:COG0444 226 AGRIVEEGPVEELFENPRHPYTRaLLS 252
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
701-929 |
3.28e-34 |
|
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: 133.45 E-value: 3.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 701 VKRISILFCCGSVITVIVHTIEHTTFGIMGERLTLRVRQKMFSAILRNEIGWFDKvdNTSSMLASRLESDATLLRTIVVD 780
Cdd:cd18557 35 LNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDK--HKTGELTSRLSSDTSVLQSAVTD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 781 RSTILLENLGLVVTAFIISFILNWRLTLVVLATYPLIISGHISEKIFMQGYGGNLSKAYLKANMLAGESISNIRTVVAFC 860
Cdd:cd18557 113 NLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFS 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15220188 861 AEEKVLDLYSKELLEPSERSFRRGQMAGILYGVSQFFIFSSYGLALWYGSILMEKG------LSSFesVMKTFMV 929
Cdd:cd18557 193 AEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGqltvgeLTSF--ILYTIMV 265
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
1015-1214 |
6.16e-34 |
|
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: 133.77 E-value: 6.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1015 LVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIkkLKLKSLRRHIGLVQQEPALFA-TTIYENILYG----KEGASE-- 1087
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV--TNVPPHLRHINMVFQSYALFPhMTVEENVAFGlkmrKVPRAEik 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1088 SEVMEAAKLANAHSFISSLPegystkvgergIQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLM 1167
Cdd:TIGR01187 79 PRVLEALRLVQLEEFADRKP-----------HQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15220188 1168 RDR--TTVVVAHRLS-TIKNSDMISVIQDGKIIEQGSHNILVENKNGPYS 1214
Cdd:TIGR01187 148 EQLgiTFVFVTHDQEeAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFV 197
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
982-1201 |
6.76e-34 |
|
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: 130.43 E-value: 6.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPsrpDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIkkLKLKSLRRHIG 1061
Cdd:cd03300 1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEPALFA-TTIYENILYG------KEGASESEVMEAAKLANAHSFISSLPEgystkvgergiQMSGGQRQRIAIARA 1134
Cdd:cd03300 76 TVFQNYALFPhLTVFENIAFGlrlkklPKAEIKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1135 VLKNPEILLLDEATSALDVESERVVQQALDRLMRDR--TTVVVAHRLS-TIKNSDMISVIQDGKIIEQGS 1201
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELgiTFVFVTHDQEeALTMSDRIAVMNKGKIQQIGT 214
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
364-588 |
7.89e-34 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 131.31 E-value: 7.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 364 KDVTFTYPSRPdvVIFDkLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGA-----VMLDGNDI--RYLDLKWLR 436
Cdd:COG1117 15 RNLNVYYGDKQ--ALKD-INLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGArvegeILLDGEDIydPDVDVVELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 437 GHIGLVNQEPVLFATTIRENIMYG------KDDATSEEITNAAkLSEAisfinNLPEgfetQVGER----GIQLSGGQKQ 506
Cdd:COG1117 92 RRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIVEES-LRKA-----ALWD----EVKDRlkksALGLSGGQQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 507 RISISRAIVKNPSILLLDEATSALD-AESEKIvqEALDRVMVGRTTVV-VAHRLS-TVRNADIIAVVGGGKIIESGSHDE 583
Cdd:COG1117 162 RLCIARALAVEPEVLLMDEPTSALDpISTAKI--EELILELKKDYTIViVTHNMQqAARVSDYTAFFYLGELVEFGPTEQ 239
|
....*
gi 15220188 584 LISNP 588
Cdd:COG1117 240 IFTNP 244
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
982-1196 |
8.93e-34 |
|
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: 129.45 E-value: 8.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPsrPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKS---LRR 1058
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1059 HIGLVQQEPALFAT-TIYENILYGKE--GASESE----VMEAAKLANAHSFISSLPEgystkvgergiQMSGGQRQRIAI 1131
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFALEvtGVPPREirkrVPAALELVGLSHKHRALPA-----------ELSGGEQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15220188 1132 ARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVVVAHRLSTIKN--SDMISVIQDGKI 1196
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDttRHRVIALERGKL 214
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
982-1208 |
9.29e-34 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 130.93 E-value: 9.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRPdvtIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYD--PTA---GIIMIDGQDI--KKLKLK 1054
Cdd:COG1117 12 IEVRNLNVYYGDKQ---ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGArveGEILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1055 SLRRHIGLVQQEPALFATTIYENILYG---KEGASESEVMEAAKlanahsfiSSLpegysTKVG----------ERGIQM 1121
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNVAYGlrlHGIKSKSELDEIVE--------ESL-----RKAAlwdevkdrlkKSALGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1122 SGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVVVAH------RLstiknSDMISVIQDGK 1195
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHnmqqaaRV-----SDYTAFFYLGE 230
|
250
....*....|...
gi 15220188 1196 IIEQGSHNILVEN 1208
Cdd:COG1117 231 LVEFGPTEQIFTN 243
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
364-588 |
2.00e-33 |
|
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: 132.10 E-value: 2.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 364 KDVTFTYPSRPDVV-IFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEP---TDGAVMLDGNDIRYLD---LKWLR 436
Cdd:COG0444 5 RNLKVYFPTRRGVVkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSekeLRKIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 437 G-HIGLVNQE------PVL-----FATTIRENIMYGKDDAT--SEEITNAAKLSEAISFINNLPEgfetqvgergiQLSG 502
Cdd:COG0444 85 GrEIQMIFQDpmtslnPVMtvgdqIAEPLRIHGGLSKAEARerAIELLERVGLPDPERRLDRYPH-----------ELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 503 GQKQRISISRAIVKNPSILLLDEATSALDAESEKIV-------QEALDrvmvgrTTVV-VAHRLSTVRN-ADIIAVVGGG 573
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDVTIQAQIlnllkdlQRELG------LAILfITHDLGVVAEiADRVAVMYAG 227
|
250
....*....|....*
gi 15220188 574 KIIESGSHDELISNP 588
Cdd:COG0444 228 RIVEEGPVEELFENP 242
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
981-1201 |
2.38e-33 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 132.58 E-value: 2.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 981 TIELKGVHFSYPSRpdvTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKkLKLKSLRRHI 1060
Cdd:COG1118 2 SIEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF-TNLPPRERRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1061 GLVQQEPALFA-TTIYENILYG--KEGASESE----VMEAAKLANAHSFISSLPEgystkvgergiQMSGGQRQRIAIAR 1133
Cdd:COG1118 78 GFVFQHYALFPhMTVAENIAFGlrVRPPSKAEirarVEELLELVQLEGLADRYPS-----------QLSGGQRQRVALAR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15220188 1134 AVLKNPEILLLDEATSALDV----ESERVVQQALDRLmrDRTTVVVAH------RLstiknSDMISVIQDGKIIEQGS 1201
Cdd:COG1118 147 ALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHDEL--GGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGT 217
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
361-579 |
2.76e-33 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 128.63 E-value: 2.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPsrPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYL---DLKWLRG 437
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 438 HIGLVNQE-PVLFATTIRENIMY-----GKDDAtseEItnAAKLSEAIS------FINNLPegfetqvgergIQLSGGQK 505
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtGKSRK---EI--RRRVREVLDlvglsdKAKALP-----------HELSGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15220188 506 QRISISRAIVKNPSILLLDEATSALDAE-SEKIVqEALDRV-MVGrTTVVVA-HRLSTVRNAD--IIAVVgGGKIIESG 579
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLDPEtSWEIM-ELLEEInRRG-TTVLIAtHDLELVDRMPkrVLELE-DGRLVRDE 219
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
61-335 |
3.24e-33 |
|
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: 130.71 E-value: 3.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 61 FFGKLINIIGLAylfpqEASHKVAKYSLDFVYLSVVILF-----SSWLEVACWMHTGERQAAKIRKAYLRSMLSQDISLF 135
Cdd:cd18573 18 AIGKLIDVASKE-----SGDIEIFGLSLKTFALALLGVFvvgaaANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 136 DTeISTGEVISAITSEILVVQDAISEKVGNFMHFISRFIAGFAIGFASVWQISLVTLSIVPFIALAGGIYAFVSSGLIVR 215
Cdd:cd18573 93 DK-NKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 216 VRKSYVKANEIAEEVIGNVRTVQAFTGEEKAVSSYQGALRNTYNYGRKAGLAKGLGLGSLHFVLFLSWALLIWFTSIVVH 295
Cdd:cd18573 172 VQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVA 251
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 15220188 296 KGIANGGESFTTMLNVVIAGLSLGQAAPDISTFMRASAAA 335
Cdd:cd18573 252 SGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGAS 291
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
361-555 |
3.41e-33 |
|
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: 127.91 E-value: 3.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPsrPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLD---LKWLRG 437
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 438 HIGLVNQEPVLFAT-TIRENIMYGKD--DATSEEItnAAKLSEAISFInnlpeGFETQVGERGIQLSGGQKQRISISRAI 514
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFALEvtGVPPREI--RKRVPAALELV-----GLSHKHRALPAELSGGEQQRVAIARAI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15220188 515 VKNPSILLLDEATSALDAESEKIVQEALDRVMVGRTTVVVA 555
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
364-579 |
4.46e-33 |
|
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: 126.40 E-value: 4.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 364 KDVTFTYPSRpdvVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHIGLVN 443
Cdd:cd03214 3 ENLSVGYGGR---TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 444 QepVLfattirenimygkddatseEITNAAKLSeaisfinnlpegfetqvgERGI-QLSGGQKQRISISRAIVKNPSILL 522
Cdd:cd03214 80 Q--AL-------------------ELLGLAHLA------------------DRPFnELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15220188 523 LDEATSALDAES-----EKIVQEALDRvmvGRTTVVVAHRLS-TVRNADIIAVVGGGKIIESG 579
Cdd:cd03214 121 LDEPTSHLDIAHqiellELLRRLARER---GKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
361-584 |
7.40e-33 |
|
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: 127.68 E-value: 7.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSrpDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYL---DLKWLRG 437
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgkALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 438 HIGLVNQEPVLFA-TTIRENIMYGKDDATS-----------EEITNAAKLSEAIsfinnlpeGFETQVGERGIQLSGGQK 505
Cdd:cd03256 79 QIGMIFQQFNLIErLSVLENVLSGRLGRRStwrslfglfpkEEKQRALAALERV--------GLLDKAYQRADQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 506 QRISISRAIVKNPSILLLDEATSALDAESEKIVQEALDRV--MVGRTTVVVAHRLSTVR-NADIIAVVGGGKIIESGSHD 582
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGPPA 230
|
..
gi 15220188 583 EL 584
Cdd:cd03256 231 EL 232
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
982-1201 |
1.60e-32 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 129.92 E-value: 1.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYP-SRPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLK---LKSLR 1057
Cdd:PRK11153 2 IELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekeLRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1058 RHIGLVQQEPALFAT-TIYENILYGKEGASES---------EVMEAAKLANAHSFISSlpegystkvgergiQMSGGQRQ 1127
Cdd:PRK11153 82 RQIGMIFQHFNLLSSrTVFDNVALPLELAGTPkaeikarvtELLELVGLSDKADRYPA--------------QLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15220188 1128 RIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDR--TTVVVAHRLSTIKN-SDMISVIQDGKIIEQGS 1201
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELglTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
982-1196 |
1.69e-32 |
|
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: 125.72 E-value: 1.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRpdvTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDI--KKLKLKSLRRH 1059
Cdd:cd03262 1 IEIKNLHKSFGDF---HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1060 IGLVQQEPALFA-TTIYENILYGK---EGASESEVMEAAklanahsfisslpEGYSTKVG------ERGIQMSGGQRQRI 1129
Cdd:cd03262 78 VGMVFQQFNLFPhLTVLENITLAPikvKGMSKAEAEERA-------------LELLEKVGladkadAYPAQLSGGQQQRV 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15220188 1130 AIARAVLKNPEILLLDEATSALDVEserVVQQALDrLMRD-----RTTVVVAHRLSTIKN-SDMISVIQDGKI 1196
Cdd:cd03262 145 AIARALAMNPKVMLFDEPTSALDPE---LVGEVLD-VMKDlaeegMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
375-588 |
2.48e-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: 126.20 E-value: 2.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 375 DVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIryLDLKWLRGHIGLVNQEPVLFA-TTI 453
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTVFQNYALFPhLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 454 RENIMYGKDDATSEEITNAAKLSEAISFINnlPEGFEtqvgERGI-QLSGGQKQRISISRAIVKNPSILLLDEATSALDA 532
Cdd:cd03300 90 FENIAFGLRLKKLPKAEIKERVAEALDLVQ--LEGYA----NRKPsQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15220188 533 ESEKIVQEALDRV--MVGRTTVVVAHRLS---TVrnADIIAVVGGGKIIESGSHDELISNP 588
Cdd:cd03300 164 KLRKDMQLELKRLqkELGITFVFVTHDQEealTM--SDRIAVMNKGKIQQIGTPEEIYEEP 222
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
378-575 |
2.84e-32 |
|
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: 125.33 E-value: 2.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 378 IFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDI--RYLDLKWLRGHIGLVNQEPVLFA-TTIR 454
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVFQQFNLFPhLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 455 ENIMY------GKDDATSEEItnAAKLSEAIsfinnlpeGFETQVGERGIQLSGGQKQRISISRAIVKNPSILLLDEATS 528
Cdd:cd03262 95 ENITLapikvkGMSKAEAEER--ALELLEKV--------GLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTS 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15220188 529 ALDAEsekIVQEALDrVMV-----GRTTVVVAHRLSTVRN-ADIIAVVGGGKI 575
Cdd:cd03262 165 ALDPE---LVGEVLD-VMKdlaeeGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
361-589 |
4.21e-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: 126.39 E-value: 4.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSRPDVVIfDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKW-LRGHI 439
Cdd:TIGR04520 1 IEVENVSFSYPESEKPAL-KNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWeIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 440 GLVNQEP--VLFATTIRENIMYGKDDA--TSEEI----TNAAKLSEAISFINNLPEgfetqvgergiQLSGGQKQRISIS 511
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLENLgvPREEMrkrvDEALKLVGMEDFRDREPH-----------LLSGGQKQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 512 RAIVKNPSILLLDEATSALDAESEKIVQEALDRVM--VGRTTVVVAHRLSTVRNADIIAVVGGGKIIESGSHDELISNPD 589
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQVE 228
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
981-1213 |
6.68e-32 |
|
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: 125.14 E-value: 6.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 981 TIELKGVHFSYPSRPDVtifSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKslRRHI 1060
Cdd:cd03296 2 SIEVRNVSKRFGDFVAL---DDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1061 GLVQQEPALFA-TTIYENILYG------KEGASESE----VMEAAKLANAHSFISSLPEgystkvgergiQMSGGQRQRI 1129
Cdd:cd03296 77 GFVFQHYALFRhMTVFDNVAFGlrvkprSERPPEAEirakVHELLKLVQLDWLADRYPA-----------QLSGGQRQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1130 AIARAVLKNPEILLLDEATSALDVESERVVQQALDRLmRDR---TTVVVAHRLS-TIKNSDMISVIQDGKIIEQGSHNIL 1205
Cdd:cd03296 146 ALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRL-HDElhvTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
....*...
gi 15220188 1206 VENKNGPY 1213
Cdd:cd03296 225 YDHPASPF 232
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
361-587 |
2.01e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 124.72 E-value: 2.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSRPDVVIfDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHIG 440
Cdd:PRK13632 8 IKVENVSFSYPNSENNAL-KNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 441 LVNQEP--VLFATTIRENIMYG------KDDATSEEITNAAKLSEAISFINNLPEgfetqvgergiQLSGGQKQRISISR 512
Cdd:PRK13632 87 IIFQNPdnQFIGATVEDDIAFGlenkkvPPKKMKDIIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15220188 513 AIVKNPSILLLDEATSALDAESEKIVQEALD--RVMVGRTTVVVAHRLSTVRNADIIAVVGGGKIIESGSHDELISN 587
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVdlRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
364-575 |
2.22e-31 |
|
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: 121.35 E-value: 2.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 364 KDVTFTYPSRPdvvIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRyLDLKWLRGHIGLVN 443
Cdd:cd03230 4 RNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK-KEPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 444 QEPVLFAT-TIRENIMYgkddatseeitnaaklseaisfinnlpegfetqvgergiqlSGGQKQRISISRAIVKNPSILL 522
Cdd:cd03230 80 EEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15220188 523 LDEATSALDAESEKIVQEALDRVMVGRTTVVVA-HRLSTVRN-ADIIAVVGGGKI 575
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEGKTILLSsHILEEAERlCDRVAILNNGRI 173
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
980-1201 |
2.30e-31 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 126.73 E-value: 2.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 980 GTIELKGVHFSYPsrpDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKslRRH 1059
Cdd:COG3839 2 ASLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1060 IGLVQQEPALF-ATTIYENILYG----KEGASE--SEVMEAAKLANAHSFISSLPEgystkvgergiQMSGGQRQRIAIA 1132
Cdd:COG3839 77 IAMVFQSYALYpHMTVYENIAFPlklrKVPKAEidRRVREAAELLGLEDLLDRKPK-----------QLSGGQRQRVALG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15220188 1133 RAVLKNPEILLLDEATSALDVESeRVvqQA---LDRLMRDR--TTVVVAHRLS---TIknSDMISVIQDGKIIEQGS 1201
Cdd:COG3839 146 RALVREPKVFLLDEPLSNLDAKL-RV--EMraeIKRLHRRLgtTTIYVTHDQVeamTL--ADRIAVMNDGRIQQVGT 217
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
363-575 |
2.33e-31 |
|
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: 122.64 E-value: 2.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 363 FKDVTFTYPSRPdvvIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLdlkwlRGHIGLV 442
Cdd:cd03235 2 VEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 443 NQEPVL---FATTIRENIM------------YGKDDAtsEEITNAAKLSEAISFINNlpegfetQVGErgiqLSGGQKQR 507
Cdd:cd03235 74 PQRRSIdrdFPISVRDVVLmglyghkglfrrLSKADK--AKVDEALERVGLSELADR-------QIGE----LSGGQQQR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 508 ISISRAIVKNPSILLLDEATSALDAESEKIVQEALDRV-MVGRTTVVVAHRLSTV-RNADIIAVVGGGKI 575
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVlEYFDRVLLLNRTVV 210
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
982-1194 |
2.43e-31 |
|
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: 122.82 E-value: 2.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPsrPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSL----R 1057
Cdd:cd03290 1 VQVTNGYFSWG--SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1058 RHIGLVQQEPALFATTIYENILYGKEGASE--SEVMEAAKLanaHSFISSLPEGYSTKVGERGIQMSGGQRQRIAIARAV 1135
Cdd:cd03290 79 YSVAYAAQKPWLLNATVEENITFGSPFNKQryKAVTDACSL---QPDIDLLPFGDQTEIGERGINLSGGQRQRICVARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220188 1136 LKNPEILLLDEATSALDVE-SERVVQQALDRLMRD--RTTVVVAHRLSTIKNSDMISVIQDG 1194
Cdd:cd03290 156 YQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
982-1200 |
3.50e-31 |
|
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: 121.98 E-value: 3.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPsrpDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKslRRHIG 1061
Cdd:cd03301 1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEPALFA-TTIYENILYG------KEGASESEVMEAAKLANAHSFISSLPEgystkvgergiQMSGGQRQRIAIARA 1134
Cdd:cd03301 76 MVFQNYALYPhMTVYDNIAFGlklrkvPKDEIDERVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15220188 1135 VLKNPEILLLDEATSALDVESERVVQQALDRLMR--DRTTVVVAH-RLSTIKNSDMISVIQDGKIIEQG 1200
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
982-1182 |
4.05e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 122.89 E-value: 4.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRPdvtIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLklkslRRHIG 1061
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEPAL---FATTIYENI---LYGKEG-------ASESEVMEAAKLANAHSFISslpegysTKVGErgiqMSGGQRQR 1128
Cdd:COG1121 79 YVPQRAEVdwdFPITVRDVVlmgRYGRRGlfrrpsrADREAVDEALERVGLEDLAD-------RPIGE----LSGGQQQR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15220188 1129 IAIARAVLKNPEILLLDEATSALDVESERVVQQALDRL-MRDRTTVVVAHRLSTI 1182
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAV 202
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1000-1200 |
4.49e-31 |
|
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: 121.63 E-value: 4.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1000 FSDFNL---LVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDI----KKLKLKSLRRHIGLVQQEPALFA- 1071
Cdd:cd03297 10 LPDFTLkidFDLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrKKINLPPQQRKIGLVFQQYALFPh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1072 TTIYENILYGKEGASESE--VMEAAKLANAHsfISSLPEGYSTkvgergiQMSGGQRQRIAIARAVLKNPEILLLDEATS 1149
Cdd:cd03297 90 LNVRENLAFGLKRKRNREdrISVDELLDLLG--LDHLLNRYPA-------QLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15220188 1150 ALDVESERVVQQALDRLMRD--RTTVVVAHRLSTI-KNSDMISVIQDGKIIEQG 1200
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKNlnIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
361-588 |
4.79e-31 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 122.51 E-value: 4.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPsrpDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIR--YLDLKWLRGH 438
Cdd:PRK09493 2 IEFKNVSKHFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 439 IGLVNQEPVLFA-TTIRENIMYG--------KDDATSEEITNAAKLseaisfinnlpeGFETQVGERGIQLSGGQKQRIS 509
Cdd:PRK09493 79 AGMVFQQFYLFPhLTALENVMFGplrvrgasKEEAEKQARELLAKV------------GLAERAHHYPSELSGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 510 ISRAIVKNPSILLLDEATSALDAEsekIVQEALdRVMV-----GRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESGSHDE 583
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSALDPE---LRHEVL-KVMQdlaeeGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQV 222
|
....*
gi 15220188 584 LISNP 588
Cdd:PRK09493 223 LIKNP 227
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
361-588 |
5.49e-31 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 125.30 E-value: 5.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYP-SRPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLD---LKWLR 436
Cdd:PRK11153 2 IELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekeLRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 437 GHIGLVNQEPVLFAT-TIRENImygkddATSEEITNAAKlsEAIsfinnlpegfETQVGER----GI---------QLSG 502
Cdd:PRK11153 82 RQIGMIFQHFNLLSSrTVFDNV------ALPLELAGTPK--AEI----------KARVTELlelvGLsdkadrypaQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 503 GQKQRISISRAIVKNPSILLLDEATSALDAESEKIVQEALDRV--MVGRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESG 579
Cdd:PRK11153 144 GQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDInrELGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQG 223
|
....*....
gi 15220188 580 SHDELISNP 588
Cdd:PRK11153 224 TVSEVFSHP 232
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
361-588 |
5.68e-31 |
|
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: 122.45 E-value: 5.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSRPDVvifDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKwlRGHIG 440
Cdd:cd03296 3 IEVRNVSKRFGDFVAL---DDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 441 LVNQEPVLFA-TTIRENIMYGKDDATSEEITNAAKLSEAISFINNLP--EGFETQVGErgiQLSGGQKQRISISRAIVKN 517
Cdd:cd03296 78 FVFQHYALFRhMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLVqlDWLADRYPA---QLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220188 518 PSILLLDEATSALDAESEKIVQEALDRVM--VGRTTVVVAHRLS-TVRNADIIAVVGGGKIIESGSHDELISNP 588
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRRWLRRLHdeLHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEVYDHP 228
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1001-1200 |
1.18e-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: 1.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1001 SDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKslRRHIGLVQQEPALFA-TTIYENIL 1079
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPhMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1080 YG------KEGASESEVMEAAKLANAHSFISSLPEgystkvgergiQMSGGQRQRIAIARAVLKNPEILLLDEATSALDV 1153
Cdd:cd03299 94 YGlkkrkvDKKEIERKVLEIAEMLGIDHLLNRKPE-----------TLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15220188 1154 ESERVVQQALDRLMRDRTTVV--VAHRLSTIKN-SDMISVIQDGKIIEQG 1200
Cdd:cd03299 163 RTKEKLREELKKIRKEFGVTVlhVTHDFEEAWAlADKVAIMLNGKLIQVG 212
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
982-1200 |
1.52e-30 |
|
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: 119.99 E-value: 1.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRpdvTIFSDFNLLVPSGKSmALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKsLRRHIG 1061
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEPALFAT-TIYE-----NILYGKEGA-SESEVMEAAKLANahsfissLPEGYSTKVGergiQMSGGQRQRIAIARA 1134
Cdd:cd03264 76 YLPQEFGVYPNfTVREfldyiAWLKGIPSKeVKARVDEVLELVN-------LGDRAKKKIG----SLSGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15220188 1135 VLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVVVAHRLSTIKNS-DMISVIQDGKIIEQG 1200
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
982-1198 |
2.81e-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: 120.23 E-value: 2.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRP-DVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKL----KLKSL 1056
Cdd:COG4181 9 IELRGLTKTVGTGAgELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALdedaRARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1057 RRHIGLVQQEPALFAT-TIYENILYGKEGASESEVMEAAK--LAnahsfisslpegystKVG--ERG----IQMSGGQRQ 1127
Cdd:COG4181 89 ARHVGFVFQSFQLLPTlTALENVMLPLELAGRRDARARARalLE---------------RVGlgHRLdhypAQLSGGEQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15220188 1128 RIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDR-TT-VVVAHRLSTIKNSDMISVIQDGKIIE 1198
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgTTlVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
380-588 |
2.99e-30 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 122.92 E-value: 2.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 380 DKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYL---DLKWLRGHIGLVNQEPvlFA------ 450
Cdd:COG4608 35 DGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLsgrELRPLRRRMQMVFQDP--YAslnprm 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 451 ---TTIRENIMYGKDDATSEEITNAAKLSEAI----SFINNLPEgfetqvgergiQLSGGQKQRISISRAIVKNPSILLL 523
Cdd:COG4608 113 tvgDIIAEPLRIHGLASKAERRERVAELLELVglrpEHADRYPH-----------EFSGGQRQRIGIARALALNPKLIVC 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15220188 524 DEATSALD----AEsekIV------QEALdrvmvGRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESGSHDELISNP 588
Cdd:COG4608 182 DEPVSALDvsiqAQ---VLnlledlQDEL-----GLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYARP 249
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
361-586 |
4.81e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 119.81 E-value: 4.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSRPdvvIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLdlkwlRGHIG 440
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 441 LVNQEPVL---FATTIRENIM------------YGKDDAtsEEITNAAKLSEAISFINnlpegfeTQVGErgiqLSGGQK 505
Cdd:COG1121 79 YVPQRAEVdwdFPITVRDVVLmgrygrrglfrrPSRADR--EAVDEALERVGLEDLAD-------RPIGE----LSGGQQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 506 QRISISRAIVKNPSILLLDEATSALDAESEKIVQEALDR-VMVGRTTVVVAHRLSTVR-NADIIAVVGGGkIIESGSHDE 583
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVReYFDRVLLLNRG-LVAHGPPEE 224
|
...
gi 15220188 584 LIS 586
Cdd:COG1121 225 VLT 227
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
361-598 |
5.73e-30 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 119.09 E-value: 5.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSRPdvVIFDklnFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDlkwlrghig 440
Cdd:COG3840 2 LRLDDLTYRYGDFP--LRFD---LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 441 lVNQEPV--------LFA-TTIRENIMYGKDDA---TSEEItnaAKLSEAI------SFINNLPEgfetqvgergiQLSG 502
Cdd:COG3840 68 -PAERPVsmlfqennLFPhLTVAQNIGLGLRPGlklTAEQR---AQVEQALervglaGLLDRLPG-----------QLSG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 503 GQKQRISISRAIVKNPSILLLDEATSALD----AESEKIVQEALDRvmVGRTTVVVAHRLSTVRN-ADIIAVVGGGKIIE 577
Cdd:COG3840 133 GQRQRVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRE--RGLTVLMVTHDPEDAARiADRVLLVADGRIAA 210
|
250 260
....*....|....*....|..
gi 15220188 578 SGSHDELIS-NPDGAYSSLLRI 598
Cdd:COG3840 211 DGPTAALLDgEPPPALAAYLGI 232
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
361-588 |
6.86e-30 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 122.18 E-value: 6.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSRPdvvIFDKLNFVIPAGKVVALVGGSGSGKSTMISLI---ERfyePTDGAVMLDGNDIrYLDLKWLRG 437
Cdd:COG1118 3 IEVRNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTLLRIIaglET---PDSGRIVLNGRDL-FTNLPPRER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 438 HIGLVNQEPVLFA-TTIRENIMYG--KDDATSEEItnAAKLSEAISFINnLpEGFEtqvGERGIQLSGGQKQRISISRAI 514
Cdd:COG1118 76 RVGFVFQHYALFPhMTVAENIAFGlrVRPPSKAEI--RARVEELLELVQ-L-EGLA---DRYPSQLSGGQRQRVALARAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15220188 515 VKNPSILLLDEATSALDA----ESEKIVQEALDRvmVGRTTVVVAH-RLSTVRNADIIAVVGGGKIIESGSHDELISNP 588
Cdd:COG1118 149 AVEPEVLLLDEPFGALDAkvrkELRRWLRRLHDE--LGGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDEVYDRP 225
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
982-1210 |
1.08e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 119.71 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRpDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIG 1061
Cdd:PRK13632 8 IKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEP--ALFATTIYENILYGKEGASES-EVM-----EAAKLANAHSFISSLPEgystkvgergiQMSGGQRQRIAIAR 1133
Cdd:PRK13632 87 IIFQNPdnQFIGATVEDDIAFGLENKKVPpKKMkdiidDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15220188 1134 AVLKNPEILLLDEATSALDVESERVVQQALDRL--MRDRTTVVVAHRLSTIKNSDMISVIQDGKIIEQGSHNILVENKN 1210
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLrkTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKE 234
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
982-1201 |
2.00e-29 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 117.55 E-value: 2.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRPdvtiFSdFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIkkLKLKSLRRHIG 1061
Cdd:COG3840 2 LRLDDLTYRYGDFP----LR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL--TALPPAERPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEPALFA-TTIYENILYG-----KEGASE-SEVMEAAKLANAHSFISSLPEgystkvgergiQMSGGQRQRIAIARA 1134
Cdd:COG3840 75 MLFQENNLFPhLTVAQNIGLGlrpglKLTAEQrAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220188 1135 VLKNPEILLLDEATSALD----VESERVVQQALDRlmRDRTTVVVAHRLSTIKN-SDMISVIQDGKIIEQGS 1201
Cdd:COG3840 144 LVRKRPILLLDEPFSALDpalrQEMLDLVDELCRE--RGLTVLMVTHDPEDAARiADRVLLVADGRIAADGP 213
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
982-1201 |
2.16e-29 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 120.98 E-value: 2.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSrpdVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKslRRHIG 1061
Cdd:PRK11432 7 VVLKNITKRFGS---NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEPALFA-TTIYENILYG--KEGASESE----VMEAAKLANAHSFisslpegystkvGERGI-QMSGGQRQRIAIAR 1133
Cdd:PRK11432 82 MVFQSYALFPhMSLGENVGYGlkMLGVPKEErkqrVKEALELVDLAGF------------EDRYVdQISGGQQQRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15220188 1134 AVLKNPEILLLDEATSALDVEservvqqaLDRLMRDR----------TTVVVAHRLS-TIKNSDMISVIQDGKIIEQGS 1201
Cdd:PRK11432 150 ALILKPKVLLFDEPLSNLDAN--------LRRSMREKirelqqqfniTSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGS 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
364-584 |
3.88e-29 |
|
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: 116.45 E-value: 3.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 364 KDVTFTYPSRPDVVIfDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYlDLKWLRGHIGLVN 443
Cdd:cd03263 4 RNLTKTYKKGTKPAV-DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 444 QEPVLFAT-TIRENIM-YGKDDATSEEITNAAKLSEAISFinNLPEGFETQVGergiQLSGGQKQRISISRAIVKNPSIL 521
Cdd:cd03263 82 QFDALFDElTVREHLRfYARLKGLPKSEIKEEVELLLRVL--GLTDKANKRAR----TLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220188 522 LLDEATSALDAESEKIVQEALDRVMVGRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESGSHDEL 584
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
359-588 |
8.68e-29 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 119.02 E-value: 8.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 359 GDILFKDVTFTYPsrpDVVIFDKLNFVIPAGKVVALVGGSGSGKST---MISLIErfyEPTDGAVMLDGNDIRYLDLKwL 435
Cdd:COG3839 2 ASLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTllrMIAGLE---DPTSGEILIGGRDVTDLPPK-D 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 436 RGhIGLVNQEPVLF-ATTIRENIMYG-------KDDATsEEITNAAKLSEAISFINNLPEgfetqvgergiQLSGGQKQR 507
Cdd:COG3839 75 RN-IAMVFQSYALYpHMTVYENIAFPlklrkvpKAEID-RRVREAAELLGLEDLLDRKPK-----------QLSGGQRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 508 ISISRAIVKNPSILLLDEATSALDAE------SE--KIVQEaldrvmVGRTTVVVAH------RLstvrnADIIAVVGGG 573
Cdd:COG3839 142 VALGRALVREPKVFLLDEPLSNLDAKlrvemrAEikRLHRR------LGTTTIYVTHdqveamTL-----ADRIAVMNDG 210
|
250
....*....|....*
gi 15220188 574 KIIESGSHDELISNP 588
Cdd:COG3839 211 RIQQVGTPEELYDRP 225
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
361-579 |
9.63e-29 |
|
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: 114.57 E-value: 9.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSRPDVV---IFDKLNFVIPAGKVVALVGGSGSGKSTMISLI--ERFYEPTDGAVMLDGndiRYLDLKWL 435
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSgkqLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLING---RPLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 436 RGHIGLVNQEPVLFAT-TIRENIMYgkddatseeitnAAKLseaisfinnlpegfetqvgeRGIqlSGGQKQRISISRAI 514
Cdd:cd03213 81 RKIIGYVPQDDILHPTlTVRETLMF------------AAKL--------------------RGL--SGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15220188 515 VKNPSILLLDEATSALDAESEKIVQEALDR-VMVGRTTVVVAHRLST--VRNADIIAVVGGGKIIESG 579
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
382-588 |
1.53e-28 |
|
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: 115.13 E-value: 1.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 382 LNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRylDLKWLRGHIGLVNQEPVLFA-TTIRENIMYG 460
Cdd:cd03299 18 VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISYVPQNYALFPhMTVYKNIAYG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 461 KDDATSEEITNAAKLSEAISFInnlpeGFETQVGERGIQLSGGQKQRISISRAIVKNPSILLLDEATSALDAESEKIVQE 540
Cdd:cd03299 96 LKKRKVDKKEIERKVLEIAEML-----GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLRE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15220188 541 ALDRVM--VGRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESGSHDELISNP 588
Cdd:cd03299 171 ELKKIRkeFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
364-579 |
2.06e-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: 114.27 E-value: 2.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 364 KDVTFTYPsrpDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKwLRGhIGLVN 443
Cdd:cd03301 4 ENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK-DRD-IAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 444 QEPVLFA-TTIRENIMYG------KDDATSEEITNAAKLSEAISFINNLPEgfetqvgergiQLSGGQKQRISISRAIVK 516
Cdd:cd03301 79 QNYALYPhMTVYDNIAFGlklrkvPKDEIDERVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRAIVR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220188 517 NPSILLLDEATSALDA--------ESEKIVQEaldrvmVGRTTVVVAH-RLSTVRNADIIAVVGGGKIIESG 579
Cdd:cd03301 148 EPKVFLMDEPLSNLDAklrvqmraELKRLQQR------LGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
1003-1200 |
3.58e-28 |
|
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: 113.42 E-value: 3.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1003 FNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIkkLKLKSLRRHIGLVQQEPALFA-TTIYENILYG 1081
Cdd:TIGR01277 17 FDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSH--TGLAPYQRPVSMLFQENNLFAhLTVRQNIGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1082 -----KEGASESEVME-AAKLANAHSFISSLPEgystkvgergiQMSGGQRQRIAIARAVLKNPEILLLDEATSALD--- 1152
Cdd:TIGR01277 95 lhpglKLNAEQQEKVVdAAQQVGIADYLDRLPE-----------QLSGGQRQRVALARCLVRPNPILLLDEPFSALDpll 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15220188 1153 -VESERVVQQALDRlmRDRTTVVVAHRLS-TIKNSDMISVIQDGKIIEQG 1200
Cdd:TIGR01277 164 rEEMLALVKQLCSE--RQRTLLMVTHHLSdARAIASQIAVVSQGKIKVVS 211
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
983-1182 |
3.99e-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: 113.40 E-value: 3.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 983 ELKGVHFSYPSRPdvtIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLklkslRRHIGL 1062
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1063 VQQEPAL---FATTIYENI---LYGKEG-------ASESEVMEAAKLANAhsfisslpegysTKVGERGI-QMSGGQRQR 1128
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVlmgLYGHKGlfrrlskADKAKVDEALERVGL------------SELADRQIgELSGGQQQR 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15220188 1129 IAIARAVLKNPEILLLDEATSALDVESERVVQQALDRL-MRDRTTVVVAHRLSTI 1182
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLV 195
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
376-589 |
7.24e-28 |
|
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: 113.30 E-value: 7.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 376 VVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYL--DLKWLRGhIGLVNQEPVLFAT-T 452
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLppHEIARLG-IGRTFQIPRLFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 453 IRENIM----------YGKDDATSEEITNAAKLSEAISFInNLPEGFETQVGErgiqLSGGQKQRISISRAIVKNPSILL 522
Cdd:cd03219 92 VLENVMvaaqartgsgLLLARARREEREARERAEELLERV-GLADLADRPAGE----LSYGQQRRLEIARALATDPKLLL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 523 LDEATSAL-DAESEKIVqEALDRVMV-GRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESGSHDELISNPD 589
Cdd:cd03219 167 LDEPAAGLnPEETEELA-ELIRELRErGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
982-1200 |
9.73e-28 |
|
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: 112.20 E-value: 9.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRPdvtifSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKslRRHIG 1061
Cdd:cd03298 1 VRLDKIRFSYGEQP-----MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEPALFA-TTIYENILYG-----KEGASESEVMEAAkLANAhsfisslpeGYSTKVGERGIQMSGGQRQRIAIARAV 1135
Cdd:cd03298 74 MLFQENNLFAhLTVEQNVGLGlspglKLTAEDRQAIEVA-LARV---------GLAGLEKRLPGELSGGERQRVALARVL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15220188 1136 LKNPEILLLDEATSALDVESERVVQQALDRLMRDR--TTVVVAHRLSTIKN-SDMISVIQDGKIIEQG 1200
Cdd:cd03298 144 VRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
977-1200 |
1.97e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 113.19 E-value: 1.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 977 NVEGTIELKGVHFSYP--SRPDVTifsDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLK 1054
Cdd:PRK13635 1 MKEEIIRVEHISFRYPdaATYALK---DVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1055 SLRRHIGLVQQEP--ALFATTIYENILYGKE--GASESE----VMEAAKLANAHSFISSLPEgystkvgergiQMSGGQR 1126
Cdd:PRK13635 78 DVRRQVGMVFQNPdnQFVGATVQDDVAFGLEniGVPREEmverVDQALRQVGMEDFLNREPH-----------RLSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15220188 1127 QRIAIARAVLKNPEILLLDEATSALDVESERVVQQALdRLMRDRTTVVV---AHRLSTIKNSDMISVIQDGKIIEQG 1200
Cdd:PRK13635 147 QRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETV-RQLKEQKGITVlsiTHDLDEAAQADRVIVMNKGEILEEG 222
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
374-572 |
2.08e-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: 111.27 E-value: 2.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 374 PDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAV----MLDGNDIRYLDLKWLRGHIGLVNQEPVLF 449
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 450 ATTIRENIMYGK--DDATSEEITNAAKLSEAISFinnLPEGFETQVGERGIQLSGGQKQRISISRAIVKNPSILLLDEAT 527
Cdd:cd03290 92 NATVEENITFGSpfNKQRYKAVTDACSLQPDIDL---LPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15220188 528 SALDAE-SEKIVQEALDRVMVG--RTTVVVAHRLSTVRNAD-IIAVVGG 572
Cdd:cd03290 169 SALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADwIIAMKDG 217
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
364-598 |
2.30e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 112.86 E-value: 2.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 364 KDVTFTYPSrpDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYlDLKWL---RGHIG 440
Cdd:PRK13639 5 RDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKY-DKKSLlevRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 441 LVNQEP--VLFATTIRENIMYGKDDA--TSEEITNAAKlsEAISFINNlpEGFETQVGErgiQLSGGQKQRISISRAIVK 516
Cdd:PRK13639 82 IVFQNPddQLFAPTVEEDVAFGPLNLglSKEEVEKRVK--EALKAVGM--EGFENKPPH---HLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 517 NPSILLLDEATSALDAE-SEKIVQEALDRVMVGRTTVVVAHRLSTV-RNADIIAVVGGGKIIESGSHDELISNPDGAYSS 594
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMgASQIMKLLYDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSDIETIRKA 234
|
....
gi 15220188 595 LLRI 598
Cdd:PRK13639 235 NLRL 238
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
706-919 |
2.37e-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: 113.41 E-value: 2.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 706 ILFCCGSVITVIVHTIEHTTFGIMGERLTLRVRQKMFSAILRNEIGWFDKvdNTSSMLASRLESDATLLRTIVVDRSTIL 785
Cdd:cd18572 40 LLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDA--TKTGELTSRLTSDCQKVSDPLSTNLNVF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 786 LENLGLVVTAFIISFILNWRLTLVVLATYPLIIsgHISEKifmqgYGG---NLSK----AYLKANMLAGESISNIRTVVA 858
Cdd:cd18572 118 LRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIA--LITKV-----YGRyyrKLSKeiqdALAEANQVAEEALSNIRTVRS 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220188 859 FCAEEKVLDLYSKELLEPSERSFRRGQMAGILYGVSQFFIFSSYGLALWYGSIL-MEKGLSS 919
Cdd:cd18572 191 FATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLvLSGRMSA 252
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
982-1208 |
2.40e-27 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 112.11 E-value: 2.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGV--HFSypsrpDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIK--KLKLKSLR 1057
Cdd:PRK09493 2 IEFKNVskHFG-----PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1058 RHIGLVQQEPALFA-TTIYENILYGK---EGASESEvmeAAKLANAhsfisslpegYSTKVG--ERG----IQMSGGQRQ 1127
Cdd:PRK09493 77 QEAGMVFQQFYLFPhLTALENVMFGPlrvRGASKEE---AEKQARE----------LLAKVGlaERAhhypSELSGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1128 RIAIARAVLKNPEILLLDEATSALDVEservVQQALDRLMRD-----RTTVVVAHRLSTIKN--SDMIsVIQDGKIIEQG 1200
Cdd:PRK09493 144 RVAIARALAVKPKLMLFDEPTSALDPE----LRHEVLKVMQDlaeegMTMVIVTHEIGFAEKvaSRLI-FIDKGRIAEDG 218
|
....*...
gi 15220188 1201 SHNILVEN 1208
Cdd:PRK09493 219 DPQVLIKN 226
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
360-589 |
2.73e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 113.19 E-value: 2.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 360 DILFKDVTFTY-PSRPdvviFDKL-----NFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLdGNDI-----R 428
Cdd:PRK13634 2 DITFQKVEHRYqYKTP----FERRalydvNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVitagkK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 429 YLDLKWLRGHIGLVNQ--EPVLFATTIRENIMYG-------KDDATseeitnaAKLSEAISFInNLPEgfetQVGERG-I 498
Cdd:PRK13634 77 NKKLKPLRKKVGIVFQfpEHQLFEETVEKDICFGpmnfgvsEEDAK-------QKAREMIELV-GLPE----ELLARSpF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 499 QLSGGQKQRISISRAIVKNPSILLLDEATSALDAESEKIVQEALDRVM--VGRTTVVVAHRLSTVRN-ADIIAVVGGGKI 575
Cdd:PRK13634 145 ELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHkeKGLTTVLVTHSMEDAARyADQIVVMHKGTV 224
|
250
....*....|....
gi 15220188 576 IESGSHDELISNPD 589
Cdd:PRK13634 225 FLQGTPREIFADPD 238
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1014-1201 |
3.86e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 111.79 E-value: 3.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1014 ALVGQSGSGKSSVLSLVLRFYD-----PTAGIIMIDGQDIKKLKLKS--LRRHIGLVQQEPALFATTIYENILYGK--EG 1084
Cdd:PRK14239 35 ALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSPRTDTvdLRKEIGMVFQQPNPFPMSIYENVVYGLrlKG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1085 ASESEVMEAA---KLANAhsfisSLPEGYSTKVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQ 1161
Cdd:PRK14239 115 IKDKQVLDEAvekSLKGA-----SIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEE 189
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15220188 1162 ALDRLMRDRTTVVVAHRL---STIknSDMISVIQDGKIIEQGS 1201
Cdd:PRK14239 190 TLLGLKDDYTMLLVTRSMqqaSRI--SDRTGFFLDGDLIEYND 230
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
982-1201 |
4.47e-27 |
|
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: 117.48 E-value: 4.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSR--------PDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFyDPTAGIIMIDGQDIKKLK- 1052
Cdd:COG4172 276 LEARDLKVWFPIKrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSr 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1053 --LKSLRRHIGLVQQEPalFAT-----TIYENILYG----KEGASESEVMEAAklanahsfISSLPE-GYSTKVGERGI- 1119
Cdd:COG4172 355 raLRPLRRRMQVVFQDP--FGSlsprmTVGQIIAEGlrvhGPGLSAAERRARV--------AEALEEvGLDPAARHRYPh 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1120 QMSGGQRQRIAIARAVLKNPEILLLDEATSALDVeserVVQ-QALD---RLMRDR--TTVVVAHRLSTIKN-SDMISVIQ 1192
Cdd:COG4172 425 EFSGGQRQRIAIARALILEPKLLVLDEPTSALDV----SVQaQILDllrDLQREHglAYLFISHDLAVVRAlAHRVMVMK 500
|
....*....
gi 15220188 1193 DGKIIEQGS 1201
Cdd:COG4172 501 DGKVVEQGP 509
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
981-1217 |
7.28e-27 |
|
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: 119.28 E-value: 7.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 981 TIELKGVHFSYpSRPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQdikklklkslrrhI 1060
Cdd:TIGR00957 636 SITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------V 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1061 GLVQQEPALFATTIYENILYGK--EGASESEVMEA-AKLANahsfISSLPEGYSTKVGERGIQMSGGQRQRIAIARAVLK 1137
Cdd:TIGR00957 702 AYVPQQAWIQNDSLRENILFGKalNEKYYQQVLEAcALLPD----LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYS 777
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1138 NPEILLLDEATSALDVEserVVQQALDR------LMRDRTTVVVAHRLSTIKNSDMISVIQDGKIIEQGSHNILVEnKNG 1211
Cdd:TIGR00957 778 NADIYLFDDPLSAVDAH---VGKHIFEHvigpegVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQ-RDG 853
|
....*.
gi 15220188 1212 PYSKLI 1217
Cdd:TIGR00957 854 AFAEFL 859
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
993-1176 |
8.15e-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: 109.11 E-value: 8.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 993 SRPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLkSLRRHIGLVQQEPALFAT 1072
Cdd:COG4133 11 RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE-DYRRRLAYLGHADGLKPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1073 -TIYENI-----LYGKEGASES--EVMEAAKLAN-AHSFISSLpegystkvgergiqmSGGQRQRIAIARAVLKNPEILL 1143
Cdd:COG4133 90 lTVRENLrfwaaLYGLRADREAidEALEAVGLAGlADLPVRQL---------------SAGQKRRVALARLLLSPAPLWL 154
|
170 180 190
....*....|....*....|....*....|...
gi 15220188 1144 LDEATSALDVESERVVQQALDRLMRDRTTVVVA 1176
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLARGGAVLLT 187
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1002-1201 |
8.47e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 111.68 E-value: 8.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1002 DFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDI--KKLKLKSLRRHIGLVQQEP--ALFATTIYEN 1077
Cdd:PRK13637 25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFEETIEKD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1078 ILYGKE--GASESEVMEAAKLANAhsfISSLP-EGYSTKvgeRGIQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVE 1154
Cdd:PRK13637 105 IAFGPInlGLSEEEIENRVKRAMN---IVGLDyEDYKDK---SPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15220188 1155 S-ERVVQQAldRLMRDR---TTVVVAHRLSTI-KNSDMISVIQDGKIIEQGS 1201
Cdd:PRK13637 179 GrDEILNKI--KELHKEynmTIILVSHSMEDVaKLADRIIVMNKGKCELQGT 228
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
380-594 |
1.13e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 113.39 E-value: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 380 DKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDlKWLRGhIGLVNQEPVLFA-TTIRENIM 458
Cdd:PRK11607 36 DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP-PYQRP-INMMFQSYALFPhMTVEQNIA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 459 YG--KDDATSEEITnaAKLSEAISFINnlpegFETQVGERGIQLSGGQKQRISISRAIVKNPSILLLDEATSALDAE-SE 535
Cdd:PRK11607 114 FGlkQDKLPKAEIA--SRVNEMLGLVH-----MQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKlRD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15220188 536 KIVQEALDRV-MVGRTTVVVAH-RLSTVRNADIIAVVGGGKIIESGSHDELISNPDGAYSS 594
Cdd:PRK11607 187 RMQLEVVDILeRVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSA 247
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
361-590 |
1.80e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 110.23 E-value: 1.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSRPDVVIfDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHIG 440
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTL-KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 441 LVNQEP--VLFATTIRENIMYGKDDATSEEITNAAKLSEAISFINNLPEG-FETQvgergiQLSGGQKQRISISRAIVKN 517
Cdd:PRK13648 87 IVFQNPdnQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERAdYEPN------ALSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15220188 518 PSILLLDEATSALDAESEKIVQEALDRVMVGR--TTVVVAHRLSTVRNADIIAVVGGGKIIESGSHDELISNPDG 590
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEE 235
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
981-1206 |
1.95e-26 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 109.33 E-value: 1.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 981 TIELKGVHFSYPSRPdvtIFSDFNLLVPSGKSMALVGQSGSGKSSVLSlVLRFYD-PTAGIIMIDG------QDIKKLKL 1053
Cdd:COG4161 2 SIQLKNINCFYGSHQ---ALFDINLECPSGETLVLLGPSGAGKSSLLR-VLNLLEtPDSGQLNIAGhqfdfsQKPSEKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1054 KSLRRHIGLVQQE----PALfatTIYENILygkE------GASESEVMEAAKlanahSFISSLpeGYSTKVGERGIQMSG 1123
Cdd:COG4161 78 RLLRQKVGMVFQQynlwPHL---TVMENLI---EapckvlGLSKEQAREKAM-----KLLARL--RLTDKADRFPLHLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1124 GQRQRIAIARAVLKNPEILLLDEATSALDVE-SERVVQQALDRLMRDRTTVVVAHRLSTI-KNSDMISVIQDGKIIEQGS 1201
Cdd:COG4161 145 GQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFArKVASQVVYMEKGRIIEQGD 224
|
....*
gi 15220188 1202 HNILV 1206
Cdd:COG4161 225 ASHFT 229
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
982-1201 |
3.07e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 110.11 E-value: 3.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRpdvTIFS-----DFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDI----KKLK 1052
Cdd:PRK13634 3 ITFQKVEHRYQYK---TPFErralyDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1053 LKSLRRHIGLVQQ--EPALFATTIYENILYGKE--GASESEvmeAAKLANAHSFISSLPEGYSTKvgeRGIQMSGGQRQR 1128
Cdd:PRK13634 80 LKPLRKKVGIVFQfpEHQLFEETVEKDICFGPMnfGVSEED---AKQKAREMIELVGLPEELLAR---SPFELSGGQMRR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15220188 1129 IAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDR--TTVVVAHRLSTIKN-SDMISVIQDGKIIEQGS 1201
Cdd:PRK13634 154 VAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSMEDAARyADQIVVMHKGTVFLQGT 229
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
364-579 |
4.76e-26 |
|
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: 107.28 E-value: 4.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 364 KDVTFTYPSRpdvVIFDKLNFVIPAGkVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYlDLKWLRGHIGLVN 443
Cdd:cd03264 4 ENLTKRYGKK---RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 444 QEPVLFAT-TIRE-----NIMYGKDDATSEeitnaAKLSEAISFINnLPEGFETQVGergiQLSGGQKQRISISRAIVKN 517
Cdd:cd03264 79 QEFGVYPNfTVREfldyiAWLKGIPSKEVK-----ARVDEVLELVN-LGDRAKKKIG----SLSGGMRRRVGIAQALVGD 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15220188 518 PSILLLDEATSALDAESEKIVQEALDRVMVGRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESG 579
Cdd:cd03264 149 PSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
665-920 |
5.32e-26 |
|
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: 109.65 E-value: 5.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 665 GTLGSFI-AGSQM--PLFALGIAQALVSYYM-DWETTQNEVKRISILFCCGSVITVIVHTIEHTTFGIMGERLTLRVRQK 740
Cdd:cd18780 1 GTIALLVsSGTNLalPYFFGQVIDAVTNHSGsGGEEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 741 MFSAILRNEIGWFDKvdNTSSMLASRLESDATLLRTIVVDRSTILLENLGLVVTAFIISFILNWRLTLVVLATYPLIISG 820
Cdd:cd18780 81 LFSAIIAQEIAFFDV--TRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 821 HISEKIFMQGYGGNLSKAYLKANMLAGESISNIRTVVAFCAEEKVLDLYSKELLEPSERSFRRGQMAGILYGVSQFFIFS 900
Cdd:cd18780 159 AVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQL 238
|
250 260
....*....|....*....|....*.
