|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
22-603 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 567.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 22 PTRFFPFVWQATEGVRPYLLLLVICTAGAATFEALLFSKIGQLVDWLSKSQPESFLSQHAsniLILISVLFANILFVNIQ 101
Cdd:COG1132 5 PRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLL---LLLLGLALLRALLSYLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 102 SIIKHQILYStFPMRLRWRFHNLLLKQSLDFFHNDFAGRLSAKVMQTALAIREFWIILGDMLAYVSIYFITVSIVLGAIS 181
Cdd:COG1132 82 RYLLARLAQR-VVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 182 PTLLIPLMVWLGLFLLSAWFFIPRLSKVSQQQADARAVMTGRVTDAYTNIQTVKLFAHAGRESQYAKASMKEFMTTVYAQ 261
Cdd:COG1132 161 WRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 262 MRLGTLFEVSINMLSAVLFVGVIGTAVWLWTQGLAALGVIAATTAMILKLNSMAEFMMWHMSALFENVGTIQDGMQTLGK 341
Cdd:COG1132 241 ARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 342 KINIQDKPEAKPLAVKQGEIVFKDVTFAY-NNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILID 420
Cdd:COG1132 321 PPEIPDPPGAVPLPPVRGEIEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILID 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 421 GQNIEDVTQDSLRANIALVTQDTSLLHRSVAENIKYGRPDATDHDMQSAVHKAKAAEFIPQLVDlkgrsGYEAQVGERGV 500
Cdd:COG1132 401 GVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPD-----GYDTVVGERGV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 501 KLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIAQMDRLIVLDEGKIAEQ 580
Cdd:COG1132 476 NLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQ 555
|
570 580
....*....|....*....|...
gi 746197230 581 GTHEELIAKNGIYAQLWKRQTGG 603
Cdd:COG1132 556 GTHEELLARGGLYARLYRLQFGE 578
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
213-600 |
1.20e-124 |
|
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: 380.70 E-value: 1.20e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 213 QADARAvmTGRVTDAYTNIQTVKLFAHAGRESQ--------YAKASMKefmttvyAQMRLGTLfevsiNMLSAVLFVgvI 284
Cdd:COG5265 212 EADSEA--NTRAVDSLLNYETVKYFGNEAREARrydealarYERAAVK-------SQTSLALL-----NFGQALIIA--L 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 285 GTAVWLWtqgLAALGVIAAT---------TAMILKL---------------NSMAEfmmwhMSALFEnvgtiqdgmqTLG 340
Cdd:COG5265 276 GLTAMML---MAAQGVVAGTmtvgdfvlvNAYLIQLyiplnflgfvyreirQALAD-----MERMFD----------LLD 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 341 KKINIQDKPEAKPLAVKQGEIVFKDVTFAYNNKNVI-DHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILI 419
Cdd:COG5265 338 QPPEVADAPDAPPLVVGGGEVRFENVSFGYDPERPIlKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILI 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 420 DGQNIEDVTQDSLRANIALVTQDTSLLHRSVAENIKYGRPDATDHDMQSAVHKAKAAEFIPQLVDlkgrsGYEAQVGERG 499
Cdd:COG5265 418 DGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPD-----GYDTRVGERG 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 500 VKLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIAQMDRLIVLDEGKIAE 579
Cdd:COG5265 493 LKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVE 572
|
410 420
....*....|....*....|.
gi 746197230 580 QGTHEELIAKNGIYAQLWKRQ 600
Cdd:COG5265 573 RGTHAELLAQGGLYAQMWARQ 593
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
24-601 |
1.35e-122 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 378.79 E-value: 1.35e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 24 RFFPFVWQAtegvRPYLLLLVICTAGAATFeAL---LFSKigQLVDwlsksqpeSFLSQHASNILILIS-----VLFANI 95
Cdd:COG2274 146 WFLRLLRRY----RRLLLQVLLASLLINLL-ALatpLFTQ--VVID--------RVLPNQDLSTLWVLAiglllALLFEG 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 96 LFVNIQSIIkhqILYSTFPMRLRW--RFHNLLLKQSLDFFHNDFAGRLSAKVMQTAlAIREFwiiLGDMLAYVSIYFITV 173
Cdd:COG2274 211 LLRLLRSYL---LLRLGQRIDLRLssRFFRHLLRLPLSFFESRSVGDLASRFRDVE-SIREF---LTGSLLTALLDLLFV 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 174 ---SIVLGAISPTLLIPLMVWLGLFLLSAWFFIPRLSKVSQQQADARAVMTGRVTDAYTNIQTVKLFAHAGRESQYAKAS 250
Cdd:COG2274 284 lifLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENL 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 251 MKEFMTTVYAQMRLGTLFEVSINMLSAVLFVGVIGTAVWLWTQG-------LAALGVIAATTAMILKL-NSMAEFMMwhM 322
Cdd:COG2274 364 LAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGqltlgqlIAFNILSGRFLAPVAQLiGLLQRFQD--A 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 323 SALFENVGTIQDgmqtlgKKINIQDKPEAKPLAVKQGEIVFKDVTFAY--NNKNVIDHFNLHIKAGEKIGIVGRSGAGKS 400
Cdd:COG2274 442 KIALERLDDILD------LPPEREEGRSKLSLPRLKGDIELENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKS 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 401 TLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANIALVTQDTSLLHRSVAENIKYGRPDATDHDMQSAVHKAKAAEFIP 480
Cdd:COG2274 516 TLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIE 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 481 QLVDlkgrsGYEAQVGERGVKLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRL 560
Cdd:COG2274 596 ALPM-----GYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRL 670
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 746197230 561 STIAQMDRLIVLDEGKIAEQGTHEELIAKNGIYAQLWKRQT 601
Cdd:COG2274 671 STIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
361-597 |
7.44e-115 |
|
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: 342.29 E-value: 7.44e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNK--NVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANIAL 438
Cdd:cd03251 1 VEFKNVTFRYPGDgpPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 439 VTQDTSLLHRSVAENIKYGRPDATDHDMQSAVHKAKAAEFIPQLVDlkgrsGYEAQVGERGVKLSGGQRQRIAIARVFLK 518
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPE-----GYDTVIGERGVKLSGGQRQRIAIARALLK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 746197230 519 DAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIAQMDRLIVLDEGKIAEQGTHEELIAKNGIYAQLW 597
Cdd:cd03251 156 DPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
361-600 |
6.36e-113 |
|
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: 337.28 E-value: 6.36e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYN-NKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANIALV 439
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 440 TQDTSLLHRSVAENIKYGRPDATDHDMQSAVHKAKAAEFIPQLVDlkgrsGYEAQVGERGVKLSGGQRQRIAIARVFLKD 519
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPD-----GYDTIVGERGLKLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 520 APILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIAQMDRLIVLDEGKIAEQGTHEELIAKNGIYAQLWKR 599
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKA 235
|
.
gi 746197230 600 Q 600
Cdd:cd03253 236 Q 236
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
170-599 |
8.74e-105 |
|
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: 328.26 E-value: 8.74e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 170 FITVSIVLGAISPtlliPLMVWLGLFLLSAWFFIPRLS-----KVSQQQADARAVMTGRVTDAYTNIQTVKLFAHAGRES 244
Cdd:COG4987 143 ILAAVAFLAFFSP----ALALVLALGLLLAGLLLPLLAarlgrRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRAL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 245 QYAKASMKEFMTTVYAQMRLGTLFEVSINMLSAVLFVGVIGTAVWLWTQGLAALGVIAATTAMILklnsmaefmmwhmsA 324
Cdd:COG4987 219 ARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAAL--------------A 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 325 LFENVGTIQDGMQTLG------KKIN-IQDK------PEAKPLAVKQGEIVFKDVTFAYNN--KNVIDHFNLHIKAGEKI 389
Cdd:COG4987 285 LFEALAPLPAAAQHLGrvraaaRRLNeLLDAppavtePAEPAPAPGGPSLELEDVSFRYPGagRPVLDGLSLTLPPGERV 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 390 GIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANIALVTQDTSLLHRSVAENIKYGRPDATDHDMQSA 469
Cdd:COG4987 365 AIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAA 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 470 VHKAKAAEFIPQLVDlkgrsGYEAQVGERGVKLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMV 549
Cdd:COG4987 445 LERVGLGDWLAALPD-----GLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA 519
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 746197230 550 DKTVIAIAHRLSTIAQMDRLIVLDEGKIAEQGTHEELIAKNGIYAQLWKR 599
Cdd:COG4987 520 GRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQR 569
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
361-600 |
8.11e-103 |
|
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: 311.40 E-value: 8.11e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNK---NVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANIA 437
Cdd:cd03249 1 IEFKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 438 LVTQDTSLLHRSVAENIKYGRPDATDHDMQSAVHKAKAAEFIPQLVDlkgrsGYEAQVGERGVKLSGGQRQRIAIARVFL 517
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPD-----GYDTLVGERGSQLSGGQKQRIAIARALL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 518 KDAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIAQMDRLIVLDEGKIAEQGTHEELIAKNGIYAQLW 597
Cdd:cd03249 156 RNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLV 235
|
...
gi 746197230 598 KRQ 600
Cdd:cd03249 236 KAQ 238
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
117-600 |
4.57e-101 |
|
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: 318.57 E-value: 4.57e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 117 LRWRFHNLLLKQSLDFFHNDFAG----RLSAKVMQ--------TALAIREFWIILGDMLAYVSIYFITVSIVLGAIsPTL 184
Cdd:TIGR02204 93 IRRAVFAHLISLSPSFFDKNRSGevvsRLTTDTTLlqsvigssLSMALRNALMCIGGLIMMFITSPKLTSLVLLAV-PLV 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 185 LIPLMvwlglfllsawFFIPRLSKVSQQQADARAVMTGRVTDAYTNIQTVKLFAHAGRESQYAKASMKEFMTTVYAQMRL 264
Cdd:TIGR02204 172 LLPIL-----------LFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRT 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 265 GTLfevsinMLSAVLFVGVIGTAVWLWTQGLAAL-GVIAATTamilklnsMAEFMMW------HMSALFENVGTIQD--- 334
Cdd:TIGR02204 241 RAL------LTAIVIVLVFGAIVGVLWVGAHDVIaGKMSAGT--------LGQFVFYavmvagSIGTLSEVWGELQRaag 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 335 GMQTLGKKINIQD--KPEAKPLAVK---QGEIVFKDVTFAY---NNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLL 406
Cdd:TIGR02204 307 AAERLIELLQAEPdiKAPAHPKTLPvplRGEIEFEQVNFAYparPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLL 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 407 LHFYHLKEGAILIDGQNIEDVTQDSLRANIALVTQDTSLLHRSVAENIKYGRPDATDHDMQSAVHKAKAAEFIPQLVDlk 486
Cdd:TIGR02204 387 LRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPE-- 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 487 grsGYEAQVGERGVKLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIAQM 566
Cdd:TIGR02204 465 ---GYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKA 541
|
490 500 510
....*....|....*....|....*....|....