gi 15220188 901 SYGLALWYGSILMEKG------LSSF 920
Cdd:cd18780 239 AIVLVLWYGGRLVIDGelttglLTSF 264
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
388-606 |
5.45e-26 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 108.52 E-value: 5.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 388 AGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYL-------------DLKWLRGHIGLVNQEPVLFA-TTI 453
Cdd:PRK10619 30 AGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLRLLRTRLTMVFQHFNLWShMTV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 454 RENIMYGKDDATSeeITNAAKLSEAISFINNLpeGF-ETQVGERGIQLSGGQKQRISISRAIVKNPSILLLDEATSALDA 532
Cdd:PRK10619 110 LENVMEAPIQVLG--LSKQEARERAVKYLAKV--GIdERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDP 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 533 EsekIVQEALdRVMV-----GRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESGSHDELISNPDGAyssllRIQEAASPNL 606
Cdd:PRK10619 186 E---LVGEVL-RIMQqlaeeGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGNPQSP-----RLQQFLKGSL 256
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
359-605 |
5.58e-26 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 116.42 E-value: 5.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 359 GDILFKDVTFTYPSRPDVVIfDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGH 438
Cdd:PTZ00243 1307 GSLVFEGVQMRYREGLPLVL-RGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQ 1385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 439 IGLVNQEPVLFATTIRENImygkD---DATSEEITNAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRISISRAIV 515
Cdd:PTZ00243 1386 FSMIPQDPVLFDGTVRQNV----DpflEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALL 1461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 516 KNPS-ILLLDEATSALDAESEKIVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVGGGKIIESGSHDELISNPDGAYSS 594
Cdd:PTZ00243 1462 KKGSgFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHS 1541
|
250
....*....|.
gi 15220188 595 LLriqEAASPN 605
Cdd:PTZ00243 1542 MV---EALGRS 1549
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
90-335 |
6.33e-26 |
|
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: 109.17 E-value: 6.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 90 FVYLSVVILFSSWLEVACWMHTGERQAAKIRKAYLRSMLSQDISLFDTEiSTGEVISAITSEILVVQDAISEKVGNFMHF 169
Cdd:cd18572 42 LLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDAT-KTGELTSRLTSDCQKVSDPLSTNLNVFLRN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 170 ISRFIAGFAIGFASVWQISLVTLSIVPFIALAGGIYAFVSSGLIVRVRKSYVKANEIAEEVIGNVRTVQAFTGEEKAVSS 249
Cdd:cd18572 121 LVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARR 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 250 YQGALRNTYNYGRKAGLAKGLGLGSLHFVLFLSWALLIWF-TSIVVHKGIANG------------GESFTTMLNVViagl 316
Cdd:cd18572 201 YERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYgGHLVLSGRMSAGqlvtfmlyqqqlGEAFQSLGDVF---- 276
|
250
....*....|....*....
gi 15220188 317 slgqaapdiSTFMRASAAA 335
Cdd:cd18572 277 ---------SSLMQAVGAA 286
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
982-1186 |
6.77e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 107.11 E-value: 6.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRPdvtIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIG 1061
Cdd:PRK10247 8 LQLQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEPALFATTIYENILYGKEgASESEVMEAAKLANAHSFisSLPEGYSTKvgerGI-QMSGGQRQRIAIARAVLKNPE 1140
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIFPWQ-IRNQQPDPAIFLDDLERF--ALPDTILTK----NIaELSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15220188 1141 ILLLDEATSALDVESERVVQQALDRLMRDRTTVV--VAHRLSTIKNSD 1186
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRYVREQNIAVlwVTHDKDEINHAD 205
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
663-916 |
7.66e-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: 109.18 E-value: 7.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 663 LCGTLGSFIAGSQMPLFALGIAQALVSYYMDWettqneVKRISILFCCGSVITVIVHTIEHTTFGIMGERLTLRVRQKMF 742
Cdd:cd07346 6 LLLLLATALGLALPLLTKLLIDDVIPAGDLSL------LLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 743 SAILRNEIGWFDKvdNTSSMLASRLESDATLLRTIVVDRSTILLENLGLVVTAFIISFILNWRLTLVVLATYPLIIsghi 822
Cdd:cd07346 80 RHLQRLSLSFFDR--NRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYV---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 823 sekIFMQGYGGNLSKAYLK-----ANMLAG--ESISNIRTVVAFCAEEKVLDLYSKELLEPSERSFRRGQMAGILYGVSQ 895
Cdd:cd07346 154 ---LILRYFRRRIRKASREvreslAELSAFlqESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIG 230
|
250 260
....*....|....*....|.
gi 15220188 896 FFIFSSYGLALWYGSILMEKG 916
Cdd:cd07346 231 LLTALGTALVLLYGGYLVLQG 251
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
372-569 |
7.81e-26 |
|
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: 106.41 E-value: 7.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 372 SRPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWlRGHIGLVNQEPVLFAT 451
Cdd:COG4133 11 RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLAYLGHADGLKPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 452 -TIRENI-----MYGKDDAtseeitnAAKLSEAISFINnLPEGFETQVGergiQLSGGQKQRISISRAIVKNPSILLLDE 525
Cdd:COG4133 90 lTVRENLrfwaaLYGLRAD-------REAIDEALEAVG-LAGLADLPVR----QLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15220188 526 ATSALDAES----EKIVQEALDRvmvGRTTVVVAHRLSTVRNADIIAV 569
Cdd:COG4133 158 PFTALDAAGvallAELIAAHLAR---GGAVLLTTHQPLELAAARVLDL 202
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
982-1200 |
9.21e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 107.69 E-value: 9.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPsrpDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYD--PTA---GIIMIDGQDIKKLKLKSL 1056
Cdd:PRK14247 4 IEIRDLKVSFG---QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEArvsGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1057 RRHIGLVQQEPALFAT-TIYENILYG----KEGASESEVMEAAKLANAHSfisSLPEGYSTKVGERGIQMSGGQRQRIAI 1131
Cdd:PRK14247 81 RRRVQMVFQIPNPIPNlSIFENVALGlklnRLVKSKKELQERVRWALEKA---QLWDEVKDRLDAPAGKLSGGQQQRLCI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1132 ARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVVVAH-RLSTIKNSDMISVIQDGKIIEQG 1200
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWG 227
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
381-579 |
1.05e-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: 106.23 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 381 KLNFVIPAGkVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDG---NDIR-YLDLKWLRGHIGLVNQEPVLFA-TTIRE 455
Cdd:cd03297 16 KIDFDLNEE-VTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSRkKINLPPQQRKIGLVFQQYALFPhLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 456 NIMYG-KDDATSEEITNAAKLSEAISFinnlpegfeTQVGERGI-QLSGGQKQRISISRAIVKNPSILLLDEATSALDAE 533
Cdd:cd03297 95 NLAFGlKRKRNREDRISVDELLDLLGL---------DHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15220188 534 SEKIVQEALDRVM--VGRTTVVVAHRLSTV-RNADIIAVVGGGKIIESG 579
Cdd:cd03297 166 LRLQLLPELKQIKknLNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
375-588 |
1.16e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 107.31 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 375 DVVIFDKLNFVIPAGKVVALVGGSGSGKSTMIS----LIERFYEP-TDGAVMLDGNDIRYLDLKWLRGHIGLVNQEPVLF 449
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRvfnrLIELYPEArVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 450 AT-TIRENIMYGKDdaTSEEITNAAKLSEAISFI---NNLPEGFETQVGERGIQLSGGQKQRISISRAIVKNPSILLLDE 525
Cdd:PRK14247 95 PNlSIFENVALGLK--LNRLVKSKKELQERVRWAlekAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220188 526 ATSALDAESEKIVQEALDRVMVGRTTVVVAH-RLSTVRNADIIAVVGGGKIIESGSHDELISNP 588
Cdd:PRK14247 173 PTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
381-589 |
1.97e-25 |
|
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: 109.43 E-value: 1.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 381 KLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDG---NDIR-YLDLKWLRGHIGLVNQEPVLFA-TTIRE 455
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRkGIFLPPEKRRIGYVFQEARLFPhLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 456 NIMYGKDDAT-SEEITNAAKLSEAIsfinnlpeGFETQVGERGIQLSGGQKQRISISRAIVKNPSILLLDEATSALDAES 534
Cdd:TIGR02142 95 NLRYGMKRARpSERRISFERVIELL--------GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15220188 535 EKIVQEALDRVM--VGRTTVVVAHRLSTV-RNADIIAVVGGGKIIESGSHDELISNPD 589
Cdd:TIGR02142 167 KYEILPYLERLHaeFGIPILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
391-588 |
2.30e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 106.40 E-value: 2.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 391 VVALVGGSGSGKSTMISLIERFYE-----PTDGAVMLDGNDI--RYLDLKWLRGHIGLVNQEPVLFATTIRENIMYG--- 460
Cdd:PRK14239 33 ITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPNPFPMSIYENVVYGlrl 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 461 ---KDDATSEEITNAAKLSEAISfinnlpEGFETQVGERGIQLSGGQKQRISISRAIVKNPSILLLDEATSALDAESEKI 537
Cdd:PRK14239 113 kgiKDKQVLDEAVEKSLKGASIW------DEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGK 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15220188 538 VQEALDRVMVGRTTVVVAHRLSTV-RNADIIAVVGGGKIIESGSHDELISNP 588
Cdd:PRK14239 187 IEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDTKQMFMNP 238
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
707-950 |
3.06e-25 |
|
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: 107.21 E-value: 3.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 707 LFCCGSVITvivhTIEHTTFGIMGERLTLRVRQKMFSAILRNEIGWFDKvdNTSSMLASRLESDATLLRTIVVDRSTILL 786
Cdd:cd18573 50 VFVVGAAAN----FGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDK--NKTGELVSRLSSDTSVVGKSLTQNLSDGL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 787 ENLGLVVTAFIISFILNWRLTLVVLATYPLIIsghisekIFMQGYGG---NLSKAYLKA----NMLAGESISNIRTVVAF 859
Cdd:cd18573 124 RSLVSGVGGIGMMLYISPKLTLVMLLVVPPIA-------VGAVFYGRyvrKLSKQVQDAladaTKVAEERLSNIRTVRAF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 860 CAEEKVLDLYSKELLEPSERSFRRGQMAGILYGVSQFFIFSSYGLALWYGSILMEKG------LSSFesVMKTFMVlivt 933
Cdd:cd18573 197 AAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGeltvgdLTSF--LMYAVYV---- 270
|
250
....*....|....*..
gi 15220188 934 ALVMGEVLALAPDLLKG 950
Cdd:cd18573 271 GSSVSGLSSFYSELMKG 287
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
361-589 |
3.46e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 107.06 E-value: 3.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTY-PSRP-DVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDI--RYLDLKWLR 436
Cdd:PRK13637 3 IKIENLTHIYmEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 437 GHIGLVNQEP--VLFATTIRENIMYGKDD--ATSEEITNAAKLSEAISFINnlpegFETQVGERGIQLSGGQKQRISISR 512
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEKDIAFGPINlgLSEEEIENRVKRAMNIVGLD-----YEDYKDKSPFELSGGQKRRVAIAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 513 AIVKNPSILLLDEATSALDAES-EKIVQEALD-RVMVGRTTVVVAHRLSTV-RNADIIAVVGGGKIIESGSHDELISNPD 589
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDPKGrDEILNKIKElHKEYNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREVFKEVE 237
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
377-587 |
3.49e-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: 105.21 E-value: 3.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 377 VIFDkLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDL-KWLRGHIGLVNQEPVLFAT-TIR 454
Cdd:cd03224 15 ILFG-VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPhERARAGIGYVPEGRRIFPElTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 455 ENIMYGKDDATSEEItnAAKLSEAISFINNLPEGFETQVGergiQLSGGQKQRISISRAIVKNPSILLLDEATSALdaeS 534
Cdd:cd03224 94 ENLLLGAYARRRAKR--KARLERVYELFPRLKERRKQLAG----TLSGGEQQMLAIARALMSRPKLLLLDEPSEGL---A 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15220188 535 EKIVQEALDRVM----VGRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESGSHDELISN 587
Cdd:cd03224 165 PKIVEEIFEAIRelrdEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLAD 222
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
361-589 |
3.94e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 106.84 E-value: 3.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTY-PSRP-DVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIR----YLDLKW 434
Cdd:PRK13641 3 IKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 435 LRGHIGLVNQ--EPVLFATTIRENIMYG-KDDATSEEitnAAKlSEAISFINNLpeGFETQVGERG-IQLSGGQKQRISI 510
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGpKNFGFSED---EAK-EKALKWLKKV--GLSEDLISKSpFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 511 SRAIVKNPSILLLDEATSALDAESEK-IVQEALDRVMVGRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESGSHDELISNP 588
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKeMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSDK 236
|
.
gi 15220188 589 D 589
Cdd:PRK13641 237 E 237
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
118-335 |
4.41e-25 |
|
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: 106.63 E-value: 4.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 118 KIRKAYLRSMLSQDISLFDTeISTGEVISAITSEILVVQDAISEKVGNFMHFISRFIAGFAIGFASVWQISLVTLSIVPF 197
Cdd:cd18784 70 RIRNLLFRSIVSQEIGFFDT-VKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 198 IALAGGIYAFVSSGLIVRVRKSYVKANEIAEEVIGNVRTVQAFTGEEKAVSSYQGALRNTYNYGRKAGLAKGLGLGSLHF 277
Cdd:cd18784 149 IAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNEL 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220188 278 VLFLSWALLIWFTSIVVHKGIANGGesftTMLNVVIAGLSLGQAAPDIST----FMRASAAA 335
Cdd:cd18784 229 TELALTVSTLYYGGHLVITGQISGG----NLISFILYQLELGSCLESVGSvytgLMQAVGAA 286
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
982-1209 |
4.65e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 106.36 E-value: 4.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSrpDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIG 1061
Cdd:PRK13647 5 IEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEP--ALFATTIYENILYG--KEGASESEVM----EAAKLANAHSFISSLPEgystkvgergiQMSGGQRQRIAIAR 1133
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGpvNMGLDKDEVErrveEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15220188 1134 AVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVVVA-HRLS-TIKNSDMISVIQDGKIIEQGSHNILVENK 1209
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDlAAEWADQVIVLKEGRVLAEGDKSLLTDED 229
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1002-1214 |
6.70e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 108.38 E-value: 6.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1002 DFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKlkSLRRHIGLVQQEPALFA-TTIYENILY 1080
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP--PYQRPINMMFQSYALFPhMTVEQNIAF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1081 G------KEGASESEVMEAAKLANAHSFISSLPEgystkvgergiQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVE 1154
Cdd:PRK11607 115 GlkqdklPKAEIASRVNEMLGLVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15220188 1155 -SERVVQQALDRLMR-DRTTVVVAH-RLSTIKNSDMISVIQDGKIIEQGSHNILVENKNGPYS 1214
Cdd:PRK11607 184 lRDRMQLEVVDILERvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYS 246
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
386-588 |
6.82e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 105.22 E-value: 6.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 386 IPAGKVVALVGGSGSGKSTMISLIERFYEPTDG-----AVMLDGNdiRYLD-----LKWLRGHIGLVNQEPVLFA-TTIR 454
Cdd:PRK11264 26 VKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTA--RSLSqqkglIRQLRQHVGFVFQNFNLFPhRTVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 455 ENIMYG----KDDATSEEITNAAKLSEAISFinnlpEGFETQVGERgiqLSGGQKQRISISRAIVKNPSILLLDEATSAL 530
Cdd:PRK11264 104 ENIIEGpvivKGEPKEEATARARELLAKVGL-----AGKETSYPRR---LSGGQQQRVAIARALAMRPEVILFDEPTSAL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15220188 531 DAEsekIVQEALDRVMV----GRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESGSHDELISNP 588
Cdd:PRK11264 176 DPE---LVGEVLNTIRQlaqeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFADP 235
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
375-588 |
7.31e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 105.13 E-value: 7.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 375 DVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYE------PTDGAVMLDGNDIRYLDLKWLRGHIGLVNQEPVL 448
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 449 FA-TTIRENIMYGKDDATSEEITNAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRISISRAIVKNPSILLLDEAT 527
Cdd:PRK14246 102 FPhLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220188 528 SALDAESEKIVQEALDRVMVGRTTVVVAHRLSTV-RNADIIAVVGGGKIIESGSHDELISNP 588
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIFTSP 243
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1002-1201 |
7.61e-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: 107.49 E-value: 7.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1002 DFNLLVPSGKSMALVGQSGSGKSSVLSLV---LRfydPTAGIIMIDG---QDI-KKLKLKSLRRHIGLVQQEPALFAT-T 1073
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIaglER---PDSGRIRLGGevlQDSaRGIFLPPHRRRIGYVFQEARLFPHlS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1074 IYENILYG----KEGASESEVMEAAKLANahsfISSLPEgystkvgeRGI-QMSGGQRQRIAIARAVLKNPEILLLDEAT 1148
Cdd:COG4148 94 VRGNLLYGrkraPRAERRISFDEVVELLG----IGHLLD--------RRPaTLSGGERQRVAIGRALLSSPRLLLMDEPL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220188 1149 SALDVESERVVQQALDRLmRDRTT---VVVAH------RLstiknSDMISVIQDGKIIEQGS 1201
Cdd:COG4148 162 AALDLARKAEILPYLERL-RDELDipiLYVSHsldevaRL-----ADHVVLLEQGRVVASGP 217
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
975-1200 |
8.17e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 105.60 E-value: 8.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 975 LSNVEGTIELKGVHFSYPSRPDVTIfSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLK 1054
Cdd:PRK13648 1 MEDKNSIIVFKNVSFQYQSDASFTL-KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1055 SLRRHIGLVQQEP--ALFATTIYENILYGKEGAS------ESEVMEAAKLANAHSFISSLPEGystkvgergiqMSGGQR 1126
Cdd:PRK13648 80 KLRKHIGIVFQNPdnQFVGSIVKYDVAFGLENHAvpydemHRRVSEALKQVDMLERADYEPNA-----------LSGGQK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15220188 1127 QRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDR--TTVVVAHRLSTIKNSDMISVIQDGKIIEQG 1200
Cdd:PRK13648 149 QRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEG 224
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
364-589 |
9.36e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 105.56 E-value: 9.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 364 KDVTFTYPSRPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHIGLVN 443
Cdd:PRK13642 8 ENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 444 QEP--VLFATTIRENIMYGKDDATSEEITNAAKLSEAISFINNLpeGFETQVGERgiqLSGGQKQRISISRAIVKNPSIL 521
Cdd:PRK13642 88 QNPdnQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNML--DFKTREPAR---LSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220188 522 LLDEATSALD----AESEKIVQEALDRVMVgrTTVVVAHRLSTVRNADIIAVVGGGKIIESGSHDELISNPD 589
Cdd:PRK13642 163 ILDESTSMLDptgrQEIMRVIHEIKEKYQL--TVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSE 232
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
364-556 |
9.75e-25 |
|
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: 103.11 E-value: 9.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 364 KDVTFTYPSRPDVVifDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYldlKWLRGHIGLVN 443
Cdd:cd03226 3 ENISFSYKKGTEIL--DDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 444 QEP--VLFATTIRENIMYGKDDAtSEEITNAAKLSEAISfINNLPEgfetqvgERGIQLSGGQKQRISISRAIVKNPSIL 521
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGLKEL-DAGNEQAETVLKDLD-LYALKE-------RHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190
....*....|....*....|....*....|....*.
gi 15220188 522 LLDEATSALDAESEKIVQEALDRVM-VGRTTVVVAH 556
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAaQGKAVIVITH 184
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
378-586 |
9.79e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 104.71 E-value: 9.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 378 IFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHIGLVNQEPVL-FATTIREN 456
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGITVREL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 457 IMYGKddatSEEITNAAKLSEA-ISFINNLPEgfETQVGE----RGIQLSGGQKQRISISRAIVKNPSILLLDEATSALD 531
Cdd:PRK11231 97 VAYGR----SPWLSLWGRLSAEdNARVNQAME--QTRINHladrRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 532 ----AESEKIVQEALDRvmvGRTTVVVAHRLSTV-RNADIIAVVGGGKIIESGSHDELIS 586
Cdd:PRK11231 171 inhqVELMRLMRELNTQ---GKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
982-1200 |
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 15220188 982 IELKGVHFSYPSRpdvTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGI-IMIDGQDIKKLKLKSLRRHI 1060
Cdd:COG1119 4 LELRNVTVRRGGK---TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1061 GLVQqePALFA-----TTIYENILYGKEGASE-----SEVMEAAklanAHSFISSLpeGYSTKVGERGIQMSGGQRQRIA 1130
Cdd:COG1119 81 GLVS--PALQLrfprdETVLDVVLSGFFDSIGlyrepTDEQRER----ARELLELL--GLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15220188 1131 IARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRD--RTTVVVAHRLstiknSDMISVI------QDGKIIEQG 1200
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHV-----EEIPPGIthvlllKDGRVVAAG 225
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
982-1201 |
1.13e-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: 103.35 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRPDVTIfSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKlKLKSLRRHIG 1061
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAV-DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEPALFAT-TIYENI-----LYGKEGASESEVMEAAK-----LANAHSFISSLpegystkvgergiqmSGGQRQRIA 1130
Cdd:cd03263 79 YCPQFDALFDElTVREHLrfyarLKGLPKSEIKEEVELLLrvlglTDKANKRARTL---------------SGGMKRKLS 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220188 1131 IARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVVVAHRLSTIKN-SDMISVIQDGKIIEQGS 1201
Cdd:cd03263 144 LAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGS 215
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
996-1210 |
1.21e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 104.74 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 996 DVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQ------DIKKLKLKSLRRHIGLVQQEPAL 1069
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1070 FA-TTIYENILYGKEGASESEVMEAAKLANAHSFISSLPEGYSTKVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEAT 1148
Cdd:PRK14246 102 FPhLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220188 1149 SALDVESERVVQQALDRLMRDRTTVVVAHRLSTI-KNSDMISVIQDGKIIEQGSHN-ILVENKN 1210
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNeIFTSPKN 245
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
982-1196 |
1.67e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 104.81 E-value: 1.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIG 1061
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEP--ALFATTIYENILYGKE--GASESE----VMEAAKLANAHSFISSLPEgystkvgergiQMSGGQRQRIAIAR 1133
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLEnkGIPHEEmkerVNEALELVGMQDFKEREPA-----------RLSGGQKQRVAIAG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15220188 1134 AVLKNPEILLLDEATSALDVESERVVQQALDRLMRDR--TTVVVAHRLSTIKNSDMISVIQDGKI 1196
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1002-1215 |
1.80e-24 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 107.43 E-value: 1.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1002 DFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKL---KLKSLRRH-IGLVQQEPALFA-TTIYE 1076
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKIsdaELREVRRKkIAMVFQSFALMPhMTVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1077 NILYGKE--GASESEVMEAAKLANAHSFISSLPEGYSTkvgergiQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVE 1154
Cdd:PRK10070 126 NTAFGMElaGINAEERREKALDALRQVGLENYAHSYPD-------ELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220188 1155 SERVVQQALDRLM--RDRTTVVVAHRL-STIKNSDMISVIQDGKIIEQGSHNILVENKNGPYSK 1215
Cdd:PRK10070 199 IRTEMQDELVKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
973-1201 |
1.83e-24 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 104.48 E-value: 1.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 973 EELSNVEGTIELKGVHFSYPSRpdvTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLK 1052
Cdd:PRK10575 3 EYTNHSDTTFALRNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1053 LKSLRRHIG-LVQQEPALFATTIYENILYGKE---------GASESE-VMEAAKLAN----AHSFISSLpegystkvger 1117
Cdd:PRK10575 80 SKAFARKVAyLPQQLPAAEGMTVRELVAIGRYpwhgalgrfGAADREkVEEAISLVGlkplAHRLVDSL----------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1118 giqmSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDR--TTVVVAHRLS-TIKNSDMISVIQDG 1194
Cdd:PRK10575 149 ----SGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINmAARYCDYLVALRGG 224
|
....*..
gi 15220188 1195 KIIEQGS 1201
Cdd:PRK10575 225 EMIAQGT 231
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
383-592 |
2.25e-24 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 107.04 E-value: 2.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 383 NFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWL----RGHIGLVNQEPVLFA-TTIRENI 457
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSFALMPhMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 458 MYGKDDATseeITNAAKLSEAISFINNLpeGFETQVGERGIQLSGGQKQRISISRAIVKNPSILLLDEATSALDAESEKI 537
Cdd:PRK10070 128 AFGMELAG---INAEERREKALDALRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15220188 538 VQEALDRVMVG--RTTVVVAHRL-STVRNADIIAVVGGGKIIESGSHDELISNPDGAY 592
Cdd:PRK10070 203 MQDELVKLQAKhqRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
982-1201 |
2.46e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 104.00 E-value: 2.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSrpDVTIFSDFNLLVPSGKSMALVGQSGSGKSSvlsLVLRF---YDPTAGIIMIDGQDIK--KLKLKSL 1056
Cdd:PRK13639 2 LETRDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKST---LFLHFngiLKPTSGEVLIKGEPIKydKKSLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1057 RRHIGLVQQEP--ALFATTIYENILYG--KEGASESEVMEAAKLANAHSFIsslpEGYSTKVGErgiQMSGGQRQRIAIA 1132
Cdd:PRK13639 77 RKTVGIVFQNPddQLFAPTVEEDVAFGplNLGLSKEEVEKRVKEALKAVGM----EGFENKPPH---HLSGGQKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15220188 1133 RAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVVVA-HRLSTI-KNSDMISVIQDGKIIEQGS 1201
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVpVYADKVYVMSDGKIIKEGT 220
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
993-1177 |
2.66e-24 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 102.17 E-value: 2.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 993 SRPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDP---TAGIIMIDGQDIkkLKLKSLRRHIGLVQQEPAL 1069
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRL--TALPAEQRRIGILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1070 FA-TTIYENILYG-----KEGASESEVMEAAKLANAHSFISSLPEgystkvgergiQMSGGQRQRIAIARAVLKNPEILL 1143
Cdd:COG4136 88 FPhLSVGENLAFAlpptiGRAQRRARVEQALEEAGLAGFADRDPA-----------TLSGGQRARVALLRALLAEPRALL 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 15220188 1144 LDEATSALDVE-SERVVQQALDRLmRDRT--TVVVAH 1177
Cdd:COG4136 157 LDEPFSKLDAAlRAQFREFVFEQI-RQRGipALLVTH 192
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
361-588 |
2.70e-24 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 106.57 E-value: 2.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSRPdvvIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKwlRGHIG 440
Cdd:PRK09452 15 VELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 441 LVNQEPVLFA-TTIRENIMYG--KDDATSEEItnAAKLSEAISFINnlPEGFetqvGERGI-QLSGGQKQRISISRAIVK 516
Cdd:PRK09452 90 TVFQSYALFPhMTVFENVAFGlrMQKTPAAEI--TPRVMEALRMVQ--LEEF----AQRKPhQLSGGQQQRVAIARAVVN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15220188 517 NPSILLLDEATSALDAESEKIVQ---EALDRVMvGRTTVVVAH----RLSTvrnADIIAVVGGGKIIESGSHDELISNP 588
Cdd:PRK09452 162 KPKVLLLDESLSALDYKLRKQMQnelKALQRKL-GITFVFVTHdqeeALTM---SDRIVVMRDGRIEQDGTPREIYEEP 236
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
364-556 |
3.35e-24 |
|
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: 102.51 E-value: 3.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 364 KDVTFTYPSRP-DVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLI---ERfyePTDGAVMLDGNDIRYLD----LKWL 435
Cdd:COG4181 12 RGLTKTVGTGAgELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLaglDR---PTSGTVRLAGQDLFALDedarARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 436 RGHIGLVNQEPVLFAT-TIRENIMY-----GKDDATSEeitnAAKLSEAISfinnlpegfetqVGERG----IQLSGGQK 505
Cdd:COG4181 89 ARHVGFVFQSFQLLPTlTALENVMLplelaGRRDARAR----ARALLERVG------------LGHRLdhypAQLSGGEQ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15220188 506 QRISISRAIVKNPSILLLDEATSALD-AESEKIVQ--EALDRVMvGRTTVVVAH 556
Cdd:COG4181 153 QRVALARAFATEPAILFADEPTGNLDaATGEQIIDllFELNRER-GTTLVLVTH 205
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
982-1201 |
3.98e-24 |
|
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: 102.13 E-value: 3.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPsrpDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKL-KSLRRHI 1060
Cdd:cd03224 1 LEVENLNAGYG---KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPhERARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1061 GLVQQEPALFAT-TIYENILYGKEGASESEVmeAAKLANAHSFISSLPEGYSTKVGergiQMSGGQRQRIAIARAVLKNP 1139
Cdd:cd03224 78 GYVPEGRRIFPElTVEENLLLGAYARRRAKR--KARLERVYELFPRLKERRKQLAG----TLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15220188 1140 EILLLDEATSALdveSERVVQQ---ALDRLMRDRTTVVV----AHRLSTIknSDMISVIQDGKIIEQGS 1201
Cdd:cd03224 152 KLLLLDEPSEGL---APKIVEEifeAIRELRDEGVTILLveqnARFALEI--ADRAYVLERGRVVLEGT 215
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
983-1176 |
4.00e-24 |
|
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: 101.56 E-value: 4.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 983 ELKGVHFSYpsRPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGqdiKKLKLKSLRRHIGL 1062
Cdd:cd03226 1 RIENISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1063 VQQEP--ALFATTIYENILYGKEGASES--------EVMEAAKLANAHSFIsslpegystkvgergiqMSGGQRQRIAIA 1132
Cdd:cd03226 76 VMQDVdyQLFTDSVREELLLGLKELDAGneqaetvlKDLDLYALKERHPLS-----------------LSGGQKQRLAIA 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15220188 1133 RAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVVVA 1176
Cdd:cd03226 139 AALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVI 182
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
982-1201 |
4.24e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 103.67 E-value: 4.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRpdvTIF-----SDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDI----KKLK 1052
Cdd:PRK13649 3 INLQNVSYTYQAG---TPFegralFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1053 LKSLRRHIGLVQQ--EPALFATTIYENILYGKE--GASESEVMEAA--KLANAhsfisslpeGYSTKVGERG-IQMSGGQ 1125
Cdd:PRK13649 80 IKQIRKKVGLVFQfpESQLFEETVLKDVAFGPQnfGVSQEEAEALAreKLALV---------GISESLFEKNpFELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15220188 1126 RQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVV-VAHRLSTIKN-SDMISVIQDGKIIEQGS 1201
Cdd:PRK13649 151 MRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
383-603 |
4.60e-24 |
|
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: 105.18 E-value: 4.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 383 NFVIPAGKVVALVGGSGSGKSTMISLI---ERfyePTDGAVMLDG----NDIRYLDLKWLRGHIGLVNQEPVLFAT-TIR 454
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIaglER---PDSGRIRLGGevlqDSARGIFLPPHRRRIGYVFQEARLFPHlSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 455 ENIMYGkddatseeITNAAKLSEAISF---INNLpeGFETQVGERGIQLSGGQKQRISISRAIVKNPSILLLDEATSALD 531
Cdd:COG4148 96 GNLLYG--------RKRAPRAERRISFdevVELL--GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 532 AES--------EKIVQEAldrvmvgRTTVV-VAHRLSTV-RNADIIAVVGGGKIIESGSHDELISNPDgaYSSLLRIQEA 601
Cdd:COG4148 166 LARkaeilpylERLRDEL-------DIPILyVSHSLDEVaRLADHVVLLEQGRVVASGPLAEVLSRPD--LLPLAGGEEA 236
|
..
gi 15220188 602 AS 603
Cdd:COG4148 237 GS 238
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1001-1210 |
5.61e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 103.32 E-value: 5.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1001 SDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDI----KKLKLKSLRRHIGLVQQ--EPALFATTI 1074
Cdd:PRK13646 24 HDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRPVRKRIGMVFQfpESQLFEDTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1075 YENILYGKEGASESevMEAAKlANAHSFISSLpeGYSTKVGERG-IQMSGGQRQRIAIARAVLKNPEILLLDEATSALDV 1153
Cdd:PRK13646 104 EREIIFGPKNFKMN--LDEVK-NYAHRLLMDL--GFSRDVMSQSpFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1154 ESERVVQQALDRLMRD--RTTVVVAHRLSTI-KNSDMISVIQDGKIIEQGSHNILVENKN 1210
Cdd:PRK13646 179 QSKRQVMRLLKSLQTDenKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKDKK 238
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
981-1202 |
5.91e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 102.01 E-value: 5.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 981 TIELKGVHFSYPSrpDVTIFsDFNLLVPSGKSMALVGQSGSGKSSVLSlVLRFYD-PTAGIIMIDG------QDIKKLKL 1053
Cdd:PRK11124 2 SIQLNGINCFYGA--HQALF-DITLDCPQGETLVLLGPSGAGKSSLLR-VLNLLEmPRSGTLNIAGnhfdfsKTPSDKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1054 KSLRRHIGLVQQE----PALfatTIYENILYGK---EGASESEVMEAAK--LANAH--SFISSLPegystkvgergIQMS 1122
Cdd:PRK11124 78 RELRRNVGMVFQQynlwPHL---TVQQNLIEAPcrvLGLSKDQALARAEklLERLRlkPYADRFP-----------LHLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1123 GGQRQRIAIARAVLKNPEILLLDEATSALDVE-SERVVQQALDRLMRDRTTVVVAHRLSTI-KNSDMISVIQDGKIIEQG 1200
Cdd:PRK11124 144 GGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVArKTASRVVYMENGHIVEQG 223
|
..
gi 15220188 1201 SH 1202
Cdd:PRK11124 224 DA 225
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1002-1213 |
6.06e-24 |
|
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: 104.81 E-value: 6.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1002 DFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDI----KKLKLKSLRRHIGLVQQEPALFA-TTIYE 1076
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrKGIFLPPEKRRIGYVFQEARLFPhLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1077 NILYGKegaseSEVMEAAKLANAHSFISSLpeGYSTKVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESE 1156
Cdd:TIGR02142 95 NLRYGM-----KRARPSERRISFERVIELL--GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRK 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1157 RVVQQALDRLMR--DRTTVVVAHRLSTIKN-SDMISVIQDGKIIEQGSHNILVENKNGPY 1213
Cdd:TIGR02142 168 YEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
982-1200 |
6.46e-24 |
|
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: 101.14 E-value: 6.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRpdvTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKlkSLRRHIG 1061
Cdd:cd03268 1 LKTNDLTKTYGKK---RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI--EALRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEPALFAT-TIYENILYGKE--GASESEVMEAAKLANahsfissLPEGYSTKVGergiQMSGGQRQRIAIARAVLKN 1138
Cdd:cd03268 76 ALIEAPGFYPNlTARENLRLLARllGIRKKRIDEVLDVVG-------LKDSAKKKVK----GFSLGMKQRLGIALALLGN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220188 1139 PEILLLDEATSALDVESERVVQQALDRLMRDRTTVVVA-HRLSTI-KNSDMISVIQDGKIIEQG 1200
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISsHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
982-1201 |
6.63e-24 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 102.08 E-value: 6.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPsrpDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIG 1061
Cdd:COG4604 2 IEIKNVSKRYG---GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEPAlFAT--TIYENILYG-------KEGASESEVMEAA----KLAN-AHSFISSLpegystkvgergiqmSGGQRQ 1127
Cdd:COG4604 79 ILRQENH-INSrlTVRELVAFGrfpyskgRLTAEDREIIDEAiaylDLEDlADRYLDEL---------------SGGQRQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1128 RIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRD--RTTVVVAHRLstikN-----SDMISVIQDGKIIEQG 1200
Cdd:COG4604 143 RAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElgKTVVIVLHDI----NfascyADHIVAMKDGRVVAQG 218
|
.
gi 15220188 1201 S 1201
Cdd:COG4604 219 T 219
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
364-584 |
8.32e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 102.79 E-value: 8.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 364 KDVTFTYP--SRPDVvifDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGndiRYLDLK--W-LRGH 438
Cdd:PRK13635 9 EHISFRYPdaATYAL---KDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG---MVLSEEtvWdVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 439 IGLVNQEP--VLFATTIRENIMYGKDDATSEEITNAAKLSEAISFINNlpEGFETQVGERgiqLSGGQKQRISISRAIVK 516
Cdd:PRK13635 83 VGMVFQNPdnQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGM--EDFLNREPHR---LSGGQKQRVAIAGVLAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15220188 517 NPSILLLDEATSALDAESEkivQEALD--RVMV--GRTTVV-VAHRLSTVRNADIIAVVGGGKIIESGSHDEL 584
Cdd:PRK13635 158 QPDIIILDEATSMLDPRGR---REVLEtvRQLKeqKGITVLsITHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
982-1201 |
8.70e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 102.86 E-value: 8.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIG 1061
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEP--ALFATTIYENILYGKE--GASESEVM----EAAKLANAHSFISSLPEgystkvgergiQMSGGQRQRIAIAR 1133
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMEnqGIPREEMIkrvdEALLAVNMLDFKTREPA-----------RLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220188 1134 AVLKNPEILLLDEATSALD----VESERVVQQALDRLmrDRTTVVVAHRLSTIKNSDMISVIQDGKIIEQGS 1201
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDptgrQEIMRVIHEIKEKY--QLTVLSITHDLDEAASSDRILVMKAGEIIKEAA 223
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
996-1201 |
9.09e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 102.01 E-value: 9.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 996 DVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIGLV-QQEPALFATTI 1074
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLpQHHLTPEGITV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1075 YENILYGKE----------GASESEVMEAakLANAHsfISSLPEgystkvgERGIQMSGGQRQRIAIARAVLKNPEILLL 1144
Cdd:PRK11231 94 RELVAYGRSpwlslwgrlsAEDNARVNQA--MEQTR--INHLAD-------RRLTDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15220188 1145 DEATSALDVEServvQQALDRLMRD-----RTTVVVAHRLS-TIKNSDMISVIQDGKIIEQGS 1201
Cdd:PRK11231 163 DEPTTYLDINH----QVELMRLMRElntqgKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGT 221
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
999-1199 |
9.15e-24 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 104.40 E-value: 9.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 999 IFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSlrRHIGLVQQEPALFA-TTIYEN 1077
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHYALFRhMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1078 ILYG----------KEGASESEVMEAAKLANahsfISSLPEGYSTkvgergiQMSGGQRQRIAIARAVLKNPEILLLDEA 1147
Cdd:PRK10851 95 IAFGltvlprrerpNAAAIKAKVTQLLEMVQ----LAHLADRYPA-------QLSGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15220188 1148 TSALDVEservVQQALDRLMRDR------TTVVVAH-RLSTIKNSDMISVIQDGKiIEQ 1199
Cdd:PRK10851 164 FGALDAQ----VRKELRRWLRQLheelkfTSVFVTHdQEEAMEVADRVVVMSQGN-IEQ 217
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
357-588 |
9.33e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 102.57 E-value: 9.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 357 VNGDILFKDVTFTYPSRPDVVIFDkLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGA---VMLDGNDIRYLDLK 433
Cdd:PRK13640 2 KDNIVEFKHVSFTYPDSKKPALND-ISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 434 WLRGHIGLVNQEP--VLFATTIRENIMYGKDDatseeitNAAKLSEAISFINNLPEgfetQVGERGIQ------LSGGQK 505
Cdd:PRK13640 81 DIREKVGIVFQNPdnQFVGATVGDDVAFGLEN-------RAVPRPEMIKIVRDVLA----DVGMLDYIdsepanLSGGQK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 506 QRISISRAIVKNPSILLLDEATSALDAESEKIVQEALDRVMV--GRTTVVVAHRLSTVRNADIIAVVGGGKIIESGSHDE 583
Cdd:PRK13640 150 QRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVE 229
|
....*
gi 15220188 584 LISNP 588
Cdd:PRK13640 230 IFSKV 234
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1009-1218 |
1.03e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 103.51 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1009 SGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIK---KLKLKSLRRHIGLVQQEPalfattiyenilYG---- 1081
Cdd:PRK11308 40 RGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkadPEAQKLLRQKIQIVFQNP------------YGslnp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1082 --KEGASESEVME-------AAKLANAHSFISSL---PEGYstkvgERGIQM-SGGQRQRIAIARAVLKNPEILLLDEAT 1148
Cdd:PRK11308 108 rkKVGQILEEPLLintslsaAERREKALAMMAKVglrPEHY-----DRYPHMfSGGQRQRIAIARALMLDPDVVVADEPV 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15220188 1149 SALDVEservVQ-QALDRLM---RDRTT--VVVAHRLSTIKN-SDMISVIQDGKIIEQGSHNILVENKNGPYSK-LIS 1218
Cdd:PRK11308 183 SALDVS----VQaQVLNLMMdlqQELGLsyVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQaLLS 256
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
376-588 |
1.05e-23 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 104.03 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 376 VVIfDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKwlRGHIGLVNQEPVLFA-TTIR 454
Cdd:PRK11432 20 TVI-DNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFPhMSLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 455 ENIMYG--KDDATSEEItnAAKLSEAISFINnlPEGFEtqvgERGI-QLSGGQKQRISISRAIVKNPSILLLDEATSALD 531
Cdd:PRK11432 97 ENVGYGlkMLGVPKEER--KQRVKEALELVD--LAGFE----DRYVdQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15220188 532 AE-----SEKI--VQEALdrvmvGRTTVVVAHRLS---TVrnADIIAVVGGGKIIESGSHDELISNP 588
Cdd:PRK11432 169 ANlrrsmREKIreLQQQF-----NITSLYVTHDQSeafAV--SDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
361-622 |
1.78e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 101.74 E-value: 1.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSrpDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHIG 440
Cdd:PRK13647 5 IEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 441 LVNQEP--VLFATTIRENIMYG------KDDATSEEITNAAKLSEAISFINNLPEgfetqvgergiQLSGGQKQRISISR 512
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGpvnmglDKDEVERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 513 AIVKNPSILLLDEATSALDAESEKIVQEALDRVMVGRTTVVVA-HRLSTVRN-ADIIAVVGGGKIIESGShDELISNPDG 590
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGD-KSLLTDEDI 230
|
250 260 270
....*....|....*....|....*....|....*
gi 15220188 591 AYSSLLRiqeaaspnlnhtpsLPVSTK---PLPEL 622
Cdd:PRK13647 231 VEQAGLR--------------LPLVAQifeDLPEL 251
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
982-1197 |
1.84e-23 |
|
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: 98.27 E-value: 1.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSrpdVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRH-I 1060
Cdd:cd03216 1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAgI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1061 GLVQQepalfattiyenilygkegasesevmeaaklanahsfisslpegystkvgergiqMSGGQRQRIAIARAVLKNPE 1140
Cdd:cd03216 78 AMVYQ-------------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1141 ILLLDEATSALDV-ESERVVQQaLDRLMRDRTTVV-VAHRLSTIKN-SDMISVIQDGKII 1197
Cdd:cd03216 103 LLILDEPTAALTPaEVERLFKV-IRRLRAQGVAVIfISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
340-596 |
2.42e-23 |
|
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: 101.47 E-value: 2.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 340 QMIERNTEDKTGRKLGNVNGDILFKDvtFTYPSRPdvvIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGA 419
Cdd:cd03291 19 ELLEKAKQENNDRKHSSDDNNLFFSN--LCLVGAP---VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 420 vmldgndIRYldlkwlRGHIGLVNQEPVLFATTIRENIMYG--KDDATSEEITNAAKLSEAISfinNLPEGFETQVGERG 497
Cdd:cd03291 94 -------IKH------SGRISFSSQFSWIMPGTIKENIIFGvsYDEYRYKSVVKACQLEEDIT---KFPEKDNTVLGEGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 498 IQLSGGQKQRISISRAIVKNPSILLLDEATSALDAESEK-IVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVGGGKII 576
Cdd:cd03291 158 ITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKeIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSY 237
|
250 260
....*....|....*....|.
gi 15220188 577 ESGSHDELIS-NPDgaYSSLL 596
Cdd:cd03291 238 FYGTFSELQSlRPD--FSSKL 256
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1002-1179 |
2.58e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 101.01 E-value: 2.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1002 DFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYD--PTA---GIIMIDGQDI--KKLKLKSLRRHIGLVQQEPALFATTI 1074
Cdd:PRK14243 28 NVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGFrveGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPKSI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1075 YENILYGKE----GASESEVMEAAkLANAhsfisSLPEGYSTKVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEATSA 1150
Cdd:PRK14243 108 YDNIAYGARingyKGDMDELVERS-LRQA-----ALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSA 181
|
170 180
....*....|....*....|....*....
gi 15220188 1151 LDVESERVVQQALDRLMRDRTTVVVAHRL 1179
Cdd:PRK14243 182 LDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
992-1200 |
2.71e-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: 2.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 992 PSRPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLV--LRFYDPTAGIIMIDGqdiKKLKLKSLRRHIGLVQQEPAL 1069
Cdd:cd03213 17 PSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLING---RPLDKRSFRKIIGYVPQDDIL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1070 FAT-TIYENILYgkegasesevmeAAKLanahsfisslpegystkvgeRGIqmSGGQRQRIAIARAVLKNPEILLLDEAT 1148
Cdd:cd03213 94 HPTlTVRETLMF------------AAKL--------------------RGL--SGGERKRVSIALELVSNPSLLFLDEPT 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15220188 1149 SALDVESERVVQQALDRLMRD-RTTVVVAHRLST--IKNSDMISVIQDGKIIEQG 1200
Cdd:cd03213 140 SGLDSSSALQVMSLLRRLADTgRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
358-607 |
2.76e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 101.62 E-value: 2.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 358 NGDILFKDVTFTYPSRP--DVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISL-----IERFYEPTDGAVMLDGNDIRYL 430
Cdd:PRK13645 4 SKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLtngliISETGQTIVGDYAIPANLKKIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 431 DLKWLRGHIGLVNQEP--VLFATTIRENIMYGKDDATSEEITNAAKLSEAISFINnLPEGFetqVGERGIQLSGGQKQRI 508
Cdd:PRK13645 84 EVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQ-LPEDY---VKRSPFELSGGQKRRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 509 SISRAIVKNPSILLLDEATSALDAESEKIVQEALDRV--MVGRTTVVVAHRLSTV-RNADIIAVVGGGKIIESGSHDELI 585
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnkEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSPFEIF 239
|
250 260 270
....*....|....*....|....*....|..