gi 746197230 567 DRLIVLDEGKIAEQGTHEELIAKNGIYAQLWKRQ 600
Cdd:TIGR02204 542 DRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
133-610 |
1.67e-98 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 312.28 E-value: 1.67e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 133 FHndfAGRLSAKVMQTALAIRE--FWIILGDMLAYVSiyfitvsivlGAISPTLLIPLMVWLG------LFLLSAWF--- 201
Cdd:PRK13657 106 WH---SQRGSGRALHTLLRGTDalFGLWLEFMREHLA----------TLVALVVLLPLALFMNwrlslvLVVLGIVYtli 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 202 --FIPRLSKVSQQQADAR-AVMTGRVTDAYTNIQTVKLFAHAGRESQYAKASMKEFMTTVYAQMRLGTLFEVSINMLSAV 278
Cdd:PRK13657 173 ttLVMRKTKDGQAAVEEHyHDLFAHVSDAIGNVSVVQSYNRIEAETQALRDIADNLLAAQMPVLSWWALASVLNRAASTI 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 279 LFVGVIGTAVWLWTQGLAALGVIAA----TTAMILKLNSMAEFMmwhmSALFENVGTIQDGMQTLGKKINIQDKPEAKPL 354
Cdd:PRK13657 253 TMLAILVLGAALVQKGQLRVGEVVAfvgfATLLIGRLDQVVAFI----NQVFMAAPKLEEFFEVEDAVPDVRDPPGAIDL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 355 AVKQGEIVFKDVTFAYNNKN-VIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLR 433
Cdd:PRK13657 329 GRVKGAVEFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLR 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 434 ANIALVTQDTSLLHRSVAENIKYGRPDATDHDMQSAVHKAKAAEFIpqlvdLKGRSGYEAQVGERGVKLSGGQRQRIAIA 513
Cdd:PRK13657 409 RNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFI-----ERKPDGYDTVVGERGRQLSGGERQRLAIA 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 514 RVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIAQMDRLIVLDEGKIAEQGTHEELIAKNGIY 593
Cdd:PRK13657 484 RALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRF 563
|
490
....*....|....*..
gi 746197230 594 AQLWKrqTGGFLIEQKV 610
Cdd:PRK13657 564 AALLR--AQGMLQEDER 578
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
27-591 |
4.06e-98 |
|
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: 310.54 E-value: 4.06e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 27 PFVWQATEGVRPYLLLLVIC---TAGAATFEALLFSKIgqLVDWLSKSQPESFLSQHasnILILISVLFANILFVNIQSI 103
Cdd:COG4988 6 KRLKRLARGARRWLALAVLLgllSGLLIIAQAWLLASL--LAGLIIGGAPLSALLPL---LGLLLAVLLLRALLAWLRER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 104 IKHQilystFPMRLRWRFHNLLLKQSLDFFHNDFAGRLSAKVMQTALAIREfwiilgDMLAYVSIYFITVsIVLGAISPT 183
Cdd:COG4988 81 AAFR-----AAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVE------ALDGYFARYLPQL-FLAALVPLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 184 LLI---PLMVWLGLFLLSAWFFIP--------RLSKVSQQQADARAVMTGRVTDAYTNIQTVKLFAHAGRESQ------- 245
Cdd:COG4988 149 ILVavfPLDWLSGLILLVTAPLIPlfmilvgkGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAEriaease 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 246 -YAKASMKefmttvyaqmrlgTLfevSINMLS-AVL-FVGVIGTAVWLWTQGLAAL-GVIAATTAM-ILKLnsMAEFMM- 319
Cdd:COG4988 229 dFRKRTMK-------------VL---RVAFLSsAVLeFFASLSIALVAVYIGFRLLgGSLTLFAALfVLLL--APEFFLp 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 320 -------WHMSAlfENVGTIQDGMQTLGKKINIQDKPEAKPLAVKQGEIVFKDVTFAY-NNKNVIDHFNLHIKAGEKIGI 391
Cdd:COG4988 291 lrdlgsfYHARA--NGIAAAEKIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVAL 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 392 VGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANIALVTQDTSLLHRSVAENIKYGRPDATDHDMQSAVH 471
Cdd:COG4988 369 VGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 472 KAKAAEFIPQLVDlkgrsGYEAQVGERGVKLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDK 551
Cdd:COG4988 449 AAGLDEFVAALPD-----GLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR 523
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 746197230 552 TVIAIAHRLSTIAQMDRLIVLDEGKIAEQGTHEELIAKNG 591
Cdd:COG4988 524 TVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
359-591 |
2.64e-95 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 291.82 E-value: 2.64e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 359 GEIVFKDVTFAYNNKN-VIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANIA 437
Cdd:cd03254 1 GEIEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 438 LVTQDTSLLHRSVAENIKYGRPDATDHDMQSAVHKAKAAEFIPQLVDlkgrsGYEAQVGERGVKLSGGQRQRIAIARVFL 517
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPN-----GYDTVLGENGGNLSQGERQLLAIARAML 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 746197230 518 KDAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIAQMDRLIVLDEGKIAEQGTHEELIAKNG 591
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
115-600 |
3.52e-95 |
|
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: 303.18 E-value: 3.52e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 115 MRLRWRFHNLLLKQSLDFFHNDFAGRL-------SAKVMQTA-----LAIREFWIILGdMLAYVSIYFITVSIVLgaisp 182
Cdd:TIGR02203 87 RDIRVRMFEKLLGLPVSFFDRQPTGTLlsritfdSEQVASAAtdafiVLVRETLTVIG-LFIVLLYYSWQLTLIV----- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 183 TLLIPLMVWLglfllsAWFFIPRLSKVSQQQADARAVMTGRVTDAYTNIQTVKLFAHAGRESQ-YAKASMkefmTTVYAQ 261
Cdd:TIGR02203 161 VVMLPVLSIL------MRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRrFDAVSN----RNRRLA 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 262 MRL---GTLFEVSINMLSAVLFVGVIGTAVWLWTQGLAALGVIAA-TTAMILklnsmaefMMWHMSALFENVGTIQDGM- 336
Cdd:TIGR02203 231 MKMtsaGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAfITAMIA--------LIRPLKSLTNVNAPMQRGLa 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 337 --QTLGKKINIQDKPEA--KPLAVKQGEIVFKDVTFAY--NNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFY 410
Cdd:TIGR02203 303 aaESLFTLLDSPPEKDTgtRAIERARGDVEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFY 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 411 HLKEGAILIDGQNIEDVTQDSLRANIALVTQDTSLLHRSVAENIKYGRP-DATDHDMQSAVHKAKAAEFIPQLVDlkgrs 489
Cdd:TIGR02203 383 EPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPL----- 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 490 GYEAQVGERGVKLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIAQMDRL 569
Cdd:TIGR02203 458 GLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRI 537
|
490 500 510
....*....|....*....|....*....|.
gi 746197230 570 IVLDEGKIAEQGTHEELIAKNGIYAQLWKRQ 600
Cdd:TIGR02203 538 VVMDDGRIVERGTHNELLARNGLYAQLHNMQ 568
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
333-603 |
2.96e-88 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 285.37 E-value: 2.96e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 333 QDGM---QTLGKKINI-QDKPEAKPLAVK-QGEIVFKDVTFAYNNKNV--IDHFNLHIKAGEKIGIVGRSGAGKSTLIQL 405
Cdd:PRK11176 309 QRGMaacQTLFAILDLeQEKDEGKRVIERaKGDIEFRNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANL 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 406 LLHFYHLKEGAILIDGQNIEDVTQDSLRANIALVTQDTSLLHRSVAENIKYGRPDA-TDHDMQSAVHKAKAAEFIPQLVD 484
Cdd:PRK11176 389 LTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDN 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 485 lkgrsGYEAQVGERGVKLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIA 564
Cdd:PRK11176 469 -----GLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIE 543
|
250 260 270
....*....|....*....|....*....|....*....
gi 746197230 565 QMDRLIVLDEGKIAEQGTHEELIAKNGIYAQLWKRQTGG 603
Cdd:PRK11176 544 KADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQFGQ 582
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
361-600 |
2.12e-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: 256.26 E-value: 2.12e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAY--NNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANIAL 438
Cdd:cd03252 1 ITFEHVRFRYkpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 439 VTQDTSLLHRSVAENIKYGRPDATDHDMQSAVHKAKAAEFIPQLvdlkgRSGYEAQVGERGVKLSGGQRQRIAIARVFLK 518
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISEL-----PEGYDTIVGEQGAGLSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 519 DAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIAQMDRLIVLDEGKIAEQGTHEELIAKNGIYAQLWK 598
Cdd:cd03252 156 NPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQ 235
|
..
gi 746197230 599 RQ 600
Cdd:cd03252 236 LQ 237
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
361-576 |
2.98e-79 |
|
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: 248.07 E-value: 2.98e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKN--VIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANIAL 438
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 439 VTQDTSLLHRSVAENIkygrpdatdhdmqsavhkakaaefipqlvdlkgrsgyeaqvgergvkLSGGQRQRIAIARVFLK 518
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------------LSGGQRQRIAIARALLR 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 746197230 519 DAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIAQMDRLIVLDEGK 576
Cdd:cd03228 114 DPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
125-602 |
4.69e-79 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 263.91 E-value: 4.69e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 125 LLKQSLDFFHNDFAGRLSAKVMQTAlAIREFwIILGDMLAYVSIYFITVSI-VLGAISPTLLIPLMVWLGLFLLSAWFFI 203
Cdd:TIGR01846 222 LLGLPLGYFESRRVGDTVARVRELE-QIRNF-LTGSALTVVLDLLFVVVFLaVMFFYSPTLTGVVIGSLVCYALLSVFVG 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 204 PRLSKVSQQQADARAVMTGRVTDAYTNIQTVKLFAhagRESQYAKASMKEFMTTVYAQMR---LGTLFEVSINMLSAvlf 280
Cdd:TIGR01846 300 PILRKRVEDKFERSAAATSFLVESVTGIETIKATA---TEPQFQNRWDRQLAAYVAASFRvtnLGNIAGQAIELIQK--- 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 281 vgvIGTAVWLWtqgLAALGVIAA--TTAMILKLNSMAEFM---MWHMSALFENVGTIQDGMQTLGKKINIQDKPEAKPLA 355
Cdd:TIGR01846 374 ---LTFAILLW---FGAHLVIGGalSPGQLVAFNMLAGRVtqpVLRLAQLWQDFQQTGIALERLGDILNSPTEPRSAGLA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 356 ---VKQGEIVFKDVTFAY--NNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQD 430
Cdd:TIGR01846 448 alpELRGAITFENIRFRYapDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPA 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 431 SLRANIALVTQDTSLLHRSVAENIKYGRPDATDHDMQSAVHKAKAAEFIPQLvdlkgRSGYEAQVGERGVKLSGGQRQRI 510
Cdd:TIGR01846 528 WLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISEL-----PQGYNTEVGEKGANLSGGQRQRI 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 511 AIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIAQMDRLIVLDEGKIAEQGTHEELIAKN 590
Cdd:TIGR01846 603 AIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQ 682
|
490
....*....|..
gi 746197230 591 GIYAQLWKRQTG 602
Cdd:TIGR01846 683 GLYARLWQQQSG 694
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
61-596 |
7.19e-76 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 255.80 E-value: 7.19e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 61 IGQLVDWL-SKSQPESFlsqhASNILILISVLFANILFVNIQSIIkHQILYSTFPMRLRWRFHNLLLKQSLDFFHNDFAG 139
Cdd:TIGR00958 184 TGRVIDTLgGDKGPPAL----ASAIFFMCLLSIASSVSAGLRGGS-FNYTMARINLRIREDLFRSLLRQDLGFFDENKTG 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 140 RLSAKVMQTALAIREfWIILgdmlaYVSIYFITVSIVLGA------ISPTLLIPLMVWLGLFLLSAWFFIPRLSKVSQQQ 213
Cdd:TIGR00958 259 ELTSRLSSDTQTMSR-SLSL-----NVNVLLRNLVMLLGLlgfmlwLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEEL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 214 ADARAVMTGRVTDAYTNIQTVKLFAHAGRESQYAKASMKEfMTTVYAQMRLGTLFEVSINMLSAVL-FVGVIGTAVWLWT 292
Cdd:TIGR00958 333 QEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEE-TLQLNKRKALAYAGYLWTTSVLGMLiQVLVLYYGGQLVL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 293 QGLAALGVIAATTAMILKLNSMAEFMMWHMSALFENVGTIQDGMQTLGKKINIQDKPEAKPLAVKqGEIVFKDVTFAYNN 372
Cdd:TIGR00958 412 TGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLTGTLAPLNLE-GLIEFQDVSFSYPN 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 373 ---KNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANIALVTQDTSLLHRS 449
Cdd:TIGR00958 491 rpdVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGS 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 450 VAENIKYGRPDATDHDMQSAVHKAKAAEFIPQLVDlkgrsGYEAQVGERGVKLSGGQRQRIAIARVFLKDAPILILDEAT 529
Cdd:TIGR00958 571 VRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPN-----GYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 746197230 530 SALDSEVEAAIQSSLNdlMVDKTVIAIAHRLSTIAQMDRLIVLDEGKIAEQGTHEELIAKNGIYAQL 596
Cdd:TIGR00958 646 SALDAECEQLLQESRS--RASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
179-612 |
6.87e-74 |
|
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: 247.49 E-value: 6.87e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 179 AISPTLLIPL---MVW-LGLFLL---SAWFFIPRLskVSQQQADARAVMTG-------RVTDAYTNIQTVKLFAHAGRES 244
Cdd:TIGR01192 141 FVALFLLIPTafaMDWrLSIVLMvlgILYILIAKL--VMQRTKNGQAAVEHhyhnvfkHVSDSISNVSVVHSYNRIEAET 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 245 QYAKASMKEFMTTVYAQMRLGTLFEVSINMLSAVLFVGVIGTAVWLWTQGLAALGVIAA----TTAMILKLNSMAEFMmw 320
Cdd:TIGR01192 219 SALKQFTNNLLSAQYPVLDWWALASGLNRMASTISMMCILVIGTVLVIKGELSVGEVIAfigfANLLIGRLDQMSGFI-- 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 321 hmSALFENVGTIQDGMQTLGKKINIQDKPEAKPLAVKQGEIVFKDVTFAY-NNKNVIDHFNLHIKAGEKIGIVGRSGAGK 399
Cdd:TIGR01192 297 --TQIFEARAKLEDFFDLEDSVFQREEPADAPELPNVKGAVEFRHITFEFaNSSQGVFDVSFEAKAGQTVAIVGPTGAGK 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 400 STLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANIALVTQDTSLLHRSVAENIKYGRPDATDHDMQSAVHKAKAAEFI 479
Cdd:TIGR01192 375 TTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFI 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 480 pqlvdLKGRSGYEAQVGERGVKLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHR 559
Cdd:TIGR01192 455 -----LKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHR 529
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 746197230 560 LSTIAQMDRLIVLDEGKIAEQGTHEELIAKNGIYAQLWKRqtGGFLIEQKVVQ 612
Cdd:TIGR01192 530 LSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLLRR--SGLLTNQPATK 580
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
171-600 |
7.19e-72 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 241.65 E-value: 7.19e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 171 ITVSIVLGAISPTL-LIplmvwLGLFLLSAWFFIPRLS-----KVSQQQADARAVMTGRVTDAYTNIQTVKLFAHAGRES 244
Cdd:PRK11160 149 LVLTIGLSFFDLTLaLT-----LGGILLLLLLLLPLLFyrlgkKPGQDLTHLRAQYRVQLTEWLQGQAELTLFGAEDRYR 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 245 QYAKASMKEFMTTVYAQMRLGTLFEVSINMLSAVLFVGVigtavwLWtqgLAALGVIAATT--AMIlklnsmAEFMMWHM 322
Cdd:PRK11160 224 QQLEQTEQQWLAAQRRQANLTGLSQALMILANGLTVVLM------LW---LAAGGVGGNAQpgALI------ALFVFAAL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 323 sALFENVGTIQDGMQTLGKKIN--------IQDKPE-----AKPLAVKQGEIVFKDVTFAY--NNKNVIDHFNLHIKAGE 387
Cdd:PRK11160 289 -AAFEALMPVAGAFQHLGQVIAsarrineiTEQKPEvtfptTSTAAADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 388 KIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANIALVTQDTSLLHRSVAENIKYGRPDATDHDMQ 467
Cdd:PRK11160 368 KVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALI 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 468 SAVHKAKAAEFipqlvdLKGRSGYEAQVGERGVKLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDL 547
Cdd:PRK11160 448 EVLQQVGLEKL------LEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEH 521
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 746197230 548 MVDKTVIAIAHRLSTIAQMDRLIVLDEGKIAEQGTHEELIAKNGIYAQLWKRQ 600
Cdd:PRK11160 522 AQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQRL 574
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
359-582 |
7.34e-68 |
|
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: 220.06 E-value: 7.34e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 359 GEIVFKDVTFAYNN--KNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANI 436
Cdd:cd03244 1 GDIEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 437 ALVTQDTSLLHRSVAENIK-YGRpdATDHDMQSAVHKAKAAEFIPQLVDlkgrsGYEAQVGERGVKLSGGQRQRIAIARV 515
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDpFGE--YSDEELWQALERVGLKEFVESLPG-----GLDTVVEEGGENLSVGQRQLLCLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 746197230 516 FLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIAQMDRLIVLDEGKIAEQGT 582
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
359-581 |
9.73e-67 |
|
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: 217.07 E-value: 9.73e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 359 GEIVFKDVTFAYNN--KNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANI 436
Cdd:cd03245 1 GRIEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 437 ALVTQDTSLLHRSVAENIKYGRPDATDHDMQSAVHKAKAAEFIPQLVDlkgrsGYEAQVGERGVKLSGGQRQRIAIARVF 516
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPN-----GLDLQIGERGRGLSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 746197230 517 LKDAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIAQMDRLIVLDEGKIAEQG 581
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
358-577 |
1.14e-64 |
|
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: 211.95 E-value: 1.14e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 358 QGEIVFKDVTFAYNNK---NVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRA 434
Cdd:cd03248 9 KGIVKFQNVTFAYPTRpdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 435 NIALVTQDTSLLHRSVAENIKYGRPDATDHDMQSAVHKAKAAEFIPQLvdlkgRSGYEAQVGERGVKLSGGQRQRIAIAR 514
Cdd:cd03248 89 KVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISEL-----ASGYDTEVGEKGSQLSGGQKQRVAIAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 746197230 515 VFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIAQMDRLIVLDEGKI 577
Cdd:cd03248 164 ALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
22-596 |
3.71e-62 |
|
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: 218.66 E-value: 3.71e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 22 PTRFFPFVWQATEGVRPYLLLLVIctAG-AATFEALL---FSKIgqLVDwlsksqpeSFLSQHASNIL-ILISVLFANIL 96
Cdd:TIGR03796 138 KPSLLRALWRRLRGSRGALLYLLL--AGlLLVLPGLVipaFSQI--FVD--------EILVQGRQDWLrPLLLGMGLTAL 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 97 FvniQSIIKHQILYSTfpMRLRW--------RFHNLLLKQSLDFFHNDFAGRLSAKVmQTALAIREFwiiLGDMLAYVSI 168
Cdd:TIGR03796 206 L---QGVLTWLQLYYL--RRLEIklavgmsaRFLWHILRLPVRFFAQRHAGDIASRV-QLNDQVAEF---LSGQLATTAL 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 169 YFITV--SIVLGAISPTLLIPLMVWLGLFLLSAWFFIPRLSKVSQQQADA-RAVMTGRVTDAYTNIQTVK-------LFA 238
Cdd:TIGR03796 277 DAVMLvfYALLMLLYDPVLTLIGIAFAAINVLALQLVSRRRVDANRRLQQdAGKLTGVAISGLQSIETLKasglesdFFS 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 239 H-AGresQYAKAsmkefmttVYAQMRLGTL---FEVSINMLSAVLFVGVIGTAVWLWTQGLAALGVIAATTAMilklnsM 314
Cdd:TIGR03796 357 RwAG---YQAKL--------LNAQQELGVLtqiLGVLPTLLTSLNSALILVVGGLRVMEGQLTIGMLVAFQSL------M 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 315 AEFMMwHMSALFENVGTIQD---GMQTLGKKINIQDKPEAK----------PLAVKQGEIVFKDVTFAYN--NKNVIDHF 379
Cdd:TIGR03796 420 SSFLE-PVNNLVGFGGTLQElegDLNRLDDVLRNPVDPLLEepegsaatsePPRRLSGYVELRNITFGYSplEPPLIENF 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 380 NLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANIALVTQDTSLLHRSVAENIKYGRP 459
Cdd:TIGR03796 499 SLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDP 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 460 DATDHDMQSAvhkAKAAEFIPQLVDLKGrsGYEAQVGERGVKLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAA 539
Cdd:TIGR03796 579 TIPDADLVRA---CKDAAIHDVITSRPG--GYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKI 653
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 746197230 540 IQSSLNDLMVdkTVIAIAHRLSTIAQMDRLIVLDEGKIAEQGTHEELIAKNGIYAQL 596
Cdd:TIGR03796 654 IDDNLRRRGC--TCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARL 708
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
360-572 |
1.21e-60 |
|
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: 210.61 E-value: 1.21e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 360 EIVFKDVTFAYNNK-NVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANIAL 438
Cdd:TIGR02857 321 SLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 439 VTQDTSLLHRSVAENIKYGRPDATDHDMQSAVHKAKAAEFIPQLvdlkgRSGYEAQVGERGVKLSGGQRQRIAIARVFLK 518
Cdd:TIGR02857 401 VPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAAL-----PQGLDTPIGEGGAGLSGGQAQRLALARAFLR 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 746197230 519 DAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIAQMDRLIVL 572
Cdd:TIGR02857 476 DAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
352-596 |
1.05e-58 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 206.62 E-value: 1.05e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 352 KPLAVKQG-EIVFKD-VTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHF--YhlkEGAILIDGQNIEDV 427
Cdd:PRK11174 340 KELASNDPvTIEAEDlEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFlpY---QGSLKINGIELREL 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 428 TQDSLRANIALVTQDTSLLHRSVAENIKYGRPDATDHDMQSAVHKAKAAEFIPQLVDlkgrsGYEAQVGERGVKLSGGQR 507
Cdd:PRK11174 417 DPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQ-----GLDTPIGDQAAGLSVGQA 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 508 QRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIAQMDRLIVLDEGKIAEQGTHEELI 587
Cdd:PRK11174 492 QRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELS 571
|
....*....