gi 15220188 586 SN----------PDGAYSSLLRIQEAASPNLN 607
Cdd:PRK13645 240 SNqelltkieidPPKLYQLMYKLKNKGIDLLN 271
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1003-1206 |
3.08e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 99.66 E-value: 3.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1003 FNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDikKLKLKSLRRHIGLVQQEPALFA-TTIYENILYG 1081
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD--HTTTPPSRRPVSMLFQENNLFShLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1082 -----KEGASESEVMEA-AKLANAHSFISSLPEgystkvgergiQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVES 1155
Cdd:PRK10771 96 lnpglKLNAAQREKLHAiARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSALDPAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15220188 1156 ERVVQQALDRLMRDR--TTVVVAHRLS-TIKNSDMISVIQDGKIIEQGSHNILV 1206
Cdd:PRK10771 165 RQEMLTLVSQVCQERqlTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
364-589 |
3.64e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 100.65 E-value: 3.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 364 KDVTFTYpsRPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHIGLVN 443
Cdd:PRK13652 7 RDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 444 QEP--VLFATTIRENIMYGKDDATSEEITNAAKLSEAISFInnlpeGFETQVGERGIQLSGGQKQRISISRAIVKNPSIL 521
Cdd:PRK13652 85 QNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHML-----GLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15220188 522 LLDEATSALDAESEKIVQEALDRVMV--GRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESGSHDELISNPD 589
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQPD 230
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
998-1215 |
4.19e-23 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 99.82 E-value: 4.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 998 TIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGII-----MIDG-QDIKKLK--LKSLRRHIGLVQQEPAL 1069
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTaRSLSQQKglIRQLRQHVGFVFQNFNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1070 FA-TTIYENILYG-----KEGASESEVMEAAKLANAhsfisslpeGYSTKVGERGIQMSGGQRQRIAIARAVLKNPEILL 1143
Cdd:PRK11264 97 FPhRTVLENIIEGpvivkGEPKEEATARARELLAKV---------GLAGKETSYPRRLSGGQQQRVAIARALAMRPEVIL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220188 1144 LDEATSALDVESERVVQQALDRLMRD-RTTVVVAHRLSTIKN-SDMISVIQDGKIIEQGSHNILVENKNGPYSK 1215
Cdd:PRK11264 168 FDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFADPQQPRTR 241
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
380-606 |
4.75e-23 |
|
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: 104.77 E-value: 4.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 380 DKLNFVIPAGKVVALVGGSGSGKST----MISLIerfyePTDGAVMLDGNDIRYLD---LKWLRGHIGLVNQEPvlFAT- 451
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--FGSl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 452 ----TIRENIMYG----KDDATSEEITN--AAKLSEAisfinnlpeGFETQVGERGI-QLSGGQKQRISISRAIVKNPSI 520
Cdd:COG4172 376 sprmTVGQIIAEGlrvhGPGLSAAERRArvAEALEEV---------GLDPAARHRYPhEFSGGQRQRIAIARALILEPKL 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 521 LLLDEATSALDAESEK-IV------QEALdrvmvGRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESGSHDELISNPDGAY 592
Cdd:COG4172 447 LVLDEPTSALDVSVQAqILdllrdlQREH-----GLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFDAPQHPY 521
|
250
....*....|....*
gi 15220188 593 S-SLLriqeAASPNL 606
Cdd:COG4172 522 TrALL----AAAPLL 532
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
982-1200 |
4.75e-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: 98.98 E-value: 4.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSY-PSRPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRhI 1060
Cdd:cd03266 2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR-L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1061 GLVQQEPALFA-TTIYENI-----LYGKEG-ASESEVMEAAKLANAHSFISSLPEGYSTkvgergiqmsgGQRQRIAIAR 1133
Cdd:cd03266 81 GFVSDSTGLYDrLTARENLeyfagLYGLKGdELTARLEELADRLGMEELLDRRVGGFST-----------GMRQKVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15220188 1134 AVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVVVA-HRLSTIKN-SDMISVIQDGKIIEQG 1200
Cdd:cd03266 150 ALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
959-1194 |
4.88e-23 |
|
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: 100.70 E-value: 4.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 959 ELLDRRTQVVGDTGEelSNVEgtielKGVHFSYPSRPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTA 1038
Cdd:cd03291 19 ELLEKAKQENNDRKH--SSDD-----NNLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1039 GIIMIDGQdikklklkslrrhIGLVQQEPALFATTIYENILYGKEgASESEVMEAAKLANAHSFISSLPEGYSTKVGERG 1118
Cdd:cd03291 92 GKIKHSGR-------------ISFSSQFSWIMPGTIKENIIFGVS-YDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15220188 1119 IQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESER-VVQQALDRLMRDRTTVVVAHRLSTIKNSDMISVIQDG 1194
Cdd:cd03291 158 ITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKeIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
981-1210 |
4.96e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 100.67 E-value: 4.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 981 TIELKGVHFSY-PSRPDVTI-FSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIK----KLKLK 1054
Cdd:PRK13641 2 SIKFENVDYIYsPGTPMEKKgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1055 SLRRHIGLVQQ--EPALFATTIYENILYGKE--GASESEVMEAAKlanahSFISSLpeGYSTKVGERG-IQMSGGQRQRI 1129
Cdd:PRK13641 82 KLRKKVSLVFQfpEAQLFENTVLKDVEFGPKnfGFSEDEAKEKAL-----KWLKKV--GLSEDLISKSpFELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1130 AIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVV-VAHRLSTI-KNSDMISVIQDGKIIEQGSHNILVE 1207
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVIlVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIFS 234
|
...
gi 15220188 1208 NKN 1210
Cdd:PRK13641 235 DKE 237
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
982-1200 |
4.97e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 104.33 E-value: 4.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSrpdVTIFSDFNLLVPSGKSMALVGQSGSGKS---SVLSLVlrfYDPTAGIIMIDGQDIKKLK-LKSLR 1057
Cdd:COG1129 5 LEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKStlmKILSGV---YQPDSGEILLDGEPVRFRSpRDAQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1058 RHIGLVQQEPALFAT-TIYENILYGKEGAS-----ESEVMEAAK--LANAHSFISslPEgysTKVGErgiqMSGGQRQRI 1129
Cdd:COG1129 79 AGIAIIHQELNLVPNlSVAENIFLGREPRRgglidWRAMRRRARelLARLGLDID--PD---TPVGD----LSVAQQQLV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220188 1130 AIARAVLKNPEILLLDEATSAL-DVESERVVQQaLDRLMRDRTTVV-VAHRLSTIKN-SDMISVIQDGKIIEQG 1200
Cdd:COG1129 150 EIARALSRDARVLILDEPTASLtEREVERLFRI-IRRLKAQGVAIIyISHRLDEVFEiADRVTVLRDGRLVGTG 222
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
361-580 |
9.55e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 99.82 E-value: 9.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSRPDV---VIFDkLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYL----DLK 433
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegrALFD-VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 434 WLRGHIGLVNQ--EPVLFATTIRENIMYGKDD-ATSEEitNAAKLS-EAISFINNLPEGFETQVGErgiqLSGGQKQRIS 509
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEETVLKDVAFGPQNfGVSQE--EAEALArEKLALVGISESLFEKNPFE----LSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15220188 510 ISRAIVKNPSILLLDEATSALDAESEKIVQEALDRV-MVGRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESGS 580
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
982-1197 |
1.02e-22 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 104.81 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPS-RPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKL---KLKSLR 1057
Cdd:PRK10535 5 LELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadALAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1058 R-HIGLVQQEPALFA-TTIYENIlygKEGASESEVMEAAKLANAHSFISSLpeGYSTKVGERGIQMSGGQRQRIAIARAV 1135
Cdd:PRK10535 85 ReHFGFIFQRYHLLShLTAAQNV---EVPAVYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220188 1136 LKNPEILLLDEATSALDVESERVVQQALDRLmRDR--TTVVVAHRLSTIKNSDMISVIQDGKII 1197
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQL-RDRghTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
364-533 |
1.45e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 97.17 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 364 KDVTFTYPSRPdvvIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEP---TDGAVMLDGNDIRylDLKWLRGHIG 440
Cdd:COG4136 5 ENLTITLGGRP---LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLT--ALPAEQRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 441 LVNQEPVLFA-TTIRENIMYgkddATSEEITNAAK-------LSEAisfinNLPeGFetqvGERGI-QLSGGQKQRISIS 511
Cdd:COG4136 80 ILFQDDLLFPhLSVGENLAF----ALPPTIGRAQRrarveqaLEEA-----GLA-GF----ADRDPaTLSGGQRARVALL 145
|
170 180
....*....|....*....|..
gi 15220188 512 RAIVKNPSILLLDEATSALDAE 533
Cdd:COG4136 146 RALLAEPRALLLDEPFSKLDAA 167
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
361-589 |
1.47e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 99.04 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSRPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHIG 440
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 441 LVNQEP--VLFATTIRENIMYGKDDATSEEITNAAKLSEAISFINNlpEGFETQVGERgiqLSGGQKQRISISRAIVKNP 518
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGM--QDFKEREPAR---LSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15220188 519 SILLLDEATSALDAESE----KIVQEALDRvmVGRTTVVVAHRLSTVRNADIIAVVGGGKIIESGSHDELISNPD 589
Cdd:PRK13650 160 KIIILDEATSMLDPEGRleliKTIKGIRDD--YQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGN 232
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
361-585 |
1.97e-22 |
|
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: 97.85 E-value: 1.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSRPdvvIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGA-VMLDGNDIRYLDLKWLRGHI 439
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 440 GLVN---QEPVLFATTIRENIMYGKDD-------ATSEEITNAAKLSEAIsfinnlpeGFETQVGERGIQLSGGQKQRIS 509
Cdd:COG1119 81 GLVSpalQLRFPRDETVLDVVLSGFFDsiglyrePTDEQRERARELLELL--------GLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 510 ISRAIVKNPSILLLDEATSALDAESEKIVQEALDRVMV-GRTTVV-VAHRLStvrnaDIIAVVG------GGKIIESGSH 581
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAeGAPTLVlVTHHVE-----EIPPGIThvlllkDGRVVAAGPK 227
|
....
gi 15220188 582 DELI 585
Cdd:COG1119 228 EEVL 231
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
378-594 |
2.27e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 98.63 E-value: 2.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 378 IFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGA-----VMLDGNDI-RYLDLKWLRGHIGLVNQEPVLFAT 451
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIfNYRDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 452 TIRENIMYG---KDDATSEEITNAA--KLSEAisfinNLPEGFETQVGERGIQLSGGQKQRISISRAIVKNPSILLLDEA 526
Cdd:PRK14271 116 SIMDNVLAGvraHKLVPRKEFRGVAqaRLTEV-----GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEP 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15220188 527 TSALDAESEKIVQEALDRVMVGRTTVVVAHRLS-TVRNADIIAVVGGGKIIESGSHDELISNPDGAYSS 594
Cdd:PRK14271 191 TSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETA 259
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
982-1201 |
3.36e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 97.95 E-value: 3.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRPdVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLV---LRFYDPTAGIIMIDGQDIKKLKLKSLRR 1058
Cdd:PRK13640 6 VEFKHVSFTYPDSK-KPALNDISFSIPRGSWTALIGHNGSGKSTISKLInglLLPDDNPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1059 HIGLVQQEP--ALFATTIYENILYGKE--GASESEVMEAAKLANAH----SFISSLPEgystkvgergiQMSGGQRQRIA 1130
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLEnrAVPRPEMIKIVRDVLADvgmlDYIDSEPA-----------NLSGGQKQRVA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15220188 1131 IARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDR--TTVVVAHRLSTIKNSDMISVIQDGKIIEQGS 1201
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
363-534 |
3.85e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.07 E-value: 3.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 363 FKDVTFTYPSRPdvvIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDgNDIRyldlkwlrghIGLV 442
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP-KGLR----------IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 443 NQEPVLFAT-TIRENIM----------------YGKDDATSEEITNAAKLSEAISFIN---------------NLPEG-F 489
Cdd:COG0488 67 PQEPPLDDDlTVLDTVLdgdaelraleaeleelEAKLAEPDEDLERLAELQEEFEALGgweaearaeeilsglGFPEEdL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15220188 490 ETQVGErgiqLSGGQKQRISISRAIVKNPSILLLDEATSALDAES 534
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
364-579 |
4.28e-22 |
|
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: 95.75 E-value: 4.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 364 KDVTFTYPSRPDVvifDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDirYLDLKWLRGHIGLVN 443
Cdd:cd03268 4 NDLTKTYGKKRVL---DDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS--YQKNIEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 444 QEPVLFAT-TIRENI-----MYGKDDATSEEITNAAKLSEAisfinnlpegfetqvGERGI-QLSGGQKQRISISRAIVK 516
Cdd:cd03268 79 EAPGFYPNlTARENLrllarLLGIRKKRIDEVLDVVGLKDS---------------AKKKVkGFSLGMKQRLGIALALLG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15220188 517 NPSILLLDEATSALDAESEKIVQEALDRVM-VGRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESG 579
Cdd:cd03268 144 NPDLLILDEPTNGLDPDGIKELRELILSLRdQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
986-1219 |
5.56e-22 |
|
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: 103.45 E-value: 5.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 986 GVHFSYPSRPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQdikklklkslrrhIGLVQQ 1065
Cdd:TIGR01271 428 GLFFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQ 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1066 EPALFATTIYENILYG--KEGASESEVMEAAKLANAhsfISSLPEGYSTKVGERGIQMSGGQRQRIAIARAVLKNPEILL 1143
Cdd:TIGR01271 495 TSWIMPGTIKDNIIFGlsYDEYRYTSVIKACQLEED---IALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYL 571
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15220188 1144 LDEATSALDVESER-VVQQALDRLMRDRTTVVVAHRLSTIKNSDMISVIQDGKIIEQGSHNILVENKNGPYSKLISL 1219
Cdd:TIGR01271 572 LDSPFTHLDVVTEKeIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLLGL 648
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
57-335 |
6.06e-22 |
|
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: 97.55 E-value: 6.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 57 VFFIFFGKLINIIglaylFPQEASHKVAKYSLDFVYLSVVILFSSWLEVACWMHTGERQAAKIRKAYLRSMLSQDISLFD 136
Cdd:cd18576 14 VFPLLAGQLIDAA-----LGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 137 tEISTGEVISAITSEILVVQDAISEKVGNFMHFISRFIAGFAIGFASVWQISLVTLSIVPFIALAggiyAFVSSGLIVRV 216
Cdd:cd18576 89 -ERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLV----AVLFGRRIRKL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 217 RKS----YVKANEIAEEVIGNVRTVQAFTGEEKAVSSYQGALRNTYNYGRKAGLAKGLGLGSLHFVLFLSWALLIWFTSI 292
Cdd:cd18576 164 SKKvqdeLAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGR 243
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 15220188 293 VVHKGIANGGESFTTMLNVVIAGLSLGQAAPDISTFMRASAAA 335
Cdd:cd18576 244 LVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGAS 286
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
374-576 |
7.57e-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: 93.65 E-value: 7.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 374 PDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGndiryldlkwlrghiglvnqEPVLFATTi 453
Cdd:cd03216 11 GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG--------------------KEVSFASP- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 454 renimygkddatseeitnaaklSEAIsfinnlpegfetqvgERGI----QLSGGQKQRISISRAIVKNPSILLLDEATSA 529
Cdd:cd03216 70 ----------------------RDAR---------------RAGIamvyQLSVGERQMVEIARALARNARLLILDEPTAA 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15220188 530 L-DAESE---KIVQEALDRvmvGRTTVVVAHRLSTVRN-ADIIAVVGGGKII 576
Cdd:cd03216 113 LtPAEVErlfKVIRRLRAQ---GVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
361-586 |
8.63e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 97.16 E-value: 8.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTY-PSRP-DVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLD----LKW 434
Cdd:PRK13646 3 IRFDNVSYTYqKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 435 LRGHIGLVNQ--EPVLFATTIRENIMYGKDD--ATSEEITNAAklseaisFINNLPEGFETQVGERG-IQLSGGQKQRIS 509
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNfkMNLDEVKNYA-------HRLLMDLGFSRDVMSQSpFQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 510 ISRAIVKNPSILLLDEATSALDAESEKIVQEALDRVMV--GRTTVVVAHRLSTV-RNADIIAVVGGGKIIESGSHDELIS 586
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTdeNKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
998-1199 |
1.20e-21 |
|
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: 96.03 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 998 TIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLK---LKSLRRHIGLVQQE------PA 1068
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkqRRAFRRDVQLVFQDspsavnPR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1069 LFATTI----YENILYGKEGASE---SEVMEAAKLANAHsfISSLPEgystkvgergiQMSGGQRQRIAIARAVLKNPEI 1141
Cdd:TIGR02769 105 MTVRQIigepLRHLTSLDESEQKariAELLDMVGLRSED--ADKLPR-----------QLSGGQLQRINIARALAVKPKL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15220188 1142 LLLDEATSALDVESERVVQQALDRLMRDRTT--VVVAHRLSTIKN-SDMISVIQDGKIIEQ 1199
Cdd:TIGR02769 172 IVLDEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSfCQRVAVMDKGQIVEE 232
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
375-565 |
1.41e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 94.78 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 375 DVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHIGLVNQEPVLFATTIR 454
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 455 ENIM--YGKDDATSEEITNAAKLSEaisFinNLPEgfetQVGERGI-QLSGGQKQRISISRAIVKNPSILLLDEATSALD 531
Cdd:PRK10247 99 DNLIfpWQIRNQQPDPAIFLDDLER---F--ALPD----TILTKNIaELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 15220188 532 AESEKIVQEALDRVMVGRTTVV--VAHRLSTVRNAD 565
Cdd:PRK10247 170 ESNKHNVNEIIHRYVREQNIAVlwVTHDKDEINHAD 205
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
998-1200 |
1.79e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 95.93 E-value: 1.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 998 TIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGI-----IMIDGQDIKKLK-LKSLRRHIGLVQQEPALFA 1071
Cdd:PRK14271 35 TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYRdVLEFRRRVGMLFQRPNPFP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1072 TTIYENILYGKEGASESEVMEAAKLANAHSFISSLPEGYSTKVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEATSAL 1151
Cdd:PRK14271 115 MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSAL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15220188 1152 DVESERVVQQALDRLMRDRTTVVVAHRLS-TIKNSDMISVIQDGKIIEQG 1200
Cdd:PRK14271 195 DPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEG 244
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1009-1221 |
1.88e-21 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 95.42 E-value: 1.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1009 SGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIK-------------KLKLKSLRRHIGLVQQEPALFA-TTI 1074
Cdd:PRK10619 30 AGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLLRTRLTMVFQHFNLWShMTV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1075 YENILYGKE---GASESEVMEAAKLanahsfisslpegYSTKVG--ERG-----IQMSGGQRQRIAIARAVLKNPEILLL 1144
Cdd:PRK10619 110 LENVMEAPIqvlGLSKQEARERAVK-------------YLAKVGidERAqgkypVHLSGGQQQRVSIARALAMEPEVLLF 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15220188 1145 DEATSALDVESERVVQQALDRLMRD-RTTVVVAHRLSTIKN-SDMISVIQDGKIIEQGSHNILVENKNGPyskliSLQQ 1221
Cdd:PRK10619 177 DEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGNPQSP-----RLQQ 250
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
729-909 |
1.90e-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: 350019 [Multi-domain] Cd Length: 289 Bit Score: 96.01 E-value: 1.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 729 MGERLTLRVRQKMFSAILRNEIGWFDKvdNTSSMLASRLESDATLLRTIVVDRSTILLENLGLVVTAFIISFILNWRLTL 808
Cdd:cd18575 63 LGERVVADLRKAVFAHLLRLSPSFFET--TRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 809 VVLATYPLIIsghisekIFMQGYGG---NLSKAYL----KANMLAGESISNIRTVVAFCAEEKVLDLYSKELLEPSERSF 881
Cdd:cd18575 141 LVLLVIPLVV-------LPIILFGRrvrRLSRASQdrlaDLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAAL 213
|
170 180
....*....|....*....|....*...
gi 15220188 882 RRGQMAGILYGVSQFFIFSSYGLALWYG 909
Cdd:cd18575 214 RRIRARALLTALVIFLVFGAIVFVLWLG 241
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
361-588 |
1.93e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 95.49 E-value: 1.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSRPdvvIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYE-----PTDGAVMLDGNDI--RYLDLK 433
Cdd:PRK14258 8 IKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIyeRRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 434 WLRGHIGLVNQEPVLFATTIRENIMYG----------KDDATSEEITNAAKLSEAIsfinnlpegfETQVGERGIQLSGG 503
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwrpklEIDDIVESALKDADLWDEI----------KHKIHKSALDLSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 504 QKQRISISRAIVKNPSILLLDEATSALD-AESEKIvqEALDRVMVGR---TTVVVAHRLSTV-RNADIIAVVGG-----G 573
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLDpIASMKV--ESLIQSLRLRselTMVIVSHNLHQVsRLSDFTAFFKGnenriG 232
|
250
....*....|....*
gi 15220188 574 KIIESGSHDELISNP 588
Cdd:PRK14258 233 QLVEFGLTKKIFNSP 247
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
982-1208 |
2.03e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 94.91 E-value: 2.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRpdvTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYD--PTA---GIIMIDGQDIKKLKLKSL 1056
Cdd:PRK14267 5 IETVNLRVYYGSN---HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElnEEArveGEVRLFGRNIYSPDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1057 --RRHIGLVQQEPALFA-TTIYENILYG----KEGASESEVMEAAKLANAHSfisSLPEGYSTKVGERGIQMSGGQRQRI 1129
Cdd:PRK14267 82 evRREVGMVFQYPNPFPhLTIYDNVAIGvklnGLVKSKKELDERVEWALKKA---ALWDEVKDRLNDYPSNLSGGQRQRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1130 AIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVVVAHR-LSTIKNSDMISVIQDGKIIEQGSHNILVEN 1208
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVFEN 238
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
981-1152 |
2.72e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 94.93 E-value: 2.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 981 TIELKGVHFSYP-SRPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKlklKSLRRh 1059
Cdd:COG4525 3 MLTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG---PGADR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1060 iGLVQQEPALFA-TTIYENILYGKEGASeseVMEAAKLANAHSFISslpegystKVG-----ERGI-QMSGGQRQRIAIA 1132
Cdd:COG4525 79 -GVVFQKDALLPwLNVLDNVAFGLRLRG---VPKAERRARAEELLA--------LVGladfaRRRIwQLSGGMRQRVGIA 146
|
170 180
....*....|....*....|
gi 15220188 1133 RAVLKNPEILLLDEATSALD 1152
Cdd:COG4525 147 RALAADPRFLLMDEPFGALD 166
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
705-916 |
2.72e-21 |
|
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: 95.48 E-value: 2.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 705 SILFCCGSVITVIVHTIEHTTF----GIMG---------------------ERLTLRVRQKMFSAILRNEIGWFDKvdNT 759
Cdd:cd18590 14 FIPYYTGRVIDILGGEYQHNAFtsaiGLMClfslgsslsaglrgglfmctlSRLNLRLRHQLFSSLVQQDIGFFEK--TK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 760 SSMLASRLESDATLLRTIVVDRSTILLENLGLVVTAFIISFILNWRLTLVVLATYPLIIsghISEKIFmQGYGGNLSKAY 839
Cdd:cd18590 92 TGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTA---IAQKVY-NTYHQKLSQAV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 840 L----KANMLAGESISNIRTVVAFCAEEKVLDLYSKELLEPSERSFRRGQMAGILYGVSQFFIFSSYGLALWYGSILMEK 915
Cdd:cd18590 168 QdsiaKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQS 247
|
.
gi 15220188 916 G 916
Cdd:cd18590 248 G 248
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1010-1227 |
3.40e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 99.54 E-value: 3.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1010 GKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKL---KLKSLRRHIGLVQQEPalFAT---------TIYE- 1076
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLspgKLQALRRDIQFIFQDP--YASldprqtvgdSIMEp 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1077 ----NILYGKEGASE-SEVMEAAKLANAHSFisSLPEgystkvgergiQMSGGQRQRIAIARAVLKNPEILLLDEATSAL 1151
Cdd:PRK10261 428 lrvhGLLPGKAAAARvAWLLERVGLLPEHAW--RYPH-----------EFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1152 DVESERVVQQALDRLMRDR--TTVVVAHRLSTIKN-SDMISVIQDGKIIEQGSHNILVENKNGPYS-KLIS---LQQRQR 1224
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDFgiAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFENPQHPYTrKLMAavpVADPSR 574
|
...
gi 15220188 1225 HHP 1227
Cdd:PRK10261 575 QRP 577
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
982-1205 |
4.02e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 94.67 E-value: 4.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSrpDVTIFSDFNLLVPSGKSMALVGQSGSGKSSV---LSLVLRfydPTAGIIMIDGQDIKKL-KLKSLR 1057
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLalhLNGLLR---PQKGKVLVSGIDTGDFsKLQGIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1058 RHIGLVQQEP--ALFATTIYENILYGKEGASESEVmEAAKLANahsfiSSLPEGYSTKVGERGIQ-MSGGQRQRIAIARA 1134
Cdd:PRK13644 77 KLVGIVFQNPetQFVGRTVEEDLAFGPENLCLPPI-EIRKRVD-----RALAEIGLEKYRHRSPKtLSGGQGQCVALAGI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15220188 1135 VLKNPEILLLDEATSALDVESERVVQQALDRLMRD-RTTVVVAHRLSTIKNSDMISVIQDGKIIEQGS-HNIL 1205
Cdd:PRK13644 151 LTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGEpENVL 223
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
982-1200 |
4.46e-21 |
|
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: 92.73 E-value: 4.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPsrpDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKlkslRRHIG 1061
Cdd:cd03269 1 LEVENVTKRFG---RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEPALF-ATTIYENILYGKE--GASESEVmeaakLANAHSFISSLpeGYSTKVGERGIQMSGGQRQRIAIARAVLKN 1138
Cdd:cd03269 74 YLPEERGLYpKMKVIDQLVYLAQlkGLKKEEA-----RRRIDEWLERL--ELSEYANKRVEELSKGNQQKVQFIAAVIHD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220188 1139 PEILLLDEATSALDVESERVVQQALDRLMRDRTTVV-VAHRLSTIKN-SDMISVIQDGKIIEQG 1200
Cdd:cd03269 147 PELLILDEPFSGLDPVNVELLKDVIRELARAGKTVIlSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
361-579 |
4.48e-21 |
|
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: 93.20 E-value: 4.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTY-PSRPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGhI 439
Cdd:cd03266 2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR-L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 440 GLVNQEPVLFA-TTIRENI-----MYG-KDDATSEEITNAAKLSEAISFINNLPEGFETqvgergiqlsgGQKQRISISR 512
Cdd:cd03266 81 GFVSDSTGLYDrLTARENLeyfagLYGlKGDELTARLEELADRLGMEELLDRRVGGFST-----------GMRQKVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15220188 513 AIVKNPSILLLDEATSALDAESEKIVQEALDRVMVGRTTVVVA-HRLSTV-RNADIIAVVGGGKIIESG 579
Cdd:cd03266 150 ALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
53-335 |
4.51e-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: 350019 [Multi-domain] Cd Length: 289 Bit Score: 94.86 E-value: 4.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 53 ASVPVFFIFFGKLINiiglaYLFPQEASHKVAKYSLDFVYLSVVILFSSWLEVACWMHTGERQAAKIRKAYLRSMLSQDI 132
Cdd:cd18575 10 AATLALGQGLRLLID-----QGFAAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLRLSP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 133 SLFDTeISTGEVISAITSEILVVQDAISEKVGNFMHFISRFIAGFAIGFASVWQISLVTLSIVPFIALAGGIYAFvssgl 212
Cdd:cd18575 85 SFFET-TRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGR----- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 213 ivRVRKSYVKANE-------IAEEVIGNVRTVQAFTGEEKAVSSYQGALRNTYNYGRKAGLAKGLGLGSLHFVLFLSWAL 285
Cdd:cd18575 159 --RVRRLSRASQDrladlsaFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVF 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 15220188 286 LIWFTSIVVHKGIANGGESFTTMLNVVIAGLSLGQAAPDISTFMRASAAA 335
Cdd:cd18575 237 VLWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAA 286
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
726-929 |
5.66e-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: 94.47 E-value: 5.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 726 FGIMGERLTLRVRQKMFSAILRNEIGWFDKvdNTSSMLASRLESDATLLRTIVVDRSTILLENLGLVVTAFIISFILNWR 805
Cdd:cd18576 60 FARVGERVVADLRKDLYRHLQRLPLSFFHE--RRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 806 LTLVVLATYPLIIsghisekIFMQGYGG---NLSK----AYLKANMLAGESISNIRTVVAFCAEEKVLDLYSKELLEPSE 878
Cdd:cd18576 138 LTLLMLATVPVVV-------LVAVLFGRrirKLSKkvqdELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVK 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15220188 879 RSFRRGQMAGILYGVSQFFIFSSYGLALWYGSILMEKG------LSSFesVMKTFMV 929
Cdd:cd18576 211 LALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGeltagdLVAF--LLYTLFI 265
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
365-579 |
6.01e-21 |
|
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: 92.56 E-value: 6.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 365 DVTFTYPSRPdvVIFDklnFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKwlRGHIGLVNQ 444
Cdd:cd03298 5 KIRFSYGEQP--MHFD---LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 445 EPVLFA-TTIRENIMYGKddatSEEITNAAKLSEAIsfinnlpEGFETQVGERGI------QLSGGQKQRISISRAIVKN 517
Cdd:cd03298 78 ENNLFAhLTVEQNVGLGL----SPGLKLTAEDRQAI-------EVALARVGLAGLekrlpgELSGGERQRVALARVLVRD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15220188 518 PSILLLDEATSALDAeseKIVQEALDRVM-----VGRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESG 579
Cdd:cd03298 147 KPVLLLDEPFAALDP---ALRAEMLDLVLdlhaeTKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
367-588 |
6.10e-21 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 94.13 E-value: 6.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 367 TFTYPS----RPDVVIFDKLNFVIPAGKVVALVGGSGSGKST---MISLIErfyEPTDGAVMLDGNDIRYLDLKWLRGHI 439
Cdd:COG4167 13 TFKYRTglfrRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTlakMLAGII---EPTSGEILINGHKLEYGDYKYRCKHI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 440 GLVNQEPvlfATTIRENIMYGKddatseeitnaaKLSEAISFINNLPEG------FET--QVG------ERGIQ-LSGGQ 504
Cdd:COG4167 90 RMIFQDP---NTSLNPRLNIGQ------------ILEEPLRLNTDLTAEereeriFATlrLVGllpehaNFYPHmLSSGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 505 KQRISISRAIVKNPSILLLDEATSALDA--ESEKI-----VQEALdrvmvGRTTVVVAHRLSTVRN-ADIIAVVGGGKII 576
Cdd:COG4167 155 KQRVALARALILQPKIIIADEALAALDMsvRSQIInlmleLQEKL-----GISYIYVSQHLGIVKHiSDKVLVMHQGEVV 229
|
250
....*....|..
gi 15220188 577 ESGSHDELISNP 588
Cdd:COG4167 230 EYGKTAEVFANP 241
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
41-335 |
7.37e-21 |
|
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: 94.54 E-value: 7.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 41 MALGSIGACIHGASVPVFFIFFGKLINiiglaYLFPQEASHKVAKYSLDFVYLSVVILFSSWLEVACWMHTGERQAAKIR 120
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLID-----DVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 121 KAYLRSMLSQDISLFDtEISTGEVISAITSEILVVQDAISEKVGNFMHFISRFIAGFAIGFASVWQISLVTLSIVPFIAL 200
Cdd:cd07346 76 RDLFRHLQRLSLSFFD-RNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 201 AGGIYAFVSSGLIVRVRKSYVKANEIAEEVIGNVRTVQAFTGEEKAVSSYQGALRNTYNYGRKAGLAKGLGLGSLHFVLF 280
Cdd:cd07346 155 ILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTA 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 15220188 281 LSWALLIWFTSIVVHKGIANGGE--SFTTMLNVVIAglSLGQAAPDISTFMRASAAA 335
Cdd:cd07346 235 LGTALVLLYGGYLVLQGSLTIGElvAFLAYLGMLFG--PIQRLANLYNQLQQALASL 289
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
361-588 |
7.79e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 93.90 E-value: 7.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSRPDVVifDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDI-RYLDLKWLRGHI 439
Cdd:PRK13644 2 IRLENVSYSYPDGTPAL--ENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgDFSKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 440 GLVNQEP--VLFATTIRENIMYGKDDATSEEITNAAKLSEAISFInnlpeGFETQVGERGIQLSGGQKQRISISRAIVKN 517
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEI-----GLEKYRHRSPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220188 518 PSILLLDEATSALDAESEKIVQEALDRVM-VGRTTVVVAHRLSTVRNADIIAVVGGGKIIESGSHDELISNP 588
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLHeKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
370-565 |
9.40e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 91.14 E-value: 9.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 370 YPSRPdvvIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDiryldlkwlrgHIGLVNQ---EP 446
Cdd:NF040873 2 YGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA-----------RVAYVPQrseVP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 447 VLFATTIRENIMYGK-------------DDATSEEITNAAKLseaisfinnlpEGFET-QVGErgiqLSGGQKQRISISR 512
Cdd:NF040873 68 DSLPLTVRDLVAMGRwarrglwrrltrdDRAAVDDALERVGL-----------ADLAGrQLGE----LSGGQRQRALLAQ 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15220188 513 AIVKNPSILLLDEATSALDAESEKIVQEALDR-VMVGRTTVVVAHRLSTVRNAD 565
Cdd:NF040873 133 GLAQEADLLLLDEPTTGLDAESRERIIALLAEeHARGATVVVVTHDLELVRRAD 186
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
997-1201 |
9.44e-21 |
|
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: 92.50 E-value: 9.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 997 VTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKlKSLRRHIGLVQ--QEPALFAT-T 1073
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLP-PHEIARLGIGRtfQIPRLFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1074 IYENilygkegaseseVMEAAKLANAHSFISSLPEGYSTKVGER--------GIQ---------MSGGQRQRIAIARAVL 1136
Cdd:cd03219 92 VLEN------------VMVAAQARTGSGLLLARARREEREARERaeellervGLAdladrpageLSYGQQRRLEIARALA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15220188 1137 KNPEILLLDEATSAL-DVESERVVqQALDRL-MRDRTTVVVAHRLSTIKN-SDMISVIQDGKIIEQGS 1201
Cdd:cd03219 160 TDPKLLLLDEPAAGLnPEETEELA-ELIRELrERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
975-1208 |
1.01e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 93.18 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 975 LSNVEGTIELKGVHFSYPSRpdvTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYD-----PTAGIIMIDGQDI- 1048
Cdd:PRK14258 1 MSKLIPAIKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIy 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1049 -KKLKLKSLRRHIGLVQQEPALFATTIYENILYGKEGASESEVMEAAKLANAHSFISSLPEGYSTKVGERGIQMSGGQRQ 1127
Cdd:PRK14258 78 eRRVNLNRLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1128 RIAIARAVLKNPEILLLDEATSALD----VESERVVQQAldRLMRDRTTVVVAHRLSTIKN-SDMISVIQD-----GKII 1197
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSL--RLRSELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQLV 235
|
250
....*....|.
gi 15220188 1198 EQGSHNILVEN 1208
Cdd:PRK14258 236 EFGLTKKIFNS 246
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
976-1208 |
1.04e-20 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 93.29 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 976 SNVEGTIELKGVHFSYPSRPdvtIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKL---K 1052
Cdd:PRK11831 2 QSVANLVDMRGVSFTRGNRC---IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMsrsR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1053 LKSLRRHIGLVQQEPALFA-TTIYENILYG-------KEGASESEVM---EAAKLANAHSFISSlpegystkvgergiQM 1121
Cdd:PRK11831 79 LYTVRKRMSMLFQSGALFTdMNVFDNVAYPlrehtqlPAPLLHSTVMmklEAVGLRGAAKLMPS--------------EL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1122 SGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDR--TTVVVAHRLSTIKN-SDMISVIQDGKIIE 1198
Cdd:PRK11831 145 SGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALgvTCVVVSHDVPEVLSiADHAYIVADKKIVA 224
|
250
....*....|
gi 15220188 1199 QGSHNILVEN 1208
Cdd:PRK11831 225 HGSAQALQAN 234
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
994-1198 |
1.14e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 93.21 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 994 RPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLK---LKSLRRHIGLVQQEpALF 1070
Cdd:PRK10419 22 HQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQD-SIS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1071 ATTIYENIlygkeGASESEVM-------EAAKLANAHSFISS--LPEGYSTKvgeRGIQMSGGQRQRIAIARAVLKNPEI 1141
Cdd:PRK10419 101 AVNPRKTV-----REIIREPLrhllsldKAERLARASEMLRAvdLDDSVLDK---RPPQLSGGQLQRVCLARALAVEPKL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1142 LLLDEATSALDVESERVVQQALDRLMRDRTT--VVVAHRLSTIKN-SDMISVIQDGKIIE 1198
Cdd:PRK10419 173 LILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
365-586 |
1.20e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 92.34 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 365 DVTFTYPSRPdvVIFDklnFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKwlRGHIGLVNQ 444
Cdd:PRK10771 6 DITWLYHHLP--MRFD---LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 445 EPVLFA-TTIRENIMYGKD---------DATSEEITNAAKLSEaisFINNLPEgfetqvgergiQLSGGQKQRISISRAI 514
Cdd:PRK10771 79 ENNLFShLTVAQNIGLGLNpglklnaaqREKLHAIARQMGIED---LLARLPG-----------QLSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15220188 515 VKNPSILLLDEATSALD----AESEKIVQEALDRVMVgrTTVVVAHRLS-TVRNADIIAVVGGGKIIESGSHDELIS 586
Cdd:PRK10771 145 VREQPILLLDEPFSALDpalrQEMLTLVSQVCQERQL--TLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
383-586 |
1.26e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 97.01 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 383 NFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLK--WLRGhIGLVNQEPVLFAT-TIRENIMY 459
Cdd:COG1129 24 SLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRdaQAAG-IAIIHQELNLVPNlSVAENIFL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 460 GKDDAT------SEEITNAAKLSEAIsfinNLPEGFETQVGErgiqLSGGQKQRISISRAIVKNPSILLLDEATSAL-DA 532
Cdd:COG1129 103 GREPRRgglidwRAMRRRARELLARL----GLDIDPDTPVGD----LSVAQQQLVEIARALSRDARVLILDEPTASLtER 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15220188 533 ESE---KIVQEALDRvmvGRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESG-----SHDELIS 586
Cdd:COG1129 175 EVErlfRIIRRLKAQ---GVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGpvaelTEDELVR 234
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
369-589 |
1.40e-20 |
|
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: 92.22 E-value: 1.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 369 TYPSRPdvvIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDL-KWLRGHIGLVNQEPV 447
Cdd:cd03218 9 RYGKRK---VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYLPQEAS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 448 LFAT-TIRENIMygkddATSEEITNAAKlsEAISFINNLPEGF--ETQVGERGIQLSGGQKQRISISRAIVKNPSILLLD 524
Cdd:cd03218 86 IFRKlTVEENIL-----AVLEIRGLSKK--EREEKLEELLEEFhiTHLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15220188 525 EATSALD----AESEKIVQEALDR---VMVG----RTTVVVAHRlstvrnadiIAVVGGGKIIESGSHDELISNPD 589
Cdd:cd03218 159 EPFAGVDpiavQDIQKIIKILKDRgigVLITdhnvRETLSITDR---------AYIIYEGKVLAEGTPEEIAANEL 225
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
998-1227 |
1.42e-20 |
|
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: 93.38 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 998 TIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDpTAGIIMIDGQDIKKLKLKSLRRHIGLVQQEPALFATTIYEN 1077
Cdd:cd03289 18 AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1078 I-LYGKEgaSESEVMEAAKLANAHSFISSLPEGYSTKVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESE 1156
Cdd:cd03289 97 LdPYGKW--SDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITY 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15220188 1157 RVVQQALDRLMRDRTTVVVAHRLSTIKNSDMISVIQDGKIIEQGSHNILVeNKNGPYSKLISLQQRQRHHP 1227
Cdd:cd03289 175 QVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLL-NEKSHFKQAISPSDRLKLFP 244
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
982-1197 |
1.46e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 92.84 E-value: 1.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVH--FsYPSRPD-VTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRR 1058
Cdd:COG1101 2 LELKNLSktF-NPGTVNeKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1059 HIGLVQQEPAL---FATTIYENIL--YGKeGASESEVM--EAAKLANAHSFISSLPEGY----STKVGergiQMSGGQRQ 1127
Cdd:COG1101 81 YIGRVFQDPMMgtaPSMTIEENLAlaYRR-GKRRGLRRglTKKRRELFRELLATLGLGLenrlDTKVG----LLSGGQRQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15220188 1128 RIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDR--TTVVVAHRLS-TIKNSDMISVIQDGKII 1197
Cdd:COG1101 156 ALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENnlTTLMVTHNMEqALDYGNRLIMMHEGRII 228
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
982-1201 |
1.51e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 93.37 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRPDVtiFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQ--DIKKLKLKSLRRH 1059
Cdd:PRK13636 6 LKVEELNYNYSDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1060 IGLVQQEP--ALFATTIYENILYG--KEGASESEVMEAAKLANAHSFISSLPEGYSTkvgergiQMSGGQRQRIAIARAV 1135
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGavNLKLPEDEVRKRVDNALKRTGIEHLKDKPTH-------CLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15220188 1136 LKNPEILLLDEATSALDVESERVVQQALDRLMR--DRTTVVVAHRLSTIK-NSDMISVIQDGKIIEQGS 1201
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGN 225
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
386-589 |
1.60e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 92.92 E-value: 1.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 386 IPAGKVVALVGGSGSGKSTMI-------SLIERFYepTDGAVMLDGNDI--RYLDLKWLRGHIGLVNQEPVLFATTIREN 456
Cdd:PRK14243 33 IPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGFR--VEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPKSIYDN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 457 IMYGK---------DDATSEEITNAAKLSEAisfinnlpegfETQVGERGIQLSGGQKQRISISRAIVKNPSILLLDEAT 527
Cdd:PRK14243 111 IAYGAringykgdmDELVERSLRQAALWDEV-----------KDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPC 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220188 528 SALDAESEKIVQEALDRVMVGRTTVVVAHRLSTV-RNADIIA------VVGGGKIIESGSHD--ELI-SNPD 589
Cdd:PRK14243 180 SALDPISTLRIEELMHELKEQYTIIIVTHNMQQAaRVSDMTAffnvelTEGGGRYGYLVEFDrtEKIfNSPQ 251
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
983-1201 |
1.62e-20 |
|
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: 91.97 E-value: 1.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 983 ELKGVHFSYPsrpDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSL-RRHIG 1061
Cdd:COG0410 5 EVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEPALFAT-TIYENILYG----KEGASESEVMEAA-----KLAnahsfisslpegysTKVGERGIQMSGGQRQRIAI 1131
Cdd:COG0410 82 YVPEGRRIFPSlTVEENLLLGayarRDRAEVRADLERVyelfpRLK--------------ERRRQRAGTLSGGEQQMLAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15220188 1132 ARAVLKNPEILLLDEATSALdveSERVVQQ---ALDRLMRDRTTVVV----AHRLSTIknSDMISVIQDGKIIEQGS 1201
Cdd:COG0410 148 GRALMSRPKLLLLDEPSLGL---APLIVEEifeIIRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEGT 219
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
380-623 |
2.09e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 93.88 E-value: 2.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 380 DKLNFVIPAGKVVALVGGSGSGKST---MISLIErfyEPTDGAVMLDGNDIRYLD---LKWLRGHIGLVNQEPvlfatti 453
Cdd:PRK11308 32 DGVSFTLERGKTLAVVGESGCGKSTlarLLTMIE---TPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQNP------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 454 renimYG------KDDATSEE-------ITNAAKLSEAISFInnlpegfeTQVGERGIQ-------LSGGQKQRISISRA 513
Cdd:PRK11308 102 -----YGslnprkKVGQILEEpllintsLSAAERREKALAMM--------AKVGLRPEHydryphmFSGGQRQRIAIARA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 514 IVKNPSILLLDEATSALDAEsekIVQEALDRVM-----VGRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESGSHDELISN 587
Cdd:PRK11308 169 LMLDPDVVVADEPVSALDVS---VQAQVLNLMMdlqqeLGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNN 245
|
250 260 270
....*....|....*....|....*....|....*..
gi 15220188 588 PDGAYS-SLLriqeAASPNLNHTPSLPvSTKPLPELP 623
Cdd:PRK11308 246 PRHPYTqALL----SATPRLNPDDRRE-RIKLTGELP 277
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
984-1155 |
2.43e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 96.29 E-value: 2.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 984 LKGVHFSYPSRPdvtIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDgqdikklklKSLRrhIGLV 1063
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---------KGLR--IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1064 QQEPALFAT-TIYENI----------------LYGKEGASESEVMEAAKL-------------ANAHSFISSL---PEGY 1110
Cdd:COG0488 67 PQEPPLDDDlTVLDTVldgdaelraleaeleeLEAKLAEPDEDLERLAELqeefealggweaeARAEEILSGLgfpEEDL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15220188 1111 STKVGErgiqMSGGQRQRIAIARAVLKNPEILLLDEATSALDVES 1155
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
997-1201 |
2.52e-20 |
|
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: 96.29 E-value: 2.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 997 VTIFSDFNLLVPSGKSMALVGQSGSGKS----SVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRR----HIGLVQQEP- 1067
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEPm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1068 ----ALFatTIYENI---LYGKEGASESEVMEAA-------KLANAHSFISSLPEgystkvgergiQMSGGQRQRIAIAR 1133
Cdd:COG4172 103 tslnPLH--TIGKQIaevLRLHRGLSGAAARARAlellervGIPDPERRLDAYPH-----------QLSGGQRQRVMIAM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15220188 1134 AVLKNPEILLLDEATSALDVeserVVQ-QALD---RLMRDRTTVVV--AHRLSTIKN-SDMISVIQDGKIIEQGS 1201
Cdd:COG4172 170 ALANEPDLLIADEPTTALDV----TVQaQILDllkDLQRELGMALLliTHDLGVVRRfADRVAVMRQGEIVEQGP 240
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
364-588 |
2.81e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 92.16 E-value: 2.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 364 KDVTFTYPSRpdvVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLK-WLRGHIGLV 442
Cdd:PRK10575 15 RNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKaFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 443 NQEPVLFATTIRENIMYGK---DDATSE-EITNAAKLSEAISFINNLPegfetqVGERGI-QLSGGQKQRISISRAIVKN 517
Cdd:PRK10575 92 QQLPAAEGMTVRELVAIGRypwHGALGRfGAADREKVEEAISLVGLKP------LAHRLVdSLSGGERQRAWIAMLVAQD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220188 518 PSILLLDEATSALDAESEKIVQEALDRV--MVGRTTVVVAHRLS-TVRNADIIAVVGGGKIIESGSHDELISNP 588
Cdd:PRK10575 166 SRCLLLDEPTSALDIAHQVDVLALVHRLsqERGLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
375-589 |
2.86e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 93.38 E-value: 2.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 375 DVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLD----GNDIRYL------------DLKWLRGH 438
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHelitnpyskkikNFKELRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 439 IGLVNQEP--VLFATTIRENIMYG-------KDDATSEEITNAAKLSEAISFINNLPegFEtqvgergiqLSGGQKQRIS 509
Cdd:PRK13631 118 VSMVFQFPeyQLFKDTIEKDIMFGpvalgvkKSEAKKLAKFYLNKMGLDDSYLERSP--FG---------LSGGQKRRVA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 510 ISRAIVKNPSILLLDEATSALDAESEK-IVQEALDRVMVGRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESGSHDELISN 587
Cdd:PRK13631 187 IAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEIFTD 266
|
..
gi 15220188 588 PD 589
Cdd:PRK13631 267 QH 268
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
361-587 |
3.46e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 92.07 E-value: 3.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSRPD---VVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKW-LR 436
Cdd:PRK13633 5 IKCKNVSYKYESNEEsteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 437 GHIGLVNQEP--VLFATTIRENIMYGKDD--ATSEEITnaAKLSEAISFINNlpegFETQVGERGIqLSGGQKQRISISR 512
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGPENlgIPPEEIR--ERVDESLKKVGM----YEYRRHAPHL-LSGGQKQRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15220188 513 AIVKNPSILLLDEATSALDAESEKIVQEALDRV--MVGRTTVVVAHRLSTVRNADIIAVVGGGKIIESGSHDELISN 587
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLDPSGRREVVNTIKELnkKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
980-1201 |
4.30e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 91.99 E-value: 4.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 980 GTIELKGVHFSYPSRP--DVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLvlrfydpTAGIIMID-GQ---------- 1046
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQL-------TNGLIISEtGQtivgdyaipa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1047 DIKKLK-LKSLRRHIGLVQQEP--ALFATTIYENILYG--KEGASESEVMEaaKLANAHSFISsLPEGYSTKvgeRGIQM 1121
Cdd:PRK13645 78 NLKKIKeVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGpvNLGENKQEAYK--KVPELLKLVQ-LPEDYVKR---SPFEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1122 SGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRD--RTTVVVAHRLSTI-KNSDMISVIQDGKIIE 1198
Cdd:PRK13645 152 SGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVlRIADEVIVMHEGKVIS 231
|
...
gi 15220188 1199 QGS 1201
Cdd:PRK13645 232 IGS 234
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
984-1196 |
4.69e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 91.28 E-value: 4.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 984 LKGVHFSYPSRpdvTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDgqdikKLKLKSLRRHIGLV 1063
Cdd:PRK11247 15 LNAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG-----TAPLAEAREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1064 QQEPALFA-TTIYENI---LYGKEGASESEVMEAAKLANahsfisslpegystKVGERGIQMSGGQRQRIAIARAVLKNP 1139
Cdd:PRK11247 87 FQDARLLPwKKVIDNVglgLKGQWRDAALQALAAVGLAD--------------RANEWPAALSGGQKQRVALARALIHRP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1140 EILLLDEATSALDVESERVVQQALDRLMRDR--TTVVVAHRLS-TIKNSDMISVIQDGKI 1196
Cdd:PRK11247 153 GLLLLDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
366-558 |
4.71e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 91.30 E-value: 4.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 366 VTFtYPSRPD-VVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDlKWLR-GHIGLVN 443
Cdd:COG1101 9 KTF-NPGTVNeKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLP-EYKRaKYIGRVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 444 QEPVL---FATTIRENIM------------YGKDDATSEEItnAAKLSEaisfinnLPEGFE----TQVGergiQLSGGQ 504
Cdd:COG1101 87 QDPMMgtaPSMTIEENLAlayrrgkrrglrRGLTKKRRELF--RELLAT-------LGLGLEnrldTKVG----LLSGGQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15220188 505 KQRISISRAIVKNPSILLLDEATSALDAESEKIVQEALDRVmVGR---TTVVVAHRL 558
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKI-VEEnnlTTLMVTHNM 209
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
386-588 |
4.76e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 93.22 E-value: 4.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 386 IPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKwlRGHIGLVNQEPVLFA-TTIRENIMYG---- 460
Cdd:PRK10851 25 IPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFRhMTVFDNIAFGltvl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 461 --KDDATSEEI-TNAAKLSEAISfINNLPEGFETQvgergiqLSGGQKQRISISRAIVKNPSILLLDEATSALDAESEKI 537
Cdd:PRK10851 103 prRERPNAAAIkAKVTQLLEMVQ-LAHLADRYPAQ-------LSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15220188 538 VQEALDRVM--VGRTTVVVAH-RLSTVRNADIIAVVGGGKIIESGSHDELISNP 588
Cdd:PRK10851 175 LRRWLRQLHeeLKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
372-632 |
5.35e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 94.14 E-value: 5.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 372 SRPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHIGLVNQEPVL-FA 450
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 451 TTIRENIMYGK-------DDATSeeiTNAAKLSEAISfinnlpEGFETQVGERGI-QLSGGQKQRISISRAIVKNPSILL 522
Cdd:PRK09536 92 FDVRQVVEMGRtphrsrfDTWTE---TDRAAVERAME------RTGVAQFADRPVtSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 523 LDEATSALDAESE----KIVQEALDRvmvGRTTVVVAHRLS-TVRNADIIAVVGGGKIIESGSHDELISNPDgaysslLR 597
Cdd:PRK09536 163 LDEPTASLDINHQvrtlELVRRLVDD---GKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVLTADT------LR 233
|
250 260 270
....*....|....*....|....*....|....*...
gi 15220188 598 IQEAASPNLNHTPSL-PVSTKPLPELPITETTS--SIH 632
Cdd:PRK09536 234 AAFDARTAVGTDPATgAPTVTPLPDPDRTEAAAdtRVH 271
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
1003-1201 |
6.46e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 90.67 E-value: 6.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1003 FNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYdPTAGIIMIDGQDIKKLKLKSLRRHIG-LVQQEPALFATTIYENI-LY 1080
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAyLSQQQSPPFAMPVFQYLaLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1081 GKEGASESEVMEA-AKLANAHSFISSLPegystkvgeRGI-QMSGGQRQRIAIARAVLK-----NPE--ILLLDEATSAL 1151
Cdd:COG4138 94 QPAGASSEAVEQLlAQLAEALGLEDKLS---------RPLtQLSGGEWQRVRLAAVLLQvwptiNPEgqLLLLDEPMNSL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15220188 1152 DveserVVQQ-ALDRLMRD-----RTTVVVAHRLS-TIKNSDMISVIQDGKIIEQGS 1201
Cdd:COG4138 165 D-----VAQQaALDRLLRElcqqgITVVMSSHDLNhTLRHADRVWLLKQGKLVASGE 216
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
361-582 |
6.52e-20 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 90.46 E-value: 6.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSrpDVVIFDkLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNdirYLDLK------- 433
Cdd:PRK11124 3 IQLNGINCFYGA--HQALFD-ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGN---HFDFSktpsdka 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 434 --WLRGHIGLVNQEPVLFA-TTIRENIM--------YGKDDATSE--EITNAAKLSEaisFINNLPegfetqvgergIQL 500
Cdd:PRK11124 77 irELRRNVGMVFQQYNLWPhLTVQQNLIeapcrvlgLSKDQALARaeKLLERLRLKP---YADRFP-----------LHL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 501 SGGQKQRISISRAIVKNPSILLLDEATSALDAE-SEKIVQEALDRVMVGRTTVVVAHRLSTVRN-ADIIAVVGGGKIIES 578
Cdd:PRK11124 143 SGGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQ 222
|
....
gi 15220188 579 GSHD 582
Cdd:PRK11124 223 GDAS 226
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
361-608 |
9.47e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 90.95 E-value: 9.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTY-PSRP--DVVIFDkLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLdgNDI------RYLD 431
Cdd:PRK13643 2 IKFEKVNYTYqPNSPfaSRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV--GDIvvsstsKQKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 432 LKWLRGHIGLVNQEP--VLFATTIRENIMYGKDD--ATSEEITNAAklSEAISFInnlpeGFETQVGERG-IQLSGGQKQ 506
Cdd:PRK13643 79 IKPVRKKVGVVFQFPesQLFEETVLKDVAFGPQNfgIPKEKAEKIA--AEKLEMV-----GLADEFWEKSpFELSGGQMR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 507 RISISRAIVKNPSILLLDEATSALDAESEKIVQEALDRV-MVGRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESGSHDEL 584
Cdd:PRK13643 152 RVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDV 231
|
250 260
....*....|....*....|....
gi 15220188 585 ISNPDgayssLLRIQEAASPNLNH 608
Cdd:PRK13643 232 FQEVD-----FLKAHELGVPKATH 250
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
982-1211 |
9.53e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 92.20 E-value: 9.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRPdvtIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKlKLKSLRRHIG 1061
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEPAL-FATTIYENIL-YGKEGASESEVMEAAklanahsfISSLPE--GYSTKVGERGIQMSGGQRQRIAIARAVLK 1137
Cdd:PRK13536 118 VVPQFDNLdLEFTVRENLLvFGRYFGMSTREIEAV--------IPSLLEfaRLESKADARVSDLSGGMKRRLTLARALIN 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15220188 1138 NPEILLLDEATSALDVESERVVQQALDRLM-RDRTTVVVAHRLSTIKN-SDMISVIQDGKIIEQGSHNILVENKNG 1211
Cdd:PRK13536 190 DPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALIDEHIG 265
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
364-598 |
9.77e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 91.06 E-value: 9.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 364 KDVTFTYPSRPDVVifDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRY--LDLKWLRGHIGL 441
Cdd:PRK13636 9 EELNYNYSDGTHAL--KGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYsrKGLMKLRESVGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 442 VNQEP--VLFATTIRENIMYG------KDDATSEEITNAAKLSeAISFINNLPEGFetqvgergiqLSGGQKQRISISRA 513
Cdd:PRK13636 87 VFQDPdnQLFSASVYQDVSFGavnlklPEDEVRKRVDNALKRT-GIEHLKDKPTHC----------LSFGQKKRVAIAGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 514 IVKNPSILLLDEATSALD----AESEKIVQEALDRvmVGRTTVVVAHRLSTVR-NADIIAVVGGGKIIESGSHDELISNP 588
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKE--LGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
250
....*....|
gi 15220188 589 DGAYSSLLRI 598
Cdd:PRK13636 234 EMLRKVNLRL 243
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
981-1200 |
1.24e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 92.98 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 981 TIELKGVHFSypsRPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHI 1060
Cdd:PRK09536 3 MIDVSDLSVE---FGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1061 GLVQQEPAL-FATTIYENILYGK----------EGASESEVMEAAKLANAHSFIsslpegystkvgERGI-QMSGGQRQR 1128
Cdd:PRK09536 80 ASVPQDTSLsFEFDVRQVVEMGRtphrsrfdtwTETDRAAVERAMERTGVAQFA------------DRPVtSLSGGERQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220188 1129 IAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVVVA-HRLS-TIKNSDMISVIQDGKIIEQG 1200
Cdd:PRK09536 148 VLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAiHDLDlAARYCDELVLLADGRVRAAG 221
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
982-1201 |
1.24e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 90.95 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSY-PSRPDVT-IFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDgqDI------KKLKL 1053
Cdd:PRK13643 2 IKFEKVNYTYqPNSPFASrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG--DIvvsstsKQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1054 KSLRRHIGLVQQEP--ALFATTIYENILYGKE----GASESEVMEAAKLANAhsfisslpeGYSTKVGERG-IQMSGGQR 1126
Cdd:PRK13643 80 KPVRKKVGVVFQFPesQLFEETVLKDVAFGPQnfgiPKEKAEKIAAEKLEMV---------GLADEFWEKSpFELSGGQM 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15220188 1127 QRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRD-RTTVVVAHRLSTIKN-SDMISVIQDGKIIEQGS 1201
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT 227
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
981-1201 |
1.27e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 89.76 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 981 TIELKGVHFSypsrPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDP----TAGIIMIDGQDIKKLKLKSl 1056
Cdd:PRK10418 4 QIELRNIALQ----AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALRG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1057 rRHIGLVQQEP-ALF------ATTIYENIL-YGKEG--ASESEVMEAAKLANAHSFISSLPegystkvgergIQMSGGQR 1126
Cdd:PRK10418 79 -RKIATIMQNPrSAFnplhtmHTHARETCLaLGKPAddATLTAALEAVGLENAARVLKLYP-----------FEMSGGML 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15220188 1127 QRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRT--TVVVAHRLSTI-KNSDMISVIQDGKIIEQGS 1201
Cdd:PRK10418 147 QRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIVEQGD 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
377-589 |
1.34e-19 |
|
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: 89.27 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 377 VIFDkLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYL--DLKWLRGhIGLVNQEPVLFAT-TI 453
Cdd:COG0410 18 VLHG-VSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLppHRIARLG-IGYVPEGRRIFPSlTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 454 RENIM---YGKDDAtseeitnaAKLSEAISFINNL-PEgfetqVGER----GIQLSGGQKQRISISRAIVKNPSILLLDE 525
Cdd:COG0410 96 EENLLlgaYARRDR--------AEVRADLERVYELfPR-----LKERrrqrAGTLSGGEQQMLAIGRALMSRPKLLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15220188 526 ATSALdaeSEKIVQEALDRVMV----GRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESGSHDELISNPD 589
Cdd:COG0410 163 PSLGL---APLIVEEIFEIIRRlnreGVTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
982-1169 |
1.41e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 89.76 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRPdvtIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKlklKSLRRhiG 1061
Cdd:PRK11248 2 LQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG---PGAER--G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEPALFA-TTIYENILYGKEGASeseVMEAAKLANAHSFISSLP-EGYstkvGERGI-QMSGGQRQRIAIARAVLKN 1138
Cdd:PRK11248 74 VVFQNEGLLPwRNVQDNVAFGLQLAG---VEKMQRLEIAHQMLKKVGlEGA----EKRYIwQLSGGQRQRVGIARALAAN 146
|
170 180 190
....*....|....*....|....*....|.
gi 15220188 1139 PEILLLDEATSALDVESERVVQQALDRLMRD 1169
Cdd:PRK11248 147 PQLLLLDEPFGALDAFTREQMQTLLLKLWQE 177
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
364-581 |
1.45e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 94.41 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 364 KDVTFTYPS-RPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWL----RGH 438
Cdd:PRK10535 8 KDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 439 IGLVNQEPVLFA-TTIRENIMYGKDDATSEEitnAAKLSEAISFINNLpeGFETQVGERGIQLSGGQKQRISISRAIVKN 517
Cdd:PRK10535 88 FGFIFQRYHLLShLTAAQNVEVPAVYAGLER---KQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15220188 518 PSILLLDEATSALDAESEKIVQEALDRVM-VGRTTVVVAHRLSTVRNADIIAVVGGGKII-ESGSH 581
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAAQAERVIEIRDGEIVrNPPAQ 228
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
382-589 |
1.45e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 89.52 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 382 LNFVIPAGKVVALVGGSGSGKSTMISLIERFYE-----PTDGAVMLDGNDIRYLDLKWL--RGHIGLVNQEPVLFA-TTI 453
Cdd:PRK14267 23 VDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPIevRREVGMVFQYPNPFPhLTI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 454 RENIMYGK------------DDATSEEITNAAKLSEAISFINNLPEgfetqvgergiQLSGGQKQRISISRAIVKNPSIL 521
Cdd:PRK14267 103 YDNVAIGVklnglvkskkelDERVEWALKKAALWDEVKDRLNDYPS-----------NLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15220188 522 LLDEATSALDAESEKIVQEALDRVMVGRTTVVVAHR-LSTVRNADIIAVVGGGKIIESGSHDELISNPD 589
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVFENPE 240
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
981-1201 |
1.51e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 89.83 E-value: 1.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 981 TIELKGVHFSYPSRpdvTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHI 1060
Cdd:PRK13548 2 MLEARNLSVRLGGR---TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1061 GLVQQEPAL-FATTIYENILYGKEGASES---------EVMEAAKLAN-AHSFISSLpegystkvgergiqmSGGQRQRI 1129
Cdd:PRK13548 79 AVLPQHSSLsFPFTVEEVVAMGRAPHGLSraeddalvaAALAQVDLAHlAGRDYPQL---------------SGGEQQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1130 AIARaVL-------KNPEILLLDEATSALDVEServvQQALDRLMRDRTT------VVVAHRLstikN-----SDMISVI 1191
Cdd:PRK13548 144 QLAR-VLaqlwepdGPPRWLLLDEPTSALDLAH----QHHVLRLARQLAHerglavIVVLHDL----NlaaryADRIVLL 214
|
250
....*....|
gi 15220188 1192 QDGKIIEQGS 1201
Cdd:PRK13548 215 HQGRLVADGT 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
982-1209 |
1.54e-19 |
|
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: 89.14 E-value: 1.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRpdvTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKL-KSLRRHI 1060
Cdd:cd03218 1 LRAENLSKRYGKR---KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1061 GLVQQEPALFAT-TIYENILygkegasesEVMEAAKLANA--HSFISSLPEGYS-TKVGER-GIQMSGGQRQRIAIARAV 1135
Cdd:cd03218 78 GYLPQEASIFRKlTVEENIL---------AVLEIRGLSKKerEEKLEELLEEFHiTHLRKSkASSLSGGERRRVEIARAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15220188 1136 LKNPEILLLDEATSALDVESERVVQQALDRLmRDRTTVVVA--HRLS-TIKNSDMISVIQDGKIIEQGSHNILVENK 1209
Cdd:cd03218 149 ATNPKFLLLDEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLItdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
727-929 |
2.09e-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: 90.30 E-value: 2.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 727 GIMGERLTLRVRQKMFSAILRNEIGWFDKvdNTSSMLASRLESDATLLRTIVVDRSTILLENLGLVVTAFIISFILNWRL 806
Cdd:cd18574 67 SVVGERVAARLRNDLFSSLLRQDIAFFDT--HRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 807 TLVVLATYPLIIsghisekIFMQGYGG---NLSKA----YLKANMLAGESISNIRTVVAFCAEEKVLDLYSKELLEPSER 879
Cdd:cd18574 145 TLLLLVIVPVVV-------LVGTLYGSflrKLSRRaqaqVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKL 217
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15220188 880 SFRRGQMAGILYGVSQFFIFSSYGLALWYGSILMEKGLSSFESVMkTFMV 929
Cdd:cd18574 218 NEKLGLGIGIFQGLSNLALNGIVLGVLYYGGSLVSRGELTAGDLM-SFLV 266
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
359-586 |
2.32e-19 |
|
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: 89.53 E-value: 2.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 359 GDILFKDVTFTYPSRPDVVIfDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEpTDGAVMLDGNDIRYLDLKWLRGH 438
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVL-ENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 439 IGLVNQEPVLFATTIRENI-MYGKddATSEEITNAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRISISRAIVKN 517
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLdPYGK--WSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15220188 518 PSILLLDEATSALDAESEKIVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVGGGKIIESGSHDELIS 586
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLN 225
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
996-1201 |
2.41e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 90.68 E-value: 2.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 996 DVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMID----GQDI-----------KKLK-LKSLRRH 1059
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKnnhelitnpysKKIKnFKELRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1060 IGLVQQEP--ALFATTIYENILYGKEGASESEVmEAAKLANAHSFISSLPEGYStkvgERG-IQMSGGQRQRIAIARAVL 1136
Cdd:PRK13631 118 VSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKS-EAKKLAKFYLNKMGLDDSYL----ERSpFGLSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15220188 1137 KNPEILLLDEATSALDVESER-VVQQALDRLMRDRTTVVVAHRLSTI-KNSDMISVIQDGKIIEQGS 1201
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGT 259
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
375-580 |
2.62e-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: 87.58 E-value: 2.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 375 DVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERF--YEPTDGAVMLDGNDIRYL--DLKWLRGhIGLVNQEPVLFa 450
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLppEERARLG-IFLAFQYPPEI- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 451 ttirenimygkddatsEEITNAaklseaiSFINNLPEGFetqvgergiqlSGGQKQRISISRAIVKNPSILLLDEATSAL 530
Cdd:cd03217 90 ----------------PGVKNA-------DFLRYVNEGF-----------SGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15220188 531 DAESEKIVQEALDRVM-VGRTTVVVAH--RLSTVRNADIIAVVGGGKIIESGS 580
Cdd:cd03217 136 DIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGD 188
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
375-584 |
2.91e-19 |
|
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: 87.81 E-value: 2.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 375 DVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYlDLKWLRGHIGLVNQEPVL-FATTI 453
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVdDELTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 454 RENI-----MYGKDDATSEEitnaaKLSEAISFInNLPEGFETQVGergiQLSGGQKQRISISRAIVKNPSILLLDEATS 528
Cdd:cd03265 91 WENLyiharLYGVPGAERRE-----RIDELLDFV-GLLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15220188 529 ALDAESE----KIVQEALDRvmVGRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESGSHDEL 584
Cdd:cd03265 161 GLDPQTRahvwEYIEKLKEE--FGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
380-556 |
3.95e-19 |
|
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: 87.91 E-value: 3.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 380 DKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDI------------RYLDLKWLrghiglvnqepv 447
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQItepgpdrmvvfqNYSLLPWL------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 448 lfatTIRENIMYGKD----DATSEEitNAAKLSEAISFINnLPEGFETQVGergiQLSGGQKQRISISRAIVKNPSILLL 523
Cdd:TIGR01184 70 ----TVRENIALAVDrvlpDLSKSE--RRAIVEEHIALVG-LTEAADKRPG----QLSGGMKQRVAIARALSIRPKVLLL 138
|
170 180 190
....*....|....*....|....*....|....*
gi 15220188 524 DEATSALDAESEKIVQEALDRVM--VGRTTVVVAH 556
Cdd:TIGR01184 139 DEPFGALDALTRGNLQEELMQIWeeHRVTVLMVTH 173
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
996-1201 |
4.51e-19 |
|
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: 87.43 E-value: 4.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 996 DVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKlKLKSLRRHIGLVQQEPAL-FATTI 1074
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVdDELTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1075 YENI-----LYGKEGASESE-VMEAAKLANAHSFISSLPEGYStkvgergiqmsGGQRQRIAIARAVLKNPEILLLDEAT 1148
Cdd:cd03265 91 WENLyiharLYGVPGAERRErIDELLDFVGLLEAADRLVKTYS-----------GGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15220188 1149 SALDVESERVVQQALDRLMRDRTTVVVahrLST------IKNSDMISVIQDGKIIEQGS 1201
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEEFGMTIL---LTThymeeaEQLCDRVAIIDHGRIIAEGT 215
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
996-1211 |
4.66e-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: 86.81 E-value: 4.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 996 DVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRF--YDPTAGIIMIDGQDIKKLKL-KSLRRHIGLVQQEPALFat 1072
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPeERARLGIFLAFQYPPEI-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1073 tiyenilygkegasesevmEAAKLANahsFISSLPEGYStkvgergiqmsGGQRQRIAIARAVLKNPEILLLDEATSALD 1152
Cdd:cd03217 90 -------------------PGVKNAD---FLRYVNEGFS-----------GGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15220188 1153 VESERVVQQALDRLMRDRTTV-VVAH--RLSTIKNSDMISVIQDGKIIEQGSHNILVE-NKNG 1211
Cdd:cd03217 137 IDALRLVAEVINKLREEGKSVlIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKELALEiEKKG 199
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
379-596 |
4.69e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 88.44 E-value: 4.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 379 FDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDL---------KWLRGHIGLVNQEP--- 446
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLyalseaerrRLLRTEWGFVHQHPrdg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 447 ----VLFATTIRENIM------YGKDDATSE------EItnaaklseAISFINNLPEGFetqvgergiqlSGGQKQRISI 510
Cdd:PRK11701 102 lrmqVSAGGNIGERLMavgarhYGDIRATAGdwlervEI--------DAARIDDLPTTF-----------SGGMQQRLQI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 511 SRAIVKNPSILLLDEATSALDAEsekiVQ-EALD--RVMV---GRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESGSHDE 583
Cdd:PRK11701 163 ARNLVTHPRLVFMDEPTGGLDVS----VQaRLLDllRGLVrelGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESGLTDQ 238
|
250
....*....|...
gi 15220188 584 LISNPDGAYSSLL 596
Cdd:PRK11701 239 VLDDPQHPYTQLL 251
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
367-579 |
4.71e-19 |
|
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: 87.20 E-value: 4.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 367 TFTYPSRPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLkwlrgHIGLvnqEP 446
Cdd:cd03220 26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGL-----GGGF---NP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 447 VLfatTIRENI-----MYGKDDAtseEItnAAKLSEAISFiNNLPEGFETQVGErgiqLSGGQKQRISISRAIVKNPSIL 521
Cdd:cd03220 98 EL---TGRENIylngrLLGLSRK---EI--DEKIDEIIEF-SELGDFIDLPVKT----YSSGMKARLAFAIATALEPDIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 522 LLDEATSALDAE-SEKIVQEALDRVMVGRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESG 579
Cdd:cd03220 165 LIDEVLAVGDAAfQEKCQRRLRELLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
364-545 |
6.28e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 88.00 E-value: 6.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 364 KDVTFTYP-SRPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDI------Ryldlkwlr 436
Cdd:COG4525 7 RHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgpgadR-------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 437 ghiGLVNQEPVLFA-TTIRENI-----MYGKDDATSEEItnAAKLSEAIsfinnlpeGFEtQVGERGI-QLSGGQKQRIS 509
Cdd:COG4525 79 ---GVVFQKDALLPwLNVLDNVafglrLRGVPKAERRAR--AEELLALV--------GLA-DFARRRIwQLSGGMRQRVG 144
|
170 180 190
....*....|....*....|....*....|....*.
gi 15220188 510 ISRAIVKNPSILLLDEATSALDAESEKIVQEALDRV 545
Cdd:COG4525 145 IARALAADPRFLLMDEPFGALDALTREQMQELLLDV 180
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
376-586 |
6.78e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 91.65 E-value: 6.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 376 VVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNdiRYLDLKWLRGH---IGLVNQEPVLFAT- 451
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGN--PCARLTPAKAHqlgIYLVPQEPLLFPNl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 452 TIRENIMYG--KDDATSEEITnaAKLSEAISFINnlpegFETQVGergiQLSGGQKQRISISRAIVKNPSILLLDEATSA 529
Cdd:PRK15439 102 SVKENILFGlpKRQASMQKMK--QLLAALGCQLD-----LDSSAG----SLEVADRQIVEILRGLMRDSRILILDEPTAS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15220188 530 LD-AESEKIVQE--ALDRVMVGrtTVVVAHRLSTVRN-ADIIAVVGGGKIIESG-----SHDELIS 586
Cdd:PRK15439 171 LTpAETERLFSRirELLAQGVG--IVFISHKLPEIRQlADRISVMRDGTIALSGktadlSTDDIIQ 234
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
998-1215 |
7.68e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 91.69 E-value: 7.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 998 TIFSDFNLLVPSGKSMALVGQSGSGKS-SVLSlVLRFYdPT------AGIIMIDGQDIKKLKLKSLRR----HIGLVQQE 1066
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALS-ILRLL-PSppvvypSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1067 PALFATTIY--ENILY---------GKEgASESEV---MEAAKLANAHSFISSLPEgystkvgergiQMSGGQRQRIAIA 1132
Cdd:PRK15134 101 PMVSLNPLHtlEKQLYevlslhrgmRRE-AARGEIlncLDRVGIRQAAKRLTDYPH-----------QLSGGERQRVMIA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1133 RAVLKNPEILLLDEATSALDVESERVVQQALDRLMR--DRTTVVVAHRLSTIKN-SDMISVIQDGKIIEQGSHNILVENK 1209
Cdd:PRK15134 169 MALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFSAP 248
|
....*.
gi 15220188 1210 NGPYSK 1215
Cdd:PRK15134 249 THPYTQ 254
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
981-1201 |
8.59e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 88.24 E-value: 8.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 981 TIELKGVHFSYPsrpDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKlkslRRHI 1060
Cdd:COG4152 1 MLELKGLTKRFG---DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1061 GLVQQEPALFAT-TIYENILY-GK-EGASESEVMEAA-----KLAnahsfissLPEGYSTKVGErgiqMSGGQRQRIAIA 1132
Cdd:COG4152 74 GYLPEERGLYPKmKVGEQLVYlARlKGLSKAEAKRRAdewleRLG--------LGDRANKKVEE----LSKGNQQKVQLI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15220188 1133 RAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVVVA-HRLSTI-KNSDMISVIQDGKIIEQGS 1201
Cdd:COG4152 142 AALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSsHQMELVeELCDRIVIINKGRKVLSGS 212
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
128-557 |
8.76e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 91.79 E-value: 8.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 128 LSQDISLFdTEISTGEVISAITSeilVVQdaisekvgnfmhfisrfiagfAIGFASV-WQIS-LVTLSIVPFIALAGG-- 203
Cdd:COG4178 130 IAEDIRLF-TETTLSLSLGLLSS---VVT---------------------LISFIGIlWSLSgSLTFTLGGYSITIPGym 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 204 -----IYAFVSSGLIVRVRKSYVKAN------------------EIAEEVignvrtvqAFTGEEKAvssYQGALRNTY-- 258
Cdd:COG4178 185 vwaalIYAIIGTLLTHLIGRPLIRLNfeqqrreadfrfalvrvrENAESI--------ALYRGEAA---ERRRLRRRFda 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 259 ---NYGRKAGLAKGLGLgslhFVLFLSWALLIwFTSIVVhkgianggesfttmLNVVIAG-LSLG---QAApdiSTFMR- 330
Cdd:COG4178 254 viaNWRRLIRRQRNLTF----FTTGYGQLAVI-FPILVA--------------APRYFAGeITLGglmQAA---SAFGQv 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 331 ASAAAYPIFQM---------IER------------NTEDKTGRKLGNVNGDILFKDVTFTYPSrpDVVIFDKLNFVIPAG 389
Cdd:COG4178 312 QGALSWFVDNYqslaewratVDRlagfeealeaadALPEAASRIETSEDGALALEDLTLRTPD--GRPLLEDLSLSLKPG 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 390 KVVALVGGSGSGKSTMISLIERFYEPTDGAVML-DGNDIRYLDlkwlrghiglvnQEPVLFATTIRENIMY--GKDDATS 466
Cdd:COG4178 390 ERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFLP------------QRPYLPLGTLREALLYpaTAEAFSD 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 467 EEITNAakLSEAisfinNLPEgFETQVGER---GIQLSGGQKQRISISRAIVKNPSILLLDEATSALDAESEKIVQEALD 543
Cdd:COG4178 458 AELREA--LEAV-----GLGH-LAERLDEEadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLR 529
|
490
....*....|....
gi 15220188 544 RVMVGRTTVVVAHR 557
Cdd:COG4178 530 EELPGTTVISVGHR 543
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
983-1201 |
9.56e-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: 9.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 983 ELKGVHFSYPsrpDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLK-LKSLRRHIG 1061
Cdd:TIGR03410 2 EVSNLNVYYG---QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPpHERARAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEPALFAT-TIYENILYGkegasesevmeAAKLANAHSFIssLPEGYS------TKVGERGIQMSGGQRQRIAIARA 1134
Cdd:TIGR03410 79 YVPQGREIFPRlTVEENLLTG-----------LAALPRRSRKI--PDEIYElfpvlkEMLGRRGGDLSGGQQQQLAIARA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1135 VLKNPEILLLDEATSALDVESERVVQQALDRL--MRDRTTVVVAHRLSTIKN-SDMISVIQDGKIIEQGS 1201
Cdd:TIGR03410 146 LVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLraEGGMAILLVEQYLDFARElADRYYVMERGRVVASGA 215
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
982-1198 |
1.09e-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: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRPdvtIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIdGQDIKklklkslrrhIG 1061
Cdd:COG0488 316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEPALFAT--TIYENILYGKEGASESEVMeaAKLAN-------AHSFISSLpegystkvgergiqmSGGQRQRIAIA 1132
Cdd:COG0488 382 YFDQHQEELDPdkTVLDELRDGAPGGTEQEVR--GYLGRflfsgddAFKPVGVL---------------SGGEKARLALA 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15220188 1133 RAVLKNPEILLLDEATSALDVESERVVQQALDRLmrDRTTVVVAH-R--LSTIKNSdmISVIQDGKIIE 1198
Cdd:COG0488 445 KLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF--PGTVLLVSHdRyfLDRVATR--ILEFEDGGVRE 509
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
375-579 |
1.17e-18 |
|
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: 85.80 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 375 DVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDlkwlRGHIGLVNQEPVLF-ATTI 453
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLPEERGLYpKMKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 454 RENIMYGKDdatseeiTNAAKLSEAISFINNLPEGFE-TQVGERGI-QLSGGQKQRISISRAIVKNPSILLLDEATSALD 531
Cdd:cd03269 88 IDQLVYLAQ-------LKGLKKEEARRRIDEWLERLElSEYANKRVeELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15220188 532 AESEKIVQEALDRVM-VGRTTVVVAHRLSTV-RNADIIAVVGGGKIIESG 579
Cdd:cd03269 161 PVNVELLKDVIRELArAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
982-1197 |
1.19e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 90.86 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSrpdVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGqdiKKLKLKS----LR 1057
Cdd:COG3845 6 LELRGITKRFGG---VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIRSprdaIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1058 RHIGLVQQEPALFAT-TIYENILYGKEGASesevMEAAKLANAHSFISSLPEGY------STKVGergiQMSGGQRQRIA 1130
Cdd:COG3845 80 LGIGMVHQHFMLVPNlTVAENIVLGLEPTK----GGRLDRKAARARIRELSERYgldvdpDAKVE----DLSVGEQQRVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1131 IARAVLKNPEILLLDEATSAL-DVESERVVqQALDRLMRDRTTVV-VAHRLSTIK-NSDMISVIQDGKII 1197
Cdd:COG3845 152 ILKALYRGARILILDEPTAVLtPQEADELF-EILRRLAAEGKSIIfITHKLREVMaIADRVTVLRRGKVV 220
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
729-937 |
1.49e-18 |
|
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: 87.48 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 729 MGERLTLRVRQKMFSAILRNEIGWFDKvdNTSSMLASRLESDATLLRTIVVDRSTILLENLGLVVTAFIISFILNWRLTL 808
Cdd:cd18552 66 VGQRVVRDLRNDLFDKLLRLPLSFFDR--NSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 809 VVLATYPLI--ISGHISEKI-----FMQGYGGNLSKaylkanmLAGESISNIRTVVAFCAEEKVLDLYSKELLEPSERSF 881
Cdd:cd18552 144 IALVVLPLAalPIRRIGKRLrkisrRSQESMGDLTS-------VLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSM 216
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15220188 882 RRGQMAGILYGVSQFFIFSSYGLALWYGSILMEKGLSSFEsvmkTFMVLIvTALVM 937
Cdd:cd18552 217 KIARARALSSPLMELLGAIAIALVLWYGGYQVISGELTPG----EFISFI-TALLL 267
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
380-619 |
1.53e-18 |
|
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: 90.90 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 380 DKLNFVIPAGKVVALVGGSGSGKS-TMIS---LIERFYEPTDGAVMLDGNDIRYLDLKWLRG----HIGLVNQEPV---- 447
Cdd:COG4172 27 KGVSFDIAAGETLALVGESGSGKSvTALSilrLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEPMtsln 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 448 -LFatTIRENIMygkddatseEI-------TNAAKLSEAISFINnlpegfetQVG----ERGI-----QLSGGQKQRISI 510
Cdd:COG4172 107 pLH--TIGKQIA---------EVlrlhrglSGAAARARALELLE--------RVGipdpERRLdayphQLSGGQRQRVMI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 511 SRAIVKNPSILLLDEATSALDAesekIVQ-EALD--RVMVGRTTVVVA---HRLSTVRN-ADIIAVVGGGKIIESGSHDE 583
Cdd:COG4172 168 AMALANEPDLLIADEPTTALDV----TVQaQILDllKDLQRELGMALLlitHDLGVVRRfADRVAVMRQGEIVEQGPTAE 243
|
250 260 270
....*....|....*....|....*....|....*..
gi 15220188 584 LISNPDGAYS-SLLriqeAASPNLNHTPsLPVSTKPL 619
Cdd:COG4172 244 LFAAPQHPYTrKLL----AAEPRGDPRP-VPPDAPPL 275
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
982-1201 |
1.55e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.17 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYpsRPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIG 1061
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEP--ALFATTIYENILYG------KEGASESEVMEAAKLANAHSFISSLPEgystkvgergiQMSGGQRQRIAIAR 1133
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGpinlglDEETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15220188 1134 AVLKNPEILLLDEATSALDVESERVVQQALDRLMRD--RTTVVVAHRLSTIKN-SDMISVIQDGKIIEQGS 1201
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGT 221
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
979-1178 |
1.85e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 90.64 E-value: 1.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 979 EGTIELKGVHFSYPSrpDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVlrfydptAG--------IIMIDGQDIkk 1050
Cdd:COG4178 360 DGALALEDLTLRTPD--GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAI-------AGlwpygsgrIARPAGARV-- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1051 lklksLrrhigLVQQEPALFATTIYENILY--GKEGASESEVMEAAKLANAHSFISSLPEgystkVGERGIQMSGGQRQR 1128
Cdd:COG4178 429 -----L-----FLPQRPYLPLGTLREALLYpaTAEAFSDAELREALEAVGLGHLAERLDE-----EADWDQVLSLGEQQR 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15220188 1129 IAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVVVAHR 1178
Cdd:COG4178 494 LAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
93-309 |
2.28e-18 |
|
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: 87.14 E-value: 2.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 93 LSVVILFSSWLEVAC---WMHTGERQAAKIRKAYLRSMLSQDISLFDTEiSTGEVISAITSEILVVQDAISEKVGNFMHF 169
Cdd:cd18589 42 MSLLTIASAVSEFVCdliYNITMSRIHSRLQGLVFAAVLRQEIAFFDSN-QTGDIVSRVTTDTEDMSESLSENLSLLMWY 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 170 ISRFIAGFAIGFASVWQISLVTLSIVPFIALAGGIYAFVSSGLIVRVRKSYVKANEIAEEVIGNVRTVQAFTGEEKAVSS 249
Cdd:cd18589 121 LARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQR 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15220188 250 YQGALRNTYNYGRKAGLAKGLGLGSLHFV-LFLSWALLiWFTSIVVHKGIANGGESFTTML 309
Cdd:cd18589 201 YRQRLQKTYRLNKKEAAAYAVSMWTSSFSgLALKVGIL-YYGGQLVTAGTVSSGDLVTFVL 260
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
375-584 |
2.69e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 87.09 E-value: 2.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 375 DVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDlkwlRGHIGLVNQEPVLFAT-TI 453
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYLPEERGLYPKmKV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 454 RENIMY-----GKDDATSEEitNAAKLSEAisfinnlpegFEtqVGERG---IQ-LSGGQKQRISISRAIVKNPSILLLD 524
Cdd:COG4152 89 GEQLVYlarlkGLSKAEAKR--RADEWLER----------LG--LGDRAnkkVEeLSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220188 525 EATSALDAES-EKIVQEALDRVMVGRTTVVVAHRLSTV-RNADIIAVVGGGKIIESGSHDEL 584
Cdd:COG4152 155 EPFSGLDPVNvELLKDVIRELAAKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEI 216
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1000-1174 |
2.76e-18 |
|
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: 85.18 E-value: 2.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1000 FSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQ----DIKKL---KLKSLRRH-IGLVQQ------ 1065
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQAsprEILALRRRtIGYVSQflrvip 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1066 ---------EPALfattiyenilygKEGASESEVMEAAK--LA--NahsfissLPEGY-----STkvgergiqMSGGQRQ 1127
Cdd:COG4778 107 rvsaldvvaEPLL------------ERGVDREEARARARelLArlN-------LPERLwdlppAT--------FSGGEQQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15220188 1128 RIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVV 1174
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
364-589 |
3.00e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 86.36 E-value: 3.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 364 KDVTFTYPSRPdvvIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWL---RGHIG 440
Cdd:PRK11831 11 RGVSFTRGNRC---IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 441 LVNQEPVLFA-TTIRENIMYGKDDAT--SEEI---TNAAKLsEAisfinnlpegfetqVGERGI------QLSGGQKQRI 508
Cdd:PRK11831 88 MLFQSGALFTdMNVFDNVAYPLREHTqlPAPLlhsTVMMKL-EA--------------VGLRGAaklmpsELSGGMARRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 509 SISRAIVKNPSILLLDEATSALDAESEKIVQEALDRV--MVGRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESGSHDELI 585
Cdd:PRK11831 153 ALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELnsALGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQALQ 232
|
....
gi 15220188 586 SNPD 589
Cdd:PRK11831 233 ANPD 236
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1002-1176 |
3.14e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 84.93 E-value: 3.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1002 DFNLlvPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKS---LRRHIGLV-QQEPALFATTIYEN 1077
Cdd:PRK10908 22 TFHM--RPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIfQDHHLLMDRTVYDN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1078 ILYGK--EGASESEVME--AAKLANAhsfisslpeGYSTKVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEATSALDV 1153
Cdd:PRK10908 100 VAIPLiiAGASGDDIRRrvSAALDKV---------GLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
170 180
....*....|....*....|...
gi 15220188 1154 ESERVVQQALDRLMRDRTTVVVA 1176
Cdd:PRK10908 171 ALSEGILRLFEEFNRVGVTVLMA 193
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
382-572 |
3.58e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 84.93 E-value: 3.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 382 LNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYL---DLKWLRGHIGLVNQEP-VLFATTIREN- 456
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrEVPFLRRQIGMIFQDHhLLMDRTVYDNv 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 457 ----IMYGkddATSEEITNaaKLSEAISFInnlpeGFETQVGERGIQLSGGQKQRISISRAIVKNPSILLLDEATSALD- 531
Cdd:PRK10908 101 aiplIIAG---ASGDDIRR--RVSAALDKV-----GLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDd 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15220188 532 AESEKIVQ--EALDRvmVGRTTVVVAHRLSTV--RNADIIAVVGG 572
Cdd:PRK10908 171 ALSEGILRlfEEFNR--VGVTVLMATHDIGLIsrRSYRMLTLSDG 213
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
997-1201 |
3.86e-18 |
|
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: 85.48 E-value: 3.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 997 VTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLkSLRRHIGLVQ--QEPALFAT-T 1073
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP-HRIARLGIARtfQNPRLFPElT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1074 IYENILYG---------------------KEGASESEVMEAAKLAN----AHSFISSLPegystkvgergiqmsGGQRQR 1128
Cdd:COG0411 96 VLENVLVAaharlgrgllaallrlprarrEEREARERAEELLERVGladrADEPAGNLS---------------YGQQRR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15220188 1129 IAIARAVLKNPEILLLDEATSAL-DVESERVVqQALDRLMRDR--TTVVVAHRLSTIKN-SDMISVIQDGKIIEQGS 1201
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLnPEETEELA-ELIRRLRDERgiTILLIEHDMDLVMGlADRIVVLDFGRVIAEGT 236
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
999-1199 |
3.97e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 84.87 E-value: 3.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 999 IFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKL----KLKSLRRHIGLVQQEPALFAT-T 1073
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaaKAELRNQKLGFIYQFHHLLPDfT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1074 IYENI----LYGKEGASESEvmeaaklANAHSFISSLpeGYSTKVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEATS 1149
Cdd:PRK11629 104 ALENVamplLIGKKKPAEIN-------SRALEMLAAV--GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15220188 1150 ALDVESERVVQQALDRLMRDRTT--VVVAHRLSTIKNSDMISVIQDGKIIEQ 1199
Cdd:PRK11629 175 NLDARNADSIFQLLGELNRLQGTafLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
982-1201 |
4.11e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 85.91 E-value: 4.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRPDVT---IFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLK-LKSLR 1057
Cdd:PRK13633 5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1058 RHIGLVQQEP--ALFATTIYENILYGKE--GASESE----VMEAAKLANAHSFISSLPEgystkvgergiQMSGGQRQRI 1129
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGPEnlGIPPEEirerVDESLKKVGMYEYRRHAPH-----------LLSGGQKQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220188 1130 AIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDR--TTVVVAHRLSTIKNSDMISVIQDGKIIEQGS 1201
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
347-586 |
4.84e-18 |
|
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: 90.35 E-value: 4.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 347 EDKTGRKLGNVNGDILFKDVTFTYPSRPDVVIFDkLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEpTDGAVMLDGND 426
Cdd:TIGR01271 1204 ENPHAQKCWPSGGQMDVQGLTAKYTEAGRAVLQD-LSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVS 1281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 427 IRYLDLKWLRGHIGLVNQEPVLFATTIRENiMYGKDDATSEEITNAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQ 506
Cdd:TIGR01271 1282 WNSVTLQTWRKAFGVIPQKVFIFSGTFRKN-LDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQ 1360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 507 RISISRAIVKNPSILLLDEATSALDAESEKIVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVGGGKIIESGSHDELIS 586
Cdd:TIGR01271 1361 LMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLN 1440
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
353-600 |
5.52e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 84.75 E-value: 5.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 353 KLGNVNGDILFKDVTFTYPSRPD-VVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNdiryld 431
Cdd:COG1134 15 RLYHEPSRSLKELLLRRRRTRREeFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 432 LKWLrghIGL---VNQEpvlfaTTIRENI-----MYGkddATSEEItnAAKLSEAISFiNNLPEGFETQVGergiQLSGG 503
Cdd:COG1134 89 VSAL---LELgagFHPE-----LTGRENIylngrLLG---LSRKEI--DEKFDEIVEF-AELGDFIDQPVK----TYSSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 504 QKQRISISRAIVKNPSILLLDEATSALDAE----SEKIVQEALDRvmvGRTTVVVAHRLSTVRN-ADIIAVVGGGKIIES 578
Cdd:COG1134 151 MRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIRELRES---GRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMD 227
|
250 260
....*....|....*....|..
gi 15220188 579 GSHDELISnpdgAYSSLLRIQE 600
Cdd:COG1134 228 GDPEEVIA----AYEALLAGRE 245
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
378-577 |
8.97e-18 |
|
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: 84.86 E-value: 8.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 378 IFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLD---LKWLRGHIGLVNQE---PVLFAT 451
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkqRRAFRRDVQLVFQDspsAVNPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 452 TIRENIMYGKDDATS-EEITNAAKLSEAISFINNLPEGFEtqvgERGIQLSGGQKQRISISRAIVKNPSILLLDEATSAL 530
Cdd:TIGR02769 106 TVRQIIGEPLRHLTSlDESEQKARIAELLDMVGLRSEDAD----KLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15220188 531 DAESEKIVQEALD--RVMVGRTTVVVAHRLSTV-RNADIIAVVGGGKIIE 577
Cdd:TIGR02769 182 DMVLQAVILELLRklQQAFGTAYLFITHDLRLVqSFCQRVAVMDKGQIVE 231
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
990-1176 |
1.02e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 82.67 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 990 SYPSRPdvtIFSDFNLLVPSGKSMALVGQSGSGKSSVLSL---VLRfydPTAGIIMIDGqdikklklkslRRHIGLVQQ- 1065
Cdd:NF040873 1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVlagVLR---PTSGTVRRAG-----------GARVAYVPQr 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1066 --EPALFATTIYENI---LYGKEG----------ASESEVMEAAKLAN-AHSFISSLpegystkvgergiqmSGGQRQRI 1129
Cdd:NF040873 64 seVPDSLPLTVRDLVamgRWARRGlwrrltrddrAAVDDALERVGLADlAGRQLGEL---------------SGGQRQRA 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15220188 1130 AIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVVVA 1176
Cdd:NF040873 129 LLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVV 175
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
369-589 |
1.07e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 83.93 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 369 TYPSRPdVVifDKLNFVIPAGKVVALVGGSGSGKST---MISLIERfyePTDGAVMLDGNDIRYLDLkWLRGH--IGLVN 443
Cdd:COG1137 12 SYGKRT-VV--KDVSLEVNQGEIVGLLGPNGAGKTTtfyMIVGLVK---PDSGRIFLDGEDITHLPM-HKRARlgIGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 444 QEPVLFAT-TIRENIM-----YGKDDATSEEITNAAkLSE-AISFINNLPegfetqvgerGIQLSGGQKQRISISRAIVK 516
Cdd:COG1137 85 QEASIFRKlTVEDNILavlelRKLSKKEREERLEEL-LEEfGITHLRKSK----------AYSLSGGERRRVEIARALAT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 517 NPSILLLDEATSALD----AESEKIVQEALDR----------VmvgRTTvvvahrLSTVRNADIIAvvgGGKIIESGSHD 582
Cdd:COG1137 154 NPKFILLDEPFAGVDpiavADIQKIIRHLKERgigvlitdhnV---RET------LGICDRAYIIS---EGKVLAEGTPE 221
|
....*..
gi 15220188 583 ELISNPD 589
Cdd:COG1137 222 EILNNPL 228
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
361-585 |
1.44e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 85.65 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSRPdvvIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYlDLKWLRGHIG 440
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 441 LVNQEPVL-FATTIREN-IMYGKDDATSeeitnaAKLSEAIsfINNLPE--GFETQVGERGIQLSGGQKQRISISRAIVK 516
Cdd:PRK13536 118 VVPQFDNLdLEFTVRENlLVFGRYFGMS------TREIEAV--IPSLLEfaRLESKADARVSDLSGGMKRRLTLARALIN 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15220188 517 NPSILLLDEATSALDAESEKIVQEALDRVMV-GRTTVVVAHRLSTV-RNADIIAVVGGGKIIESGSHDELI 585
Cdd:PRK13536 190 DPQLLILDEPTTGLDPHARHLIWERLRSLLArGKTILLTTHFMEEAeRLCDRLCVLEAGRKIAEGRPHALI 260
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
983-1217 |
1.54e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 83.58 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 983 ELKGVHFSYPSRPdvtIFSDFNLLVPSGKSMALVGQSGSGKSSvLSLVL---RFYDPTAGIIMIDGQDIKKLKL-KSLRR 1058
Cdd:COG0396 2 EIKNLHVSVEGKE---ILKGVNLTIKPGEVHAIMGPNGSGKST-LAKVLmghPKYEVTSGSILLDGEDILELSPdERARA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1059 HIGLVQQEP--------ALFATTIYENILYGKEGASES--EVMEAAKLAN-AHSFIS-SLPEGYStkvgergiqmsGGQR 1126
Cdd:COG0396 78 GIFLAFQYPveipgvsvSNFLRTALNARRGEELSAREFlkLLKEKMKELGlDEDFLDrYVNEGFS-----------GGEK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1127 QRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMR-DRTTVVVAH--RLSTIKNSDMISVIQDGKIIEQGSHN 1203
Cdd:COG0396 147 KRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSpDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGKE 226
|
250
....*....|....*
gi 15220188 1204 ILVE-NKNGpYSKLI 1217
Cdd:COG0396 227 LALElEEEG-YDWLK 240
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
982-1211 |
1.62e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 84.86 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPsrpDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKlKLKSLRRHIG 1061
Cdd:PRK13537 8 IDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQ----EPALfatTIYENIL-----YGKEGASESE----VMEAAKLANAHSfisslpegysTKVGErgiqMSGGQRQR 1128
Cdd:PRK13537 84 VVPQfdnlDPDF---TVRENLLvfgryFGLSAAAARAlvppLLEFAKLENKAD----------AKVGE----LSGGMKRR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1129 IAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLM-RDRTTVVVAHRLSTIKN-SDMISVIQDGKIIEQGSHNILV 1206
Cdd:PRK13537 147 LTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALI 226
|
....*
gi 15220188 1207 ENKNG 1211
Cdd:PRK13537 227 ESEIG 231
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
361-575 |
1.92e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 83.57 E-value: 1.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSRpdvVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAvMLDGNdiryLDLKWLRGHIG 440
Cdd:PRK11247 13 LLLNAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAGT----APLAEAREDTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 441 LVNQEPVLFA-TTIRENIMYG-----KDDATseeitnaaklsEAISFInnlpeGFETQVGERGIQLSGGQKQRISISRAI 514
Cdd:PRK11247 85 LMFQDARLLPwKKVIDNVGLGlkgqwRDAAL-----------QALAAV-----GLADRANEWPAALSGGQKQRVALARAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220188 515 VKNPSILLLDEATSALDAESEKIVQEALDRVMV--GRTTVVVAHRLS-TVRNADIIAVVGGGKI 575
Cdd:PRK11247 149 IHRPGLLLLDEPLGALDALTRIEMQDLIESLWQqhGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
988-1200 |
2.01e-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: 82.58 E-value: 2.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 988 HFSYPSRPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLkslrrHIGLvqqEP 1067
Cdd:cd03220 26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGL-----GGGF---NP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1068 ALfatTIYENI-----LYGKEGASESEVMEaaklanahsFI---SSLPEGYSTKVGErgiqMSGGQRQRIAIARAVLKNP 1139
Cdd:cd03220 98 EL---TGRENIylngrLLGLSRKEIDEKID---------EIiefSELGDFIDLPVKT----YSSGMKARLAFAIATALEP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15220188 1140 EILLLDEATSALDVESERVVQQALDRLMRDRTTVV-VAHRLSTIKN-SDMISVIQDGKIIEQG 1200
Cdd:cd03220 162 DILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVIlVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
998-1201 |
2.43e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 83.50 E-value: 2.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 998 TIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIGLVQQEPALFA-TTIYE 1076
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGdITVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1077 NILYGKEGAS------ESEVMEAAKLANAHSFISSLpegystkVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEATSA 1150
Cdd:PRK10253 101 LVARGRYPHQplftrwRKEDEEAVTKAMQATGITHL-------ADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15220188 1151 LDVESERVVQQALDRLMRDR--TTVVVAHRLS-TIKNSDMISVIQDGKIIEQGS 1201
Cdd:PRK10253 174 LDISHQIDLLELLSELNREKgyTLAAVLHDLNqACRYASHLIALREGKIVAQGA 227
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
984-1200 |
2.58e-17 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 85.47 E-value: 2.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 984 LKGVHFSYPsrpDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKslRRHIGLV 1063
Cdd:PRK11000 6 LRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1064 QQEPALFA-TTIYENILYGKE--GASESE----VMEAAKLANAHSFISSLPEGystkvgergiqMSGGQRQRIAIARAVL 1136
Cdd:PRK11000 81 FQSYALYPhLSVAENMSFGLKlaGAKKEEinqrVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRTLV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15220188 1137 KNPEILLLDEATSALDVeSERVVQQA-LDRLMR--DRTTVVVAH-RLSTIKNSDMISVIQDGKIIEQG 1200
Cdd:PRK11000 150 AEPSVFLLDEPLSNLDA-ALRVQMRIeISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
364-586 |
2.68e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 83.28 E-value: 2.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 364 KDVTFTYPSRPdvvIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHIGLVN 443
Cdd:PRK13548 6 RNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 444 QEPVL-FATTIRENIMYGKDDATSEEITNAAKLSEAIsfinnlpegfeTQVG-----ERGI-QLSGGQKQRISISRAIV- 515
Cdd:PRK13548 83 QHSSLsFPFTVEEVVAMGRAPHGLSRAEDDALVAAAL-----------AQVDlahlaGRDYpQLSGGEQQRVQLARVLAq 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15220188 516 -----KNPSILLLDEATSALD-AESEKIVQEALDRVMVGRTTV-VVAHRLS-TVRNADIIAVVGGGKIIESGSHDELIS 586
Cdd:PRK13548 152 lwepdGPPRWLLLDEPTSALDlAHQHHVLRLARQLAHERGLAViVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVLT 230
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
382-584 |
2.69e-17 |
|
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: 82.57 E-value: 2.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 382 LNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWL--RGhIGLVNQEPVLFAT-TIRENIM 458
Cdd:TIGR03410 19 VSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERarAG-IAYVPQGREIFPRlTVEENLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 459 YGKDdatseeiTNAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRISISRAIVKNPSILLLDEATSALDAESEKIV 538
Cdd:TIGR03410 98 TGLA-------ALPRRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15220188 539 QEALDRV--MVGRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESGSHDEL 584
Cdd:TIGR03410 171 GRVIRRLraEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
375-579 |
2.90e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 82.81 E-value: 2.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 375 DVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLI---ERfYEPTDGAVMLDGNDIryLDLK----WLRGhIGLVNQEPV 447
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDGEDI--LELSpderARAG-IFLAFQYPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 448 LF------------ATTIRENIMYGKDDatSEEITNAAK-LSEAISFIN-NLPEGFetqvgergiqlSGGQKQRISISRA 513
Cdd:COG0396 88 EIpgvsvsnflrtaLNARRGEELSAREF--LKLLKEKMKeLGLDEDFLDrYVNEGF-----------SGGEKKRNEILQM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15220188 514 IVKNPSILLLDEATSALDAESEKIVQEALDRVMV-GRTTVVVAH--RLSTVRNADIIAVVGGGKIIESG 579
Cdd:COG0396 155 LLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSpDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSG 223
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1002-1201 |
3.29e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 84.54 E-value: 3.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1002 DFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQ---DI-KKLKLKSLRRHIGLVQQEPALFA-TTIYE 1076
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAeKGICLPPEKRRIGYVFQDARLFPhYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1077 NILYGKEGASESEVMEAAKLANAHSFISSLPegystkvgergIQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESE 1156
Cdd:PRK11144 96 NLRYGMAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15220188 1157 RVVQQALDRLMRDRTT--VVVAHRLSTI-KNSDMISVIQDGKIIEQGS 1201
Cdd:PRK11144 165 RELLPYLERLAREINIpiLYVSHSLDEIlRLADRVVVLEQGKVKAFGP 212
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1002-1177 |
3.76e-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: 82.13 E-value: 3.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1002 DFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLrrhigLVQQEPALFA-TTIYENI-L 1079
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENIaL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1080 YGKEGASESEVMEAAKLANAHSFISSLPEGYSTKVGergiQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVV 1159
Cdd:TIGR01184 78 AVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPG----QLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180
....*....|....*....|
gi 15220188 1160 QQALDRLMRDR--TTVVVAH 1177
Cdd:TIGR01184 154 QEELMQIWEEHrvTVLMVTH 173
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
695-909 |
3.91e-17 |
|
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: 83.51 E-value: 3.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 695 ETTQNEVKRISILFCCGSVITVIVHTIEHTTFGIMGERLTLRVRQKMFSAILRNEIGWFDKVdNTSSMLaSRLESDATLL 774
Cdd:cd18784 29 EKSQDKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTV-KTGDIT-SRLTSDTTTM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 775 RTIVVDRSTILLENLGLVVTAFIISFILNWRLTLVVLATYPLIIsghISEKIFMQGYgGNLSK----AYLKANMLAGESI 850
Cdd:cd18784 107 SDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIA---IVSKVYGDYY-KKLSKavqdSLAKANEVAEETI 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15220188 851 SNIRTVVAFCAEEKVLDLYSKELLEPSERSFRRGQMAGILYGVSQFFIFSSYGLALWYG 909
Cdd:cd18784 183 SSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYG 241
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
355-559 |
4.19e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 81.79 E-value: 4.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 355 GNVNGDILfKDVTFTypsrpdvvifdklnfvIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKW 434
Cdd:PRK11629 18 GSVQTDVL-HNVSFS----------------IGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 435 ---LRGH-IGLVNQ-EPVLFATTIRENI----MYGKDdATSEEITNAAKLSEAIsfinnlpeGFETQVGERGIQLSGGQK 505
Cdd:PRK11629 81 kaeLRNQkLGFIYQfHHLLPDFTALENVamplLIGKK-KPAEINSRALEMLAAV--------GLEHRANHRPSELSGGER 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15220188 506 QRISISRAIVKNPSILLLDEATSALDAESEKIVQEALDRVMVGRTT--VVVAHRLS 559
Cdd:PRK11629 152 QRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTafLVVTHDLQ 207
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
994-1152 |
4.70e-17 |
|
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: 81.55 E-value: 4.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 994 RPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLV---LRFYDPTAGIIMIDGQDIKKlklKSLRRHIGLVQQEPALF 1070
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNGQPRKP---DQFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1071 AT-TIYENILY------GKEGASESEVMEAAKLANAHSFISSLPegystkvGERGIQMSGGQRQRIAIARAVLKNPEILL 1143
Cdd:cd03234 94 PGlTVRETLTYtailrlPRKSSDAIRKKRVEDVLLRDLALTRIG-------GNLVKGISGGERRRVSIAVQLLWDPKVLI 166
|
....*....