gi 746197230 588 AKNGIYAQL 596
Cdd:PRK11174 572 QAGGLFATL 580
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
171-596 |
1.97e-57 |
|
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: 205.36 E-value: 1.97e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 171 ITVSIVLGAISPTLLIPLMVWLGLFLLSAWFFIPRLSKVSQQQADARAVMTGRVTDAYTNIQTVKlfAHAGRESQYAKAS 250
Cdd:TIGR01193 284 VIVGLFLVRQNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIK--SLTSEAERYSKID 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 251 mKEFMTTVYAQMRLgTLFEVSINMLSAVLfvGVIGTAVWLWTqglAALGVIAA--TTAMILKLNSMAEFMMwhmsALFEN 328
Cdd:TIGR01193 362 -SEFGDYLNKSFKY-QKADQGQQAIKAVT--KLILNVVILWT---GAYLVMRGklTLGQLITFNALLSYFL----TPLEN 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 329 VGTIQDGMQTlGKKINIQ------------DKPEAKPLAVKQGEIVFKDVTFAYN-NKNVIDHFNLHIKAGEKIGIVGRS 395
Cdd:TIGR01193 431 IINLQPKLQA-ARVANNRlnevylvdsefiNKKKRTELNNLNGDIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMS 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 396 GAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANIALVTQDTSLLHRSVAENIKYG-RPDATDHDMQSAVHKAK 474
Cdd:TIGR01193 510 GSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAE 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 475 AAEFIPQLvdlkgRSGYEAQVGERGVKLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMvDKTVI 554
Cdd:TIGR01193 590 IKDDIENM-----PLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQ-DKTII 663
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 746197230 555 AIAHRLSTIAQMDRLIVLDEGKIAEQGTHEELIAKNGIYAQL 596
Cdd:TIGR01193 664 FVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
125-600 |
8.19e-55 |
|
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: 197.87 E-value: 8.19e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 125 LLKQSLDFFHNDFAGRLSAKVMQTAlAIRE--------------FWII-LGDMLAYvSIYFITVSIVLGAIsptlLIPLM 189
Cdd:TIGR03797 219 LLRLPVSFFRQYSTGDLASRAMGIS-QIRRilsgstlttllsgiFALLnLGLMFYY-SWKLALVAVALALV----AIAVT 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 190 VWLGLFllsawffipRLSKVSQQQAdaravMTGRVtdaytNIQTVKLFAH------AGRESQYAKASMKEFMTTVYAQMR 263
Cdd:TIGR03797 293 LVLGLL---------QVRKERRLLE-----LSGKI-----SGLTVQLINGisklrvAGAENRAFARWAKLFSRQRKLELS 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 264 LG------TLFEVSINML-SAVLFvgviGTAVWLWTQGLAALGV-IAATTAMILKLNSMAEFmmwhmsalfenVGTIQDG 335
Cdd:TIGR03797 354 AQrienllTVFNAVLPVLtSAALF----AAAISLLGGAGLSLGSfLAFNTAFGSFSGAVTQL-----------SNTLISI 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 336 MQTL-----GKKInIQDKPE---AKPLAVK-QGEIVFKDVTFAY--NNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQ 404
Cdd:TIGR03797 419 LAVIplwerAKPI-LEALPEvdeAKTDPGKlSGAIEVDRVTFRYrpDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLR 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 405 LLLHFYHLKEGAILIDGQNIEDVTQDSLRANIALVTQDTSLLHRSVAENIKYGRPDATDhDMQSAVHKAKAAEFIPQLvd 484
Cdd:TIGR03797 498 LLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLD-EAWEAARMAGLAEDIRAM-- 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 485 lkgRSGYEAQVGERGVKLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVdkTVIAIAHRLSTIA 564
Cdd:TIGR03797 575 ---PMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKV--TRIVIAHRLSTIR 649
|
490 500 510
....*....|....*....|....*....|....*.
gi 746197230 565 QMDRLIVLDEGKIAEQGTHEELIAKNGIYAQLWKRQ 600
Cdd:TIGR03797 650 NADRIYVLDAGRVVQQGTYDELMAREGLFAQLARRQ 685
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
349-603 |
4.05e-54 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 194.17 E-value: 4.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 349 PEAKPLAvkQGEIVFKDVTFAY-NNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDV 427
Cdd:PRK10790 331 NDDRPLQ--SGRIDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSL 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 428 TQDSLRANIALVTQDTSLLHRSVAENIKYGRpDATDHDMQSAVHKAKAAEFIPQLVDlkgrsGYEAQVGERGVKLSGGQR 507
Cdd:PRK10790 409 SHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPD-----GLYTPLGEQGNNLSVGQK 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 508 QRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIAQMDRLIVLDEGKIAEQGTHEELI 587
Cdd:PRK10790 483 QLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLL 562
|
250
....*....|....*.
gi 746197230 588 AKNGIYAQLWKRQTGG 603
Cdd:PRK10790 563 AAQGRYWQMYQLQLAG 578
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
284-600 |
2.91e-53 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 191.46 E-value: 2.91e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 284 IGTAVWLWTQGLAALGVIAaTTAMILKLnsmaefMMWHMSALFENVGTIQDG-------MQTLGKKINIQDKPEakPLAV 356
Cdd:PRK10789 239 IGGGSWMVVNGSLTLGQLT-SFVMYLGL------MIWPMLALAWMFNIVERGsaaysriRAMLAEAPVVKDGSE--PVPE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 357 KQGEIVFKDVTFAY--NNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRA 434
Cdd:PRK10789 310 GRGELDVNIRQFTYpqTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRS 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 435 NIALVTQDTSLLHRSVAENIKYGRPDATDHDMQSAVHKAKAAEFI---PQlvdlkgrsGYEAQVGERGVKLSGGQRQRIA 511
Cdd:PRK10789 390 RLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDIlrlPQ--------GYDTEVGERGVMLSGGQKQRIS 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 512 IARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIAQMDRLIVLDEGKIAEQGTHEELIAKNG 591
Cdd:PRK10789 462 IARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSG 541
|
....*....
gi 746197230 592 IYAQLWKRQ 600
Cdd:PRK10789 542 WYRDMYRYQ 550
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
116-560 |
4.61e-53 |
|
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: 189.88 E-value: 4.61e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 116 RLRWRFHNLLLKQSLDF---FHN-DFAGRLSAKVMQTA-LAIRefwiILGDMLAYVSIYFITVSiVLGAISPTLLIPLMV 190
Cdd:TIGR02868 87 ALRVRVYERLARQALAGrrrLRRgDLLGRLGADVDALQdLYVR----VIVPAGVALVVGAAAVA-AIAVLSVPAALILAA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 191 WLGLFLLSAWFFIPRLSKVSQQ-QADARAVMTGRVTDAYtniqtvklfahAGRESQYAKASMKEFMTTVY-AQMRLGTLF 268
Cdd:TIGR02868 162 GLLLAGFVAPLVSLRAARAAEQaLARLRGELAAQLTDAL-----------DGAAELVASGALPAALAQVEeADRELTRAE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 269 E--VSINMLSAVLFVGVIGTAVW--LWTQGLAAL-GVIAATTAMILKLNSMAefmmwhmsaLFENVGTIQDGMQTLGK-- 341
Cdd:TIGR02868 231 RraAAATALGAALTLLAAGLAVLgaLWAGGPAVAdGRLAPVTLAVLVLLPLA---------AFEAFAALPAAAQQLTRvr 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 342 ----KIN----------IQDKPEAKPLAVKQGEIVFKDVTFAY-NNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLL 406
Cdd:TIGR02868 302 aaaeRIVevldaagpvaEGSAPAAGAVGLGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATL 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 407 LHFYHLKEGAILIDGQNIEDVTQDSLRANIALVTQDTSLLHRSVAENIKYGRPDATDHDMQSAVHKAKAAEFIPQLVDlk 486
Cdd:TIGR02868 382 AGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPD-- 459
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 746197230 487 grsGYEAQVGERGVKLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRL 560
Cdd:TIGR02868 460 ---GLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
361-581 |
5.89e-48 |
|
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: 165.56 E-value: 5.89e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAY--NNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVtQDSLRANIAL 438
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 439 VTQDTSLLHRSVAENIkygrpdatdhdmqsavhkakaaefipqlvdlkgrsgyeaqvgerGVKLSGGQRQRIAIARVFLK 518
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------------GRRFSGGERQRLALARILLQ 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 746197230 519 DAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIAQMDRLIVLDEGKIAEQG 581
Cdd:cd03247 116 DAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
357-582 |
6.04e-47 |
|
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: 164.12 E-value: 6.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 357 KQGEIVFKDVTFAY--NNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRA 434
Cdd:cd03369 3 EHGEIEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 435 NIALVTQDTSLLHRSVAENIkygrpDATDHDMQSAVHKAkaaefipqlvdLKgrsgyeaqVGERGVKLSGGQRQRIAIAR 514
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNL-----DPFDEYSDEEIYGA-----------LR--------VSEGGLNLSQGQRQLLCLAR 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 746197230 515 VFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIAQMDRLIVLDEGKIAEQGT 582
Cdd:cd03369 139 ALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
361-589 |
1.04e-44 |
|
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: 158.65 E-value: 1.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNN-KNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANIALV 439
Cdd:COG1122 1 IELENLSFSYPGgTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 440 TQ--DTSLLHRSVAENIKYG-----RPDAtdhDMQSAVHKAkAAEFipQLVDLKGRSGYEaqvgergvkLSGGQRQRIAI 512
Cdd:COG1122 81 FQnpDDQLFAPTVEEDVAFGpenlgLPRE---EIRERVEEA-LELV--GLEHLADRPPHE---------LSGGQKQRVAI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 513 ARVFLKDAPILILDEATSALD----SEVEAAIQsSLNDLmvDKTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEELI 587
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDprgrRELLELLK-RLNKE--GKTVIIVTHDLDLVAELaDRVIVLDDGRIVADGTPREVF 222
|
..
gi 746197230 588 AK 589
Cdd:COG1122 223 SD 224
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
349-589 |
2.21e-44 |
|
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: 166.46 E-value: 2.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 349 PEAKPLAVKQGEIVFKDVTFAYNNKN--VIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIED 426
Cdd:COG4618 319 PERMPLPRPKGRLSVENLTVVPPGSKrpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQ 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 427 VTQDSLRANIALVTQDTSLLHRSVAENIkyGR-PDATDHDMQSAVHKAKAAEFIPQLVDlkgrsGYEAQVGERGVKLSGG 505
Cdd:COG4618 399 WDREELGRHIGYLPQDVELFDGTIAENI--ARfGDADPEKVVAAAKLAGVHEMILRLPD-----GYDTRIGEGGARLSGG 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 506 QRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDK-TVIAIAHRLSTIAQMDRLIVLDEGKIAEQGTHE 584
Cdd:COG4618 472 QRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGaTVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRD 551
|
....*
gi 746197230 585 ELIAK 589
Cdd:COG4618 552 EVLAR 556
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
361-588 |
2.47e-43 |
|
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: 162.77 E-value: 2.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKN-----VIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRA- 434
Cdd:COG1123 261 LEVRNLSKRYPVRGkggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREl 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 435 --NIALVTQD--TSLLHR-SVAENIkyGRPDATDHDMQSAVHKAKAAEFIpQLVDL----KGRSGYEaqvgergvkLSGG 505
Cdd:COG1123 341 rrRVQMVFQDpySSLNPRmTVGDII--AEPLRLHGLLSRAERRERVAELL-ERVGLppdlADRYPHE---------LSGG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 506 QRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDL--MVDKTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGT 582
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLqrELGLTYLFISHDLAVVRYIaDRVAVMYDGRIVEDGP 488
|
....*.
gi 746197230 583 HEELIA 588
Cdd:COG1123 489 TEEVFA 494
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
361-577 |
3.07e-43 |
|
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: 152.76 E-value: 3.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAY--NNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANIAL 438
Cdd:cd03246 1 LEVENVSFRYpgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 439 VTQDTSLLHRSVAENIkygrpdatdhdmqsavhkakaaefipqlvdlkgrsgyeaqvgergvkLSGGQRQRIAIARVFLK 518
Cdd:cd03246 81 LPQDDELFSGSIAENI-----------------------------------------------LSGGQRQRLGLARALYG 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 519 DAPILILDEATSALDSEVEAAIQSSLNDL-MVDKTVIAIAHRLSTIAQMDRLIVLDEGKI 577
Cdd:cd03246 114 NPRILVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
349-598 |
6.74e-43 |
|
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: 166.27 E-value: 6.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 349 PEAKPlavKQGEIVFKDVTFAYNN--KNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIED 426
Cdd:TIGR00957 1276 PSGWP---PRGRVEFRNYCLRYREdlDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAK 1352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 427 VTQDSLRANIALVTQDTSLLHRSVAENIK-YGRpdATDHDMQSAVHKAKAAEFIPQLVDlkgrsGYEAQVGERGVKLSGG 505
Cdd:TIGR00957 1353 IGLHDLRFKITIIPQDPVLFSGSLRMNLDpFSQ--YSDEEVWWALELAHLKTFVSALPD-----KLDHECAEGGENLSVG 1425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 506 QRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIAQMDRLIVLDEGKIAEQGTHEE 585
Cdd:TIGR00957 1426 QRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSN 1505
|
250
....*....|...
gi 746197230 586 LIAKNGIYAQLWK 598
Cdd:TIGR00957 1506 LLQQRGIFYSMAK 1518
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
358-598 |
7.03e-43 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 165.97 E-value: 7.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 358 QGEIVFKDVTFAYNNK-NVIDHFNLHIKAGEK--IGIVGRSGAGKSTLIQLLLHFYHLK--------------------- 413
Cdd:PTZ00265 1163 KGKIEIMDVNFRYISRpNVPIYKDLTFSCDSKktTAIVGETGSGKSTVMSLLMRFYDLKndhhivfknehtndmtneqdy 1242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 414 ---------------------------------EGAILIDGQNIEDVTQDSLRANIALVTQDTSLLHRSVAENIKYGRPD 460
Cdd:PTZ00265 1243 qgdeeqnvgmknvnefsltkeggsgedstvfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKED 1322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 461 ATDHDMQSAVHKAKAAEFIPQLVDlkgrsGYEAQVGERGVKLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAI 540
Cdd:PTZ00265 1323 ATREDVKRACKFAAIDEFIESLPN-----KYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1397
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 746197230 541 QSSLNDL--MVDKTVIAIAHRLSTIAQMDRLIVLDEGK-----IAEQGTHEELI-AKNGIYAQLWK 598
Cdd:PTZ00265 1398 EKTIVDIkdKADKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEELLsVQDGVYKKYVK 1463
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
361-589 |
1.11e-42 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 153.30 E-value: 1.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGqniEDVTQDS--LRANIAL 438
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLG---EDVARDPaeVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 439 VTQDTSL-LHRSVAENIKYGrpdATDHDMQSAVHKAKAAEFIpQLVDLKGRSGyeAQVGergvKLSGGQRQRIAIARVFL 517
Cdd:COG1131 78 VPQEPALyPDLTVRENLRFF---ARLYGLPRKEARERIDELL-ELFGLTDAAD--RKVG----TLSGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 746197230 518 KDAPILILDEATSALDSEVEAAIQSSLNDLMVD-KTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEELIAK 589
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERLcDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
361-589 |
1.52e-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: 150.04 E-value: 1.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVT--FAYNNKNV--IDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRA-- 434
Cdd:cd03258 2 IELKNVSkvFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 435 -NIALVTQDTSLL-HRSVAENIKYgrPDATDHdMQSAVHKAKAAEFIpQLVDLKGRSG-YEAQvgergvkLSGGQRQRIA 511
Cdd:cd03258 82 rRIGMIFQHFNLLsSRTVFENVAL--PLEIAG-VPKAEIEERVLELL-ELVGLEDKADaYPAQ-------LSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 512 IARVFLKDAPILILDEATSALDSEVEAAIQSSLNDL--MVDKTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEELIA 588
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDInrELGLTIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVEEVFA 230
|
.
gi 746197230 589 K 589
Cdd:cd03258 231 N 231
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
361-587 |
2.35e-41 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 150.19 E-value: 2.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANIALVT 440
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 441 QDTSLLHR-SVAENIKYGR---------PDATDHDmqsAVHKA-KAAEfipqLVDLKGRSgyeaqVGErgvkLSGGQRQR 509
Cdd:COG1120 82 QEPPAPFGlTVRELVALGRyphlglfgrPSAEDRE---AVEEAlERTG----LEHLADRP-----VDE----LSGGERQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 510 IAIARVFLKDAPILILDEATSALD----SEVEAAIQsSLNDLMvDKTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHE 584
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDlahqLEVLELLR-RLARER-GRTVVMVLHDLNLAARYaDRLVLLKDGRIVAQGPPE 223
|
...