gi 15220188 1144 LDEATSALD 1152
Cdd:cd03234 167 LDEPTSGLD 175
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
373-580 |
5.25e-17 |
|
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: 87.38 E-value: 5.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 373 RPDVvifDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRyLDLKWLRGHIGLVNQEPVLFA-T 451
Cdd:TIGR01257 943 RPAV---DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE-TNLDAVRQSLGMCPQHNILFHhL 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 452 TIRENIM-YGKDDATSEEitnAAKLsEAISFINNlpEGFETQVGERGIQLSGGQKQRISISRAIVKNPSILLLDEATSAL 530
Cdd:TIGR01257 1019 TVAEHILfYAQLKGRSWE---EAQL-EMEAMLED--TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGV 1092
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15220188 531 DAESEKIVQEALDRVMVGRTTVVVAHRLStvrNADI----IAVVGGGKIIESGS 580
Cdd:TIGR01257 1093 DPYSRRSIWDLLLKYRSGRTIIMSTHHMD---EADLlgdrIAIISQGRLYCSGT 1143
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
373-540 |
5.62e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 80.69 E-value: 5.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 373 RPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHIGLVNQ-EPVLfat 451
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGHRNAmKPAL--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 452 TIRENI-----MYGKDDATSEEITNAAKLSEaisfINNLPEGFetqvgergiqLSGGQKQRISISRAIVKNPSILLLDEA 526
Cdd:PRK13539 89 TVAENLefwaaFLGGEELDIAAALEAVGLAP----LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEP 154
|
170
....*....|....
gi 15220188 527 TSALDAESEKIVQE 540
Cdd:PRK13539 155 TAALDAAAVALFAE 168
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
370-545 |
5.70e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 82.05 E-value: 5.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 370 YPSRPdvvIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIryldlKWLRGHIGLVNQ-EPVL 448
Cdd:PRK11248 11 YGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV-----EGPGAERGVVFQnEGLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 449 FATTIRENIMYGKDDATSEEITNAAKLSEAISFINnlPEGFEtqvgERGI-QLSGGQKQRISISRAIVKNPSILLLDEAT 527
Cdd:PRK11248 83 PWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVG--LEGAE----KRYIwQLSGGQRQRVGIARALAANPQLLLLDEPF 156
|
170
....*....|....*...
gi 15220188 528 SALDAESEKIVQEALDRV 545
Cdd:PRK11248 157 GALDAFTREQMQTLLLKL 174
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
380-596 |
6.61e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 83.60 E-value: 6.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 380 DKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYL-DLKWL--RGHIGLVNQEPV-------LF 449
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMkDDEWRavRSDIQMIFQDPLaslnprmTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 450 ATTIRENIMYGKDDATSEEITN-----AAKLSEAISFINNLPEGFetqvgergiqlSGGQKQRISISRAIVKNPSILLLD 524
Cdd:PRK15079 118 GEIIAEPLRTYHPKLSRQEVKDrvkamMLKVGLLPNLINRYPHEF-----------SGGQCQRIGIARALILEPKLIICD 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15220188 525 EATSALD----AESEKIVQEaLDRVMvGRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESGSHDELISNPDGAYSSLL 596
Cdd:PRK15079 187 EPVSALDvsiqAQVVNLLQQ-LQREM-GLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHNPLHPYTKAL 261
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
376-548 |
7.54e-17 |
|
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: 80.94 E-value: 7.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 376 VVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDiRYLDL------KWL---RGHIGLVNQ-- 444
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDG-GWVDLaqasprEILalrRRTIGYVSQfl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 445 -------------EPVLFAttirenimyGKDDATSEEItnAAKLSEAIsfinNLPEG--------FetqvgergiqlSGG 503
Cdd:COG4778 103 rviprvsaldvvaEPLLER---------GVDREEARAR--ARELLARL----NLPERlwdlppatF-----------SGG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15220188 504 QKQRISISRAIVKNPSILLLDEATSALDAESEKIV----QEALDR--VMVG 548
Cdd:COG4778 157 EQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVveliEEAKARgtAIIG 207
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
982-1177 |
7.83e-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: 78.64 E-value: 7.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRPdvtIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIdGQDIKklklkslrrhIG 1061
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVK----------IG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQepalfattiyenilygkegasesevmeaaklanahsfisslpegystkvgergiqMSGGQRQRIAIARAVLKNPEI 1141
Cdd:cd03221 67 YFEQ-------------------------------------------------------LSGGEKMRLALAKLLLENPNL 91
|
170 180 190
....*....|....*....|....*....|....*.
gi 15220188 1142 LLLDEATSALDVESERVVQQALDRLmrDRTTVVVAH 1177
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALKEY--PGTVILVSH 125
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
986-1218 |
8.63e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 83.22 E-value: 8.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 986 GVHF------SYPSRPDVTI--FSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKL---KLK 1054
Cdd:PRK15079 15 KVHFdikdgkQWFWQPPKTLkaVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMkddEWR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1055 SLRRHIGLVQQEPalFAT-----TIYENI-----LYGKEgASESEVMEAAK--------LANahsFISSLPEgystkvge 1116
Cdd:PRK15079 95 AVRSDIQMIFQDP--LASlnprmTIGEIIaeplrTYHPK-LSRQEVKDRVKammlkvglLPN---LINRYPH-------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1117 rgiQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDR--TTVVVAHRLSTIKN-SDMISVIQD 1193
Cdd:PRK15079 161 ---EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHiSDRVLVMYL 237
|
250 260
....*....|....*....|....*.
gi 15220188 1194 GKIIEQGSHNILVENKNGPYSK-LIS 1218
Cdd:PRK15079 238 GHAVELGTYDEVYHNPLHPYTKaLMS 263
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
357-577 |
1.01e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 80.39 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 357 VNGDILFKDVTFTYPSRPDV--------------------VIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYE-- 414
Cdd:COG2401 4 YNPFFVLMRVTKVYSSVLDLservaivleafgvelrvverYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgt 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 415 PTDGAVMLDGNDIryldlkwlrghiglvNQEpvlfaTTIRENIMYGKDDATSEEITNAAKLSEAISFINNLPEgfetqvg 494
Cdd:COG2401 84 PVAGCVDVPDNQF---------------GRE-----ASLIDAIGRKGDFKDAVELLNAVGLSDAVLWLRRFKE------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 495 ergiqLSGGQKQRISISRAIVKNPSILLLDEATSALDAESEKIV----QEALDRvmVGRTTVVVAHRlSTVRNA---DII 567
Cdd:COG2401 137 -----LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVarnlQKLARR--AGITLVVATHH-YDVIDDlqpDLL 208
|
250
....*....|
gi 15220188 568 AVVGGGKIIE 577
Cdd:COG2401 209 IFVGYGGVPE 218
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
377-586 |
1.18e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.57 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 377 VIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHIGLVNQEPVLFA-TTIRE 455
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGdITVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 456 NIMYG------------KDDatsEEITNAAKLSEAISFINNlpEGFETqvgergiqLSGGQKQRISISRAIVKNPSILLL 523
Cdd:PRK10253 101 LVARGryphqplftrwrKED---EEAVTKAMQATGITHLAD--QSVDT--------LSGGQRQRAWIAMVLAQETAIMLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15220188 524 DEATSALDAESEKIVQEALDRV--MVGRTTVVVAHRLS-TVRNADIIAVVGGGKIIESGSHDELIS 586
Cdd:PRK10253 168 DEPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVT 233
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
982-1219 |
1.29e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 82.06 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRP--DVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLK------- 1052
Cdd:PRK13651 3 IKVKNIVKIFNKKLptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1053 -----------------LKSLRRHIGLVQQ--EPALFATTIYENILYG--KEGASESEvmeAAKLANAHSFISSLPEGYS 1111
Cdd:PRK13651 83 vleklviqktrfkkikkIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGpvSMGVSKEE---AKKRAAKYIELVGLDESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1112 TKvgeRGIQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRD-RTTVVVAHRL-STIKNSDMIS 1189
Cdd:PRK13651 160 QR---SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLdNVLEWTKRTI 236
|
250 260 270
....*....|....*....|....*....|....*..
gi 15220188 1190 VIQDGKIIEQG-------SHNILVENKNGPySKLISL 1219
Cdd:PRK13651 237 FFKDGKIIKDGdtydilsDNKFLIENNMEP-PKLLNF 272
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
982-1201 |
1.30e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 84.33 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRPdVTIFSDFNLLvpSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLK-LKSLRRHI 1060
Cdd:PRK15439 12 LCARSISKQYSGVE-VLKGIDFTLH--AGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKAHQLGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1061 GLVQQEPALFAT-TIYENILYGKEGASESEVMEAAKLANAHSFISSLPEGYSTKVGERgiqmsggqrQRIAIARAVLKNP 1139
Cdd:PRK15439 89 YLVPQEPLLFPNlSVKENILFGLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADR---------QIVEILRGLMRDS 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220188 1140 EILLLDEATSALD-VESERVVQQALDRLMRDRTTVVVAHRLSTIKN-SDMISVIQDGKIIEQGS 1201
Cdd:PRK15439 160 RILILDEPTASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGK 223
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1010-1201 |
1.39e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 81.04 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1010 GKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIGLVQQ-----------------EPALFAT 1072
Cdd:COG4167 39 GQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMIFQdpntslnprlnigqileEPLRLNT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1073 TIYENilygkegASESEVMEAAKLanahsfISSLPEGYSTKvgergIQM-SGGQRQRIAIARAVLKNPEILLLDEATSAL 1151
Cdd:COG4167 119 DLTAE-------EREERIFATLRL------VGLLPEHANFY-----PHMlSSGQKQRVALARALILQPKIIIADEALAAL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15220188 1152 DVeSERvvQQALDRLMRDRTT-----VVVAHRLSTIKN-SDMISVIQDGKIIEQGS 1201
Cdd:COG4167 181 DM-SVR--SQIINLMLELQEKlgisyIYVSQHLGIVKHiSDKVLVMHQGEVVEYGK 233
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
995-1197 |
1.44e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 84.21 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 995 PDVTIFSDFNLLVPSGKSMALVGQSGSGKSS---VLSLVLRF--YDptaGIIMIDGQDIKKLKLK-SLRRHIGLVQQEPA 1068
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTlmkVLSGVYPHgtYE---GEIIFEGEELQASNIRdTERAGIAIIHQELA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1069 LFAT-TIYENILYGKE----GASESEVM--EAAK-LANAHSFISSlpegySTKVGERGiqmsGGQRQRIAIARAVLKNPE 1140
Cdd:PRK13549 93 LVKElSVLENIFLGNEitpgGIMDYDAMylRAQKlLAQLKLDINP-----ATPVGNLG----LGQQQLVEIAKALNKQAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1141 ILLLDEATSALdVESERVVQQALDRLMRDR--TTVVVAHRLSTIKN-SDMISVIQDGKII 1197
Cdd:PRK13549 164 LLILDEPTASL-TESETAVLLDIIRDLKAHgiACIYISHKLNEVKAiSDTICVIRDGRHI 222
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
997-1199 |
1.63e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 80.21 E-value: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 997 VTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLK---SLR-RHIGLVQQEPALFAT 1072
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRaKHVGFVFQSFMLIPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1073 -TIYENI----LYGKEGASESEVMEAAKLANAhsfisslpeGYSTKVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEA 1147
Cdd:PRK10584 103 lNALENVelpaLLRGESSRQSRNGAKALLEQL---------GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15220188 1148 TSALDVESERVVQQALDRLMRDRTT--VVVAHRLSTIKNSDMISVIQDGKIIEQ 1199
Cdd:PRK10584 174 TGNLDRQTGDKIADLLFSLNREHGTtlILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
725-916 |
1.69e-16 |
|
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: 81.32 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 725 TFGIMGERLTLRVRQKMFSAILRNEIGWFDKVDntSSMLASRLESDATLLRTIVVDRSTILLENLGLVVTAFIISFILNW 804
Cdd:cd18542 62 LAEKASQKVAYDLRNDLYDHLQRLSFSFHDKAR--TGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINW 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 805 RLTLVVLATYPLIIsghisekIFMQGYGGNLSKAYLKA-------NMLAGESISNIRTVVAFCAEEKVLDLYSKELLEPS 877
Cdd:cd18542 140 KLTLISLAIIPFIA-------LFSYVFFKKVRPAFEEIreqegelNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYR 212
|
170 180 190
....*....|....*....|....*....|....*....
gi 15220188 878 ERSFRRGQMAGILYGVSQFFIFSSYGLALWYGSILMEKG 916
Cdd:cd18542 213 DLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVING 251
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1010-1201 |
1.79e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 83.99 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1010 GKSMALVGQSGSGKSSVLSLVLRFYdPTAGIIMIDGQDIKKLKLKSL---RRHIGLVQQEP--ALFATTIYENILygKEG 1084
Cdd:PRK15134 312 GETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPnsSLNPRLNVLQII--EEG 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1085 ---------ASESE-----VMEAAKL--ANAHSFISslpegystkvgergiQMSGGQRQRIAIARAVLKNPEILLLDEAT 1148
Cdd:PRK15134 389 lrvhqptlsAAQREqqviaVMEEVGLdpETRHRYPA---------------EFSGGQRQRIAIARALILKPSLIILDEPT 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15220188 1149 SALDveseRVVQQALDRLMRdrtTVVVAHRLSTIKNS-DM---------ISVIQDGKIIEQGS 1201
Cdd:PRK15134 454 SSLD----KTVQAQILALLK---SLQQKHQLAYLFIShDLhvvralchqVIVLRQGEVVEQGD 509
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
361-557 |
1.83e-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: 78.35 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSrpDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAV-MLDGNDIRYLDlkwlrghi 439
Cdd:cd03223 1 IELENLSLATPD--GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIgMPEGEDLLFLP-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 440 glvnQEPVLFATTIRENIMYGKDDAtseeitnaaklseaisfinnlpegfetqvgergiqLSGGQKQRISISRAIVKNPS 519
Cdd:cd03223 71 ----QRPYLPLGTLREQLIYPWDDV-----------------------------------LSGGEQQRLAFARLLLHKPK 111
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15220188 520 ILLLDEATSALDAESEK----IVQEALdrvmvgrTTVV-VAHR 557
Cdd:cd03223 112 FVFLDEATSALDEESEDrlyqLLKELG-------ITVIsVGHR 147
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
349-577 |
3.12e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.19 E-value: 3.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 349 KTGRKLGNvngDIL-FKDVTFTYPSRPdvvIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVmldgndi 427
Cdd:COG0488 306 PPPERLGK---KVLeLEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV------- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 428 ryldlKWlrGH---IGLVNQEPVLFAT--TIRENIMYGKDDATSEEITNAAKlseaiSFinnlpeGF-----ETQVGErg 497
Cdd:COG0488 373 -----KL--GEtvkIGYFDQHQEELDPdkTVLDELRDGAPGGTEQEVRGYLG-----RF------LFsgddaFKPVGV-- 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 498 iqLSGGQKQRISISRAIVKNPSILLLDEATSALDAESEKIVQEALDR----VmvgrttVVVAH-R--LSTVrnADIIAVV 570
Cdd:COG0488 433 --LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDfpgtV------LLVSHdRyfLDRV--ATRILEF 502
|
....*..
gi 15220188 571 GGGKIIE 577
Cdd:COG0488 503 EDGGVRE 509
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
981-1152 |
4.51e-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: 4.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 981 TIELKGVHFSYPSrpDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSlrRHI 1060
Cdd:PRK11650 3 GLKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--RDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1061 GLVQQEPALFA-TTIYENILYG-K-EGASESE----VMEAAKLANAHSFISSLPEgystkvgergiQMSGGQRQRIAIAR 1133
Cdd:PRK11650 79 AMVFQNYALYPhMSVRENMAYGlKiRGMPKAEieerVAEAARILELEPLLDRKPR-----------ELSGGQRQRVAMGR 147
|
170
....*....|....*....
gi 15220188 1134 AVLKNPEILLLDEATSALD 1152
Cdd:PRK11650 148 AIVREPAVFLFDEPLSNLD 166
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
361-542 |
4.60e-16 |
|
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: 76.33 E-value: 4.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSRPdvvIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGN-DIRYLDlkwlrghi 439
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTvKIGYFE-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 440 glvnqepvlfattirenimygkddatseeitnaaklseaisfinnlpegfetqvgergiQLSGGQKQRISISRAIVKNPS 519
Cdd:cd03221 70 -----------------------------------------------------------QLSGGEKMRLALAKLLLENPN 90
|
170 180
....*....|....*....|...
gi 15220188 520 ILLLDEATSALDAESEKIVQEAL 542
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEAL 113
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
365-586 |
5.55e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 79.67 E-value: 5.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 365 DVTFTYPSRPdvvIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLD--LKWLRGHIGLV 442
Cdd:PRK13638 6 DLWFRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKrgLLALRQQVATV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 443 NQEP--VLFATTIRENIMYGKDDATSEEITNAAKLSEAISFINnlPEGFETQvgerGIQ-LSGGQKQRISISRAIVKNPS 519
Cdd:PRK13638 83 FQDPeqQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVD--AQHFRHQ----PIQcLSHGQKKRVAIAGALVLQAR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15220188 520 ILLLDEATSALDAESEKIVQEALDRVMV-GRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESGSHDELIS 586
Cdd:PRK13638 157 YLLLDEPTAGLDPAGRTQMIAIIRRIVAqGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFA 225
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
361-587 |
6.80e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 80.13 E-value: 6.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSRPDVVI--FDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIR---------- 428
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKnkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 429 YLD--------------LKWLRGHIGLVNQ--EPVLFATTIRENIMYGkddATSEEITNAAKLSEAISFIN--NLPEGFe 490
Cdd:PRK13651 83 VLEklviqktrfkkikkIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFG---PVSMGVSKEEAKKRAAKYIElvGLDESY- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 491 tqVGERGIQLSGGQKQRISISRAIVKNPSILLLDEATSALDAESEKIVQEALDRV-MVGRTTVVVAHRLSTV-RNADIIA 568
Cdd:PRK13651 159 --LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVlEWTKRTI 236
|
250
....*....|....*....
gi 15220188 569 VVGGGKIIESGSHDELISN 587
Cdd:PRK13651 237 FFKDGKIIKDGDTYDILSD 255
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
339-586 |
7.20e-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: 82.16 E-value: 7.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 339 FQMIERNTEDKTGRKLgnvngdILFKDVTFTYPS--RPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPT 416
Cdd:TIGR03269 264 VSEVEKECEVEVGEPI------IKVRNVSKRYISvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPT 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 417 DGAV-MLDGNDirYLDLK----WLRG----HIGLVNQEPVLFA-TTIRENIMygkdDATSEEITNAAKLSEAISFINNLp 486
Cdd:TIGR03269 338 SGEVnVRVGDE--WVDMTkpgpDGRGrakrYIGILHQEYDLYPhRTVLDNLT----EAIGLELPDELARMKAVITLKMV- 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 487 eGFETQVGERGI-----QLSGGQKQRISISRAIVKNPSILLLDEATSALDAESEKIVQEAL--DRVMVGRTTVVVAHRLS 559
Cdd:TIGR03269 411 -GFDEEKAEEILdkypdELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkAREEMEQTFIIVSHDMD 489
|
250 260
....*....|....*....|....*...
gi 15220188 560 TVRN-ADIIAVVGGGKIIESGSHDELIS 586
Cdd:TIGR03269 490 FVLDvCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
998-1209 |
7.37e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 78.40 E-value: 7.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 998 TIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKS-LRRHIGLVQQEPALFAT-TIY 1075
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARRGIGYLPQEASIFRRlSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1076 EN---ILYGKEGASESEVMEAAKLANAHSFISSLPEGYstkvgerGIQMSGGQRQRIAIARAVLKNPEILLLDEATSALD 1152
Cdd:PRK10895 97 DNlmaVLQIRDDLSAEQREDRANELMEEFHIEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1153 VESERVVQQALDRLmRDR--TTVVVAHRL-STIKNSDMISVIQDGKIIEQGSHNILVENK 1209
Cdd:PRK10895 170 PISVIDIKRIIEHL-RDSglGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDE 228
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1000-1216 |
1.06e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 78.43 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1000 FSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSL----RRHI-----GLVQQEPA-- 1068
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaeRRRLlrtewGFVHQHPRdg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1069 -LFATTIYENI----------LYGKEGASESEVMEAAKLANAHsfISSLPEGYStkvgergiqmsGGQRQRIAIARAVLK 1137
Cdd:PRK11701 102 lRMQVSAGGNIgerlmavgarHYGDIRATAGDWLERVEIDAAR--IDDLPTTFS-----------GGMQQRLQIARNLVT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1138 NPEILLLDEATSALDVEservVQQALDRLMRDRTT------VVVAHRLSTIKN-SDMISVIQDGKIIEQGSHNILVENKN 1210
Cdd:PRK11701 169 HPRLVFMDEPTGGLDVS----VQARLLDLLRGLVRelglavVIVTHDLAVARLlAHRLLVMKQGRVVESGLTDQVLDDPQ 244
|
....*.
gi 15220188 1211 GPYSKL 1216
Cdd:PRK11701 245 HPYTQL 250
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
374-596 |
1.08e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 78.20 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 374 PDVVIFDKLNFVIPAGKVVALVGGSGSGKS----TMISLIERFYEPTDGAVMLDGNDIRYLDlkwLRG-HIGLVNQEP-- 446
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCA---LRGrKIATIMQNPrs 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 447 -----VLFATTIRENIM-YGK--DDATSEEITNAAKLSEAISFINNLPegFEtqvgergiqLSGGQKQRISISRAIVKNP 518
Cdd:PRK10418 91 afnplHTMHTHARETCLaLGKpaDDATLTAALEAVGLENAARVLKLYP--FE---------MSGGMLQRMMIALALLCEA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 519 SILLLDEATSALDAESEKIVQEALDRVMVGRT--TVVVAHRLSTV-RNADIIAVVGGGKIIESGSHDELISNPDGAYSSL 595
Cdd:PRK10418 160 PFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRS 239
|
.
gi 15220188 596 L 596
Cdd:PRK10418 240 L 240
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
987-1214 |
1.24e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 79.77 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 987 VHFSYPSrPDVTIFSDFNLLVPSGKSMALVGQSGSGKS-SVLSL--VLRFYDPTAGIIMIDGQDIKKLKLKSLRR----H 1059
Cdd:PRK09473 20 VTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALmgLLAANGRIGGSATFNGREILNLPEKELNKlraeQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1060 IGLVQQEPAlfaTTIYEnilYGKEGASESEV-MEAAKLANAHSFISSLPEGYSTKVGERGIQM-------SGGQRQRIAI 1131
Cdd:PRK09473 99 ISMIFQDPM---TSLNP---YMRVGEQLMEVlMLHKGMSKAEAFEESVRMLDAVKMPEARKRMkmyphefSGGMRQRVMI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1132 ARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTT--VVVAHRLSTIKNS-DMISVIQDGKIIEQGSHNILVEN 1208
Cdd:PRK09473 173 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaiIMITHDLGVVAGIcDKVLVMYAGRTMEYGNARDVFYQ 252
|
....*.
gi 15220188 1209 KNGPYS 1214
Cdd:PRK09473 253 PSHPYS 258
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
680-916 |
1.33e-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: 78.63 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 680 ALGIAQ-ALVSYYMDWETTQNEVKRISILFCCGSVITVIVHTIEHTTFGIMGERLTLRVRQKMFSAILRNEIGWFDKvdN 758
Cdd:cd18551 13 AASLAQpLLVKNLIDALSAGGSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDR--R 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 759 TSSMLASRLESDATLLRTIVVDRSTILLENLGLVVTAFIISFILNWRLTLVVLATYPL--IISGHISEKIF-----MQGY 831
Cdd:cd18551 91 RSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLafLIILPLGRRIRkaskrAQDA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 832 GGNLSkAYLkanmlaGESISNIRTVVAFCAEEKVLDLYSKELlepsERSFRRG-QMAGI---LYGVSQFFIFSSYGLALW 907
Cdd:cd18551 171 LGELS-AAL------ERALSAIRTVKASNAEERETKRGGEAA----ERLYRAGlKAAKIealIGPLMGLAVQLALLVVLG 239
|
....*....
gi 15220188 908 YGSILMEKG 916
Cdd:cd18551 240 VGGARVASG 248
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
110-273 |
1.36e-15 |
|
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: 78.74 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 110 HTGERQAAKIRKAYLRSMLSQDISLFDTEiSTGEVISAITSEilvVQDAISekvgNFMHFISrfiagfaIGFASVWQ--- 186
Cdd:cd18574 68 VVGERVAARLRNDLFSSLLRQDIAFFDTH-RTGELVNRLTAD---VQEFKS----SFKQCVS-------QGLRSVTQtvg 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 187 --ISLVTLS---------IVPFIALAGGIYAFVSSGLIVRVRKSYVKANEIAEEVIGNVRTVQAFTGEEKAVSSYQGALR 255
Cdd:cd18574 133 cvVSLYLISpkltllllvIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVE 212
|
170
....*....|....*...
gi 15220188 256 NTynygrkAGLAKGLGLG 273
Cdd:cd18574 213 KA------AKLNEKLGLG 224
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
389-586 |
1.49e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 81.63 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 389 GKVVALVGGSGSGKSTMISLIErFYEPTD----GAVMLDGndiRYLDLKWLRGHIGLVNQEPVLFAT-TIRENIMY---- 459
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALA-FRSPKGvkgsGSVLLNG---MPIDAKEMRAISAYVQQDDLFIPTlTVREHLMFqahl 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 460 --GKDDATSEEITNAAKLSEAISFIN--NLpegfETQVGERGIQLSGGQKQRISISRAIVKNPSILLLDEATSALDAESE 535
Cdd:TIGR00955 127 rmPRRVTKKEKRERVDEVLQALGLRKcaNT----RIGVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMA 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15220188 536 KIVQEALDRV-MVGRTTVVVAHRLST--VRNADIIAVVGGGKIIESGSHDELIS 586
Cdd:TIGR00955 203 YSVVQVLKGLaQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1009-1201 |
1.57e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 81.63 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1009 SGKSMALVGQSGSGKSSVLSlVLRFYDPT----AGIIMIDGqdiKKLKLKSLRRHIGLVQQEPALFAT-TIYENILY--- 1080
Cdd:TIGR00955 50 PGELLAVMGSSGAGKTTLMN-ALAFRSPKgvkgSGSVLLNG---MPIDAKEMRAISAYVQQDDLFIPTlTVREHLMFqah 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1081 -------GKEGASE--SEVMEAAKLANAHSfisslpegysTKVGERGIQ--MSGGQRQRIAIARAVLKNPEILLLDEATS 1149
Cdd:TIGR00955 126 lrmprrvTKKEKRErvDEVLQALGLRKCAN----------TRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15220188 1150 ALDVESERVVQQALDRL-MRDRTTVVVAHRLST--IKNSDMISVIQDGKIIEQGS 1201
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLaQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGS 250
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
386-577 |
1.81e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 77.80 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 386 IPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLD---LKWLRGHIGLVNQEP---VLFATTIRENI-- 457
Cdd:PRK10419 35 LKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQDSisaVNPRKTVREIIre 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 458 ----MYGKDDATSE----EITNAAKLSEAIsfINNLPEgfetqvgergiQLSGGQKQRISISRAIVKNPSILLLDEATSA 529
Cdd:PRK10419 115 plrhLLSLDKAERLarasEMLRAVDLDDSV--LDKRPP-----------QLSGGQLQRVCLARALAVEPKLLILDEAVSN 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15220188 530 LDA--ESEKIVQEALDRVMVGRTTVVVAHRLSTV-RNADIIAVVGGGKIIE 577
Cdd:PRK10419 182 LDLvlQAGVIRLLKKLQQQFGTACLFITHDLRLVeRFCQRVMVMDNGQIVE 232
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
375-590 |
1.89e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 78.69 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 375 DVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYlDLKWLRGHIGLV----NQEPVLfa 450
Cdd:PRK13537 19 DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVGVVpqfdNLDPDF-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 451 tTIRENIM-----YGKDDATSEEITnaAKLSEaisfINNLPEGFETQVGErgiqLSGGQKQRISISRAIVKNPSILLLDE 525
Cdd:PRK13537 96 -TVRENLLvfgryFGLSAAAARALV--PPLLE----FAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15220188 526 ATSALDAESEKIVQEALDRVMV-GRTTVVVAHRLSTV-RNADIIAVVGGGKIIESGSHDELISNPDG 590
Cdd:PRK13537 165 PTTGLDPQARHLMWERLRSLLArGKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALIESEIG 231
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
361-588 |
1.96e-15 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 79.50 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSRPDVVifDKLNFVIPAGKVVALVGGSGSGKST---MISLIERFyepTDGAVMLDGNDIRYLDLKwLRG 437
Cdd:PRK11650 4 LKLQAVRKSYDGKTQVI--KGIDLDVADGEFIVLVGPSGCGKSTllrMVAGLERI---TSGEIWIGGRVVNELEPA-DRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 438 hIGLVNQEPVLFA-TTIRENIMYG-------KDDaTSEEITNAAKLSEAISFINNLPEgfetqvgergiQLSGGQKQRIS 509
Cdd:PRK11650 78 -IAMVFQNYALYPhMSVRENMAYGlkirgmpKAE-IEERVAEAARILELEPLLDRKPR-----------ELSGGQRQRVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 510 ISRAIVKNPSILLLDEATSALDAeseKI-VQ-----EALDRVMvGRTTVVVAH-RLSTVRNADIIAVVGGGKIIESGSHD 582
Cdd:PRK11650 145 MGRAIVREPAVFLFDEPLSNLDA---KLrVQmrleiQRLHRRL-KTTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPV 220
|
....*.
gi 15220188 583 ELISNP 588
Cdd:PRK11650 221 EVYEKP 226
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
382-602 |
2.32e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 77.75 E-value: 2.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 382 LNFVIPAGKVVALVGGSGSGKSTMI----------SLIERFYEPTDGAVMLDGNDIRylDLKWLRGHIGLVNQEPVLF-A 450
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLrhlsglitgdKSAGSHIELLGRTVQREGRLAR--DIRKSRANTGYIFQQFNLVnR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 451 TTIRENIMYGKDDATSEEIT-----NAAKLSEAISFINNLpeGFETQVGERGIQLSGGQKQRISISRAIVKNPSILLLDE 525
Cdd:PRK09984 101 LSVLENVLIGALGSTPFWRTcfswfTREQKQRALQALTRV--GMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 526 ATSALDAESEKIVQEALDRVMV--GRTTVVVAHRLS-TVRNADIIAVVGGGKIIESGSHDELISNP-DGAYSSLLRIQEA 601
Cdd:PRK09984 179 PIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQFDNERfDHLYRSINRVEEN 258
|
.
gi 15220188 602 A 602
Cdd:PRK09984 259 A 259
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1004-1200 |
2.53e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 77.34 E-value: 2.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1004 NLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHiGLVQ--QEPALFAT-TIYENILY 1080
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM-GVVRtfQHVRLFREmTVIENLLV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1081 GKEGASESEVM------------EAAKLANAHSFISslpegystKVGERGI------QMSGGQRQRIAIARAVLKNPEIL 1142
Cdd:PRK11300 104 AQHQQLKTGLFsgllktpafrraESEALDRAATWLE--------RVGLLEHanrqagNLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15220188 1143 LLDEATSALDVESERVVQQALDRLMRDRTTVV--VAHRLSTIKN-SDMISVIQDGKIIEQG 1200
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIAELRNEHNVTVllIEHDMKLVMGiSDRIYVVNQGTPLANG 236
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
90-525 |
3.38e-15 |
|
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: 80.23 E-value: 3.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 90 FVYLSVVILFSSWLEVACWMHTGERQAAKIRKAYLRSMLSQDISLFDtEISTGEVISAITSEIlvvqDAISEkvgNFMHF 169
Cdd:COG4615 54 FAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLE-RIGAARLLAALTEDV----RTISQ---AFVRL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 170 ISRFIAGFAIGFASV------WQISLVTLSivpFIALAGGIYAFvssgLIVRVRKSYVKANEIAEEVIGNVRTV------ 237
Cdd:COG4615 126 PELLQSVALVLGCLAylawlsPPLFLLTLV---LLGLGVAGYRL----LVRRARRHLRRAREAEDRLFKHFRALlegfke 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 238 --------QAFTGEEKAVSSYQGA---LRNTYNYGRKAGLAKGLGLGSLHFVLFLSWALLIWFTSIVVhkGIAnggesfT 306
Cdd:COG4615 199 lklnrrrrRAFFDEDLQPTAERYRdlrIRADTIFALANNWGNLLFFALIGLILFLLPALGWADPAVLS--GFV------L 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 307 TML-------NVV---------------IAGLSLGQAAPDISTFMRASAAAYPIFQMIErntedktgrklgnvngdilFK 364
Cdd:COG4615 271 VLLflrgplsQLVgalptlsranvalrkIEELELALAAAEPAAADAAAPPAPADFQTLE-------------------LR 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 365 DVTFTYPSRPDVVIFD--KLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHIGLV 442
Cdd:COG4615 332 GVTYRYPGEDGDEGFTlgPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAV 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 443 NQEPVLFATtireniMYGKDDATSEEITNA----AKLSEAISFINNlpeGFETqvgergIQLSGGQKQRISISRAIVKNP 518
Cdd:COG4615 412 FSDFHLFDR------LLGLDGEADPARAREllerLELDHKVSVEDG---RFST------TDLSQGQRKRLALLVALLEDR 476
|
....*..
gi 15220188 519 SILLLDE 525
Cdd:COG4615 477 PILVFDE 483
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
360-588 |
5.45e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 78.15 E-value: 5.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 360 DILFKDVTFTYPsrpDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDG---NDIRYLDlkwlR 436
Cdd:PRK11000 3 SVTLRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEkrmNDVPPAE----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 437 GhIGLVNQEPVLFA-TTIRENIMYGKDDAtseeitnAAKLSEAISFINNLPEGFetQVG---ERGIQ-LSGGQKQRISIS 511
Cdd:PRK11000 76 G-VGMVFQSYALYPhLSVAENMSFGLKLA-------GAKKEEINQRVNQVAEVL--QLAhllDRKPKaLSGGQRQRVAIG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 512 RAIVKNPSILLLDEATSALDAesekivqeALdRVM-----------VGRTTVVVAH-RLSTVRNADIIAVVGGGKIIESG 579
Cdd:PRK11000 146 RTLVAEPSVFLLDEPLSNLDA--------AL-RVQmrieisrlhkrLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
....*....
gi 15220188 580 SHDELISNP 588
Cdd:PRK11000 217 KPLELYHYP 225
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
372-542 |
5.97e-15 |
|
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: 74.84 E-value: 5.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 372 SRPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHIGLVNQEPVLFAT 451
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 452 TIRENIMYGKDDATSEEITNAAklseaisfinnlpegfeTQVGERGI------QLSGGQKQRISISRAIVKNPSILLLDE 525
Cdd:cd03231 89 SVLENLRFWHADHSDEQVEEAL-----------------ARVGLNGFedrpvaQLSAGQQRRVALARLLLSGRPLWILDE 151
|
170
....*....|....*..
gi 15220188 526 ATSALDAESEKIVQEAL 542
Cdd:cd03231 152 PTTALDKAGVARFAEAM 168
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
373-579 |
6.06e-15 |
|
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: 75.39 E-value: 6.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 373 RPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEP---TDGAVMLDGndiRYLDLKWLRGHIGLVNQEPVLF 449
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNG---QPRKPDQFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 450 AT-TIRENIMYGKDDATSEEITNAAKLSEAISFInnLPEGFETQVGERGIQ-LSGGQKQRISISRAIVKNPSILLLDEAT 527
Cdd:cd03234 94 PGlTVRETLTYTAILRLPRKSSDAIRKKRVEDVL--LRDLALTRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15220188 528 SALDAESEKIVQEALDRVMVGRTTVVVA-H--RLSTVRNADIIAVVGGGKIIESG 579
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARRNRIVILTiHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
380-619 |
7.87e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 78.98 E-value: 7.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 380 DKLNFVIPAGKVVALVGGSGSGKS-TMISLIERFYEP----TDGAVMLDGNDIRYLDLKWLRG----HIGLVNQEPVLFA 450
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQEPMVSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 451 TTIR--ENIMY---------GKDDATSE--------EITNAAKLseaisfINNLPEgfetqvgergiQLSGGQKQRISIS 511
Cdd:PRK15134 106 NPLHtlEKQLYevlslhrgmRREAARGEilncldrvGIRQAAKR------LTDYPH-----------QLSGGERQRVMIA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 512 RAIVKNPSILLLDEATSALD----AESEKIVQEaLDRVMvGRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESGSHDELIS 586
Cdd:PRK15134 169 MALLTRPELLIADEPTTALDvsvqAQILQLLRE-LQQEL-NMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFS 246
|
250 260 270
....*....|....*....|....*....|....
gi 15220188 587 NPDGAYS-SLLRIQEAASPnlnhtPSLPVSTKPL 619
Cdd:PRK15134 247 APTHPYTqKLLNSEPSGDP-----VPLPEPASPL 275
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
374-576 |
8.79e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.53 E-value: 8.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 374 PDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRY------LDLKwlrghIGLVNQEPV 447
Cdd:COG3845 16 GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIrsprdaIALG-----IGMVHQHFM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 448 LFAT-TIRENIMYGKDDA------TSEEITNAAKLSEAIsfinnlpeGFE----TQVGergiQLSGGQKQRISISRAIVK 516
Cdd:COG3845 91 LVPNlTVAENIVLGLEPTkggrldRKAARARIRELSERY--------GLDvdpdAKVE----DLSVGEQQRVEILKALYR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220188 517 NPSILLLDEATSAL-DAESEKiVQEALdRVMV--GRTTVVVAHRLSTVR-NADIIAVVGGGKII 576
Cdd:COG3845 159 GARILILDEPTAVLtPQEADE-LFEIL-RRLAaeGKSIIFITHKLREVMaIADRVTVLRRGKVV 220
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
995-1198 |
1.53e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.03 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 995 PDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIK-KLKLKSLRRHIGLVQQE----PAL 1069
Cdd:PRK11288 15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGVAIIYQElhlvPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1070 fatTIYENILYGKEGAS-----ESEVMEAAKLANAHSFISSLPEgysTKVGErgiqMSGGQRQRIAIARAVLKNPEILLL 1144
Cdd:PRK11288 95 ---TVAENLYLGQLPHKggivnRRLLNYEAREQLEHLGVDIDPD---TPLKY----LSIGQRQMVEIAKALARNARVIAF 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15220188 1145 DEATSALdveSERVVQQ--ALDRLMRDRTTVV--VAHRLSTI-KNSDMISVIQDGKIIE 1198
Cdd:PRK11288 165 DEPTSSL---SAREIEQlfRVIRELRAEGRVIlyVSHRMEEIfALCDAITVFKDGRYVA 220
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
989-1201 |
1.95e-14 |
|
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: 78.90 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 989 FSYPSRPDVtifSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKlKLKSLRRHIGLVQQEPA 1068
Cdd:TIGR01257 938 FEPSGRPAV---DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNI 1013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1069 LFA-TTIYENILYGKEGASESEvmEAAKLAnahsfISSLPE--GYSTKVGERGIQMSGGQRQRIAIARAVLKNPEILLLD 1145
Cdd:TIGR01257 1014 LFHhLTVAEHILFYAQLKGRSW--EEAQLE-----MEAMLEdtGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLD 1086
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15220188 1146 EATSALDVESERVVQQALDRLMRDRTTVVVAHRLSTIKN-SDMISVIQDGKIIEQGS 1201
Cdd:TIGR01257 1087 EPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGT 1143
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1004-1201 |
2.99e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 74.28 E-value: 2.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1004 NLLVPSGKSMALVGQSGSGKSSVL----SLVLRFYDPTAGIIMIdGQDIKKL-----KLKSLRRHIGLVQQEPALF-ATT 1073
Cdd:PRK09984 24 DLNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDKSAGSHIELL-GRTVQREgrlarDIRKSRANTGYIFQQFNLVnRLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1074 IYENILYGKEGAS---ESEVMEAAKLANAHSFISSLPEGYSTKVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEATSA 1150
Cdd:PRK09984 103 VLENVLIGALGSTpfwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIAS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15220188 1151 LDVESERVVQQAL-DRLMRDRTTVVVA-HRLS-TIKNSDMISVIQDGKIIEQGS 1201
Cdd:PRK09984 183 LDPESARIVMDTLrDINQNDGITVVVTlHQVDyALRYCERIVALRQGHVFYDGS 236
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
380-589 |
3.38e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 73.87 E-value: 3.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 380 DKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIryldlKWLRGH----IGLVN--QEPVLFAT-T 452
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHI-----EGLPGHqiarMGVVRtfQHVRLFREmT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 453 IRENIMYGKD------------------DATSEEITNAAKLSEAIsfinNLPEGFETQVGergiQLSGGQKQRISISRAI 514
Cdd:PRK11300 97 VIENLLVAQHqqlktglfsgllktpafrRAESEALDRAATWLERV----GLLEHANRQAG----NLAYGQQRRLEIARCM 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15220188 515 VKNPSILLLDEATSALDAESEKIVQEALD--RVMVGRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESGSHDELISNPD 589
Cdd:PRK11300 169 VTQPEILMLDEPAAGLNPKETKELDELIAelRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEIRNNPD 246
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
982-1197 |
3.49e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.58 E-value: 3.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSrpdVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIK-KLKLKSLRRHI 1060
Cdd:PRK10762 5 LQLKGIDKAFPG---VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1061 GLVQQEPALFAT-TIYENILYGKE-----GASESEVM--EAAKLanahsfISSLPEGYSTK--VGERGIqmsgGQRQRIA 1130
Cdd:PRK10762 82 GIIHQELNLIPQlTIAENIFLGREfvnrfGRIDWKKMyaEADKL------LARLNLRFSSDklVGELSI----GEQQMVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220188 1131 IARAVLKNPEILLLDEATSAL-DVESErvvqqALDRLMRD-----RTTVVVAHRLSTI-KNSDMISVIQDGKII 1197
Cdd:PRK10762 152 IAKVLSFESKVIIMDEPTDALtDTETE-----SLFRVIRElksqgRGIVYISHRLKEIfEICDDVTVFRDGQFI 220
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
706-1146 |
3.52e-14 |
|
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: 76.76 E-value: 3.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 706 ILFCCGSVITVIVHTIEHTTFGIMGERLTLRVRQKMFSAILRNEIGWFDKVdNTSSMLASrLESDATLLrTIVVDRSTIL 785
Cdd:COG4615 52 LLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLERI-GAARLLAA-LTEDVRTI-SQAFVRLPEL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 786 LENLGLVVTAFIISFILNWRLTLVVLATYPLIISGhisekifmqgYGGNLSKAYlKANMLAGES----ISNIRTVVAFCA 861
Cdd:COG4615 129 LQSVALVLGCLAYLAWLSPPLFLLTLVLLGLGVAG----------YRLLVRRAR-RHLRRAREAedrlFKHFRALLEGFK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 862 E-----EKVLDLYSKELLEPSERsFRRGQMAGILY-----GVSQFFIFSSYGLALWYGSILmekgLSSFESVMKTFmVLI 931
Cdd:COG4615 198 ElklnrRRRRAFFDEDLQPTAER-YRDLRIRADTIfalanNWGNLLFFALIGLILFLLPAL----GWADPAVLSGF-VLV 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 932 VTALV--MGEVLALAPDLLKGN---QMVVSVFELLDRRTQVVGDTGEELSNVE-GTIELKGVHFSYPSRPDVTIFS--DF 1003
Cdd:COG4615 272 LLFLRgpLSQLVGALPTLSRANvalRKIEELELALAAAEPAAADAAAPPAPADfQTLELRGVTYRYPGEDGDEGFTlgPI 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1004 NLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIGLVQQEPALFATtiyeniLYGKE 1083
Cdd:COG4615 352 DLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDR------LLGLD 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1084 GASESEVMEA--AKLANAHsfisslpegystKVGERG-----IQMSGGQRQRIAIARAVLKNPEILLLDE 1146
Cdd:COG4615 426 GEADPARAREllERLELDH------------KVSVEDgrfstTDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
363-586 |
4.28e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.49 E-value: 4.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 363 FKDVTFTYPSrpdVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLK-WLRGHIGL 441
Cdd:PRK11288 7 FDGIGKTFPG---VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGVAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 442 VNQE----PVLfatTIRENIMYGKDDATSEEITNAAKLSEAISFINNLPEGF--ETQVGErgiqLSGGQKQRISISRAIV 515
Cdd:PRK11288 84 IYQElhlvPEM---TVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIdpDTPLKY----LSIGQRQMVEIAKALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 516 KNPSILLLDEATSALDA-ESE---KIVQEALDRvmvGRTTVVVAHRLSTV-RNADIIAVVGGGKIIESG------SHDEL 584
Cdd:PRK11288 157 RNARVIAFDEPTSSLSArEIEqlfRVIRELRAE---GRVILYVSHRMEEIfALCDAITVFKDGRYVATFddmaqvDRDQL 233
|
..