gi 746197230 585 ELI 587
Cdd:COG1120 224 EVL 226
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
363-581 |
7.20e-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: 145.34 E-value: 7.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 363 FKDVTFAYNNKN----VIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSL---RAN 435
Cdd:cd03257 4 VKNLSVSFPTGGgsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 436 IALVTQD--TSL--LHR---SVAENIKYgrpdatdHDMQSAvhKAKAAEFIPQLvdLKGRSGYEAQVGERGVKLSGGQRQ 508
Cdd:cd03257 84 IQMVFQDpmSSLnpRMTigeQIAEPLRI-------HGKLSK--KEARKEAVLLL--LVGVGLPEEVLNRYPHELSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 746197230 509 RIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDL--MVDKTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQG 581
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLqeELGLTLLFITHDLGVVAKIaDRVAVMYAGKIVEEG 228
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
361-577 |
2.08e-39 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 143.42 E-value: 2.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANIALVT 440
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 441 QDTSLLHRSVAENIKYgrPDATDHDmqsAVHKAKAAEFIPQLvdlkGRSGY--EAQVGErgvkLSGGQRQRIAIARVFLK 518
Cdd:COG4619 81 QEPALWGGTVRDNLPF--PFQLRER---KFDRERALELLERL----GLPPDilDKPVER----LSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 746197230 519 DAPILILDEATSALDSEVEAAIQSSLNDLMVDK--TVIAIAHRLSTIAQM-DRLIVLDEGKI 577
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYLAEEgrAVLWVSHDPEQIERVaDRVLTLEAGRL 209
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
361-576 |
2.39e-39 |
|
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: 142.99 E-value: 2.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHF-----NLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGqniedvtqdslraN 435
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFtlkdiNLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 436 IALVTQDTSLLHRSVAENIKYGRPdaTDHDMQSAVHKAKAAEfiPQLVDLKGrsGYEAQVGERGVKLSGGQRQRIAIARV 515
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKP--FDEERYEKVIKACALE--PDLEILPD--GDLTEIGEKGINLSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 746197230 516 FLKDAPILILDEATSALDSEVEAAI--QSSLNDLMVDKTVIAIAHRLSTIAQMDRLIVLDEGK 576
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVGRHIfeNCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
362-576 |
4.46e-39 |
|
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: 142.61 E-value: 4.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 362 VFKDVTFAYNNKN--VIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANIALV 439
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 440 TQ--DTSLLHRSVAENIKYGRPDA--TDHDMQSAVHKAkAAEFipQLVDLKGRSGYEaqvgergvkLSGGQRQRIAIARV 515
Cdd:cd03225 81 FQnpDDQFFGPTVEEEVAFGLENLglPEEEIEERVEEA-LELV--GLEGLRDRSPFT---------LSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 746197230 516 FLKDAPILILDEATSALDSEVEAAIQSSLNDLMVD-KTVIAIAHRLSTIAQ-MDRLIVLDEGK 576
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEgKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
366-588 |
4.93e-39 |
|
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: 143.79 E-value: 4.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 366 VTF--AYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANIALVTQD- 442
Cdd:COG1124 9 VSYgqGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 443 -TSL-----LHRSVAENIK-YGRPDatdhdmqsavHKAKAAEFIpQLVDLKG--RSGYEAQvgergvkLSGGQRQRIAIA 513
Cdd:COG1124 89 yASLhprhtVDRILAEPLRiHGLPD----------REERIAELL-EQVGLPPsfLDRYPHQ-------LSGGQRQRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 746197230 514 RVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDK--TVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEELIA 588
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHLcDRVAVMQNGRIVEELTVADLLA 228
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
343-589 |
4.96e-39 |
|
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: 150.96 E-value: 4.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 343 INIQDKPEAKPLAVKQGEIVFKDVTFAY--NNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILID 420
Cdd:TIGR01842 299 ANYPSRDPAMPLPEPEGHLSVENVTIVPpgGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLD 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 421 GQNIEDVTQDSLRANIALVTQDTSLLHRSVAENIKYGRPDATDHDMQSAVHKAKAAEFIPQLVDlkgrsGYEAQVGERGV 500
Cdd:TIGR01842 379 GADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPD-----GYDTVIGPGGA 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 501 KLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDK-TVIAIAHRLSTIAQMDRLIVLDEGKIAE 579
Cdd:TIGR01842 454 TLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGiTVVVITHRPSLLGCVDKILVLQDGRIAR 533
|
250
....*....|
gi 746197230 580 QGTHEELIAK 589
Cdd:TIGR01842 534 FGERDEVLAK 543
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
361-590 |
8.21e-39 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 142.92 E-value: 8.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVtqdslRANIALVT 440
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 441 QDTSLLHR---SVAENIKYG---------RPDATDHDmqsAVHKA-KAAEfipqLVDLKGRsgyeaQVGErgvkLSGGQR 507
Cdd:COG1121 82 QRAEVDWDfpiTVRDVVLMGrygrrglfrRPSRADRE---AVDEAlERVG----LEDLADR-----PIGE----LSGGQQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 508 QRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDL-MVDKTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEE 585
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREYfDRVLLLNRGLVAHGPPEEV 225
|
....*
gi 746197230 586 LIAKN 590
Cdd:COG1121 226 LTPEN 230
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
376-530 |
1.26e-38 |
|
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: 139.32 E-value: 1.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 376 IDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANIALVTQDTSLL-HRSVAENI 454
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 746197230 455 KYGrpdATDHDMQSAVHKAKAAEFIPQL--VDLKGRSgyeaqVGERGVKLSGGQRQRIAIARVFLKDAPILILDEATS 530
Cdd:pfam00005 81 RLG---LLLKGLSKREKDARAEEALEKLglGDLADRP-----VGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
361-591 |
1.48e-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: 1.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTqDSLRANIALVT 440
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 441 QDTSL-LHRSVAENIKYgrpDATDHDMQSAVHKAKAAEFIPQL---VDLKGRSGyeaqvgergvKLSGGQRQRIAIARVF 516
Cdd:COG4555 81 DERGLyDRLTVRENIRY---FAELYGLFDEELKKRIEELIELLgleEFLDRRVG----------ELSTGMKKKVALARAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 746197230 517 LKDAPILILDEATSALDseVEA--AIQSSLNDLM-VDKTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEELIAKNG 591
Cdd:COG4555 148 VHDPKVLLLDEPTNGLD--VMArrLLREILRALKkEGKTVLFSSHIMQEVEALcDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
359-596 |
4.29e-38 |
|
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: 141.58 E-value: 4.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 359 GEIVFKDVTFAYNN--KNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANI 436
Cdd:cd03288 18 GEIKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 437 ALVTQDTSLLHRSVAENIKYGRpDATDHDMQSAVHKAKAAEFIPQLvdlkgRSGYEAQVGERGVKLSGGQRQRIAIARVF 516
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSL-----PGGLDAVVTEGGENFSVGQRQLFCLARAF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 517 LKDAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIAQMDRLIVLDEGKIAEQGTHEELIA-KNGIYAQ 595
Cdd:cd03288 172 VRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAqEDGVFAS 251
|
.
gi 746197230 596 L 596
Cdd:cd03288 252 L 252
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
40-591 |
7.99e-38 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 150.51 E-value: 7.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 40 LLLLVICTAgaaTFEALLFSKIGQLVDWLSKSQPESFLSQHASNILILISVLFANILFVNIQSIIKHQILYSTfpmRLRW 119
Cdd:PLN03232 914 VMILLVCYL---TTEVLRVSSSTWLSIWTDQSTPKSYSPGFYIVVYALLGFGQVAVTFTNSFWLISSSLHAAK---RLHD 987
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 120 RFHNLLLKQSLDFFHNDFAGRLSAKVMQTALAIREFWIILGDMLAYVSIYFITVSIVLGAISPTLLIPLMVWLGLFLLSA 199
Cdd:PLN03232 988 AMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAY 1067
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 200 WFFIPRLSKVSQQQADARAVMTGRVTDAYTNIQTVKLFAHAGRESQYAKASMKEfmttvyaQMRLgTLFEVSINMLSAVL 279
Cdd:PLN03232 1068 LYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDN-------NIRF-TLANTSSNRWLTIR 1139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 280 FVGVIGTAVWLwTQGLAALG--------VIAATTAMILKLNSMAEFMMwhmSALFENVGTIQDGMQTLGKKINIQDKPEA 351
Cdd:PLN03232 1140 LETLGGVMIWL-TATFAVLRngnaenqaGFASTMGLLLSYTLNITTLL---SGVLRQASKAENSLNSVERVGNYIDLPSE 1215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 352 KPLAVKQ----------GEIVFKDVTFAYNNK--NVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILI 419
Cdd:PLN03232 1216 ATAIIENnrpvsgwpsrGSIKFEDVHLRYRPGlpPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMI 1295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 420 DGQNIEDVTQDSLRANIALVTQDTSLLHRSVAENIKygrP--DATDHDMQSAVHKAkaaefipQLVDLKGRS--GYEAQV 495
Cdd:PLN03232 1296 DDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNID---PfsEHNDADLWEALERA-------HIKDVIDRNpfGLDAEV 1365
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 496 GERGVKLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIAQMDRLIVLDEG 575
Cdd:PLN03232 1366 SEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSG 1445
|
570
....*....|....*.
gi 746197230 576 KIAEQGTHEELIAKNG 591
Cdd:PLN03232 1446 QVLEYDSPQELLSRDT 1461
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
361-580 |
9.06e-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: 139.53 E-value: 9.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKN----VIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDslranI 436
Cdd:cd03293 1 LEVRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 437 ALVTQDTSLL-HRSVAENIKYGrPDATDHDMQSAvhKAKAAEFIpQLVDLKGRSG-YEAQvgergvkLSGGQRQRIAIAR 514
Cdd:cd03293 76 GYVFQQDALLpWLTVLDNVALG-LELQGVPKAEA--RERAEELL-ELVGLSGFENaYPHQ-------LSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 746197230 515 VFLKDAPILILDEATSALDseveAAIQSSLNDLMVD------KTVIAIAHRLSTIAQM-DRLIVLDE--GKIAEQ 580
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALD----ALTREQLQEELLDiwretgKTVLLVTHDIDEAVFLaDRVVVLSArpGRIVAE 215
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
361-589 |
1.46e-37 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 142.52 E-value: 1.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDV--TFAYNNKNVI--DHFNLHIKAGEKIGIVGRSGAGKSTLIQL--LLhfyhlkE----GAILIDGQNIEDVTQD 430
Cdd:COG1135 2 IELENLskTFPTKGGPVTalDDVSLTIEKGEIFGIIGYSGAGKSTLIRCinLL------ErptsGSVLVDGVDLTALSER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 431 SLRA---NIALVTQDTSLLH-RSVAENI-------KYGRPDAtdhdmqsavhKAKAAEFIpQLVDLKGRSG-YEAQvger 498
Cdd:COG1135 76 ELRAarrKIGMIFQHFNLLSsRTVAENValpleiaGVPKAEI----------RKRVAELL-ELVGLSDKADaYPSQ---- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 499 gvkLSGGQRQRIAIARVfLKDAP-ILILDEATSALDSEVEAAIQSSLNDLmVDK---TVIAIAHRLSTIAQM-DRLIVLD 573
Cdd:COG1135 141 ---LSGGQKQRVGIARA-LANNPkVLLCDEATSALDPETTRSILDLLKDI-NRElglTIVLITHEMDVVRRIcDRVAVLE 215
|
250
....*....|....*.
gi 746197230 574 EGKIAEQGTHEELIAK 589
Cdd:COG1135 216 NGRIVEQGPVLDVFAN 231
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
361-581 |
2.31e-37 |
|
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: 138.04 E-value: 2.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDslRANIALVT 440
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 441 QDTSLL-HRSVAENIKYGrpdATDHDMQSAVHKAKAAEFIpQLVDLkgrsgyEAQVGERGVKLSGGQRQRIAIARVFLKD 519
Cdd:cd03259 79 QDYALFpHLTVAENIAFG---LKLRGVPKAEIRARVRELL-ELVGL------EGLLNRYPHELSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 746197230 520 APILILDEATSALDSEVEAAIQSSLNDLM--VDKTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQG 581
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKELQreLGITTIYVTHDQEEALALaDRIAVMNEGRIVQVG 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
363-576 |
4.13e-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: 135.45 E-value: 4.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 363 FKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANIALVTQd 442
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 443 tsllhrsvaenikygrpdatdhdmqsavhkakaaefipqlvdlkgrsgyeaqvgergvkLSGGQRQRIAIARVFLKDAPI 522
Cdd:cd00267 81 -----------------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 746197230 523 LILDEATSALDSEVEAAIQSSLNDLMVD-KTVIAIAHRLSTIAQ-MDRLIVLDEGK 576
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
361-576 |
8.17e-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: 135.39 E-value: 8.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDS--LRANIAL 438
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 439 VTQDTSLL-HRSVAENIKYGrpdatdhdmqsavhkakaaefipqlvdlkgrsgyeaqvgergvkLSGGQRQRIAIARVFL 517
Cdd:cd03229 81 VFQDFALFpHLTVLENIALG--------------------------------------------LSGGQQQRVALARALA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 746197230 518 KDAPILILDEATSALDSEVEAAIQSSLNDL--MVDKTVIAIAHRLSTIAQM-DRLIVLDEGK 576
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
361-586 |
1.06e-36 |
|
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: 136.54 E-value: 1.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLK-----EGAILIDGQNIEDVTQD--SLR 433
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYDLDVDvlELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 434 ANIALVTQDTSLLHRSVAENIKYGrpdATDHDMQSAVHKAKAAEFIPQLVDLKGRsgyeaqVGER--GVKLSGGQRQRIA 511
Cdd:cd03260 81 RRVGMVFQKPNPFPGSIYDNVAYG---LRLHGIKLKEELDERVEEALRKAALWDE------VKDRlhALGLSGGQQQRLC 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 746197230 512 IARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEEL 586
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
361-590 |
1.17e-36 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 136.81 E-value: 1.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVidHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDvTQDSLRAnIALVT 440
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA-LPPAERP-VSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 441 QDTSLL-HRSVAENIKYG-----RPDATDhdmQSAVHKAkAAEFipQLVDLKGRsgYEAQvgergvkLSGGQRQRIAIAR 514
Cdd:COG3840 78 QENNLFpHLTVAQNIGLGlrpglKLTAEQ---RAQVEQA-LERV--GLAGLLDR--LPGQ-------LSGGQRQRVALAR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 515 VFLKDAPILILDEATSALDseveAAIQSSLNDLmVDK-------TVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEEL 586
Cdd:COG3840 143 CLVRKRPILLLDEPFSALD----PALRQEMLDL-VDElcrerglTVLMVTHDPEDAARIaDRVLLVADGRIAADGPTAAL 217
|
....
gi 746197230 587 IAKN 590
Cdd:COG3840 218 LDGE 221
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
361-588 |
1.83e-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: 136.66 E-value: 1.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNN-KNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANIALV 439
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 440 TQDTSLL-HRSVAENI-------KYGRPDAtdhdmqsavhKAKAAEFIpQLVDLKgrsgyEAQVGER-GVKLSGGQRQRI 510
Cdd:cd03295 81 IQQIGLFpHMTVEENIalvpkllKWPKEKI----------RERADELL-ALVGLD-----PAEFADRyPHELSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 511 AIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDL--MVDKTVIAIAHRL-STIAQMDRLIVLDEGKIAEQGTHEELI 587
Cdd:cd03295 145 GVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLqqELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
.
gi 746197230 588 A 588
Cdd:cd03295 225 R 225
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
297-591 |
3.33e-36 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 145.65 E-value: 3.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 297 ALGVIAATTAmILKLNSMAEFmmwHMSALfENVGTIQDGMQTLGKKINIQDKPEAKPLAvkqGEIVFKDVTFAY--NNKN 374
Cdd:PLN03130 1182 ALNITSLLTA-VLRLASLAEN---SLNAV-ERVGTYIDLPSEAPLVIENNRPPPGWPSS---GSIKFEDVVLRYrpELPP 1253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 375 VIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANIALVTQDTSLLHRSVAENI 454
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL 1333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 455 KygrP--DATDHDMQSAVHKAKAAEFIPqlvdlKGRSGYEAQVGERGVKLSGGQRQRIAIARVFLKDAPILILDEATSAL 532
Cdd:PLN03130 1334 D---PfnEHNDADLWESLERAHLKDVIR-----RNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAV 1405
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 746197230 533 DSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIAQMDRLIVLDEGKIAEQGTHEELIAKNG 591
Cdd:PLN03130 1406 DVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
361-579 |
4.13e-36 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 134.79 E-value: 4.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKN-VIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDS---LRANI 436
Cdd:COG2884 2 IRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 437 ALVTQDTSLL-HRSVAENIKY-----GRPDAtdhDMQSAVHKAKAaefipqLVDLKGRsgYEAQVGErgvkLSGGQRQRI 510
Cdd:COG2884 82 GVVFQDFRLLpDRTVYENVALplrvtGKSRK---EIRRRVREVLD------LVGLSDK--AKALPHE----LSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 746197230 511 AIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDL-MVDKTVIaIA-HRLSTIAQMD-RLIVLDEGKIAE 579
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPETSWEIMELLEEInRRGTTVL-IAtHDLELVDRMPkRVLELEDGRLVR 217
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
361-579 |
4.64e-36 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 135.99 E-value: 4.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKN----VIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDslranI 436
Cdd:COG1116 8 LELRGVSKRFPTGGggvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 437 ALVTQDTSLL-HRSVAENIKYGRPDAtdhDMQSAVHKAKAAEFIpQLVDLKGRSG-YEAQvgergvkLSGGQRQRIAIAR 514
Cdd:COG1116 83 GVVFQEPALLpWLTVLDNVALGLELR---GVPKAERRERARELL-ELVGLAGFEDaYPHQ-------LSGGMRQRVAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 746197230 515 VFLKDAPILILDEATSALDseveAAIQSSLNDLMVD------KTVIAIAH------RLStiaqmDRLIVLDE--GKIAE 579
Cdd:COG1116 152 ALANDPEVLLMDEPFGALD----ALTRERLQDELLRlwqetgKTVLFVTHdvdeavFLA-----DRVVVLSArpGRIVE 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
361-588 |
7.47e-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: 141.19 E-value: 7.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNN--KNVIDHFNLHIKAGEKIGIVGRSGAGKSTL----IQLLLHFYHLkEGAILIDGQNIEDVTQDSLRA 434
Cdd:COG1123 5 LEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLalalMGLLPHGGRI-SGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 435 NIALVTQD--TSLLHRSVAENIKYGrpdATDHDMQSAVHKAKAAEfIPQLVDLKGRSG-YEAQvgergvkLSGGQRQRIA 511
Cdd:COG1123 84 RIGMVFQDpmTQLNPVTVGDQIAEA---LENLGLSRAEARARVLE-LLEAVGLERRLDrYPHQ-------LSGGQRQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 512 IARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVD--KTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEELIA 588
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErgTTVLLITHDLGVVAEIaDRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
361-577 |
1.17e-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: 133.38 E-value: 1.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKN----VIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIE---DVTQDSLR 433
Cdd:cd03255 1 IELKNLSKTYGGGGekvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISklsEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 434 A-NIALVTQDTSLL-HRSVAENIKY-----GRPdatdhdmqSAVHKAKAAEFIpQLVDLKGRSGYEAQvgergvKLSGGQ 506
Cdd:cd03255 81 RrHIGFVFQSFNLLpDLTALENVELplllaGVP--------KKERRERAEELL-ERVGLGDRLNHYPS------ELSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 746197230 507 RQRIAIARVFLKDAPILILDEATSALDSEVEAAIQS---SLNDLMvDKTVIAIAHRLSTIAQMDRLIVLDEGKI 577
Cdd:cd03255 146 QQRVAIARALANDPKIILADEPTGNLDSETGKEVMEllrELNKEA-GTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
364-581 |
7.50e-35 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 129.86 E-value: 7.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 364 KDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANIALVTQdt 443
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 444 sllhrsvaenikygrpdatdhdmqsAVHKAKAAEFIPQLVDlkgrsgyeaqvgergvKLSGGQRQRIAIARVFLKDAPIL 523
Cdd:cd03214 81 -------------------------ALELLGLAHLADRPFN----------------ELSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 746197230 524 ILDEATSALDSEVEAAIQSSLNDL--MVDKTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQG 581
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRLarERGKTVVMVLHDLNLAARYaDRVILLKDGRIVAQG 180
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
361-588 |
8.97e-35 |
|
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: 131.47 E-value: 8.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQD---SLRANIA 437
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 438 LVTQD----TSLlhrSVAENIKYgrPDATDHDMQSAVHKAKAAEFIpQLVDLKGR-SGYEAQvgergvkLSGGQRQRIAI 512
Cdd:cd03261 81 MLFQSgalfDSL---TVFENVAF--PLREHTRLSEEEIREIVLEKL-EAVGLRGAeDLYPAE-------LSGGMKKRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 746197230 513 ARVFLKDAPILILDEATSALDSEVEAAIQSSLNDL--MVDKTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEELIA 588
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTPEELRA 226
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
361-586 |
2.19e-34 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 133.68 E-value: 2.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDV-TQDslRaNIALV 439
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLpPEK--R-NVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 440 TQDTSLL-HRSVAENIKYG-RpdatDHDMQSAVHKAKAAEFIpQLVDLKGrsgyeaqVGERGVK-LSGGQRQRIAIARVF 516
Cdd:COG3842 83 FQDYALFpHLTVAENVAFGlR----MRGVPKAEIRARVAELL-ELVGLEG-------LADRYPHqLSGGQQQRVALARAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 746197230 517 LKDAPILILDEATSALDSEVEAAIQSSLNDLM--VDKTVIAIAHRLS---TIAqmDRLIVLDEGKIAEQGTHEEL 586
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLREEMREELRRLQreLGITFIYVTHDQEealALA--DRIAVMNDGRIEQVGTPEEI 223
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
363-578 |
7.09e-34 |
|
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: 128.42 E-value: 7.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 363 FKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVtqdslRANIALVTQD 442
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 443 TSLLHR---SVAENIKYGR-PDATDHDMQSAVHKAKAAEfipqLVDLKGRSGY-EAQVGErgvkLSGGQRQRIAIARVFL 517
Cdd:cd03235 77 RSIDRDfpiSVRDVVLMGLyGHKGLFRRLSKADKAKVDE----ALERVGLSELaDRQIGE----LSGGQQQRVLLARALV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 746197230 518 KDAPILILDEATSALDSEVEAAIQSSLNDL-MVDKTVIAIAHRLSTI-AQMDRLIVLDEGKIA 578
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVlEYFDRVLLLNRTVVA 211
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
361-588 |
7.24e-34 |
|
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: 129.33 E-value: 7.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQD---SLRANIA 437
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyELRRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 438 LVTQD----TSLlhrSVAENIKYG-RpdatdhdmqsaVHKAKAAEFIPQLVDLKgrsgyEAQVGERGVK------LSGGQ 506
Cdd:COG1127 86 MLFQGgalfDSL---TVFENVAFPlR-----------EHTDLSEAEIRELVLEK-----LELVGLPGAAdkmpseLSGGM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 507 RQRIAIARVFLKDAPILILDEATSALD---SEVeaaiqssLNDLMVD------KTVIAIAHRLSTIAQM-DRLIVLDEGK 576
Cdd:COG1127 147 RKRVALARALALDPEILLYDEPTAGLDpitSAV-------IDELIRElrdelgLTSVVVTHDLDSAFAIaDRVAVLADGK 219
|
250
....*....|..