gi 15220188 585 IS 586
Cdd:PRK11288 234 VQ 235
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
378-538 |
4.65e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 72.89 E-value: 4.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 378 IFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKW---LRG-HIGLVNQEPVLFAT-T 452
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakLRAkHVGFVFQSFMLIPTlN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 453 IRENI-----MYGKDDATSEEitNAAKLSEAISF---INNLPEgfetqvgergiQLSGGQKQRISISRAIVKNPSILLLD 524
Cdd:PRK10584 105 ALENVelpalLRGESSRQSRN--GAKALLEQLGLgkrLDHLPA-----------QLSGGEQQRVALARAFNGRPDVLFAD 171
|
170
....*....|....*
gi 15220188 525 EATSALDAES-EKIV 538
Cdd:PRK10584 172 EPTGNLDRQTgDKIA 186
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
378-587 |
4.85e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 73.00 E-value: 4.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 378 IFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDL--KWLRGhIGLVNQEPVLFAT-TIR 454
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhaRARRG-IGYLPQEASIFRRlSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 455 ENIMYG---KDDATSEEITNAAklseaisfiNNLPEGFETQ--VGERGIQLSGGQKQRISISRAIVKNPSILLLDEATSA 529
Cdd:PRK10895 97 DNLMAVlqiRDDLSAEQREDRA---------NELMEEFHIEhlRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15220188 530 LDAES----EKIVQEALDRvmvGRTTVVVAHRL-STVRNADIIAVVGGGKIIESGSHDELISN 587
Cdd:PRK10895 168 VDPISvidiKRIIEHLRDS---GLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
977-1194 |
6.17e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.98 E-value: 6.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 977 NVEGTIELKGVHFSYPSrpdVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLK-S 1055
Cdd:PRK09700 1 MATPYISMAGIGKSFGP---VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1056 LRRHIGLVQQEPALF-ATTIYENILYGKE------GASESEVMEAAKLANAHSFISSLPEGYSTKVGErgiqMSGGQRQR 1128
Cdd:PRK09700 78 AQLGIGIIYQELSVIdELTVLENLYIGRHltkkvcGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15220188 1129 IAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVV-VAHRLSTIKN-SDMISVIQDG 1194
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDG 221
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
994-1170 |
6.88e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 71.83 E-value: 6.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 994 RPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIG-LVQQEPALfat 1072
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGhRNAMKPAL--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1073 TIYENI-----LYGKEGASESEVMEAAKLANahsfISSLPEGYstkvgergiqMSGGQRQRIAIARAVLKNPEILLLDEA 1147
Cdd:PRK13539 89 TVAENLefwaaFLGGEELDIAAALEAVGLAP----LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEP 154
|
170 180
....*....|....*....|...
gi 15220188 1148 TSALDVESERVVQqaldRLMRDR 1170
Cdd:PRK13539 155 TAALDAAAVALFA----ELIRAH 173
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
372-543 |
8.54e-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: 71.24 E-value: 8.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 372 SRPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHIGLVNQEPVLFAT 451
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 452 TIRENIMYGKDDATSEEITnaakLSEAIsfinnlpegfeTQVGERGI------QLSGGQKQRISISRAIVKNPSILLLDE 525
Cdd:TIGR01189 89 SALENLHFWAAIHGGAQRT----IEDAL-----------AAVGLTGFedlpaaQLSAGQQRRLALARLWLSRRPLWILDE 153
|
170
....*....|....*...
gi 15220188 526 ATSALDAESEKIVQEALD 543
Cdd:TIGR01189 154 PTTALDKAGVALLAGLLR 171
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
995-1198 |
1.04e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 75.21 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 995 PDVTIFSDFNLLVPSGKSMALVGQSGSGKSS---VLSLVLRF--YDptaGIIMIDGQ-----DIKKlklkSLRRHIGLVQ 1064
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTlmkVLSGVYPHgsYE---GEILFDGEvcrfkDIRD----SEALGIVIIH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1065 QEPALFA-TTIYENILYGKEGASE-----SEVMEAAK--LANAhsfisSLPEGYSTKVGERGIqmsgGQRQRIAIARAVL 1136
Cdd:NF040905 85 QELALIPyLSIAENIFLGNERAKRgvidwNETNRRARelLAKV-----GLDESPDTLVTDIGV----GKQQLVEIAKALS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15220188 1137 KNPEILLLDEATSAL-DVESERVvqqaLDRLMRDR----TTVVVAHRLSTI-KNSDMISVIQDGKIIE 1198
Cdd:NF040905 156 KDVKLLILDEPTAALnEEDSAAL----LDLLLELKaqgiTSIIISHKLNEIrRVADSITVLRDGRTIE 219
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
365-623 |
1.15e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 73.61 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 365 DVTFTYPSrPDVVIFDKLNFVIPAGKVVALVGGSGSGKS-TMISLIERFYEP--TDGAVMLDGNDIRYL---DLKWLRG- 437
Cdd:PRK09473 19 RVTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREILNLpekELNKLRAe 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 438 HIGLVNQEPVlfaTT------IRENIM--------YGKDDATSEEIT--NAAKLSEAISFINNLPEGFetqvgergiqlS 501
Cdd:PRK09473 98 QISMIFQDPM---TSlnpymrVGEQLMevlmlhkgMSKAEAFEESVRmlDAVKMPEARKRMKMYPHEF-----------S 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 502 GGQKQRISISRAIVKNPSILLLDEATSALDAESEKIVQEALDRVM--VGRTTVVVAHRLSTVRN-ADIIAVVGGGKIIES 578
Cdd:PRK09473 164 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKreFNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEY 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 15220188 579 GSHDELISNPDGAYSSLLriqeaaspnLNHTPSLPVSTKPLPELP 623
Cdd:PRK09473 244 GNARDVFYQPSHPYSIGL---------LNAVPRLDAEGESLLTIP 279
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
380-596 |
1.47e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 75.28 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 380 DKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLD---LKWLRGHIGLVNQEPvlFAT----- 451
Cdd:PRK10261 341 EKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDP--YASldprq 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 452 TIRENIM-----YGKDDATSEeitnAAKLSEAISFINNLPEgfetQVGERGIQLSGGQKQRISISRAIVKNPSILLLDEA 526
Cdd:PRK10261 419 TVGDSIMeplrvHGLLPGKAA----AARVAWLLERVGLLPE----HAWRYPHEFSGGQRQRICIARALALNPKVIIADEA 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220188 527 TSALDAE-SEKIVQEALD--RVMvGRTTVVVAHRLSTV-RNADIIAVVGGGKIIESGSHDELISNPDGAYSSLL 596
Cdd:PRK10261 491 VSALDVSiRGQIINLLLDlqRDF-GIAYLFISHDMAVVeRISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKL 563
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
998-1200 |
1.62e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.22 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 998 TIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIGLVQQEPALFATTIYEN 1077
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEVDWSFPVLVEDV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1078 ILYGKEG---------ASESEVMEAAkLANAhsfisSLPEGYSTKVGErgiqMSGGQRQRIAIARAVLKNPEILLLDEAT 1148
Cdd:PRK15056 101 VMMGRYGhmgwlrrakKRDRQIVTAA-LARV-----DMVEFRHRQIGE----LSGGQKKRVFLARAIAQQGQVILLDEPF 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15220188 1149 SALDVESE-RVVqqALDRLMRD--RTTVVVAHRLSTIKNSDMISVIQDGKIIEQG 1200
Cdd:PRK15056 171 TGVDVKTEaRII--SLLRELRDegKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
63-289 |
1.64e-13 |
|
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: 72.37 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 63 GKLINIIGlaylfpQEASHKVAKYSLDFVYL-SVVILFSSWLEVACWMHTGERQAAKIRKAYLRSMLSQDISLFDtEIST 141
Cdd:cd18590 20 GRVIDILG------GEYQHNAFTSAIGLMCLfSLGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFE-KTKT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 142 GEVISAITSEILVVQDAISEKVGNFMHFISRFIAGFAIGFASVWQISLVTLSIVPFIALAGGIYAFVSSGLIVRVRKSYV 221
Cdd:cd18590 93 GDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIA 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15220188 222 KANEIAEEVIGNVRTVQAFTGEEKAVSSYQGALRNTYNYGRKAGLAKGLGLGsLHFVLFLSWALLIWF 289
Cdd:cd18590 173 KAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLL-VRRVLQLGVQVLMLY 239
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
368-579 |
1.64e-13 |
|
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: 71.59 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 368 FTYPSRPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNdIRYLDLKWLRGHIGLV--NQE 445
Cdd:cd03267 26 LFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VPWKRRKKFLRRIGVVfgQKT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 446 PVLFATTIRENI-----MYGKDDAtsEEITNAAKLSEAIsfinNLPEGFETQVgeRgiQLSGGQKQRISISRAIVKNPSI 520
Cdd:cd03267 105 QLWWDLPVIDSFyllaaIYDLPPA--RFKKRLDELSELL----DLEELLDTPV--R--QLSLGQRMRAEIAAALLHEPEI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220188 521 LLLDEATSALDAESEKIVQEALDRVMVGRTTVVV--AHRLSTV-RNADIIAVVGGGKIIESG 579
Cdd:cd03267 175 LFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLltSHYMKDIeALARRVLVIDKGRLLYDG 236
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
729-908 |
1.99e-13 |
|
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: 72.54 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 729 MGERLTLRVRQKMFSAILRNEIGWFDKvDNTSSmLASRLESDATLLRTIVVDRSTILLENLGLVVTAFIISFILNWRLTL 808
Cdd:cd18563 70 LGERITADLRRDLYEHLQRLSLSFFDK-RQTGS-LMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLAL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 809 VVLATYPLIIsghisekIFMQGYGGNLSKAYLKA-------NMLAGESISNIRTVVAFCAEEKV---LDLYSKELLEPSE 878
Cdd:cd18563 148 LVLIPVPLVV-------WGSYFFWKKIRRLFHRQwrrwsrlNSVLNDTLPGIRVVKAFGQEKREikrFDEANQELLDANI 220
|
170 180 190
....*....|....*....|....*....|
gi 15220188 879 RSFRRGQMAGILYGvsqfFIFSSYGLALWY 908
Cdd:cd18563 221 RAEKLWATFFPLLT----FLTSLGTLIVWY 246
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1005-1200 |
2.07e-13 |
|
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: 74.45 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1005 LLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGII-------MIDGQDIKKLKLKSLRRHIGLVQQEPALFA-TTIYE 1076
Cdd:TIGR03269 305 LEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKPGPDGRGRAKRYIGILHQEYDLYPhRTVLD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1077 NIL--YGKEGASESEVMEAAKLANAHSFisslPEGYSTKVGER-GIQMSGGQRQRIAIARAVLKNPEILLLDEATSALDV 1153
Cdd:TIGR03269 385 NLTeaIGLELPDELARMKAVITLKMVGF----DEEKAEEILDKyPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDP 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15220188 1154 ESERVVQQAL--DRLMRDRTTVVVAHRLSTIKN-SDMISVIQDGKIIEQG 1200
Cdd:TIGR03269 461 ITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIG 510
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
699-920 |
2.42e-13 |
|
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: 72.04 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 699 NEVKRISILFCCGSVITVIVHTIEHTTFGIMGERLTLRVRQKMFSAILRNEIGWFDKvdNTSSMLASRLESD----ATLL 774
Cdd:cd18544 38 QGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDR--TPVGRLVTRVTNDtealNELF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 775 RTIVVDrstiLLENLGLVVTAFIISFILNWRLTLVVLATYPLIIsghisekIFMQGYGGNLSKAYLK-----ANMLA--G 847
Cdd:cd18544 116 TSGLVT----LIGDLLLLIGILIAMFLLNWRLALISLLVLPLLL-------LATYLFRKKSRKAYREvreklSRLNAflQ 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15220188 848 ESISNIRTVVAFCAEEKVL---DLYSKELLEPSERSFRrgqMAGILYGVSQFFIFSSYGLALWYGSILMEKGLSSF 920
Cdd:cd18544 185 ESISGMSVIQLFNREKREFeefDEINQEYRKANLKSIK---LFALFRPLVELLSSLALALVLWYGGGQVLSGAVTL 257
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
361-597 |
2.62e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.84 E-value: 2.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYpsRPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHIG 440
Cdd:PRK15056 7 IVVNDVTVTW--RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 441 LVNQEPVLFATTIRENIMYGK-------DDATSEEitnAAKLSEAISFINNLpEGFETQVGErgiqLSGGQKQRISISRA 513
Cdd:PRK15056 85 QSEEVDWSFPVLVEDVVMMGRyghmgwlRRAKKRD---RQIVTAALARVDMV-EFRHRQIGE----LSGGQKKRVFLARA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 514 IVKNPSILLLDEATSALDAESE-KIVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVGGGKIIESGSHDELIS--NPDG 590
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEaRIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTETTFTaeNLEL 236
|
....*..
gi 15220188 591 AYSSLLR 597
Cdd:PRK15056 237 AFSGVLR 243
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1000-1196 |
2.95e-13 |
|
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: 69.38 E-value: 2.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1000 FSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRH-IGLV----QQEPALFATTI 1074
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVpedrKREGLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1075 YENILygkegasesevmeaaklanahsfISSLpegystkvgergiqMSGGQRQRIAIARAVLKNPEILLLDEATSALDVE 1154
Cdd:cd03215 96 AENIA-----------------------LSSL--------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15220188 1155 SERVVQQALDRLMRDRTTVVVahrLST-----IKNSDMISVIQDGKI 1196
Cdd:cd03215 139 AKAEIYRLIRELADAGKAVLL---ISSeldelLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1002-1201 |
2.99e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 71.58 E-value: 2.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1002 DFNLLVPSGksmaLVGQSGSGKSSV---LSLVLRfydPTAGIIMIDGQ--DIKKLKLKSLRRHIGLVQQEP--ALFATTI 1074
Cdd:PRK13638 23 DFSLSPVTG----LVGANGCGKSTLfmnLSGLLR---PQKGAVLWQGKplDYSKRGLLALRQQVATVFQDPeqQIFYTDI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1075 YENILYGKE--GASESEVM----EAAKLANAHSFisslpegystkvGERGIQ-MSGGQRQRIAIARAVLKNPEILLLDEA 1147
Cdd:PRK13638 96 DSDIAFSLRnlGVPEAEITrrvdEALTLVDAQHF------------RHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15220188 1148 TSALDVES--------ERVVQQAldrlmrdRTTVVVAHRLSTIKN-SDMISVIQDGKIIEQGS 1201
Cdd:PRK13638 164 TAGLDPAGrtqmiaiiRRIVAQG-------NHVIISSHDIDLIYEiSDAVYVLRQGQILTHGA 219
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
382-588 |
3.00e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.12 E-value: 3.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 382 LNFVIPAGKVVALVGGSGSGKSTMISLIERFYePTDGAVMLDGNDIRYLDLKWLRGHIG-LVNQEPVLFATTIRENI-MY 459
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAyLSQQQTPPFAMPVFQYLtLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 460 GKDDATSEEITNAakLSEAISFINnLPEGFETQVGergiQLSGGQKQRISISRAIVK-----NPS--ILLLDEATSALDa 532
Cdd:PRK03695 94 QPDKTRTEAVASA--LNEVAEALG-LDDKLGRSVN----QLSGGEWQRVRLAAVVLQvwpdiNPAgqLLLLDEPMNSLD- 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15220188 533 esekIVQE-ALDRVMV-----GRTTVVVAHRLS-TVRNADIIAVVGGGKIIESGSHDELISNP 588
Cdd:PRK03695 166 ----VAQQaALDRLLSelcqqGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1003-1201 |
3.18e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 70.73 E-value: 3.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1003 FNLLVPSGKSMALVGQSGSGKSSVLSL---VLrfydPTAGIIMIDGQDIKKLKLKSLRRHIG-LVQQEPALFATTIYENI 1078
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARmagLL----PGSGSIQFAGQPLEAWSAAELARHRAyLSQQQTPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1079 -LYGKEGASE-------SEVMEAAKLANahsfisslpegystKVGERGIQMSGGQRQRIAIARAVLK-----NPE--ILL 1143
Cdd:PRK03695 91 tLHQPDKTRTeavasalNEVAEALGLDD--------------KLGRSVNQLSGGEWQRVRLAAVVLQvwpdiNPAgqLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15220188 1144 LDEATSALDveserVVQQ-ALDRLMRD-----RTTVVVAHRLS-TIKNSDMISVIQDGKIIEQGS 1201
Cdd:PRK03695 157 LDEPMNSLD-----VAQQaALDRLLSElcqqgIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGR 216
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
361-586 |
3.45e-13 |
|
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: 73.68 E-value: 3.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPsrpDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERF--YEPTDGAVM----------------- 421
Cdd:TIGR03269 1 IEVKNLTKKFD---GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 422 -----------LDGNDIRYLDL-----KWLRGHIGLVNQEPvlFA----TTIRENIMYGKDDA---TSEEITNAAKLSEa 478
Cdd:TIGR03269 78 vgepcpvcggtLEPEEVDFWNLsdklrRRIRKRIAIMLQRT--FAlygdDTVLDNVLEALEEIgyeGKEAVGRAVDLIE- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 479 isfinnlpegfETQVGER----GIQLSGGQKQRISISRAIVKNPSILLLDEATSALDAESEKIVQEALDRVMV--GRTTV 552
Cdd:TIGR03269 155 -----------MVQLSHRithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasGISMV 223
|
250 260 270
....*....|....*....|....*....|....*
gi 15220188 553 VVAHRLSTVRN-ADIIAVVGGGKIIESGSHDELIS 586
Cdd:TIGR03269 224 LTSHWPEVIEDlSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
982-1178 |
3.89e-13 |
|
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: 68.72 E-value: 3.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSrpDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVlrfydptAGIIMIDGQDIKKLklksLRRHIG 1061
Cdd:cd03223 1 IELENLSLATPD--GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRAL-------AGLWPWGSGRIGMP----EGEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEPALFATTIYENILY--GKEgasesevmeaaklanahsfisslpegystkvgergiqMSGGQRQRIAIARAVLKNP 1139
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIYpwDDV-------------------------------------LSGGEQQRLAFARLLLHKP 110
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15220188 1140 EILLLDEATSALDVESERVVQQALDRLMrdrTTVV-VAHR 1178
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQLLKELG---ITVIsVGHR 147
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
996-1201 |
5.26e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 70.44 E-value: 5.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 996 DVTIFSDFNLLVPSGKSMALVGQSGSGKSSvLSLVLR---FYDPTAGIIMIDGQDIKKLKlKSLRRHIG--LVQQEP--- 1067
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKST-LSKVIAghpAYKILEGDILFKGESILDLE-PEERAHLGifLAFQYPiei 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1068 -----ALFATTIYEN--ILYGKEGASESE----VMEAAKLAN-AHSFIS-SLPEGYstkvgergiqmSGGQRQRIAIARA 1134
Cdd:CHL00131 97 pgvsnADFLRLAYNSkrKFQGLPELDPLEfleiINEKLKLVGmDPSFLSrNVNEGF-----------SGGEKKRNEILQM 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1135 VLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVV-VAH--RLSTIKNSDMISVIQDGKIIEQGS 1201
Cdd:CHL00131 166 ALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
996-1197 |
5.40e-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: 72.94 E-value: 5.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 996 DVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYdPTA---GIIMIDGQDIKKLKLKSL-RRHIGLVQQEPALFA 1071
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGtwdGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1072 T-TIYENILYGKEGASESEVME-AAKLANAHSFIS--SLPEGYSTK-VGERGiqmsGGQRQRIAIARAVLKNPEILLLDE 1146
Cdd:TIGR02633 92 ElSVAENIFLGNEITLPGGRMAyNAMYLRAKNLLRelQLDADNVTRpVGDYG----GGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15220188 1147 ATSAL-DVESERVVQQALDRLMRDRTTVVVAHRLSTIKN-SDMISVIQDGKII 1197
Cdd:TIGR02633 168 PSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
378-581 |
6.72e-13 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 69.82 E-value: 6.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 378 IFDKLNFVIPAGKVVALVGGSGSGKSTMISLI--ERFYEPTDGAVMLDGNDIRYLDLKWLRGH-IGLVNQEPV------- 447
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPEDRAGEgIFMAFQYPVeipgvsn 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 448 -LFATTIRENIMYGKDDATSEEITNAAKLSEAISFINnLPEGFETQVGERGiqLSGGQKQRISISRAIVKNPSILLLDEA 526
Cdd:PRK09580 96 qFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLK-MPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPELCILDES 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15220188 527 TSALDAESEKIVQEALDRVMVG-RTTVVVAH--RLSTVRNADIIAVVGGGKIIESGSH 581
Cdd:PRK09580 173 DSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDF 230
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
982-1179 |
7.57e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 69.76 E-value: 7.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRpdvTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQdikklklksLRrhIG 1061
Cdd:PRK09544 5 VSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEPALFAT---TIyENILYGKEGASESEVMEAAKLANAHSFISSLPEgystkvgergiQMSGGQRQRIAIARAVLKN 1138
Cdd:PRK09544 71 YVPQKLYLDTTlplTV-NRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQ-----------KLSGGETQRVLLARALLNR 138
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15220188 1139 PEILLLDEATSALDVESERVVQQALDRLMRDRTTVV--VAHRL 1179
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVlmVSHDL 181
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
363-561 |
7.90e-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: 68.42 E-value: 7.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 363 FKDVTFTYPS-RPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTM---------ISLIErfyeptdGAVMLDGndiRYLDL 432
Cdd:cd03232 6 WKNLNYTVPVkGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLldvlagrktAGVIT-------GEILING---RPLDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 433 KWLRGhIGLVNQEPVLFAT-TIRENIMYgkddatseeitnAAKLseaisfinnlpegfetqvgeRGiqLSGGQKQRISIS 511
Cdd:cd03232 76 NFQRS-TGYVEQQDVHSPNlTVREALRF------------SALL--------------------RG--LSVEQRKRLTIG 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15220188 512 RAIVKNPSILLLDEATSALDAESEKIVQEALDRV-MVGRTTVVVAHRLSTV 561
Cdd:cd03232 121 VELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLaDSGQAILCTIHQPSAS 171
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
979-1146 |
9.64e-13 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 69.29 E-value: 9.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 979 EGTIELKGVHFSYPSRPDVtifSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKL-KSLR 1057
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVV---KDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMhKRAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1058 RHIGLVQQEPALFAT-TIYENILygkegAseseVMEAAKL--ANAHSFISSLPEGYS-TKVGE-RGIQMSGGQRQRIAIA 1132
Cdd:COG1137 78 LGIGYLPQEASIFRKlTVEDNIL-----A----VLELRKLskKEREERLEELLEEFGiTHLRKsKAYSLSGGERRRVEIA 148
|
170
....*....|....
gi 15220188 1133 RAVLKNPEILLLDE 1146
Cdd:COG1137 149 RALATNPKFILLDE 162
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
998-1197 |
9.98e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.83 E-value: 9.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 998 TIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKklklkslrrhiglVQQEpalfaTTIYEN 1077
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQ-------------FGRE-----ASLIDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1078 ILYGKEGASESEVMEAAKLANAHSFISSLPEgystkvgergiqMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESER 1157
Cdd:COG2401 106 IGRKGDFKDAVELLNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15220188 1158 VVQQALDRLMRDR--TTVVVAHRlstiknSDMISVIQDGKII 1197
Cdd:COG2401 174 RVARNLQKLARRAgiTLVVATHH------YDVIDDLQPDLLI 209
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
41-335 |
1.17e-12 |
|
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: 70.14 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 41 MALGSIGACIHGASVPVFFIFFGKLINIIglaylFPQEASHKVAKYSLDFVYLSVVILFSSWLEVACWMHTGERQAAKIR 120
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDI-----FVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 121 KAYLRSMLSQDISLFDTEiSTGEVISAITSEILVVQDAISEKVGNFMHFISRFIAGFAIGFASVWQISLVTLSIVPFIAL 200
Cdd:cd18552 76 NDLFDKLLRLPLSFFDRN-SSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 201 aggiyafvssgLIVRVRKSYVKA-----------NEIAEEVIGNVRTVQAFTGEEKAVSSYQGALRNTYNYGRKAGLAKG 269
Cdd:cd18552 155 -----------PIRRIGKRLRKIsrrsqesmgdlTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARA 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15220188 270 LGLGSLHFVLFLSWALLIWFTSIVVHKGIANGGE--SFTTMLNVVIAGL-SLGQAapdISTFMRASAAA 335
Cdd:cd18552 224 LSSPLMELLGAIAIALVLWYGGYQVISGELTPGEfiSFITALLLLYQPIkRLSNV---NANLQRGLAAA 289
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
374-586 |
1.18e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.88 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 374 PDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYePT---DGAVMLDGNDIRYLDLKWL-RGHIGLVNQEPVLF 449
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRDTeRAGIAIIHQELALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 450 AT-TIRENIMYGKDDATSEEITNAAKLSEAISFINNLpeGFETQVGERGIQLSGGQKQRISISRAIVKNPSILLLDEATS 528
Cdd:PRK13549 95 KElSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTA 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15220188 529 ALdAESE-----KIVQEALDRvmvGRTTVVVAHRLSTVRN-ADIIAVVGGGKII-----ESGSHDELIS 586
Cdd:PRK13549 173 SL-TESEtavllDIIRDLKAH---GIACIYISHKLNEVKAiSDTICVIRDGRHIgtrpaAGMTEDDIIT 237
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
981-1198 |
1.18e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 71.93 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 981 TIELKGVHFSYPSRPdvtiFS--DFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRR 1058
Cdd:PRK10522 322 TLELRNVTFAYQDNG----FSvgPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRK 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1059 HIGLVQQEPALFATtiyeniLYGKEGasesevmEAAKLANAHSFISSLpeGYSTKVGERG-----IQMSGGQRQRIAIAR 1133
Cdd:PRK10522 398 LFSAVFTDFHLFDQ------LLGPEG-------KPANPALVEKWLERL--KMAHKLELEDgrisnLKLSKGQKKRLALLL 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15220188 1134 AVLKNPEILLLDEATSALDVESERVVQQALDRLMRD--RTTVVVAHRLSTIKNSDMISVIQDGKIIE 1198
Cdd:PRK10522 463 ALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEmgKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
994-1215 |
1.24e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.20 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 994 RPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQ----------DIKKLKLKSLRR----H 1059
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELSEQSAAQMRHvrgaD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1060 IGLVQQEP-----ALFAT--TIYENILYgKEGASESEVMEAAK-------LANAHSFISSLPEgystkvgergiQMSGGQ 1125
Cdd:PRK10261 106 MAMIFQEPmtslnPVFTVgeQIAESIRL-HQGASREEAMVEAKrmldqvrIPEAQTILSRYPH-----------QLSGGM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1126 RQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVV--VAHRLSTIKN-SDMISVIQDGKIIEQGSH 1202
Cdd:PRK10261 174 RQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVifITHDMGVVAEiADRVLVMYQGEAVETGSV 253
|
250
....*....|...
gi 15220188 1203 NILVENKNGPYSK 1215
Cdd:PRK10261 254 EQIFHAPQHPYTR 266
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1004-1209 |
1.32e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 68.75 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1004 NLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKL-KSLRRHIGLVQQEPALFA-TTIYENILYG 1081
Cdd:PRK11614 25 SLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTaKIMREAVAIVPEGRRVFSrMTVEENLAMG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1082 KEGASESEVMEaaKLANAHSFISSLPEGYSTKVGergiQMSGGQRQRIAIARAVLKNPEILLLDEATSALdveSERVVQQ 1161
Cdd:PRK11614 105 GFFAERDQFQE--RIKWVYELFPRLHERRIQRAG----TMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL---APIIIQQ 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15220188 1162 ALDRLMRDR----TTVVVAHRLS-TIKNSDMISVIQDGKIIEQGSHNILVENK 1209
Cdd:PRK11614 176 IFDTIEQLReqgmTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLANE 228
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
988-1200 |
1.58e-12 |
|
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: 68.51 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 988 HFSYPSRPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRhIGLV--QQ 1065
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRR-IGVVfgQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1066 E------PAL----FATTIY--ENILYGKEGASESEVMEAAKLANahsfisslpegysTKVgeRgiQMSGGQRQRIAIAR 1133
Cdd:cd03267 104 TqlwwdlPVIdsfyLLAAIYdlPPARFKKRLDELSELLDLEELLD-------------TPV--R--QLSLGQRMRAEIAA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1134 AVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVVV--AHRLSTI-KNSDMISVIQDGKIIEQG 1200
Cdd:cd03267 167 ALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLltSHYMKDIeALARRVLVIDKGRLLYDG 236
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
375-580 |
1.61e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 68.90 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 375 DVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERF--YEPTDGAVMLDGNDIRYLDLKwLRGHIGL----------- 441
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHLGIflafqypieip 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 442 -VNQEPVLFATTIRENIMYGKDDATS-------EEITNAAKLSEaiSFIN-NLPEGFetqvgergiqlSGGQKQRISISR 512
Cdd:CHL00131 98 gVSNADFLRLAYNSKRKFQGLPELDPlefleiiNEKLKLVGMDP--SFLSrNVNEGF-----------SGGEKKRNEILQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15220188 513 AIVKNPSILLLDEATSALDAESEKIVQEALDRVM-VGRTTVVVAH--RLSTVRNADIIAVVGGGKIIESGS 580
Cdd:CHL00131 165 MALLDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
725-919 |
2.00e-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: 69.42 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 725 TFGIMGERLTLRVRQKMFSAILRNEIGWFDKvdNTSSMLASRLESDATLLRTIVVDRSTILLENLGLVVTAFIISFILNW 804
Cdd:cd18589 59 IYNITMSRIHSRLQGLVFAAVLRQEIAFFDS--NQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSP 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 805 RLTLVVLATYPLI-----ISGHisekiFMQGYGGNLSKAYLKANMLAGESISNIRTVVAFCAEEKVLDLYSKELlepsER 879
Cdd:cd18589 137 KLALLTALGLPLLllvpkFVGK-----FQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRL----QK 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15220188 880 SFRRGQMAGILYGVSQFFI-FSSYGLA---LWYGSILMEKGLSS 919
Cdd:cd18589 208 TYRLNKKEAAAYAVSMWTSsFSGLALKvgiLYYGGQLVTAGTVS 251
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
381-599 |
2.28e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 69.90 E-value: 2.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 381 KLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDG-------NDIryldlkWL---RGHIGLVNQEPVLFA 450
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaeKGI------CLppeKRRIGYVFQDARLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 451 -TTIRENIMYGKDDATSEEITNAAKLSEAISFINNLPegfetqvgergIQLSGGQKQRISISRAIVKNPSILLLDEATSA 529
Cdd:PRK11144 90 hYKVRGNLRYGMAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLAS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 530 LDAESEKIVQEALDRVM--VGRTTVVVAHRLSTV-RNADIIAVVGGGKIIESGSHDELISN-------PDGAYSSLLRIQ 599
Cdd:PRK11144 159 LDLPRKRELLPYLERLAreINIPILYVSHSLDEIlRLADRVVVLEQGKVKAFGPLEEVWASsamrpwlPKEEQSSILKVT 238
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
373-623 |
2.36e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.42 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 373 RPDVVIFDKLNFVIPAGKVVALVGGSGSGKS-TMISLIeRFYEPTDGAVMLDG-------------NDIRYLDLKWLRG- 437
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALM-RLLEQAGGLVQCDKmllrrrsrqvielSEQSAAQMRHVRGa 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 438 HIGLVNQEPVL-----------FATTIRENIMYGKDDATSEeitnAAKLSEAIsfinNLPEGfETQVGERGIQLSGGQKQ 506
Cdd:PRK10261 105 DMAMIFQEPMTslnpvftvgeqIAESIRLHQGASREEAMVE----AKRMLDQV----RIPEA-QTILSRYPHQLSGGMRQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 507 RISISRAIVKNPSILLLDEATSALDAESE-KIVQeaLDRVM---VGRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESGSH 581
Cdd:PRK10261 176 RVMIAMALSCRPAVLIADEPTTALDVTIQaQILQ--LIKVLqkeMSMGVIFITHDMGVVAEiADRVLVMYQGEAVETGSV 253
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 15220188 582 DELISNPDGAYS-SLLriqeAASPNLNHTPSLPVSTK-PLPELP 623
Cdd:PRK10261 254 EQIFHAPQHPYTrALL----AAVPQLGAMKGLDYPRRfPLISLE 293
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
993-1164 |
2.95e-12 |
|
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: 67.00 E-value: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 993 SRPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKlKSLRRHIGLVQQEPALFAT 1072
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQR-DEPHENILYLGHLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1073 -TIYENILYgkegasesevmeaakLANAHSFISSLPEGYSTKVGERGI------QMSGGQRQRIAIARAVLKNPEILLLD 1145
Cdd:TIGR01189 88 lSALENLHF---------------WAAIHGGAQRTIEDALAAVGLTGFedlpaaQLSAGQQRRLALARLWLSRRPLWILD 152
|
170
....*....|....*....
gi 15220188 1146 EATSALDVESERVVQQALD 1164
Cdd:TIGR01189 153 EPTTALDKAGVALLAGLLR 171
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
367-588 |
3.00e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 68.28 E-value: 3.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 367 TFTYPS----RPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHIGLV 442
Cdd:PRK15112 13 TFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 443 NQEPvlfATTI--RENIMYGKD-------DATSEEitNAAKLSEAISFINNLPEgfetQVGERGIQLSGGQKQRISISRA 513
Cdd:PRK15112 93 FQDP---STSLnpRQRISQILDfplrlntDLEPEQ--REKQIIETLRQVGLLPD----HASYYPHMLAPGQKQRLGLARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 514 IVKNPSILLLDEATSALDAEsekiVQEALDRVMV------GRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESGSHDELIS 586
Cdd:PRK15112 164 LILRPKVIIADEALASLDMS----MRSQLINLMLelqekqGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLA 239
|
..
gi 15220188 587 NP 588
Cdd:PRK15112 240 SP 241
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
992-1200 |
4.71e-12 |
|
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: 66.52 E-value: 4.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 992 PSRPDVTIFSDFNLLVPSGKSMALVGQSGSGKSS---VLSLVLRFYDPTAGIIMIDGQDIKKLKlKSLRRHIGLVQQEPA 1068
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkALANRTEGNVSVEGDIHYNGIPYKEFA-EKYPGEIIYVSEEDV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1069 LFATTIYEnilygkegasesEVMEAAKLANAHSFIsslpegystkvgeRGIqmSGGQRQRIAIARAVLKNPEILLLDEAT 1148
Cdd:cd03233 94 HFPTLTVR------------ETLDFALRCKGNEFV-------------RGI--SGGERKRVSIAEALVSRASVLCWDNST 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220188 1149 SALDVEServvqqALDRLMRDRTTVVVAHRLSTIKNS----------DMISVIQDGKIIEQG 1200
Cdd:cd03233 147 RGLDSST------ALEILKCIRTMADVLKTTTFVSLYqasdeiydlfDKVLVLYEGRQIYYG 202
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
378-560 |
6.71e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 69.91 E-value: 6.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 378 IFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTD--GAVMLDGNDIRYLDLKwlrgHIGLVNQEPVLFA-TTIR 454
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILK----RTGFVTQDDILYPhLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 455 ENIMYGKDDATSEEITNAAKLSEAISFINNL--PEGFETQVGE---RGIqlSGGQKQRISISRAIVKNPSILLLDEATSA 529
Cdd:PLN03211 159 ETLVFCSLLRLPKSLTKQEKILVAESVISELglTKCENTIIGNsfiRGI--SGGERKRVSIAHEMLINPSLLILDEPTSG 236
|
170 180 190
....*....|....*....|....*....|..
gi 15220188 530 LDAESE-KIVQEALDRVMVGRTTVVVAHRLST 560
Cdd:PLN03211 237 LDATAAyRLVLTLGSLAQKGKTIVTSMHQPSS 268
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
998-1200 |
7.83e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 69.52 E-value: 7.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 998 TIFSDFNLLVPSGKSMALVGQSGSGKSSVL-SLVLRFYDPT-AGIIMIDGQDIKKLKLKslrrHIGLVQQEPALFA-TTI 1074
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLLnALAGRIQGNNfTGTILANNRKPTKQILK----RTGFVTQDDILYPhLTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1075 YENILYGKEGASESEVMEAAKLANAHSFISSL--PEGYSTKVGE---RGIqmSGGQRQRIAIARAVLKNPEILLLDEATS 1149
Cdd:PLN03211 158 RETLVFCSLLRLPKSLTKQEKILVAESVISELglTKCENTIIGNsfiRGI--SGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15220188 1150 ALDVESE-RVVQQALDRLMRDRTTVVVAHRLST--IKNSDMISVIQDGKIIEQG 1200
Cdd:PLN03211 236 GLDATAAyRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFG 289
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
982-1201 |
9.18e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 66.64 E-value: 9.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYP-------------------SRPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIM 1042
Cdd:COG1134 5 IEVENVSKSYRlyhepsrslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1043 IDGqdikklKLKSLrrhIGL---VQQEpalfaTTIYENI-----LYGkegASESEVmeAAKLANAHSFiSSLPEGYSTKV 1114
Cdd:COG1134 85 VNG------RVSAL---LELgagFHPE-----LTGRENIylngrLLG---LSRKEI--DEKFDEIVEF-AELGDFIDQPV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1115 GergiQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVV-VAHRLSTIKN-SDMISVIQ 1192
Cdd:COG1134 145 K----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIfVSHSMGAVRRlCDRAIWLE 220
|
....*....
gi 15220188 1193 DGKIIEQGS 1201
Cdd:COG1134 221 KGRLVMDGD 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
996-1207 |
1.31e-11 |
|
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: 68.68 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 996 DVTIFSDFNLLVPSGKSMALVGQSGSGKSsVLSLVLR---FYDPTAGIIM------------------------------ 1042
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKS-VLMHVLRgmdQYEPTSGRIIyhvalcekcgyverpskvgepcpvcggtle 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1043 ---IDGQDIKKLKLKSLRRHIG-LVQQEPALFAT-TIYENILYGKEGA---SESEVMEAAKLANahsfisslpegySTKV 1114
Cdd:TIGR03269 91 peeVDFWNLSDKLRRRIRKRIAiMLQRTFALYGDdTVLDNVLEALEEIgyeGKEAVGRAVDLIE------------MVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1115 GER----GIQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDR--TTVVVAHRLSTIKN-SDM 1187
Cdd:TIGR03269 159 SHRithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEVIEDlSDK 238
|
250 260
....*....|....*....|
gi 15220188 1188 ISVIQDGKIIEQGSHNILVE 1207
Cdd:TIGR03269 239 AIWLENGEIKEEGTPDEVVA 258
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
993-1163 |
1.63e-11 |
|
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: 64.82 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 993 SRPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKlKSLRRHIGLVQQEPALFAT 1072
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQR-DSIARGLLYLGHAPGIKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1073 -TIYENILYGKEGASESEVMEAAKLANAHSFiSSLPEGystkvgergiQMSGGQRQRIAIARAVLKNPEILLLDEATSAL 1151
Cdd:cd03231 88 lSVLENLRFWHADHSDEQVEEALARVGLNGF-EDRPVA----------QLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170
....*....|..
gi 15220188 1152 DVESERVVQQAL 1163
Cdd:cd03231 157 DKAGVARFAEAM 168
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1007-1194 |
1.87e-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: 64.57 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1007 VPSGKSMALVGQSGSGKSSVLS-LVLRfydPTAGII----MIDGQDIKklklKSLRRHIGLVQQEPALFAT-TIYENILY 1080
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDvLAGR---KTAGVItgeiLINGRPLD----KNFQRSTGYVEQQDVHSPNlTVREALRF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1081 gkegasesevmeAAKLanahsfisslpegystkvgeRGIqmSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQ 1160
Cdd:cd03232 103 ------------SALL--------------------RGL--SVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIV 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 15220188 1161 QALDRLMRD-RTTVVVAHRLS--TIKNSDMISVIQDG 1194
Cdd:cd03232 149 RFLKKLADSgQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
343-534 |
2.12e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 68.60 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 343 ERNTEDKTGRklgnvngDILF-KDVTFTYP-SRPDVVIFDKLN-FVIPaGKVVALVGGSGSGKSTMIS-LIERFYEP--T 416
Cdd:TIGR00956 748 EKDMEKESGE-------DIFHwRNLTYEVKiKKEKRVILNNVDgWVKP-GTLTALMGASGAGKTTLLNvLAERVTTGviT 819
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 417 DGAVMLDGndiRYLDLKWLRgHIGLVNQEPVLFAT-TIRENIMYGKDDATSEEITNAAKLS--EAISFINNLPEGFETQV 493
Cdd:TIGR00956 820 GGDRLVNG---RPLDSSFQR-SIGYVQQQDLHLPTsTVRESLRFSAYLRQPKSVSKSEKMEyvEEVIKLLEMESYADAVV 895
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15220188 494 GERGIQLSGGQKQRISISRAIVKNPSILL-LDEATSALDAES 534
Cdd:TIGR00956 896 GVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQT 937
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
386-587 |
3.46e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 64.52 E-value: 3.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 386 IPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDI-RYLDLKWLRGHIGLVNQEPVLFA-TTIRENIMYGKDD 463
Cdd:PRK11614 28 INQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDItDWQTAKIMREAVAIVPEGRRVFSrMTVEENLAMGGFF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 464 ATSEEitnaakLSEAISFINNL-PEGFETQVgERGIQLSGGQKQRISISRAIVKNPSILLLDEATSALdaeSEKIVQEAL 542
Cdd:PRK11614 108 AERDQ------FQERIKWVYELfPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL---APIIIQQIF 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15220188 543 DRVMV----GRTTVVVAHRLS-TVRNADIIAVVGGGKIIESGSHDELISN 587
Cdd:PRK11614 178 DTIEQlreqGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLAN 227
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
372-586 |
3.52e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.12 E-value: 3.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 372 SRPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKW-LRGHIGLVNQE-PVLF 449
Cdd:PRK09700 14 SFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLaAQLGIGIIYQElSVID 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 450 ATTIRENIMYGK---DDATSEEITNAAKLSEAISFInNLPEGFETQVGERGIQLSGGQKQRISISRAIVKNPSILLLDEA 526
Cdd:PRK09700 94 ELTVLENLYIGRhltKKVCGVNIIDWREMRVRAAMM-LLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15220188 527 TSAL-DAESEKIVQEALDRVMVGRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESG-----SHDELIS 586
Cdd:PRK09700 173 TSSLtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGmvsdvSNDDIVR 239
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
111-335 |
4.37e-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: 65.15 E-value: 4.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 111 TGERQAAKIRKAYLRSMLSQDISLFDTeISTGEVISAITSEILVVQDAISEKVGNFMHFISRFIAGFAIGFASVWQISLV 190
Cdd:cd18542 66 ASQKVAYDLRNDLYDHLQRLSFSFHDK-ARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 191 TLSIVPFIALAGGIYAFVSSGLIVRVRKSYVKANEIAEEVIGNVRTVQAFTGEEKAVSSYQGALRNTYNYGRKAGLAKGL 270
Cdd:cd18542 145 SLAIIPFIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAK 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15220188 271 GLGSLHFVLFLSWALLIWFTSIVVHKGIANGGE--SFTTMLNVVIAGL-SLGQAapdISTFMRASAAA 335
Cdd:cd18542 225 YWPLMDFLSGLQIVLVLWVGGYLVINGEITLGElvAFISYLWMLIWPVrQLGRL---INDMSRASASA 289
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
382-596 |
9.94e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.88 E-value: 9.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 382 LNFVIPAGKVVALVGGSGSGKST----MISLIerfyePTDGAVMLDGNDIRYLDLKWL---RGHIGLVNQEP-------- 446
Cdd:PRK15134 305 ISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPnsslnprl 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 447 -VLfaTTIRENIMYGKDDATSEEITnaAKLSEAISFINNLPEGFETQVGErgiqLSGGQKQRISISRAIVKNPSILLLDE 525
Cdd:PRK15134 380 nVL--QIIEEGLRVHQPTLSAAQRE--QQVIAVMEEVGLDPETRHRYPAE----FSGGQRQRIAIARALILKPSLIILDE 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15220188 526 ATSALDaeseKIVQE---ALDRVMVGR---TTVVVAHRLSTVRN-ADIIAVVGGGKIIESGSHDELISNPDGAYSSLL 596
Cdd:PRK15134 452 PTSSLD----KTVQAqilALLKSLQQKhqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQL 525
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
984-1177 |
1.06e-10 |
|
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: 65.73 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 984 LKGVHFSYPsrPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVlrfydptAGIimidGQDIKKLKLKSLRRHIGLV 1063
Cdd:TIGR03719 7 MNRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AGV----DKDFNGEARPQPGIKVGYL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1064 QQEPALFAT-TIYENI-------------------LYGKEGASESEVM-EAAKL------ANAHSFISSL---------P 1107
Cdd:TIGR03719 74 PQEPQLDPTkTVRENVeegvaeikdaldrfneisaKYAEPDADFDKLAaEQAELqeiidaADAWDLDSQLeiamdalrcP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1108 EGySTKVGErgiqMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLmrDRTTVVVAH 1177
Cdd:TIGR03719 154 PW-DADVTK----LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY--PGTVVAVTH 216
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
365-565 |
1.49e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.89 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 365 DVTFTYPSRPdvvIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIR-----YLDLKWLRGHI 439
Cdd:PRK13540 6 ELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKkdlctYQKQLCFVGHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 440 GLVNqePVLfatTIRENIMYG-KDDATSEEITNAAKLSEAISFInNLPEGFetqvgergiqLSGGQKQRISISRAIVKNP 518
Cdd:PRK13540 83 SGIN--PYL---TLRENCLYDiHFSPGAVGITELCRLFSLEHLI-DYPCGL----------LSSGQKRQVALLRLWMSKA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15220188 519 SILLLDEATSALDAES-EKIVQEALDRVMVGRTTVVVAHRLSTVRNAD 565
Cdd:PRK13540 147 KLWLLDEPLVALDELSlLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
372-544 |
1.50e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 62.13 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 372 SRPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIR------YLDLKWLrGHIGLVNqe 445
Cdd:PRK13538 10 ERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRrqrdeyHQDLLYL-GHQPGIK-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 446 PVLfatTIRENIMY---GKDDATSEEITNA-AKLSEAisfinnlpeGFEtQVGERgiQLSGGQKQRISISRAIVKNPSIL 521
Cdd:PRK13538 87 TEL---TALENLRFyqrLHGPGDDEALWEAlAQVGLA---------GFE-DVPVR--QLSAGQQRRVALARLWLTRAPLW 151
|
170 180
....*....|....*....|...
gi 15220188 522 LLDEATSALDAESEKIVQEALDR 544
Cdd:PRK13538 152 ILDEPFTAIDKQGVARLEALLAQ 174
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
111-265 |
1.78e-10 |
|
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: 63.22 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 111 TGERQAAKIRKAYLRSMLSQDISLFDTEiSTGEVISAITSEILVVQDAISEKVGNF-MHFISrFIAGFAIGFASVWQISL 189
Cdd:cd18551 63 TGERVVLDLRRRLWRRLLRLPVSFFDRR-RSGDLVSRVTNDTTLLRELITSGLPQLvTGVLT-VVGAVVLMFLLDWVLTL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 190 VTLSIVPfiaLAGGIYAFVSSglivRVRKSYVKA-------NEIAEEVIGNVRTVQAFTGEEKAVSSYQGALRNTYNYGR 262
Cdd:cd18551 141 VTLAVVP---LAFLIILPLGR----RIRKASKRAqdalgelSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGL 213
|
...
gi 15220188 263 KAG 265
Cdd:cd18551 214 KAA 216
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
364-534 |
2.36e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 64.75 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 364 KDVTFTYPsrPDVVIFDK--LNFvIPAGKVvALVGGSGSGKSTMISLIERFYEPTDG-AVMLDGNDIRYLDlkwlrghig 440
Cdd:PRK11819 10 NRVSKVVP--PKKQILKDisLSF-FPGAKI-GVLGLNGAGKSTLLRIMAGVDKEFEGeARPAPGIKVGYLP--------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 441 lvnQEPVLFAT-TIRENIM-------------------YGKDDATSEE-ITNAAKLSEAISFIN---------------N 484
Cdd:PRK11819 77 ---QEPQLDPEkTVRENVEegvaevkaaldrfneiyaaYAEPDADFDAlAAEQGELQEIIDAADawdldsqleiamdalR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15220188 485 LPEGfETQVGergiQLSGGQKQRISISRAIVKNPSILLLDEATSALDAES 534
Cdd:PRK11819 154 CPPW-DAKVT----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
732-916 |
2.72e-10 |
|
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: 63.00 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 732 RLTLRVRQKMFSAILRNEIGWFDKvdNTSSMLASRLeSDATLLRTIVVDRSTILLENLGLVVTAFIISFILNWRLTLVVL 811
Cdd:cd18782 72 RIDLELGGTIIDHLLRLPLGFFDK--RPVGELSTRI-SELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 812 ATYPLIisghisekIFMQGYGGNLSKAYLKANMLAG--------ESISNIRTVVAFCAEEKVLDLYSKELLEPSERSFRR 883
Cdd:cd18782 149 ATVPLQ--------LLLTFLFGPILRRQIRRRAEASaktqsylvESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKL 220
|
170 180 190
....*....|....*....|....*....|...
gi 15220188 884 GQMAGILYGVSQFFIFSSYGLALWYGSILMEKG 916
Cdd:cd18782 221 TVLGTTSGSLSQFLNKLSSLLVLWVGAYLVLRG 253
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
697-916 |
3.16e-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: 62.81 E-value: 3.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 697 TQNEVKRISILFCCGSVITVIVHTIEHTTFGIMGERLTLRVRQKMFSAILRNEIGWFDKvdNTSSMLASRLESDATLLRT 776
Cdd:cd18541 35 TASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQK--NRTGDLMARATNDLNAVRM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 777 IVVDRSTILLENLGLVVTAFIISFILNWRLTLVVLATYPLIIsghisekIFMQGYGGNLSKAYLKA-------NMLAGES 849
Cdd:cd18541 113 ALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLA-------LLVYRLGKKIHKRFRKVqeafsdlSDRVQES 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15220188 850 ISNIRTVVAFCAEEKVLDLYSKELLEPSERSFRRGQMAGILYGVSQFFIFSSYGLALWYGSILMEKG 916
Cdd:cd18541 186 FSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRG 252
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
380-597 |
3.74e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 62.84 E-value: 3.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 380 DKLNFVIPAGKVVALVGGSGSGKS----TMISLIErfyepTDGAVM-----LDGNDIRYLDLKWLRGHIG----LVNQEP 446
Cdd:PRK11022 24 DRISYSVKQGEVVGIVGESGSGKSvsslAIMGLID-----YPGRVMaekleFNGQDLQRISEKERRNLVGaevaMIFQDP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 447 VLF---ATTIRENIM------YGKDDATSE----EITNAAKLSEAISFINNLPEgfetqvgergiQLSGGQKQRISISRA 513
Cdd:PRK11022 99 MTSlnpCYTVGFQIMeaikvhQGGNKKTRRqraiDLLNQVGIPDPASRLDVYPH-----------QLSGGMSQRVMIAMA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 514 IVKNPSILLLDEATSALDAESEKIVQEALDRVMVGRTT--VVVAHRLSTV-RNADIIAVVGGGKIIESGSHDELISNPDG 590
Cdd:PRK11022 168 IACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMalVLITHDLALVaEAAHKIIVMYAGQVVETGKAHDIFRAPRH 247
|
....*...
gi 15220188 591 AYS-SLLR 597
Cdd:PRK11022 248 PYTqALLR 255
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
389-556 |
3.98e-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: 61.66 E-value: 3.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 389 GKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDI----RYLDLKwlrghiglvnqepvlFATTIRENIMYGKDDA 464
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVsykpQYIKAD---------------YEGTVRDLLSSITKDF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 465 TSE-----EITNAAKLSEAISfiNNLPEgfetqvgergiqLSGGQKQRISISRAIVKNPSILLLDEATSALDAESEKIVQ 539
Cdd:cd03237 90 YTHpyfktEIAKPLQIEQILD--REVPE------------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMAS 155
|
170
....*....|....*....
gi 15220188 540 EALDRVMVG--RTTVVVAH 556
Cdd:cd03237 156 KVIRRFAENneKTAFVVEH 174
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
363-525 |
4.74e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 63.84 E-value: 4.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 363 FKDVTFTYPSRPDVVifDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLRGHIGLV 442
Cdd:PRK10522 325 LRNVTFAYQDNGFSV--GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 443 NQEPVLFATTIrENIMYGKDDATSEEITNAAKLSEAISFINNlpegfetQVgeRGIQLSGGQKQRISISRAIVKNPSILL 522
Cdd:PRK10522 403 FTDFHLFDQLL-GPEGKPANPALVEKWLERLKMAHKLELEDG-------RI--SNLKLSKGQKKRLALLLALAEERDILL 472
|
...
gi 15220188 523 LDE 525
Cdd:PRK10522 473 LDE 475
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
725-912 |
9.15e-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: 61.37 E-value: 9.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 725 TFGIMGERLTLRVRQKMFSAILRNEIGWFDKvdNTSSMLASRLESDATLLRTIVVDRSTILLENLGLVVTAFIISFILNW 804
Cdd:cd18564 77 LTALVGQRVVLDLRRDLFAHLQRLSLSFHDR--RRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDW 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 805 RLTLVVLATYPLIIsghisekIFMQGYGGNLSKAYLKANM-------LAGESISNIRTVVAFCAEEKVLDLYSKEllepS 877
Cdd:cd18564 155 QLALIALAVAPLLL-------LAARRFSRRIKEASREQRRregalasVAQESLSAIRVVQAFGREEHEERRFARE----N 223
|
170 180 190
....*....|....*....|....*....|....*....
gi 15220188 878 ERSFRRG----QMAGILYGVSQFFIFSSYGLALWYGSIL 912
Cdd:cd18564 224 RKSLRAGlraaRLQALLSPVVDVLVAVGTALVLWFGAWL 262
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
364-534 |
9.77e-10 |
|
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: 62.65 E-value: 9.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 364 KDVTFTYPsrPDVVIFD--KLNFvIPAGKVvALVGGSGSGKSTMISLIERFYEPTDG-AVMLDGNDIRYLDlkwlrghig 440
Cdd:TIGR03719 8 NRVSKVVP--PKKEILKdiSLSF-FPGAKI-GVLGLNGAGKSTLLRIMAGVDKDFNGeARPQPGIKVGYLP--------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 441 lvnQEPVLFAT-TIRENIM-------------------YGKDDATSEE-ITNAAKLSEAISFIN---------------N 484
Cdd:TIGR03719 75 ---QEPQLDPTkTVRENVEegvaeikdaldrfneisakYAEPDADFDKlAAEQAELQEIIDAADawdldsqleiamdalR 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15220188 485 LPEGfETQVGErgiqLSGGQKQRISISRAIVKNPSILLLDEATSALDAES 534
Cdd:TIGR03719 152 CPPW-DADVTK----LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1009-1197 |
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 15220188 1009 SGKSMALVGQSGSGKSSVLSLVLRFYDPT-AGIIMIDGQDIKKLKLKSLRRHIglvqqepalfattiyenilygkegase 1087
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPgGGVIYIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1088 sevmeaaklanahsfisslpegystkVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALD--- 1164
Cdd:smart00382 54 --------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrl 107
|
170 180 190
....*....|....*....|....*....|....*.
gi 15220188 1165 ---RLMRDRTTVVVAHRLSTIKNSDMISVIQDGKII 1197
Cdd:smart00382 108 lllLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIV 143
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1003-1215 |
1.15e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 61.46 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1003 FNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDP----TAGIIMIDGQDIKKL----KLKSLRRHIGLVQQEP------- 1067
Cdd:COG4170 26 VSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLspreRRKIIGREIAMIFQEPsscldps 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1068 ALFATTIYENILygkegASESEVM----------EAAKLANA-----HSFI-SSLPEgystkvgergiQMSGGQRQRIAI 1131
Cdd:COG4170 106 AKIGDQLIEAIP-----SWTFKGKwwqrfkwrkkRAIELLHRvgikdHKDImNSYPH-----------ELTEGECQKVMI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1132 ARAVLKNPEILLLDEATSALDVESERVVQQALDRL--MRDRTTVVVAHRLSTIKN-SDMISVIQDGKIIEQGSHNILVEN 1208
Cdd:COG4170 170 AMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLnqLQGTSILLISHDLESISQwADTITVLYCGQTVESGPTEQILKS 249
|
....*..
gi 15220188 1209 KNGPYSK 1215
Cdd:COG4170 250 PHHPYTK 256
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
998-1201 |
1.19e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 60.61 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 998 TIFSDFNLLVPSGKSMALVGQSGSGKSSVL-SLVLRFYDPTA-------GIIMIDGQDIKKLKLKSL-RRHIGLVQQEPA 1068
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLkALAGDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLaRLRAVLPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1069 LFATTIYENILYG------KEGASESEVMEAAKLANAHSfisslpeGYSTKVGERGIQMSGGQRQRIAIARAVLK----- 1137
Cdd:PRK13547 95 AFAFSAREIVLLGrypharRAGALTHRDGEIAWQALALA-------GATALVGRDVTTLSGGELARVQFARVLAQlwpph 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15220188 1138 ----NPEILLLDEATSALDVESERVVQQALDRLMRDRTTVVVA--HRLS-TIKNSDMISVIQDGKIIEQGS 1201
Cdd:PRK13547 168 daaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAivHDPNlAARHADRIAMLADGAIVAHGA 238
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1002-1217 |
1.22e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 61.26 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1002 DFNLLVPSGKSMALVGQSGSGKSS---VLSLVLRfydPTAGIIMIDGQDIKKLKlKSLRRHIGLV----QQ--------- 1065
Cdd:COG4586 40 DISFTIEPGEIVGFIGPNGAGKSTtikMLTGILV---PTSGEVRVLGYVPFKRR-KEFARRIGVVfgqrSQlwwdlpaid 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1066 -----------EPALFATTIYEniLygkegaseSEVMEAAKLANahsfisslpegysTKVgeRgiQMSGGQRQRIAIARA 1134
Cdd:COG4586 116 sfrllkaiyriPDAEYKKRLDE--L--------VELLDLGELLD-------------TPV--R--QLSLGQRMRCELAAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1135 VLKNPEILLLDEATSALDVESERVVQQALDRLMRDR-TTVVVA-HRLSTIKN-SDMISVIQDGKIIEQGSHNILVEnKNG 1211
Cdd:COG4586 169 LLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgTTILLTsHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKE-RFG 247
|
....*.
gi 15220188 1212 PYSKLI 1217
Cdd:COG4586 248 PYKTIV 253
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
351-575 |
1.44e-09 |
|
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: 62.26 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 351 GRKLGNVNgdILFKDVTFTYPSRpdvVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVML-DGNDIRY 429
Cdd:TIGR03719 315 GPRLGDKV--IEAENLTKAFGDK---LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKLAY 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 430 LDlkwlRGHIGLVNQepvlfaTTIRENIMYGKD--DATSEEITNAAKLSeAISFinnlpEGFETQ--VGergiQLSGGQK 505
Cdd:TIGR03719 390 VD----QSRDALDPN------KTVWEEISGGLDiiKLGKREIPSRAYVG-RFNF-----KGSDQQkkVG----QLSGGER 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15220188 506 QRISISRAIVKNPSILLLDEATSALDAESEKIVQEALDRvmVGRTTVVVAH------RLSTvrnaDIIAVVGGGKI 575
Cdd:TIGR03719 450 NRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLN--FAGCAVVISHdrwfldRIAT----HILAFEGDSHV 519
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
372-558 |
1.65e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.94 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 372 SRPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLR-GHIGLVNQEPVLFA 450
Cdd:PRK10762 13 AFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQeAGIGIIHQELNLIP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 451 T-TIRENIMYGKddatseEITNA------AKL-SEAISFIN--NLPEGFETQVGErgiqLSGGQKQRISISRAIVKNPSI 520
Cdd:PRK10762 93 QlTIAENIFLGR------EFVNRfgridwKKMyAEADKLLArlNLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15220188 521 LLLDEATSAL-DAESE---KIVQEALDRvmvGRTTVVVAHRL 558
Cdd:PRK10762 163 IIMDEPTDALtDTETEslfRVIRELKSQ---GRGIVYISHRL 201
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
389-568 |
1.77e-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: 57.77 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 389 GKVVALVGGSGSGKSTMISLIERFYEPTDGAV-MLDGNDIRYLDLKWLRGHIglvnqepvlfattirenimygkddatse 467
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGViYIDGEDILEEVLDQLLLII---------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 468 eitnaaklseaisfinnlpegfetqVGERGIQLSGGQKQRISISRAIVKNPSILLLDEATSALDAESEKIVQEALDRVMV 547
Cdd:smart00382 54 -------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLL 108
|
170 180
....*....|....*....|....*..
gi 15220188 548 ------GRTTVVVAHRLSTVRNADIIA 568
Cdd:smart00382 109 lllkseKNLTVILTTNDEKDLGPALLR 135
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
374-578 |
1.84e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 61.73 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 374 PDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYePT---DGAVMLDGNDIRYLDLK--WLRGhIGLVNQE--- 445
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEVCRFKDIRdsEALG-IVIIHQElal 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 446 -PVLfatTIRENIMYGKDDATSEEITNAAKLSEAISFIN--NLPEGFETQVGERGIqlsgGQKQRISISRAIVKNPSILL 522
Cdd:NF040905 90 iPYL---SIAENIFLGNERAKRGVIDWNETNRRARELLAkvGLDESPDTLVTDIGV----GKQQLVEIAKALSKDVKLLI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220188 523 LDEATSAL-DAESEKIvqeaLDRVM----VGRTTVVVAHRLSTVRN-ADIIAVVGGGKIIES 578
Cdd:NF040905 163 LDEPTAALnEEDSAAL----LDLLLelkaQGITSIIISHKLNEIRRvADSITVLRDGRTIET 220
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
368-561 |
2.28e-09 |
|
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: 58.43 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 368 FTYPSRPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTM---ISLIERFYEPTDGAVMLDGNDIRYLDLKWlRGHIGLVNQ 444
Cdd:cd03233 12 TTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLlkaLANRTEGNVSVEGDIHYNGIPYKEFAEKY-PGEIIYVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 445 EPVLFAT-TIRENIMYgkddatseeitnAAKLsEAISFInnlpegfetqvgeRGIqlSGGQKQRISISRAIVKNPSILLL 523
Cdd:cd03233 91 EDVHFPTlTVRETLDF------------ALRC-KGNEFV-------------RGI--SGGERKRVSIAEALVSRASVLCW 142
|
170 180 190
....*....|....*....|....*....|....*...
gi 15220188 524 DEATSALDAESekivqeALDRVMVGRTtvvVAHRLSTV 561
Cdd:cd03233 143 DNSTRGLDSST------ALEILKCIRT---MADVLKTT 171
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
361-539 |
2.49e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 61.80 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSRPdvVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVmldgndiryldLKWLRGHIG 440
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV-----------FRSAKVRMA 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 441 LVNQEPVlfattirenimYGKDdatseeITNAAKLSEAISFINNLPEGFETQVGERGIQ----------LSGGQKQRISI 510
Cdd:PLN03073 576 VFSQHHV-----------DGLD------LSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTgnlalqpmytLSGGQKSRVAF 638
|
170 180 190
....*....|....*....|....*....|
gi 15220188 511 SRAIVKNPSILLLDEATSALDAES-EKIVQ 539
Cdd:PLN03073 639 AKITFKKPHILLLDEPSNHLDLDAvEALIQ 668
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
993-1197 |
2.96e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.90 E-value: 2.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 993 SRPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIK-KLKLKSLRRHIGLVQQEPALF- 1070
Cdd:PRK10982 7 SFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQELNLVl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1071 ATTIYENILYGKEGASESEVMEAAKLANAHSFISSLPEGYSTKvgERGIQMSGGQRQRIAIARAVLKNPEILLLDEATSA 1150
Cdd:PRK10982 87 QRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPR--AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15220188 1151 LdveSERVVQQALD--RLMRDR--TTVVVAHRLSTI-KNSDMISVIQDGKII 1197
Cdd:PRK10982 165 L---TEKEVNHLFTiiRKLKERgcGIVYISHKMEEIfQLCDEITILRDGQWI 213
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
90-344 |
3.19e-09 |
|
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: 59.71 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 90 FVYLSVVIL--FSSWLEVACWMHTGERQAAKIRKAYLRSMLSQDISLFDTeISTGEVISAITSEIlvvqDAISEkvgNFM 167
Cdd:cd18544 45 LLYLGLLLLsfLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDR-TPVGRLVTRVTNDT----EALNE---LFT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 168 HFISRFIAGFA--IGFASV-----WQISLVTLSIVPFIALAGGIYAFVSSGLIVRVRKSYVKANEIAEEVIGNVRTVQAF 240
Cdd:cd18544 117 SGLVTLIGDLLllIGILIAmfllnWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 241 TGEEKAVSSYQGALRNTYNYGRKAGLAKGLGLGSLHFVLFLSWALLIWFTSIVVHKGIANGGesfttmlnVVIAGLSLgq 320
Cdd:cd18544 197 NREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVLSGAVTLG--------VLYAFIQY-- 266
|
250 260
....*....|....*....|....
gi 15220188 321 aapdISTFMRasaaayPIFQMIER 344
Cdd:cd18544 267 ----IQRFFR------PIRDLAEK 280
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
344-559 |
3.36e-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: 61.30 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 344 RNTEDKTGR-KLGNVNGDILFKDVTFTYPSRpDVVIfDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYePTDGAVML 422
Cdd:TIGR00954 434 RNSNLVPGRgIVEYQDNGIKFENIPLVTPNG-DVLI-ESLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGRLT 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 423 dgndiryldlKWLRGHIGLVNQEPVLFATTIRENIMY----------GKDDATSEEITNAAKLSEAIsfinnlpegfETQ 492
Cdd:TIGR00954 511 ----------KPAKGKLFYVPQRPYMTLGTLRDQIIYpdssedmkrrGLSDKDLEQILDNVQLTHIL----------ERE 570
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220188 493 VGERGIQ-----LSGGQKQRISISRAIVKNPSILLLDEATSALDAESEKIVQEALDRvmVGRTTVVVAHRLS 559
Cdd:TIGR00954 571 GGWSAVQdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHRKS 640
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
386-580 |
3.49e-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: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 386 IPAGKVVALVGGSGSGKSTMIslIERFYePTdGAVMLDGNDIRYLDLKWLRG--HIG---LVNQEPV------------- 447
Cdd:cd03271 18 IPLGVLTCVTGVSGSGKSSLI--NDTLY-PA-LARRLHLKKEQPGNHDRIEGleHIDkviVIDQSPIgrtprsnpatytg 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 448 LFaTTIRE----------------NIMY-GKD-----DATSEEitnAAKLSEAISFINNLPEGFET------QVGERGIQ 499
Cdd:cd03271 94 VF-DEIRElfcevckgkrynretlEVRYkGKSiadvlDMTVEE---ALEFFENIPKIARKLQTLCDvglgyiKLGQPATT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 500 LSGGQKQRISISRAIVK---NPSILLLDEATSALDAESEKIVQEALDR-VMVGRTTVVVAHRLSTVRNADII------AV 569
Cdd:cd03271 170 LSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRlVDKGNTVVVIEHNLDVIKCADWIidlgpeGG 249
|
250
....*....|.
gi 15220188 570 VGGGKIIESGS 580
Cdd:cd03271 250 DGGGQVVASGT 260
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1007-1215 |
4.96e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 59.37 E-value: 4.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1007 VPSGKSMALVGQSGSGKSsVLSLVLRFYDPTAGIIM-----IDGQDIKKLKLKSLRRHIG----LVQQEPALFATTIYeN 1077
Cdd:PRK11022 30 VKQGEVVGIVGESGSGKS-VSSLAIMGLIDYPGRVMaekleFNGQDLQRISEKERRNLVGaevaMIFQDPMTSLNPCY-T 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1078 ILYgkegasesEVMEAAKlanAHsfisslpEGYSTKV-GERGI--------------------QMSGGQRQRIAIARAVL 1136
Cdd:PRK11022 108 VGF--------QIMEAIK---VH-------QGGNKKTrRQRAIdllnqvgipdpasrldvyphQLSGGMSQRVMIAMAIA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1137 KNPEILLLDEATSALDVESERVVQQALDRLMR--DRTTVVVAHRLSTIKNS-DMISVIQDGKIIEQGSHNILVENKNGPY 1213
Cdd:PRK11022 170 CRPKLLIADEPTTALDVTIQAQIIELLLELQQkeNMALVLITHDLALVAEAaHKIIVMYAGQVVETGKAHDIFRAPRHPY 249
|
..
gi 15220188 1214 SK 1215
Cdd:PRK11022 250 TQ 251
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
704-928 |
5.23e-09 |
|
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: 59.00 E-value: 5.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 704 ISILFCCGSVITVIVHTIEHTTFGIMGERLTLRVRQKMFSAILRNEIGWFDkvdntsSM----LASRLeSDATLLRTIVV 779
Cdd:cd18570 44 ISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFE------TRktgeIISRF-NDANKIREAIS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 780 DRSTILLENLGLVVTAFIISFILNWRLTLVVLATYPL-IISGHISEKIF-------MQgyggnlSKAYLKANMLagESIS 851
Cdd:cd18570 117 STTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLyILIILLFNKPFkkknrevME------SNAELNSYLI--ESLK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 852 NIRTVVAFCAEEKVLDLYSKELLEPSERSFRRGQMaGILYGVSQFFIFSSYGLA-LWYGSIL-MEKGLS-----SFESVM 924
Cdd:cd18570 189 GIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKL-SNLQSSIKGLISLIGSLLiLWIGSYLvIKGQLSlgqliAFNALL 267
|
....
gi 15220188 925 KTFM 928
Cdd:cd18570 268 GYFL 271
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
90-244 |
5.48e-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: 350009 [Multi-domain] Cd Length: 313 Bit Score: 59.12 E-value: 5.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 90 FVYLSVVILFS-------SWLEVACWMHTGERQAAKIRKAYLRSMLSQDISLFDTEiSTGEVISAITSEILVVQDAISEK 162
Cdd:cd18565 53 LWLLGGLTVAAflleslfQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDR-QTGDLMSVLNNDVNQLERFLDDG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 163 VGNFMHFISRFIAGFAIGFASVWQISLVTLSIVPFIALAGGIYAFVSSGLIVRVRKSYVKANEIAEEVIGNVRTVQAFTG 242
Cdd:cd18565 132 ANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTA 211
|
..
gi 15220188 243 EE 244
Cdd:cd18565 212 ED 213
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1000-1189 |
6.59e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.21 E-value: 6.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1000 FSDFNLLVPS-GKSMALVGQSGSGKSSVLSL--------------------VLRFYdptAGIIMidgQD-IKKLKLKSLR 1057
Cdd:PRK13409 88 FKLYGLPIPKeGKVTGILGPNGIGKTTAVKIlsgelipnlgdyeeepswdeVLKRF---RGTEL---QNyFKKLYNGEIK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1058 --RHIGLVQQEPALFATTIYEnILygkEGASES----EVMEAAKLANahsfisslpegystkVGERGI-QMSGGQRQRIA 1130
Cdd:PRK13409 162 vvHKPQYVDLIPKVFKGKVRE-LL---KKVDERgkldEVVERLGLEN---------------ILDRDIsELSGGELQRVA 222
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1131 IARAVLKNPEILLLDEATSALDVEsERV-VQQALDRLMRDRTTVVVAHRLSTIknsDMIS 1189
Cdd:PRK13409 223 IAAALLRDADFYFFDEPTSYLDIR-QRLnVARLIRELAEGKYVLVVEHDLAVL---DYLA 278
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
377-580 |
7.40e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 58.30 E-value: 7.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 377 VIFDKLNFVIPAGKVVALVGGSGSGKSTMI-SLIERFYEPTD-------GAVMLDGNDIRYLDLKWL-RGHIGLVNQEPV 447
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLkALAGDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLaRLRAVLPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 448 LFATTIRENIMYG------KDDATSEEITNAAKLSEAISfinnlpeGFETQVGERGIQLSGGQKQRISISRAIVK----- 516
Cdd:PRK13547 95 AFAFSAREIVLLGrypharRAGALTHRDGEIAWQALALA-------GATALVGRDVTTLSGGELARVQFARVLAQlwpph 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220188 517 ----NPSILLLDEATSALDAESEKIVQEALDRVM----VGRTTVVVAHRLSTvRNADIIAVVGGGKIIESGS 580
Cdd:PRK13547 168 daaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLArdwnLGVLAIVHDPNLAA-RHADRIAMLADGAIVAHGA 238
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
987-1186 |
9.41e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.88 E-value: 9.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 987 VHFSYPSRPdvtIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKlKLKSLRRHIGLVQQE 1066
Cdd:PRK13540 7 LDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1067 PALFAT-TIYENILYGKEGASES-EVMEAAKLANAHSFIsSLPEGYstkvgergiqMSGGQRQRIAIARAVLKNPEILLL 1144
Cdd:PRK13540 83 SGINPYlTLRENCLYDIHFSPGAvGITELCRLFSLEHLI-DYPCGL----------LSSGQKRQVALLRLWMSKAKLWLL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15220188 1145 DEATSALDvesERVVQQALDRLMRDR----TTVVVAHRLSTIKNSD 1186
Cdd:PRK13540 152 DEPLVALD---ELSLLTIITKIQEHRakggAVLLTSHQDLPLNKAD 194
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
703-913 |
1.04e-08 |
|
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: 57.86 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 703 RISILFCCGSVITVIVHTIEHTTFGIMGERLTLRVRQKMFSAILRNEIGWFDKVDNTSSMlaSRLESDATLLRTIVVDRS 782
Cdd:cd18545 41 IIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKIL--SRVINDVNSLSDLLSNGL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 783 TILLENLGLVVTAFIISFILNWRLTLVVLATYPLIISGHISEKIFMQgyggnlsKAYLK-----ANMLAG--ESISNIRT 855
Cdd:cd18545 119 INLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRAR-------KAWQRvrkkiSNLNAYlhESISGIRV 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15220188 856 VVAFCAEEKVLDLYsKELLEPSERSFRRGQMagilygVSQFF-----IFSSYGLAL--WYGSILM 913
Cdd:cd18545 192 IQSFAREDENEEIF-DELNRENRKANMRAVR------LNALFwplveLISALGTALvyWYGGKLV 249
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
60-264 |
1.10e-08 |
|
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: 58.18 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 60 IFFGKLINIIGLAYLFPQEAS-HKVAKYSLDFVYLSVVILFSSWLEVACWMHTGERQAAKIRKAYLRSMLSQDISLFDTE 138
Cdd:cd18547 20 YLLGKAIDLIIEGLGGGGGVDfSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 139 iSTGEVISAITSEILVVQDAISEKVGNFMHFISRFIAGFAIGFASVWQISLVTLSIVPFIALAGGIYAFVSSGLIVRVRK 218
Cdd:cd18547 100 -SHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTKFIAKRSQKYFRKQQK 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15220188 219 SYVKANEIAEEVIGNVRTVQAFTGEEKAVSSYQGALRNTYNYGRKA 264
Cdd:cd18547 179 ALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKA 224
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
982-1196 |
1.18e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 59.49 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRPdvTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGqdikKLKLKSLRRH-- 1059
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSA----KVRMAVFSQHhv 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1060 IGL-VQQEPALFATTIYENILYGKEGASESEVMEAAKLAnahsfissLPEGYStkvgergiqMSGGQRQRIAIARAVLKN 1138
Cdd:PLN03073 583 DGLdLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLA--------LQPMYT---------LSGGQKSRVAFAKITFKK 645
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15220188 1139 PEILLLDEATSALDVESERVVQQALdrLMRDRTTVVVAHRLSTIKNS-DMISVIQDGKI 1196
Cdd:PLN03073 646 PHILLLDEPSNHLDLDAVEALIQGL--VLFQGGVLMVSHDEHLISGSvDELWVVSEGKV 702
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
993-1165 |
1.35e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 56.35 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 993 SRPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKlKSLRR------HIGLVQqe 1066
Cdd:PRK13538 10 ERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR-DEYHQdllylgHQPGIK-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1067 PALfatTIYEN--ILYGKEGASESEVMEAAkLAnahsfisslpegystKVGERGI------QMSGGQRQRIAIARAVLKN 1138
Cdd:PRK13538 87 TEL---TALENlrFYQRLHGPGDDEALWEA-LA---------------QVGLAGFedvpvrQLSAGQQRRVALARLWLTR 147
|
170 180
....*....|....*....|....*..
gi 15220188 1139 PEILLLDEATSALDVESERVVQQALDR 1165
Cdd:PRK13538 148 APLWILDEPFTAIDKQGVARLEALLAQ 174
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
375-576 |
1.37e-08 |
|
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: 59.07 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 375 DVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYE--PTDGAVMLDGNDIRYLDLKWL-RGHIGLVNQEPVLFAT 451
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 452 -TIRENIMYGKDDATSEEITNAAKLSE---------AISFINNlpegfETQVGERGiqlsGGQKQRISISRAIVKNPSIL 521
Cdd:TIGR02633 93 lSVAENIFLGNEITLPGGRMAYNAMYLraknllrelQLDADNV-----TRPVGDYG----GGQQQLVEIAKALNKQARLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15220188 522 LLDEATSAL-DAESEKIVQEALDRVMVGRTTVVVAHRLSTVRN-ADIIAVVGGGKII 576
Cdd:TIGR02633 164 ILDEPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1002-1177 |
1.46e-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: 57.03 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1002 DFNLLVPSG---KS--MALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKklkLKSlrrhiglvQQEPALFATTIYE 1076
Cdd:cd03237 12 EFTLEVEGGsisESevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS---YKP--------QYIKADYEGTVRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1077 nILYGKEGAS------ESEVMEAAKLANAHSfiSSLPEgystkvgergiqMSGGQRQRIAIARAVLKNPEILLLDEATSA 1150
Cdd:cd03237 81 -LLSSITKDFythpyfKTEIAKPLQIEQILD--REVPE------------LSGGELQRVAIAACLSKDADIYLLDEPSAY 145
|
170 180
....*....|....*....|....*....
gi 15220188 1151 LDVESERVVQQALDRLM--RDRTTVVVAH 1177
Cdd:cd03237 146 LDVEQRLMASKVIRRFAenNEKTAFVVEH 174
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1000-1189 |
1.56e-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: 56.99 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1000 FSDFNLLVP-SGKSMALVGQSGSGKSSVLSL--------------------VLRFYDPTAgiIMIDGQDIKKLKLKSLRR 1058
Cdd:cd03236 15 FKLHRLPVPrEGQVLGLVGPNGIGKSTALKIlagklkpnlgkfddppdwdeILDEFRGSE--LQNYFTKLLEGDVKVIVK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1059 hIGLVQQEPALFATTIYENILYGKEGASESEVMEAAKLanahsfisslpegysTKVGERGI-QMSGGQRQRIAIARAVLK 1137
Cdd:cd03236 93 -PQYVDLIPKAVKGKVGELLKKKDERGKLDELVDQLEL---------------RHVLDRNIdQLSGGELQRVAIAAALAR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15220188 1138 NPEILLLDEATSALDVESERVVQQALDRLMRD-RTTVVVAHRLSTIknsDMIS 1189
Cdd:cd03236 157 DADFYFFDEPSSYLDIKQRLNAARLIRELAEDdNYVLVVEHDLAVL---DYLS 206
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1122-1189 |
1.77e-08 |
|
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: 58.64 E-value: 1.77e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1122 SGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLM--RDRTTVVVAHRLSTIknsDMIS 1189
Cdd:COG1245 457 SGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAenRGKTAMVVDHDIYLI---DYIS 523
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1122-1189 |
1.99e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.67 E-value: 1.99e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1122 SGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLM--RDRTTVVVAHRLSTIknsDMIS 1189
Cdd:PRK13409 455 SGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAeeREATALVVDHDIYMI---DYIS 521
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
984-1155 |
2.17e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.21 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 984 LKGVHFSYPsrPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSlvlrfydptagiIM------IDGQ-----DIKklk 1052
Cdd:PRK11819 9 MNRVSKVVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLR------------IMagvdkeFEGEarpapGIK--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1053 lkslrrhIGLVQQEPALFAT-TIYENI-------------------LYGKEGASESEVM-EAAKL------ANAHSFISS 1105
Cdd:PRK11819 72 -------VGYLPQEPQLDPEkTVRENVeegvaevkaaldrfneiyaAYAEPDADFDALAaEQGELqeiidaADAWDLDSQ 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15220188 1106 L---------PEGySTKVGergiQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVES 1155
Cdd:PRK11819 145 LeiamdalrcPPW-DAKVT----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
727-920 |
3.36e-08 |
|
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: 56.33 E-value: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 727 GIMGERLTLRVRQKMFSAILRNEIGWFDKvdNTSSMLASRLESDATLLRTIV----VDrstiLLENLGLVVTAFIISFIL 802
Cdd:cd18540 67 GKIEMGVSYDLRKKAFEHLQTLSFSYFDK--TPVGWIMARVTSDTQRLGEIIswglVD----LVWGITYMIGILIVMLIL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 803 NWRLTLVVLATYPLIISghISekIFMQgyggnlsKAYLKAN--------MLAG---ESISNIRTVVAFCAEEKVLDLYSK 871
Cdd:cd18540 141 NWKLALIVLAVVPVLAV--VS--IYFQ-------KKILKAYrkvrkinsRITGafnEGITGAKTTKTLVREEKNLREFKE 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15220188 872 ELLEPSERSFRRGQMAGILYGVSQFFIFSSYGLALWYGSILMEKGLSSF 920
Cdd:cd18540 210 LTEEMRRASVRAARLSALFLPIVLFLGSIATALVLWYGGILVLAGAITI 258
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
728-920 |
3.69e-08 |
|
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: 56.26 E-value: 3.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 728 IMGERLTLRVRQKMFSAILRNEIGWFDKvdNTSSMLASRLESDATLLRTIVVDRSTILLENLGLVVTAFIISFILNWRLT 807
Cdd:cd18547 71 RVSQRTVYDLRKDLFEKLQRLPLSYFDT--HSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLT 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 808 LVVLATYPL------IISGHiSEKIFM--QGYGGNLskaylkaNMLAGESISNIRTVVAFCAEEKVL---DLYSKELLEP 876
Cdd:cd18547 149 LIVLVTVPLsllvtkFIAKR-SQKYFRkqQKALGEL-------NGYIEEMISGQKVVKAFNREEEAIeefDEINEELYKA 220
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15220188 877 SERSFRrgqMAGILYGVSQFFIFSSYGLALWYGSILMEKG------LSSF 920
Cdd:cd18547 221 SFKAQF---YSGLLMPIMNFINNLGYVLVAVVGGLLVINGaltvgvIQAF 267
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
687-916 |
6.33e-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: 55.53 E-value: 6.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 687 LVSYYMDWETTQNEVKRIsILFCCGSVITVIVHTIEH---TTFG-IMGERLTLRVRQKMFSAILRNEIGWFDKvdNTSSM 762
Cdd:cd18549 24 IVRYIIDDLLPSKNLRLI-LIIGAILLALYILRTLLNyfvTYWGhVMGARIETDMRRDLFEHLQKLSFSFFDN--NKTGQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 763 LASRLESDatlLRTI-----------VVdrSTILLenlglvVTAFIISFILNWRLTLVVLATYPLIIsghisekIFMQGY 831
Cdd:cd18549 101 LMSRITND---LFDIselahhgpedlFI--SIITI------IGSFIILLTINVPLTLIVFALLPLMI-------IFTIYF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 832 GGNLSKAYLKA-------NMLAGESISNIRTVVAFCAEEKVLDLYSK---ELLEPSERSFRrgQMAgILYGVSQFFIFSS 901
Cdd:cd18549 163 NKKMKKAFRRVrekigeiNAQLEDSLSGIRVVKAFANEEYEIEKFDEgndRFLESKKKAYK--AMA-YFFSGMNFFTNLL 239
|
250
....*....|....*
gi 15220188 902 YGLALWYGSILMEKG 916
Cdd:cd18549 240 NLVVLVAGGYFIIKG 254
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
378-1166 |
6.82e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.43 E-value: 6.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 378 IFDKLNFVIPAGKVVALVGGSGSGKSTMI----SLIERFYEPTDGAVMLDG---NDIRyldlKWLRG----------HIG 440
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLktiaSNTDGFHIGVEGVITYDGitpEEIK----KHYRGdvvynaetdvHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 441 -LVNQEPVLFATTIR--ENimygKDDATSEEiTNAAKLSEAISFINNLPEGFETQVGE---RGIqlSGGQKQRISISRAI 514
Cdd:TIGR00956 152 hLTVGETLDFAARCKtpQN----RPDGVSRE-EYAKHIADVYMATYGLSHTRNTKVGNdfvRGV--SGGERKRVSIAEAS 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 515 VKNPSILLLDEATSALDAESekivqeALDRVMVGRTTVVVAHRLSTV------RNA----DIIAVVGGGKIIESGSHDE- 583
Cdd:TIGR00956 225 LGGAKIQCWDNATRGLDSAT------ALEFIRALKTSANILDTTPLVaiyqcsQDAyelfDKVIVLYEGYQIYFGPADKa 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 584 LISNPDGAYSSLLR------IQEAASPNlNHTPsLPVSTKPLPELP----------------------------ITETTS 629
Cdd:TIGR00956 299 KQYFEKMGFKCPDRqttadfLTSLTSPA-ERQI-KPGYEKKVPRTPqefetywrnspeyaqlmkeideyldrcsESDTKE 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 630 SIHQSVN--QPDTTK-----------QAKVTVGRLYSMIRPDWKYGLCGTLG----SFIAGSqmpLFaLGIAQALVSYYm 692
Cdd:TIGR00956 377 AYRESHVakQSKRTRpsspytvsfsmQVKYCLARNFLRMKGNPSFTLFMVFGniimALILSS---VF-YNLPKNTSDFY- 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 693 dwetTQNEVKRISILFCCGSVITVIVHTIEH---------------TTFGIMGERLTLRVrqKMFSAILRNEIGWFdkvd 757
Cdd:TIGR00956 452 ----SRGGALFFAILFNAFSSLLEIASMYEArpivekhrkyalyhpSADAIASIISEIPF--KIIESVVFNIILYF---- 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 758 ntssMLASRLESDATLLRTIVVDRSTILLENLGLVVTAFIISFIL-NWRLTLVVLATYplIISGHISEKIFMQGYggnlS 836
Cdd:TIGR00956 522 ----MVNFRRTAGRFFFYLLILFICTLAMSHLFRSIGAVTKTLSEaMTPAAILLLALS--IYTGFAIPRPSMLGW----S 591
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 837 K--------AYLKANMLAGE-------------------SISNIRTVVAFCA----EEKVL-DLYSKELLEPSERSFRRG 884
Cdd:TIGR00956 592 KwiyyvnplAYAFESLMVNEfhgrrfecsqyvpsgggydNLGVTNKVCTVVGaepgQDYVDgDDYLKLSFQYYNSHKWRN 671
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 885 qmAGILYGVSQFFIFsSYGLALWYGSILMEKG-LSSFESVMKTFMVlivtalVMGEVLALAPDLLKgNQMVVSVFELLDR 963
Cdd:TIGR00956 672 --FGIIIGFTVFFFF-VYILLTEFNKGAKQKGeILVFRRGSLKRAK------KAGETSASNKNDIE-AGEVLGSTDLTDE 741
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 964 RTQVVGDTGEELSNVEGTIELKGVHFSYP-SRPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDP---TAG 1039
Cdd:TIGR00956 742 SDDVNDEKDMEKESGEDIFHWRNLTYEVKiKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGG 821
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1040 IIMIDGQDIKklklKSLRRHIGLVQQEPALFAT-TIYENILYGKEGASESEVMEAAKLANAHSFISSLP-EGYSTK-VGE 1116
Cdd:TIGR00956 822 DRLVNGRPLD----SSFQRSIGYVQQQDLHLPTsTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEmESYADAvVGV 897
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|.
gi 15220188 1117 RGIQMSGGQRQRIAIARAVLKNPEILL-LDEATSALDVESERVVQQALDRL 1166
Cdd:TIGR00956 898 PGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
452-579 |
7.06e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 57.16 E-value: 7.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 452 TIRENIMYGKDDATSEEITNAAKLSeaisFINNLPEGFETQ------VGERGIQ-LSGGQKQRISISRAIVKNPSILLLD 524
Cdd:PLN03140 969 TVRESLIYSAFLRLPKEVSKEEKMM----FVDEVMELVELDnlkdaiVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMD 1044
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15220188 525 EATSALDAESEKIVQEAL-DRVMVGRTTVVVAHRLSTvrnaDIIAVVG-------GGKIIESG 579
Cdd:PLN03140 1045 EPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPSI----DIFEAFDelllmkrGGQVIYSG 1103
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
974-1183 |
8.55e-08 |
|
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: 56.68 E-value: 8.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 974 ELSNVEGTIELKGVHFSYPSRpDVTIfSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGqdikklkl 1053
Cdd:TIGR00954 444 IVEYQDNGIKFENIPLVTPNG-DVLI-ESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-------- 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1054 kslRRHIGLVQQEPALFATTIYENILY-------GKEGASESEVMEAAKLANAHSFISSlpEGYSTKVGERGIQMSGGQR 1126
Cdd:TIGR00954 514 ---KGKLFYVPQRPYMTLGTLRDQIIYpdssedmKRRGLSDKDLEQILDNVQLTHILER--EGGWSAVQDWMDVLSGGEK 588
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15220188 1127 QRIAIARAVLKNPEILLLDEATSALDVEservVQQALDRLMRDR--TTVVVAHRLSTIK 1183
Cdd:TIGR00954 589 QRIAMARLFYHKPQFAILDECTSAVSVD----VEGYMYRLCREFgiTLFSVSHRKSLWK 643
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1010-1201 |
1.05e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 54.80 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1010 GKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIGLVQQEPAlfaTTIYENILYGK------E 1083
Cdd:PRK15112 39 GQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPS---TSLNPRQRISQildfplR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1084 GASESEVMEAAKLANAH-SFISSLPE--GYSTKVgergiqMSGGQRQRIAIARAVLKNPEILLLDEATSALDVEservVQ 1160
Cdd:PRK15112 116 LNTDLEPEQREKQIIETlRQVGLLPDhaSYYPHM------LAPGQKQRLGLARALILRPKVIIADEALASLDMS----MR 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15220188 1161 QALDRLMRDR------TTVVVAHRLSTIKN-SDMISVIQDGKIIEQGS 1201
Cdd:PRK15112 186 SQLINLMLELqekqgiSYIYVTQHLGMMKHiSDQVLVMHQGEVVERGS 233
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
361-561 |
1.66e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 53.96 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSRpdvVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNdiryldlkwLRghIG 440
Cdd:PRK09544 5 VSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 441 LVNQEPVLFAT---TIrENIMYGKDDATSEEITNAAKLSEAISFINnlpegFETQvgergiQLSGGQKQRISISRAIVKN 517
Cdd:PRK09544 71 YVPQKLYLDTTlplTV-NRFLRLRPGTKKEDILPALKRVQAGHLID-----APMQ------KLSGGETQRVLLARALLNR 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15220188 518 PSILLLDEATSALDAESEKIVQEALD--RVMVGRTTVVVAHRLSTV 561
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDqlRRELDCAVLMVSHDLHLV 184
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1000-1189 |
1.73e-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: 55.56 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1000 FSDFNLLVP-SGKSMALVGQSGSGKSSVLSL--------------------VLRFYdptAGIIMidgQD-IKKLKLKSLR 1057
Cdd:COG1245 88 FRLYGLPVPkKGKVTGILGPNGIGKSTALKIlsgelkpnlgdydeepswdeVLKRF---RGTEL---QDyFKKLANGEIK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1058 --RHIGLVQQEPALFATTIYEnILygkEGASE----SEVMEAAKLANahsfisslpegystkVGERGI-QMSGGQRQRIA 1130
Cdd:COG1245 162 vaHKPQYVDLIPKVFKGTVRE-LL---EKVDErgklDELAEKLGLEN---------------ILDRDIsELSGGELQRVA 222
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15220188 1131 IARAVLKNPEILLLDEATSALDVeSERV-VQQALDRLMR-DRTTVVVAHRLSTIknsDMIS 1189
Cdd:COG1245 223 IAAALLRDADFYFFDEPSSYLDI-YQRLnVARLIRELAEeGKYVLVVEHDLAIL---DYLA 279
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
380-587 |
1.84e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 54.32 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 380 DKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIrYLDLKWLRGHIGLV----NQ----EPVL--F 449
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVP-FKRRKEFARRIGVVfgqrSQlwwdLPAIdsF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 450 aTTIREniMYGKDDATSEEitNAAKLSEAIS---FINnlpegfeTQVgeRgiQLSGGQKQRISISRAIVKNPSILLLDEA 526
Cdd:COG4586 118 -RLLKA--IYRIPDAEYKK--RLDELVELLDlgeLLD-------TPV--R--QLSLGQRMRCELAAALLHRPKILFLDEP 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15220188 527 TSALDAESEKIVQEALDRVMVGR-TTVVVA-HRLstvrnADIIA------VVGGGKIIESGSHDELISN 587
Cdd:COG4586 182 TIGLDVVSKEAIREFLKEYNRERgTTILLTsHDM-----DDIEAlcdrviVIDHGRIIYDGSLEELKER 245
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
727-916 |
1.89e-07 |
|
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: 54.03 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 727 GIMGERLTLRVRQKMFSAILRNEIGWFDKvdNTSSMLASRLESD----ATLLRTIVVDrstiLLENLGLVVTAFIISFIL 802
Cdd:cd18546 64 GRTGERLLYDLRLRVFAHLQRLSLDFHER--ETSGRIMTRMTSDidalSELLQTGLVQ----LVVSLLTLVGIAVVLLVL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 803 NWRLTLVVLATYPLIIsghisekIFMQGYGGNLSKAYLKANMLAG-------ESISNIRTVVAFCAEEKVLDLYSKElle 875
Cdd:cd18546 138 DPRLALVALAALPPLA-------LATRWFRRRSSRAYRRARERIAavnadlqETLAGIRVVQAFRRERRNAERFAEL--- 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15220188 876 pSERsFRRGQMAGILYgVSQFFIF------SSYGLALWYGSILMEKG 916
Cdd:cd18546 208 -SDD-YRDARLRAQRL-VAIYFPGvellgnLATAAVLLVGAWRVAAG 251
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
993-1220 |
1.95e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 53.64 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 993 SRPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSvLSLVL---RFYDPTAGIIMIDGQDIkkLKLKSLRRH---IGLVQQE 1066
Cdd:PRK09580 10 SVEDKAILRGLNLEVRPGEVHAIMGPNGSGKST-LSATLagrEDYEVTGGTVEFKGKDL--LELSPEDRAgegIFMAFQY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1067 PA--------LFATTIYeNILYGKEGASESEVMEAAKLANAHSFISSLPEGYSTKVGERGiqMSGGQRQRIAIARAVLKN 1138
Cdd:PRK09580 87 PVeipgvsnqFFLQTAL-NAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1139 PEILLLDEATSALDVESERVVQQALDRLmRD--RTTVVVAH--RLSTIKNSDMISVIQDGKIIEQGSHNILVENKNGPYS 1214
Cdd:PRK09580 164 PELCILDESDSGLDIDALKIVADGVNSL-RDgkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFTLVKQLEEQGYG 242
|
....*.
gi 15220188 1215 KLISLQ 1220
Cdd:PRK09580 243 WLTEQQ 248
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
111-244 |
2.54e-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: 350008 [Multi-domain] Cd Length: 307 Bit Score: 54.06 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 111 TGERQAAKIRKAYLRSMLSQDISLFDTEiSTGEVISAITSEILVVQDAISEKVGNFMHFISRFIAGFAIGFASVWQISLV 190
Cdd:cd18564 81 VGQRVVLDLRRDLFAHLQRLSLSFHDRR-RTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALI 159
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 15220188 191 TLSIVPFIALAggiyAFVSSGLIV----RVRKSYVKANEIAEEVIGNVRTVQAFTGEE 244
Cdd:cd18564 160 ALAVAPLLLLA----ARRFSRRIKeasrEQRRREGALASVAQESLSAIRVVQAFGREE 213
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1119-1192 |
2.60e-07 |
|
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: 52.19 E-value: 2.60e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15220188 1119 IQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMR--DRTTVVVAHRLSTIKN-SDMISVIQ 1192
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYlSDRIHVFE 146
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1020-1197 |
2.63e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 54.64 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1020 GSGKSSVLSLVLRFYDPTAGIIMIDGqdiKKLKLKS----LRRHIGLV----QQEpALFAT-TIYENIL------YGKEG 1084
Cdd:COG1129 288 GAGRTELARALFGADPADSGEIRLDG---KPVRIRSprdaIRAGIAYVpedrKGE-GLVLDlSIRENITlasldrLSRGG 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1085 -ASESEVMEAAKlanahSFISSL---PEGYSTKVGergiQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQ 1160
Cdd:COG1129 364 lLDRRRERALAE-----EYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIY 434
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15220188 1161 QALDRLMRDRTTVVVAhrlST-----IKNSDMISVIQDGKII 1197
Cdd:COG1129 435 RLIRELAAEGKAVIVI---SSelpelLGLSDRILVMREGRIV 473
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
726-937 |
2.96e-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: 53.56 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 726 FGIMGERLTLRVRQKmFSAILRNEIgwFDKVDN----------TSSMLaSRLESDAT--------LLRTIVvdRSTILLe 787
Cdd:cd18548 55 AGILAGYFAAKASQG-FGRDLRKDL--FEKIQSfsfaeidkfgTSSLI-TRLTNDVTqvqnfvmmLLRMLV--RAPIML- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 788 nlglvVTAFIISFILNWRLTLVVLATYPLIISG-----HISEKIF--MQgyggnlsKAYLKANMLAGESISNIRTVVAFC 860
Cdd:cd18548 128 -----IGAIIMAFRINPKLALILLVAIPILALVvflimKKAIPLFkkVQ-------KKLDRLNRVVRENLTGIRVIRAFN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 861 AEEKVLDLY---SKELLEPSERSFRrgqMAGILYGVSQFFIFSSYGLALWYGSILMEKGLSSFESVMK--TFMVLIVTAL 935
Cdd:cd18548 196 REDYEEERFdkaNDDLTDTSLKAGR---LMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLVAfiNYLMQILMSL 272
|
..
gi 15220188 936 VM 937
Cdd:cd18548 273 MM 274
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
983-1154 |
2.96e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.96 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 983 ELKGVHFSYPsrpDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLrfydptagiimidGQdikkLKLKSLRRHIGl 1062
Cdd:PRK11147 321 EMENVNYQID---GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLML-------------GQ----LQADSGRIHCG- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1063 VQQEPALF---------ATTIYENILYGKEgasesEVMEAAKLANAHSFISSL---PEGYSTKVGergiQMSGGQRQRIA 1130
Cdd:PRK11147 380 TKLEVAYFdqhraeldpEKTVMDNLAEGKQ-----EVMVNGRPRHVLGYLQDFlfhPKRAMTPVK----ALSGGERNRLL 450
|
170 180
....*....|....*....|....
gi 15220188 1131 IARAVLKNPEILLLDEATSALDVE 1154
Cdd:PRK11147 451 LARLFLKPSNLLILDEPTNDLDVE 474
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
972-1164 |
3.69e-07 |
|
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: 54.56 E-value: 3.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 972 GEELSNVegTIELKGVHFSYPSRpdvTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIdGQDIKkl 1051
Cdd:TIGR03719 315 GPRLGDK--VIEAENLTKAFGDK---LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK-- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1052 klkslrrhIGLV-QQEPALFAT-TIYENILYGkegaseSEVMEAAKLA-NAHSFISSLpeGYS-----TKVGergiQMSG 1123
Cdd:TIGR03719 387 --------LAYVdQSRDALDPNkTVWEEISGG------LDIIKLGKREiPSRAYVGRF--NFKgsdqqKKVG----QLSG 446
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15220188 1124 GQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALD 1164
Cdd:TIGR03719 447 GERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALL 487
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
983-1197 |
4.58e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.88 E-value: 4.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 983 ELKGVhfSYPSRPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRH-IG 1061
Cdd:COG3845 259 EVENL--SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1062 LVQQEP---ALFAT-TIYENIL---YGKEGASESEVMEAAKL-ANAHSFISSL---PEGYSTKVGergiQMSGGQRQRIA 1130
Cdd:COG3845 337 YIPEDRlgrGLVPDmSVAENLIlgrYRRPPFSRGGFLDRKAIrAFAEELIEEFdvrTPGPDTPAR----SLSGGNQQKVI 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220188 1131 IARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVVVahrLST-----IKNSDMISVIQDGKII 1197
Cdd:COG3845 413 LARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLL---ISEdldeiLALSDRIAVMYEGRIV 481
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
997-1201 |
5.74e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.34 E-value: 5.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 997 VTIFSDFNLLVPSGKSMALVGQSGSGKSSVL----SLVLRFYDPTAGIIMIDG---QDIKKLKLKSL------RRHIG-L 1062
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLktiaSNTDGFHIGVEGVITYDGitpEEIKKHYRGDVvynaetDVHFPhL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1063 VQQEPALFAT------TIYENIlygkegaseSEVMEAAKLANAHSFISSLPEGYSTKVGE---RGIqmSGGQRQRIAIAR 1133
Cdd:TIGR00956 154 TVGETLDFAArcktpqNRPDGV---------SREEYAKHIADVYMATYGLSHTRNTKVGNdfvRGV--SGGERKRVSIAE 222
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220188 1134 AVLKNPEILLLDEATSALD----VESERVVQQALDRLmrDRTTVVVAHRLS--TIKNSDMISVIQDGKIIEQGS 1201
Cdd:TIGR00956 223 ASLGGAKIQCWDNATRGLDsataLEFIRALKTSANIL--DTTPLVAIYQCSqdAYELFDKVIVLYEGYQIYFGP 294
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
732-872 |
5.91e-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: 52.48 E-value: 5.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 732 RLTLRV----RQKMFSAILRNEIGWFDKVDntSSMLASRLESDATLLRTIVVdRSTILLENLGLVVTAFIISFILNWRLT 807
Cdd:cd18543 65 RLSLGVehdlRTDLFAHLQRLDGAFHDRWQ--SGQLLSRATSDLSLVQRFLA-FGPFLLGNLLTLVVGLVVMLVLSPPLA 141
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220188 808 LVVLATYP-LIISGHISEKIFM------QGYGGNLSkaylkanMLAGESISNIRTVVAFCAEEKVLDLYSKE 872
Cdd:cd18543 142 LVALASLPpLVLVARRFRRRYFpasrraQDQAGDLA-------TVVEESVTGIRVVKAFGRERRELDRFEAA 206
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
364-585 |
6.95e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 52.13 E-value: 6.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 364 KDVTFTYPSRPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGndirylDLKWLRGHIGLVN 443
Cdd:PRK13546 25 KDALIPKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG------EVSVIAISAGLSG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 444 QepvlfaTTIRENI------MYGKDDATSEEITNAAKLSEAISFINNLPEGFetqvgergiqlSGGQKQRISISRAIVKN 517
Cdd:PRK13546 99 Q------LTGIENIefkmlcMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKY-----------SSGMRAKLGFSINITVN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15220188 518 PSILLLDEATSALDaesEKIVQEALDRVM----VGRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESGSHDELI 585
Cdd:PRK13546 162 PDILVIDEALSVGD---QTFAQKCLDKIYefkeQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVL 231
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
90-297 |
6.99e-07 |
|
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: 52.47 E-value: 6.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 90 FVYLSVVILFSSWLEVACWMHTGERQAAKIRKAYLRSMLSQDISLFDTEiSTGEVISAITSEILVVQDAISEKVGNFMHF 169
Cdd:cd18545 46 FLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSR-PVGKILSRVINDVNSLSDLLSNGLINLIPD 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 170 ISRFIAGFAIGFASVWQISLVTLSIVPFIALaggiyafVSSGLIVRVRKSYVKANE-IA------EEVIGNVRTVQAFTG 242
Cdd:cd18545 125 LLTLVGIVIIMFSLNVRLALVTLAVLPLLVL-------VVFLLRRRARKAWQRVRKkISnlnaylHESISGIRVIQSFAR 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15220188 243 EEKAVSSYQGALRNTYNYGRKAGLAKGLGLGSLHFVLFLSWALLIWFTSIVVHKG 297
Cdd:cd18545 198 EDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTALVYWYGGKLVLGG 252
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
737-920 |
7.08e-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: 7.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 737 VRQKMFSAILRNEIGWFDkvDNTSSMLASRLESDATLLRTIVVDRSTILLENLGLVVTAFIISFILNWRLTLVVLATYPL 816
Cdd:cd18565 89 LRTDTYDHVQRLDMAFFE--DRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 817 IISGHIsekIFMQgyggNLSKAYLKANMLAGE-------SISNIRTVVAFCAEEkvldlYSKELLEPSERSFRRGQMAGI 889
Cdd:cd18565 167 IIAGTY---WFQR----RIEPRYRAVREAVGDlnarlenNLSGIAVIKAFTAED-----FERERVADASEEYRDANWRAI 234
|
170 180 190
....*....|....*....|....*....|....*.
gi 15220188 890 -----LYGVSQFFIFSSYGLALWYGSILMEKGLSSF 920
Cdd:cd18565 235 rlraaFFPVIRLVAGAGFVATFVVGGYWVLDGPPLF 270
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
993-1154 |
7.35e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.39 E-value: 7.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 993 SRPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKlklKSLRRHIGLVQQEPALFAT 1072
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR---GDRSRFMAYLGHLPGLKAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1073 -TIYENI--LYGKEGaSESEVMEAAKLAnahsfISSLPEGYSTKVGergiQMSGGQRQRIAIARAVLKNPEILLLDEATS 1149
Cdd:PRK13543 97 lSTLENLhfLCGLHG-RRAKQMPGSALA-----IVGLAGYEDTLVR----QLSAGQKKRLALARLWLSPAPLWLLDEPYA 166
|
....*
gi 15220188 1150 ALDVE 1154
Cdd:PRK13543 167 NLDLE 171
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
729-916 |
8.88e-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: 349994 [Multi-domain] Cd Length: 294 Bit Score: 52.10 E-value: 8.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 729 MGERLTLRVRQKMFSAILRNEIGWFDKVdNTSSmLASRLESDATLLRTIVVDRSTILLENLGLVVTAFIISFILNWRLTL 808
Cdd:cd18550 66 IGQGVMYDLRVQLYAHLQRMSLAFFTRT-RTGE-IQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLAL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 809 VVLATYPLII-----SGHISEKIFMQGYGGNlskaylkANM--LAGE--SISNIRTVVAFCAEEKVLDLYSKEllepSER 879
Cdd:cd18550 144 LSLVLLPLFVlptrrVGRRRRKLTREQQEKL-------AELnsIMQEtlSVSGALLVKLFGREDDEAARFARR----SRE 212
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15220188 880 SFR---RGQMAGILYGVSqFFIFSSYGLAL--WYGSILMEKG 916
Cdd:cd18550 213 LRDlgvRQALAGRWFFAA-LGLFTAIGPALvyWVGGLLVIGG 253
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
372-538 |
1.03e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.81 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 372 SRPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLK-WLRGHIGLVNQE-PVLF 449
Cdd:PRK10982 7 SFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKeALENGISMVHQElNLVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 450 ATTIRENIMYGKDDATSEEITNAAKLSEAISFINNLpeGFETQVGERGIQLSGGQKQRISISRAIVKNPSILLLDEATSA 529
Cdd:PRK10982 87 QRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDEL--DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
....*....
gi 15220188 530 LdaeSEKIV 538
Cdd:PRK10982 165 L---TEKEV 170
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
730-916 |
1.07e-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: 51.77 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 730 GERLTLRVRQKMFSAILRNEIGWFDkvDNTSSMLASRLESDATLLRTIVVDRSTILLENLGLVVTAFIISFILNWRLTLV 809
Cdd:cd18778 68 EQKVVADLRSDLYDKLQRLSLRYFD--DRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 810 VLATYPLIIsghisekIFMQGYGGNLSKAYLKANMLAGE-------SISNIRTVVAFCAEEkvldlYSKELLEPSERSFR 882
Cdd:cd18778 146 TLIPIPFLA-------LGAWLYSKKVRPRYRKVREALGElnallqdNLSGIREIQAFGREE-----EEAKRFEALSRRYR 213
|
170 180 190
....*....|....*....|....*....|....*....
gi 15220188 883 RGQMAGILYG-----VSQFFIFSSYGLALWYGSILMEKG 916
Cdd:cd18778 214 KAQLRAMKLWaifhpLMEFLTSLGTVLVLGFGGRLVLAG 252
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
361-566 |
1.16e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.71 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 361 ILFKDVTFTYPSRPdvvIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIerfyepTDGAVMLDGNDIRYLDLK------- 433
Cdd:PRK10938 261 IVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI------TGDHPQGYSNDLTLFGRRrgsgeti 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 434 W-LRGHIGLVNQEPVL---FATTIRENIMYGKDD------ATSEeitnaAKLSEAISFINNLpeGFETQVGERGIQ-LSG 502
Cdd:PRK10938 332 WdIKKHIGYVSSSLHLdyrVSTSVRNVILSGFFDsigiyqAVSD-----RQQKLAQQWLDIL--GIDKRTADAPFHsLSW 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15220188 503 GQKQRISISRAIVKNPSILLLDEATSALDAESEKIVQEALDrVMV--GRTTVV------------VAHRLSTVRNADI 566
Cdd:PRK10938 405 GQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVD-VLIseGETQLLfvshhaedapacITHRLEFVPDGDI 481
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
500-585 |
1.59e-06 |
|
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: 52.71 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 500 LSGGQKQRISISRAIVK---NPSILLLDEATSALDAESEKIVQEALDR-VMVGRTTVVVAHRLSTVRNADIIAVVG---- 571
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHFDDIKKLLEVLQRlVDKGNTVVVIEHNLDVIKTADYIIDLGpegg 909
|
90
....*....|....*.
gi 15220188 572 --GGKIIESGSHDELI 585
Cdd:TIGR00630 910 dgGGTVVASGTPEEVA 925
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
116-335 |
1.79e-06 |
|
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: 51.25 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 116 AAKIRKAYLRSMLSQDISLFDtEISTGEVISAITSEILVVQDAISekvgNFMHFISR--FIAGFAIGFASV--WQISLVT 191
Cdd:cd18548 71 GRDLRKDLFEKIQSFSFAEID-KFGTSSLITRLTNDVTQVQNFVM----MLLRMLVRapIMLIGAIIMAFRinPKLALIL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 192 LSIVPFIALAGGIYAFVSSGLIVRVRKSYVKANEIAEEVIGNVRTVQAFTGEEKAVSSYQGALRNTYNYGRKAGLAKGLG 271
Cdd:cd18548 146 LVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALL 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15220188 272 LGSLHFVLFLSWALLIWFTSIVVHKGIANGGE--SFTTMLNVVIAGLSLGQAApdISTFMRASAAA 335
Cdd:cd18548 226 NPLMMLIMNLAIVAILWFGGHLINAGSLQVGDlvAFINYLMQILMSLMMLSMV--FVMLPRASASA 289
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
381-579 |
2.61e-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: 48.86 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 381 KLNFVIPAGKVVALVGGSGSGKSTMISliERFYEptDGAVMLDGNDIRYLDlkwlrghiglvnqEPVLFATTIRENIMYG 460
Cdd:cd03238 13 NLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYA--SGKARLISFLPKFSR-------------NKLIFIDQLQFLIDVG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 461 kddatseeitnaaklseaisfINNLPEGFETQVgergiqLSGGQKQRISISRAIVKNP--SILLLDEATSALDAESEKIV 538
Cdd:cd03238 76 ---------------------LGYLTLGQKLST------LSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQL 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15220188 539 QEALDR-VMVGRTTVVVAHRLSTVRNADIIAVVG------GGKIIESG 579
Cdd:cd03238 129 LEVIKGlIDLGNTVILIEHNLDVLSSADWIIDFGpgsgksGGKVVFSG 176
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
500-624 |
2.76e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 52.14 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 500 LSGGQKQRISISR---AIVKNPSILLLDEATSALDAES-EKIVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVG---- 571
Cdd:PRK00635 810 LSGGEIQRLKLAYellAPSKKPTLYVLDEPTTGLHTHDiKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLELGpegg 889
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 15220188 572 --GGKIIESGSHDELIS-NPDGAyssllriqEAASPNLNHTPSLPVSTKPLPELPI 624
Cdd:PRK00635 890 nlGGYLLASCSPEELIHlHTPTA--------KALRPYLSSPQELPYLPDPSPKPPV 937
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
57-244 |
2.98e-06 |
|
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: 50.53 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 57 VFFIFFGKLINIIGLAY----------LFPQEASHKVAKYSLDFVYLSVVILFSSWLeVACWMHT-GERQAAKIRKAYLR 125
Cdd:cd18549 5 FLDLFCAVLIAALDLVFplivryiiddLLPSKNLRLILIIGAILLALYILRTLLNYF-VTYWGHVmGARIETDMRRDLFE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 126 SMLSQDISLFDtEISTGEVISAITSEILvvqdaiseKVGNFMH------FIS--RFIAGFAIGFASVWQISLVTLSIVPF 197
Cdd:cd18549 84 HLQKLSFSFFD-NNKTGQLMSRITNDLF--------DISELAHhgpedlFISiiTIIGSFIILLTINVPLTLIVFALLPL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15220188 198 IAlaggIYAFVSSGLIVRV-RKSYVKANEI---AEEVIGNVRTVQAFTGEE 244
Cdd:cd18549 155 MI----IFTIYFNKKMKKAfRRVREKIGEInaqLEDSLSGIRVVKAFANEE 201
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
385-572 |
4.16e-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: 4.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 385 VIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKwlrghiglvnqepvlfattirenimygkdda 464
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQY------------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 465 tseeitnaaklseaisfinnlpegfetqvgergIQLSGGQKQRISISRAIVKNPSILLLDEATSALDAESEKIVQEALDR 544
Cdd:cd03222 70 ---------------------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRR 116
|
170 180 190
....*....|....*....|....*....|.
gi 15220188 545 VMV--GRTTVVVAHRLSTVRN-ADIIAVVGG 572
Cdd:cd03222 117 LSEegKKTALVVEHDLAVLDYlSDRIHVFEG 147
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1000-1196 |
4.59e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 50.82 E-value: 4.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1000 FSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSlRRHIGLV-----QQEPALFA-TT 1073
Cdd:PRK15439 279 FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-RLARGLVylpedRQSSGLYLdAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1074 IYENI---LYGKEGASESEVMEAAKLANAHSFISSLPEGYSTKVGergiQMSGGQRQRIAIARAVLKNPEILLLDEATSA 1150
Cdd:PRK15439 358 LAWNVcalTHNRRGFWIKPARENAVLERYRRALNIKFNHAEQAAR----TLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15220188 1151 LDVESERVVQQALDRLMRDRTTVV-VAHRLSTI-KNSDMISVIQDGKI 1196
Cdd:PRK15439 434 VDVSARNDIYQLIRSIAAQNVAVLfISSDLEEIeQMADRVLVMHQGEI 481
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
389-572 |
4.91e-06 |
|
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: 49.29 E-value: 4.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 389 GKVVALVGGSGSGKSTMISLIE--------RFYEPTDGAVMLD---GNDIRYLDLKWLRGHIGL------VNQEPVLFAT 451
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYFTKLLEGDVKVivkpqyVDLIPKAVKG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 452 TIRENIMYGKDDATSEEITNAAKLseaisfinnlpegfeTQVGERGI-QLSGGQKQRISISRAIVKNPSILLLDEATSAL 530
Cdd:cd03236 106 KVGELLKKKDERGKLDELVDQLEL---------------RHVLDRNIdQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15220188 531 DAESE----KIVQEALDRvmvGRTTVVVAHRLSTVRN-ADIIAVVGG 572
Cdd:cd03236 171 DIKQRlnaaRLIRELAED---DNYVLVVEHDLAVLDYlSDYIHCLYG 214
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
996-1227 |
5.47e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.55 E-value: 5.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 996 DVTIFSDFNL-LVPsGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDgqdiKKLKLKSLRRHiglvQQEpalfatti 1074
Cdd:PRK10636 324 DRIILDSIKLnLVP-GSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA----KGIKLGYFAQH----QLE-------- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1075 yenilYGKegASESEVMEAAKLA--NAHSFISSLPEGYS---TKVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEATS 1149
Cdd:PRK10636 387 -----FLR--ADESPLQHLARLApqELEQKLRDYLGGFGfqgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTN 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1150 ALDVESERVVQQALDRLmrDRTTVVVAHRLSTIKN-SDMISVIQDGKiieqgshnilVENKNG---PYSKLISLQQRQRH 1225
Cdd:PRK10636 460 HLDLDMRQALTEALIDF--EGALVVVSHDRHLLRStTDDLYLVHDGK----------VEPFDGdleDYQQWLSDVQKQEN 527
|
..
gi 15220188 1226 HP 1227
Cdd:PRK10636 528 QT 529
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
982-1177 |
6.02e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 50.28 E-value: 6.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRPdvtIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIImidgqdikklklK-SLRRHI 1060
Cdd:PRK15064 320 LEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------KwSENANI 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1061 GLVQQEPAL-FAT--TIYENI-LYGKEGASESEV--MEAAKLANAHSFisslpeGYSTKVgergiqMSGGQRQRIAIARA 1134
Cdd:PRK15064 385 GYYAQDHAYdFENdlTLFDWMsQWRQEGDDEQAVrgTLGRLLFSQDDI------KKSVKV------LSGGEKGRMLFGKL 452
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15220188 1135 VLKNPEILLLDEATSALDVESERVVQQALDrlMRDRTTVVVAH 1177
Cdd:PRK15064 453 MMQKPNVLVMDEPTNHMDMESIESLNMALE--KYEGTLIFVSH 493
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
982-1193 |
8.58e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.01 E-value: 8.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 982 IELKGVHFSYPSRPdvtIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLV-----------LRFYDPTAGiimiDGQDIKK 1050
Cdd:PRK10938 261 IVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpqgysndLTLFGRRRG----SGETIWD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1051 LKlkslrRHIGLVQQEPAL---FATTIYENILYG-------KEGASESEvmeaAKLANahSFISSLpeGYSTKVGERGIQ 1120
Cdd:PRK10938 334 IK-----KHIGYVSSSLHLdyrVSTSVRNVILSGffdsigiYQAVSDRQ----QKLAQ--QWLDIL--GIDKRTADAPFH 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1121 -MSGGQrQRIA-IARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVV-------------VAHRLSTIKNS 1185
Cdd:PRK10938 401 sLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLlfvshhaedapacITHRLEFVPDG 479
|
....*...
gi 15220188 1186 DMISVIQD 1193
Cdd:PRK10938 480 DIYRYVQT 487
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1115-1198 |
8.98e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 49.35 E-value: 8.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1115 GERGIQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTVV-----------VAHRLSTIk 1183
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLlttqymeeaeqLAHELTVI- 217
|
90
....*....|....*
gi 15220188 1184 nsDMISVIQDGKIIE 1198
Cdd:NF000106 218 --DRGRVIADGKVDE 230
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
359-584 |
1.06e-05 |
|
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: 49.44 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 359 GDILFK--DVTFTYPSRPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPT-DGAVMLDGN--DIRYLdLK 433
Cdd:TIGR02633 254 GDVILEarNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKpvDIRNP-AQ 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 434 WLRGHIGLVNQEpvlfatTIRENIMygKDDATSEEITNAAKlsEAISFINNLPEGFETQVGERGIQ-------------- 499
Cdd:TIGR02633 333 AIRAGIAMVPED------RKRHGIV--PILGVGKNITLSVL--KSFCFKMRIDAAAELQIIGSAIQrlkvktaspflpig 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 500 -LSGGQKQRISISRAIVKNPSILLLDEATSALD----AESEKIVQEALDRvmvGRTTVVVAHRLSTVRN-ADIIAVVGGG 573
Cdd:TIGR02633 403 rLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDvgakYEIYKLINQLAQE---GVAIIVVSSELAEVLGlSDRVLVIGEG 479
|
250
....*....|.
gi 15220188 574 KIIESGSHDEL 584
Cdd:TIGR02633 480 KLKGDFVNHAL 490
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
499-624 |
1.18e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 49.03 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 499 QLSGGQKQRISISRAIVKNPSILLLDEATSALDAESEKIVQEALDRVMVGRTTVV--VAHRLSTVRN-ADIIAVVGGGKI 575
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTIllISHDLQMLSQwADKINVLYCGQT 237
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 15220188 576 IESGSHDELISNPDGAYS-SLLRiqeaASPNLNHT-------PSLPVSTKPLPELPI 624
Cdd:PRK15093 238 VETAPSKELVTTPHHPYTqALIR----AIPDFGSAmphksrlNTLPGAIPLLEHLPI 290
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
351-543 |
1.29e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.35 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 351 GRKLGNVNgdILFKDVTFTYPSRpdvVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLdGNDIryl 430
Cdd:PRK11819 317 GPRLGDKV--IEAENLSKSFGDR---LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV--- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 431 dlkwlrgHIGLVNQEpvlfattiRENImygKDDATseeitnaakLSEAISfinnlpEGFET-QVGERGI----------- 498
Cdd:PRK11819 388 -------KLAYVDQS--------RDAL---DPNKT---------VWEEIS------GGLDIiKVGNREIpsrayvgrfnf 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15220188 499 ----------QLSGGQKQRISISRAIVKNPSILLLDEATSALDAESEKIVQEALD 543
Cdd:PRK11819 435 kggdqqkkvgVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALL 489
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
1113-1188 |
2.76e-05 |
|
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: 47.22 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1113 KVGERGIQMSGGQRQRIAIARAVLK---NPEILLLDEATSALDVESERVVQQALDRLMRDRTTVVVA-HRLSTIKNSDMI 1188
Cdd:cd03271 162 KLGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIeHNLDVIKCADWI 241
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
774-944 |
3.30e-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: 47.17 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 774 LRTIVVDRSTILLENLGLVVTAFIISFILNWRLTLVVLATYPLIISGHISEKIFMQGYGGNLSKAYLKANMLAGESISNI 853
Cdd:cd18568 111 IRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGI 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 854 RTVVAFCAEEKVL----DLYSKELlepsERSFRRGQMAGILYGVSQFFIFSSYGLALWYGSILMEKGLSSFESVMkTFMV 929
Cdd:cd18568 191 ATIKALAAERPIRwrweNKFAKAL----NTRFRGQKLSIVLQLISSLINHLGTIAVLWYGAYLVISGQLTIGQLV-AFNM 265
|
170
....*....|....*
gi 15220188 930 LIvtALVMGEVLALA 944
Cdd:cd18568 266 LF--GSVINPLLALV 278
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1010-1177 |
3.43e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.32 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1010 GKSMALVGQSGSGKSSVLS-LVLRFYD--PTAGIIM-----IDGQDIKKL---------KLKSLRRHIGLVQQEPALFAT 1072
Cdd:PLN03073 203 GRHYGLVGRNGTGKTTFLRyMAMHAIDgiPKNCQILhveqeVVGDDTTALqcvlntdieRTQLLEEEAQLVAQQRELEFE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1073 TIYENILYGKEGASESEVM-----------EAAKLANAHSFISSLPEG--YSTKVGERGI-QMSGGQRQRIAIARAVLKN 1138
Cdd:PLN03073 283 TETGKGKGANKDGVDKDAVsqrleeiykrlELIDAYTAEARAASILAGlsFTPEMQVKATkTFSGGWRMRIALARALFIE 362
|
170 180 190
....*....|....*....|....*....|....*....
gi 15220188 1139 PEILLLDEATSALDVESERVVQQALdrLMRDRTTVVVAH 1177
Cdd:PLN03073 363 PDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSH 399
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
364-583 |
3.58e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.96 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 364 KDVTFTYPSRPdvvIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVmldgndiryldlKWlrghiglvn 443
Cdd:PRK15064 323 ENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------KW--------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 444 qepvlfatTIRENIMYGKDDaTSEEITNAAKLSEAISFINNlPEGFETQVgeRGI----------------QLSGGQKQR 507
Cdd:PRK15064 379 --------SENANIGYYAQD-HAYDFENDLTLFDWMSQWRQ-EGDDEQAV--RGTlgrllfsqddikksvkVLSGGEKGR 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 508 ISISRAIVKNPSILLLDEATSALDAESEKIVQEALDrvMVGRTTVVVAH------RLSTvrnaDIIAVVGGGKIIESGSH 581
Cdd:PRK15064 447 MLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALE--KYEGTLIFVSHdrefvsSLAT----RIIEITPDGVVDFSGTY 520
|
..
gi 15220188 582 DE 583
Cdd:PRK15064 521 EE 522
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1014-1180 |
4.49e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.92 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1014 ALVGQSGSGKSSVLS-LVLRfydPTAGiiMIDGqDIK----KLKLKSLRRHIGLVQQ----EPALfatTIYENILYG--- 1081
Cdd:PLN03140 910 ALMGVSGAGKTTLMDvLAGR---KTGG--YIEG-DIRisgfPKKQETFARISGYCEQndihSPQV---TVRESLIYSafl 980
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1082 ---KEGASES------EVMEAAKLANAHSFISSLP--EGYSTKvgergiqmsggQRQRIAIARAVLKNPEILLLDEATSA 1150
Cdd:PLN03140 981 rlpKEVSKEEkmmfvdEVMELVELDNLKDAIVGLPgvTGLSTE-----------QRKRLTIAVELVANPSIIFMDEPTSG 1049
|
170 180 190
....*....|....*....|....*....|..
gi 15220188 1151 LDVESERVVQQALdRLMRD--RTTVVVAHRLS 1180
Cdd:PLN03140 1050 LDARAAAIVMRTV-RNTVDtgRTVVCTIHQPS 1080
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
375-575 |
4.66e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.86 E-value: 4.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 375 DVVIFD--KLNFVipAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVML-DGNDIRYL---DLKWLRGhiglvNQEPVL 448
Cdd:PRK10636 324 DRIILDsiKLNLV--PGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLGYFaqhQLEFLRA-----DESPLQ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 449 FATTIRENIMygkddatseeitnAAKLSEAI-SFinnlpeGFE-TQVGERGIQLSGGQKQRISISRAIVKNPSILLLDEA 526
Cdd:PRK10636 397 HLARLAPQEL-------------EQKLRDYLgGF------GFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEP 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15220188 527 TSALDAESEKIVQEALdrVMVGRTTVVVAHRLSTVRN-ADIIAVVGGGKI 575
Cdd:PRK10636 458 TNHLDLDMRQALTEAL--IDFEGALVVVSHDRHLLRStTDDLYLVHDGKV 505
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
383-583 |
4.99e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.21 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 383 NFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGndiryldlkwlrghiglvnqEPVLFATT---IRENIMY 459
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG--------------------KPIDIRSPrdaIRAGIML 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 460 GKDDATSEEITNAAKLSE--AIS----------FINNlpeGFETQVGERGIQ---------------LSGGQKQRISISR 512
Cdd:PRK11288 333 CPEDRKAEGIIPVHSVADniNISarrhhlragcLINN---RWEAENADRFIRslniktpsreqlimnLSGGNQQKAILGR 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220188 513 AIVKNPSILLLDEATSALD--AESEkIVQEALDRVMVGRTTVVVAHRLSTVRN-ADIIAVVGGGKIIESGSHDE 583
Cdd:PRK11288 410 WLSEDMKVILLDEPTRGIDvgAKHE-IYNVIYELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQ 482
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1007-1179 |
5.46e-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: 47.70 E-value: 5.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1007 VPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKlKLKSLRRHIGLVQQEPALfattiyENILYGKE--- 1083
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQFDAI------DDLLTGREhly 2034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1084 ------GASESEVMEAAKLAnahsfISSLpeGYSTKVGERGIQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESER 1157
Cdd:TIGR01257 2035 lyarlrGVPAEEIEKVANWS-----IQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARR 2107
|
170 180
....*....|....*....|...
gi 15220188 1158 VVQQALDRLMRD-RTTVVVAHRL 1179
Cdd:TIGR01257 2108 MLWNTIVSIIREgRAVVLTSHSM 2130
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
386-556 |
5.64e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.50 E-value: 5.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 386 IPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDgndIR------YLDLKwlrghiglvnqepvlFATTIRENIMY 459
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE---LKisykpqYIKPD---------------YDGTVEDLLRS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 460 GKDDATS----EEITNaaKLseaisfinNLPEGFETQVGErgiqLSGGQKQRISISRAIVKNPSILLLDEATSALDAESE 535
Cdd:PRK13409 424 ITDDLGSsyykSEIIK--PL--------QLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQR 489
|
170 180
....*....|....*....|...
gi 15220188 536 KIVQEALDRVMVGR--TTVVVAH 556
Cdd:PRK13409 490 LAVAKAIRRIAEEReaTALVVDH 512
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
90-250 |
6.40e-05 |
|
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: 46.33 E-value: 6.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 90 FVYLSVVILFSSWLEVACWMHTGERQAAKIRKAYLRSMLSQDISLFDTEIStGEVISAITSEIlvvqDAISEKVGNfmHF 169
Cdd:cd18546 45 YLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHERETS-GRIMTRMTSDI----DALSELLQT--GL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 170 ISRFIAGFAIGFASV------WQISLVTLSIVPFIALAGGIYAFVSSGLIVRVRksyvkaNEIAE------EVIGNVRTV 237
Cdd:cd18546 118 VQLVVSLLTLVGIAVvllvldPRLALVALAALPPLALATRWFRRRSSRAYRRAR------ERIAAvnadlqETLAGIRVV 191
|
170
....*....|...
gi 15220188 238 QAFTGEEKAVSSY 250
Cdd:cd18546 192 QAFRRERRNAERF 204
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1088-1155 |
7.68e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.87 E-value: 7.68e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15220188 1088 SEVMEAAKLaNAHSFISSLpegystkvgergiqmSGGQRQRIAIARAVLKNPEILLLDEATSALDVES 1155
Cdd:PRK11147 140 NEVLAQLGL-DPDAALSSL---------------SGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
494-607 |
1.04e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.88 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 494 GERGIQLSGGQKQRISISRAIVKNPSILLLDEATSALDAESEKIVQEALdRVMV--GRTTVVVAHRLSTVRN-ADIIAVV 570
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEV-RSMVrdGATVLLTTQYMEEAEQlAHELTVI 217
|
90 100 110
....*....|....*....|....*....|....*..
gi 15220188 571 GGGKIIESGSHDELISNPDGaysSLLRIQEAASPNLN 607
Cdd:NF000106 218 DRGRVIADGKVDELKTKVGG---RTLQIRPAHAAELD 251
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
970-1196 |
1.19e-04 |
|
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: 46.36 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 970 DTGEELsnvegtIELKGVHFSYPSRPDVTIFSDFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPT-AGIIMIDGQDI 1048
Cdd:TIGR02633 252 EIGDVI------LEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPV 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1049 K-KLKLKSLRRHIGLVQQE-------PALfatTIYENILYG--KEGASESEVMEAAKLANAHSFISSLPEGYSTKVGERG 1118
Cdd:TIGR02633 326 DiRNPAQAIRAGIAMVPEDrkrhgivPIL---GVGKNITLSvlKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIG 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1119 iQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTT-VVVAHRLSTIKN-SDMISVIQDGKI 1196
Cdd:TIGR02633 403 -RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAiIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1004-1200 |
1.38e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.78 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1004 NLLVPSGKSMALVGQSGSGKSSvLSLVLrfydptAG-IIMIDG------QDIKKLKLKSL---------RRHIGLVQQEP 1067
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSA-LARAL------AGeLPLLSGerqsqfSHITRLSFEQLqklvsdewqRNNTDMLSPGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1068 ALFATTIYENILygkEGASESEVME--AAKLAnahsfISSLpegystkVGERGIQMSGGQRQRIAIARAVLKNPEILLLD 1145
Cdd:PRK10938 96 DDTGRTTAEIIQ---DEVKDPARCEqlAQQFG-----ITAL-------LDRRFKYLSTGETRKTLLCQALMSEPDLLILD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15220188 1146 EATSALDVESERVVQQALDRLMRDRTTVV-VAHRLSTIKN-SDMISVIQDGKIIEQG 1200
Cdd:PRK10938 161 EPFDGLDVASRQQLAELLASLHQSGITLVlVLNRFDEIPDfVQFAGVLADCTLAETG 217
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
175-297 |
1.63e-04 |
|
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: 45.28 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 175 AGFAIGFASV-----WQISLVTLSIVPFIALAGGIYAFVSSGLIVRVRKSYVKANEIAEEVIGNVRTVQAFTGEEKAVSS 249
Cdd:cd18782 126 VLFSVIYIAVlfsysPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWR 205
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 15220188 250 YQGALRNTYNYGRKAGLAKGLGLGSLHFVLFLSWALLIWFTSIVVHKG 297
Cdd:cd18782 206 WQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSLLVLWVGAYLVLRG 253
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
375-534 |
1.85e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.71 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 375 DVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIerfyeptDGAVMLDGNDIRYL-DLKWLRghiglVNQEP------V 447
Cdd:PRK11147 15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDDGRIIYEqDLIVAR-----LQQDPprnvegT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 448 LF---ATTIRENIMYGKD----------DATSEEITNAAKLSEAISfINNLPEgFETQVGERGIQ-----------LSGG 503
Cdd:PRK11147 83 VYdfvAEGIEEQAEYLKRyhdishlvetDPSEKNLNELAKLQEQLD-HHNLWQ-LENRINEVLAQlgldpdaalssLSGG 160
|
170 180 190
....*....|....*....|....*....|.
gi 15220188 504 QKQRISISRAIVKNPSILLLDEATSALDAES 534
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1015-1177 |
2.26e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.27 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1015 LVGQSGSGKSS---VLSLVLrfyDPTAGIIMIDgqdiKKLKLKSLRR-----------------HIGL--VQQEpalfat 1072
Cdd:PRK15064 32 LIGANGCGKSTfmkILGGDL---EPSAGNVSLD----PNERLGKLRQdqfafeeftvldtvimgHTELweVKQE------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1073 tiyENILYGKEGASESEVMEAAKLANAHSFIsslpEGYS--TKVGE----RGI----------QMSGGQRQRIAIARAVL 1136
Cdd:PRK15064 99 ---RDRIYALPEMSEEDGMKVADLEVKFAEM----DGYTaeARAGElllgVGIpeeqhyglmsEVAPGWKLRVLLAQALF 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15220188 1137 KNPEILLLDEATSALDVESERVVQQALDRlmRDRTTVVVAH 1177
Cdd:PRK15064 172 SNPDILLLDEPTNNLDINTIRWLEDVLNE--RNSTMIIISH 210
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1109-1196 |
2.71e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.11 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1109 GYSTKVGergiQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLM-RDRTTVVVAHRLSTIKN-SD 1186
Cdd:PRK10982 384 GHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIIISSEMPELLGiTD 459
|
90
....*....|
gi 15220188 1187 MISVIQDGKI 1196
Cdd:PRK10982 460 RILVMSNGLV 469
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
379-576 |
3.27e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 44.62 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 379 FDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLD-LKWLRGHIGLV----NQEPVLFATTI 453
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSpRDAIRAGIAYVpedrKGEGLVLDLSI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 454 RENIMYGKDDATSEE--ITNAAKLSEAISFINNL---PEGFETQVGergiQLSGGQKQRISISRAIVKNPSILLLDEATS 528
Cdd:COG1129 348 RENITLASLDRLSRGglLDRRRERALAEEYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEPTR 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15220188 529 ALD--AESE--KIVQEALDRvmvGRTTVVVahrlST-----VRNADIIAVVGGGKII 576
Cdd:COG1129 424 GIDvgAKAEiyRLIRELAAE---GKAVIVI----SSelpelLGLSDRILVMREGRIV 473
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
112-289 |
3.35e-04 |
|
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: 44.04 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 112 GERQAAKIRKAYLRSMLSQDISLFDtEISTGEVISAITSEILVVQDAISEKVGNFMHFISRFIAGFAIGFASVWQISLVT 191
Cdd:cd18563 71 GERITADLRRDLYEHLQRLSLSFFD-KRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 192 LSIVPFIALagGIYAF--VSSGLIVRVRKSYVKANEIAEEVIGNVRTVQAFTGEEKAVSSYQGALRNTYNYGRKAGLAKG 269
Cdd:cd18563 150 LIPVPLVVW--GSYFFwkKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWA 227
|
170 180
....*....|....*....|
gi 15220188 270 LGLGSLHFVLFLSwALLIWF 289
Cdd:cd18563 228 TFFPLLTFLTSLG-TLIVWY 246
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
117-244 |
3.67e-04 |
|
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: 44.06 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 117 AKIRKAYLRSMLSQDISLFDTEiSTGEVISAITSEILVVQDAISEKVGNFMHFISRFIAGFAIGFASVWQISLVTLSIVP 196
Cdd:cd18778 73 ADLRSDLYDKLQRLSLRYFDDR-QTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIP 151
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 15220188 197 FIALAGGIYAFVSSGLIVRVRKSYVKANEIAEEVIGNVRTVQAFTGEE 244
Cdd:cd18778 152 FLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREE 199
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
109-310 |
5.16e-04 |
|
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: 43.59 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 109 MHTGERQAAKIRKAYLRSMLSQDISLFDTeISTGEVISAItSEILVVQDAISEKVGN-FMHFISRFIAGFAIGFASvWQI 187
Cdd:cd18570 67 LKLSQKLDIRLILGYFKHLLKLPLSFFET-RKTGEIISRF-NDANKIREAISSTTISlFLDLLMVIISGIILFFYN-WKL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 188 SLVTLSIVPfialaggIYAFvssgLIVRVRKSYVKAN-EIAE----------EVIGNVRTVQAFTGEEKAVSSYQGALRN 256
Cdd:cd18570 144 FLITLLIIP-------LYIL----IILLFNKPFKKKNrEVMEsnaelnsyliESLKGIETIKSLNAEEQFLKKIEKKFSK 212
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15220188 257 TYNYGRKAGLAKGLGLGSLHFVLFLSWALLIWFTSIVVHKGIANGGE--SFTTMLN 310
Cdd:cd18570 213 LLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGSYLVIKGQLSLGQliAFNALLG 268
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1004-1215 |
5.20e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 43.64 E-value: 5.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1004 NLLVPSGKSMALVGQSGSGKS----SVLSLVLRFYDPTAGIIMIDGQDIKKLKLKSLRRHIG----LVQQEP-------A 1068
Cdd:PRK15093 27 SMTLTEGEIRGLVGESGSGKSliakAICGVTKDNWRVTADRMRFDDIDLLRLSPRERRKLVGhnvsMIFQEPqscldpsE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1069 LFATTIYENI-----------LYGKEGASESEVMEAAKLANAHSFISSLPegystkvgergIQMSGGQRQRIAIARAVLK 1137
Cdd:PRK15093 107 RVGRQLMQNIpgwtykgrwwqRFGWRKRRAIELLHRVGIKDHKDAMRSFP-----------YELTEGECQKVMIAIALAN 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1138 NPEILLLDEATSALDVESERVVQQALDRLMRDRTTVV--VAHRLSTI-KNSDMISVIQDGKIIEQGSHNILVENKNGPYS 1214
Cdd:PRK15093 176 QPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTIllISHDLQMLsQWADKINVLYCGQTVETAPSKELVTTPHHPYT 255
|
.
gi 15220188 1215 K 1215
Cdd:PRK15093 256 Q 256
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
377-567 |
5.27e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.55 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 377 VIFDkLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIRYLDLKWLrGHIGlvNQEPVLFATTIREN 456
Cdd:PRK13541 15 NLFD-LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC-TYIG--HNLGLKLEMTVFEN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 457 IMYGKDDATSEEITNAA----KLSEAISfinnlpegfetqvgERGIQLSGGQKQRISISRAIVKNPSILLLDEATSALDA 532
Cdd:PRK13541 91 LKFWSEIYNSAETLYAAihyfKLHDLLD--------------EKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSK 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 15220188 533 ESEKIVQEALdrVM---VGRTTVVVAHRLSTVRNADII 567
Cdd:PRK13541 157 ENRDLLNNLI--VMkanSGGIVLLSSHLESSIKSAQIL 192
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
359-531 |
6.04e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.01 E-value: 6.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 359 GDILF--KDVTFTYPSRPDVVIFDKLNFVIPAGKVVALVGGSGSGKS-TMISLIERFY-EPTDGAVMLDGNDIR------ 428
Cdd:NF040905 254 GEVVFevKNWTVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYgRNISGTVFKDGKEVDvstvsd 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 429 -------YL--DlkwlRGHIGLVNQEpvlfatTIRENImygkddatseEITNAAKLSEAiSFINnlpEGFETQVGER--- 496
Cdd:NF040905 334 aidaglaYVteD----RKGYGLNLID------DIKRNI----------TLANLGKVSRR-GVID---ENEEIKVAEEyrk 389
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15220188 497 -------GI-----QLSGGQKQRISISRAIVKNPSILLLDEATSALD 531
Cdd:NF040905 390 kmniktpSVfqkvgNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1121-1196 |
7.29e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.45 E-value: 7.29e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15220188 1121 MSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALDRLMRDRTTV--VVAHRLSTIKNSDMISVIQDGKI 1196
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIilVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1109-1201 |
7.83e-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: 7.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1109 GYsTKVGERGIQMSGGQRQRIAIARAVLK---NPEILLLDEATSALDVESERVVQQALDRLMRDRTTVVV-AHRLSTIKN 1184
Cdd:TIGR00630 819 GY-IRLGQPATTLSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVViEHNLDVIKT 897
|
90 100
....*....|....*....|...
gi 15220188 1185 SDMISVI------QDGKIIEQGS 1201
Cdd:TIGR00630 898 ADYIIDLgpeggdGGGTVVASGT 920
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1017-1159 |
1.06e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.78 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1017 GQSGSGKSSVLSLVLRFYDPTAGIIMIDGQDIKKLKlKSLRRHIGlvQQEPALFATTIYENILYGKEGASESEVMEAAkl 1096
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA-KPYCTYIG--HNLGLKLEMTVFENLKFWSEIYNSAETLYAA-- 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15220188 1097 anAHSFisSLPEGYSTKVgergIQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVV 1159
Cdd:PRK13541 108 --IHYF--KLHDLLDEKC----YSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLL 162
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1124-1152 |
1.21e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.19 E-value: 1.21e-03
10 20
....*....|....*....|....*....
gi 15220188 1124 GQRQRIAIARAVLKNPEILLLDEATSALD 1152
Cdd:NF033858 401 GIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1120-1196 |
1.40e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 42.61 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1120 QMSGGQRQRIAIARAVLKNPEILLLDEATSALDV----ESERVVQQALDRLMrdrTTVVVAHRLSTIKN-SDMISVIQDG 1194
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVgakyEIYKLINQLVQQGV---AIIVISSELPEVLGlSDRVLVMHEG 481
|
..
gi 15220188 1195 KI 1196
Cdd:PRK13549 482 KL 483
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
341-591 |
1.47e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 42.85 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 341 MIERNTEDK-TGRK--LGNVNGDILF--KDVTftypsRPDVVIFDKLNFVIPAGKVVALVGGSGSGKSTMISLIERFYEP 415
Cdd:PRK09700 241 MVGRELQNRfNAMKenVSNLAHETVFevRNVT-----SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKR 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 416 TDGAVMLDGNDIR----YLDLKWLRGHIGLVNQEPVLFAT-TIRENImygkddATSEEITNAaKLSEAISFINNLPEGFE 490
Cdd:PRK09700 316 AGGEIRLNGKDISprspLDAVKKGMAYITESRRDNGFFPNfSIAQNM------AISRSLKDG-GYKGAMGLFHEVDEQRT 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 491 TQ------------VGERGIQLSGGQKQRISISRAIVKNPSILLLDEATSALD----AESEKIVQEALDRvmvGRTTVVV 554
Cdd:PRK09700 389 AEnqrellalkchsVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDvgakAEIYKVMRQLADD---GKVILMV 465
|
250 260 270
....*....|....*....|....*....|....*..
gi 15220188 555 AHRLstvrnADIIAVVGGGKIIESGSHDELISNPDGA 591
Cdd:PRK09700 466 SSEL-----PEIITVCDRIAVFCEGRLTQILTNRDDM 497
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
119-258 |
1.64e-03 |
|
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: 42.08 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 119 IRKAYLRSMLSQDISLFDtEISTGEVISAITSEILVVQDAISeKVGNFMHFISRFIAGFAIGFASVWQISLVTLSIVPFI 198
Cdd:cd18543 74 LRTDLFAHLQRLDGAFHD-RWQSGQLLSRATSDLSLVQRFLA-FGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPL 151
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15220188 199 ALAGgiyafvssgliVRVRKSYVKAN-----------EIAEEVIGNVRTVQAFTGEEKAVSSYQGALRNTY 258
Cdd:cd18543 152 VLVA-----------RRFRRRYFPASrraqdqagdlaTVVEESVTGIRVVKAFGRERRELDRFEAAARRLR 211
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
499-560 |
1.89e-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: 42.46 E-value: 1.89e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15220188 499 QLSGGQKQRISISRAIVKNPSILLLDEATSALD----AESEKIVQEALDRvmvGRTTVVVAHRLST 560
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqrLNVARLIRELAEE---GKYVLVVEHDLAI 274
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
500-579 |
1.93e-03 |
|
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: 41.09 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 500 LSGGQKQRISISRAIVKNPS--ILLLDEATSAL-DAESEKIVqEALDRVM-VGRTTVVVAHRLSTVRNADIIAVVG---- 571
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLhPRDNDRLI-ETLKRLRdLGNTVLVVEHDEDTIRAADHVIDIGpgag 216
|
90
....*....|
gi 15220188 572 --GGKIIESG 579
Cdd:cd03270 217 vhGGEIVAQG 226
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
377-571 |
1.99e-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: 40.42 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 377 VIFDKLNFVIPAGKVVALVGGSGSGKSTMIslierfyeptdgavmldgndiryldlkwlrghiglvnqEPVLFATTIREN 456
Cdd:cd03227 9 SYFVPNDVTFGEGSLTIITGPNGSGKSTIL--------------------------------------DAIGLALGGAQS 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 457 IMYGKDDATSEEITNAAKLsEAISFInnlpegfetqvgergIQLSGGQKQRISISRAI----VKNPSILLLDEATSALDA 532
Cdd:cd03227 51 ATRRRSGVKAGCIVAAVSA-ELIFTR---------------LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDP 114
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15220188 533 ESEKIVQEALDRVMVGRTTVVVA-HRLSTVRNADIIAVVG 571
Cdd:cd03227 115 RDGQALAEAILEHLVKGAQVIVItHLPELAELADKLIHIK 154
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
94-200 |
2.11e-03 |
|
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: 41.70 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 94 SVVILFSSWLEVacwmHTGERQAAKIRKAYLRSMLSQDISLFdTEISTGEVISAITSEILVVQDAIS----EKVGNFMHF 169
Cdd:cd18550 53 ALLGVVQTYLSA----RIGQGVMYDLRVQLYAHLQRMSLAFF-TRTRTGEIQSRLNNDVGGAQSVVTgtltSVVSNVVTL 127
|
90 100 110
....*....|....*....|....*....|.
gi 15220188 170 ISRFIAGFAIGfasvWQISLVTLSIVPFIAL 200
Cdd:cd18550 128 VATLVAMLALD----WRLALLSLVLLPLFVL 154
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
389-556 |
2.65e-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: 42.08 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 389 GKVVALVGGSGSGKSTMISLIERFYEPTDGAVmlDGN-DIRYldlK--WLRGHIGLvnqepvlfatTIRENIM--YGKDD 463
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDlKISY---KpqYISPDYDG----------TVEEFLRsaNTDDF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 464 ATS---EEITNaaKLSeaisfINNLpegFETQVGErgiqLSGGQKQRISISRAIVKNPSILLLDEATSALDAESEKIVQE 540
Cdd:COG1245 431 GSSyykTEIIK--PLG-----LEKL---LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAK 496
|
170
....*....|....*...
gi 15220188 541 ALDRVMVGR--TTVVVAH 556
Cdd:COG1245 497 AIRRFAENRgkTAMVVDH 514
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1121-1200 |
2.78e-03 |
|
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: 40.00 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1121 MSGGQRQRIAIARAVLKNPE--ILLLDEATSALDVESERVVQQALDRLMRDRTTV-VVAHRLSTIKNSDMI------SVI 1191
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTViLIEHNLDVLSSADWIidfgpgSGK 167
|
....*....
gi 15220188 1192 QDGKIIEQG 1200
Cdd:cd03238 168 SGGKVVFSG 176
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1113-1164 |
3.65e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.26 E-value: 3.65e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 15220188 1113 KVGergiQMSGGQRQRIAIARAVLKNPEILLLDEATSALDVESERVVQQALD 1164
Cdd:PRK11819 442 KVG----VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALL 489
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
500-594 |
3.95e-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: 41.54 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 500 LSGGQKQRISISRAI------VknpsILLLDEATSAL-DAESEKIVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVG- 571
Cdd:TIGR00630 489 LSGGEAQRIRLATQIgsgltgV----LYVLDEPSIGLhQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVIDIGp 564
|
90 100 110
....*....|....*....|....*....|.
gi 15220188 572 -----GGKIIESGSHDELISNPD---GAYSS 594
Cdd:TIGR00630 565 gagehGGEVVASGTPEEILANPDsltGQYLS 595
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
390-428 |
5.10e-03 |
|
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.
Pssm-ID: 428926 Cd Length: 192 Bit Score: 39.65 E-value: 5.10e-03
10 20 30
....*....|....*....|....*....|....*....
gi 15220188 390 KVVALVGGSGSGKSTMISLIERFYEPTDGAVMLDGNDIR 428
Cdd:pfam06414 12 KAILLGGQPGAGKTELARALLDELGRQGNVVRIDPDDFR 50
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
495-558 |
5.29e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.95 E-value: 5.29e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15220188 495 ERGI-QLSGGQKQRISISRAIVKNPSILLLDEATSALDAESEKIVQEALDRVMVGRTTVVVAHRL 558
Cdd:PRK13409 207 DRDIsELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
500-589 |
5.65e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.21 E-value: 5.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 500 LSGGQKQRISISRAIVKNP---SILLLDEATSALDAESEKIVQEALDR-VMVGRTTVVVAHRLSTVRNAD-IIAV----- 569
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLHFEDIRKLLEVLHRlVDKGNTVVVIEHNLDVIKTADwIIDLgpegg 910
|
90 100
....*....|....*....|
gi 15220188 570 VGGGKIIESGSHDELISNPD 589
Cdd:PRK00349 911 DGGGEIVATGTPEEVAKVEA 930
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
992-1200 |
6.17e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.80 E-value: 6.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 992 PSRPDVTIFS--DFNLLVPSGKSMALVGQSGSGKSSVLSLVLRFYDPTAGIIMIDGqDIKKLKLKSlrrhiGLVQQepal 1069
Cdd:PRK13546 30 PKHKNKTFFAldDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-EVSVIAISA-----GLSGQ---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 1070 faTTIYENILYG--------KE-GASESEVMEAAKLANahsFISSLPEGYSTkvgergiqmsgGQRQRIAIARAVLKNPE 1140
Cdd:PRK13546 100 --LTGIENIEFKmlcmgfkrKEiKAMTPKIIEFSELGE---FIYQPVKKYSS-----------GMRAKLGFSINITVNPD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15220188 1141 ILLLDEatsALDVESERVVQQALDRLM----RDRTTVVVAHRLSTIKN-SDMISVIQDGKIIEQG 1200
Cdd:PRK13546 164 ILVIDE---ALSVGDQTFAQKCLDKIYefkeQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYG 225
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
499-594 |
9.73e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.23 E-value: 9.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220188 499 QLSGGQKQRISISRAIVKNPSILLLDEATSALDAESEKIVQEALdrVMVGRTTVVVAHR---LSTVRnADIIAVVGGGKI 575
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSHArefLNTVV-TDILHLHGQKLV 420
|
90 100
....*....|....*....|....*.
gi 15220188 576 IESGSHD-------ELISNPDGAYSS 594
Cdd:PLN03073 421 TYKGDYDtfertreEQLKNQQKAFES 446
|
|
| |