gi 746197230 577 IAEQGTHEELIA 588
Cdd:COG1127 220 IIAEGTPEELLA 231
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
67-587 |
1.30e-33 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 137.60 E-value: 1.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 67 WLSKSQPESFLSQHASNILILISVLFANILFVNIQSIIkhqilySTFPMRLRWR-FHNLLLKQ----SLDFFH------- 134
Cdd:PTZ00243 984 WLSMWSTRSFKLSAATYLYVYLGIVLLGTFSVPLRFFL------SYEAMRRGSRnMHRDLLRSvsrgTMSFFDttplgri 1057
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 135 -NDFA---GRLSAKVMQTALAIREFwiiLGDMLAYVSIYFITVSIVLGAISPTLLI--PLMVwlglFLLSAWFFIPRLSK 208
Cdd:PTZ00243 1058 lNRFSrdiDILDNTLPMSYLYLLQC---LFSICSSILVTSASQPFVLVALVPCGYLyyRLMQ----FYNSANREIRRIKS 1130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 209 VsqqqadARAVMTGRVTDAYTNIQTVklfahagreSQYAKAS--MKE---FMTTVY--------AQMRLGTLFE-VSINM 274
Cdd:PTZ00243 1131 V------AKSPVFTLLEEALQGSATI---------TAYGKAHlvMQEalrRLDVVYscsylenvANRWLGVRVEfLSNIV 1195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 275 LSAVLFVGVIGTAVWLWTQ--GLAALGVIAA--TTAMI-----------LKLNSMAEFMMW-------HMSALFENVGTI 332
Cdd:PTZ00243 1196 VTVIALIGVIGTMLRATSQeiGLVSLSLTMAmqTTATLnwlvrqvatveADMNSVERLLYYtdevpheDMPELDEEVDAL 1275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 333 --QDGMQ---TLGKKINIQDKPEAKPLAVKQGEIVFKDVTFAYNN--KNVIDHFNLHIKAGEKIGIVGRSGAGKSTLiql 405
Cdd:PTZ00243 1276 erRTGMAadvTGTVVIEPASPTSAAPHPVQAGSLVFEGVQMRYREglPLVLRGVSFRIAPREKVGIVGRTGSGKSTL--- 1352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 406 LLHFYHLKE---GAILIDGQNIEDVTQDSLRANIALVTQDTSLLHRSVAENIkygrpdatDHDMQSAVHKAKAAEfipQL 482
Cdd:PTZ00243 1353 LLTFMRMVEvcgGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV--------DPFLEASSAEVWAAL---EL 1421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 483 VDLKGR-----SGYEAQVGERGVKLSGGQRQRIAIARVFLKDAPILIL-DEATSALDSEVEAAIQSSLNDLMVDKTVIAI 556
Cdd:PTZ00243 1422 VGLRERvasesEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITI 1501
|
570 580 590
....*....|....*....|....*....|.
gi 746197230 557 AHRLSTIAQMDRLIVLDEGKIAEQGTHEELI 587
Cdd:PTZ00243 1502 AHRLHTVAQYDKIIVMDHGAVAEMGSPRELV 1532
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
361-577 |
1.87e-33 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 125.59 E-value: 1.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDvTQDSLRANIALVT 440
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 441 QDTSLLHR-SVAENIKYgrpdatdhdmqsavhkakaaefipqlvdlkgrsgyeaqvgergvklSGGQRQRIAIARVFLKD 519
Cdd:cd03230 80 EEPSLYENlTVRENLKL----------------------------------------------SGGMKQRLALAQALLHD 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 520 APILILDEATSALDSEVEAAIQSSLNDLMVD-KTVIAIAHRLSTIAQM-DRLIVLDEGKI 577
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRELKKEgKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
361-580 |
1.37e-32 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 125.16 E-value: 1.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKN----VIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLL--LhfyhLK--EGAILIDGQNIEDVTQDSL 432
Cdd:COG1136 5 LELRNLTKSYGTGEgevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILggL----DRptSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 433 ----RANIALVTQDTSLL-HRSVAENIKY-----GRPDATDhdmqsavhKAKAAEFIpQLVDLKGRSGYEAQvgergvKL 502
Cdd:COG1136 81 arlrRRHIGFVFQFFNLLpELTALENVALplllaGVSRKER--------RERARELL-ERVGLGDRLDHRPS------QL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 503 SGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVD--KTVIAIAHRLSTIAQMDRLIVLDEGKIAEQ 580
Cdd:COG1136 146 SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElgTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
357-586 |
1.69e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 126.26 E-value: 1.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 357 KQGEIVFKDVTFAYNN--KNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRA 434
Cdd:PRK13632 4 KSVMIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 435 NIALVTQ--DTSLLHRSVAENIKYGRPDA--TDHDMQSAVhkakaaEFIPQLVDLKGRSGYEAQvgergvKLSGGQRQRI 510
Cdd:PRK13632 84 KIGIIFQnpDNQFIGATVEDDIAFGLENKkvPPKKMKDII------DDLAKKVGMEDYLDKEPQ------NLSGGQKQRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 746197230 511 AIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDL--MVDKTVIAIAHRLSTIAQMDRLIVLDEGKIAEQGTHEEL 586
Cdd:PRK13632 152 AIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLrkTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEI 229
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
361-581 |
1.91e-32 |
|
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: 124.14 E-value: 1.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVidHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQnieDVT-QDSLRANIALV 439
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV---DVTaAPPADRPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 440 TQDTSLL-HRSVAENIKYGRPDA---TDHDmQSAVHKAKAaefipqlvdlkgRSGYEAQVGERGVKLSGGQRQRIAIARV 515
Cdd:cd03298 76 FQENNLFaHLTVEQNVGLGLSPGlklTAED-RQAIEVALA------------RVGLAGLEKRLPGELSGGERQRVALARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 746197230 516 FLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDK--TVIAIAHRLSTIAQM-DRLIVLDEGKIAEQG 581
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRLaQRVVFLDNGRIAAQG 211
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
361-588 |
6.41e-32 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 123.57 E-value: 6.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQD--SLRANIAL 438
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDinKLRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 439 VTQDTSLL-HRSVAENIKYGrpdatdhdmQSAVHKAKAAEFIPQLVDLKGRSGYEAQVGERGVKLSGGQRQRIAIARvfl 517
Cdd:COG1126 82 VFQQFNLFpHLTVLENVTLA---------PIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIAR--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 518 kdA----PILIL-DEATSALD----SEVEAAIQSSLNDLMvdkTVIAIAHRLS---TIAqmDRLIVLDEGKIAEQGTHEE 585
Cdd:COG1126 150 --AlamePKVMLfDEPTSALDpelvGEVLDVMRDLAKEGM---TMVVVTHEMGfarEVA--DRVVFMDGGRIVEEGPPEE 222
|
...
gi 746197230 586 LIA 588
Cdd:COG1126 223 FFE 225
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
361-577 |
1.83e-31 |
|
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: 121.48 E-value: 1.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQD--SLRANIAL 438
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 439 VTQDTSLL-HRSVAENIKYGrpdatdhdmQSAVHKAKAAEFIPQLVDLKGRSGYEAQVGERGVKLSGGQRQRIAIARVFL 517
Cdd:cd03262 81 VFQQFNLFpHLTVLENITLA---------PIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 746197230 518 KDAPILILDEATSALDSEVEAAIQSSLNDLMVDK-TVIAIAHRLS---TIAqmDRLIVLDEGKI 577
Cdd:cd03262 152 MNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGmTMVVVTHEMGfarEVA--DRVIFMDDGRI 213
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
298-600 |
4.21e-31 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 129.76 E-value: 4.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 298 LGVIAATTAMILKLNSMAEFM--MWHMSALFEnvgtiqdgmqTLGKKINIQDKPEAKPLA-VKQgeIVFKDVTFAYNNKN 374
Cdd:PTZ00265 329 LGVLISMFMLTIILPNITEYMksLEATNSLYE----------IINRKPLVENNDDGKKLKdIKK--IQFKNVRFHYDTRK 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 375 VIDHF---NLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILI-DGQNIEDVTQDSLRANIALVTQDTSLLHRSV 450
Cdd:PTZ00265 397 DVEIYkdlNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSI 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 451 AENIKYGRPDATD---------------------------------HDMQSA------VHKAKAAEFI--PQLVDLKGR- 488
Cdd:PTZ00265 477 KNNIKYSLYSLKDlealsnyynedgndsqenknkrnscrakcagdlNDMSNTtdsnelIEMRKNYQTIkdSEVVDVSKKv 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 489 ----------SGYEAQVGERGVKLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLM--VDKTVIAI 556
Cdd:PTZ00265 557 lihdfvsalpDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIII 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 557 AHRLSTIAQMDRLIVL----------------------------------------------DEGK-IAEQGTHEELIA- 588
Cdd:PTZ00265 637 AHRLSTIRYANTIFVLsnrergstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinNAGSyIIEQGTHDALMKn 716
|
410
....*....|..
gi 746197230 589 KNGIYAQLWKRQ 600
Cdd:PTZ00265 717 KNGIYYTMINNQ 728
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
378-589 |
5.03e-31 |
|
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: 121.98 E-value: 5.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 378 HFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRA----NIALVTQDTSLL-HRSVAE 452
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpHRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 453 NIKYGRPDAtdhDMQSAVHKAKAAEFIpQLVDLKGRSgyEAQVGErgvkLSGGQRQRIAIARVFLKDAPILILDEATSAL 532
Cdd:cd03294 122 NVAFGLEVQ---GVPRAEREERAAEAL-ELVGLEGWE--HKYPDE----LSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 533 DSEVEAAIQSSLNDL--MVDKTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEELIAK 589
Cdd:cd03294 192 DPLIRREMQDELLRLqaELQKTIVFITHDLDEALRLgDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
359-586 |
7.37e-31 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 123.64 E-value: 7.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 359 GEIVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDV-TQDslRaNIA 437
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLpPKD--R-NIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 438 LVTQDTSLL-HRSVAENIKYG-----RPDAtdhDMQSAVhkAKAAEfIPQLVDLKGRsgYEAQvgergvkLSGGQRQRIA 511
Cdd:COG3839 79 MVFQSYALYpHMTVYENIAFPlklrkVPKA---EIDRRV--REAAE-LLGLEDLLDR--KPKQ-------LSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 512 IARVFLKDAPILILDEATSALD--------SEVeAAIQSSLNdlmvdKTVIAIAHRLS---TIAqmDRLIVLDEGKIAEQ 580
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDaklrvemrAEI-KRLHRRLG-----TTTIYVTHDQVeamTLA--DRIAVMNDGRIQQV 215
|
....*.
gi 746197230 581 GTHEEL 586
Cdd:COG3839 216 GTPEEL 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
375-589 |
1.06e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 125.90 E-value: 1.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 375 VIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVT-QDSLRANIALVTQDTSLL-HRSVAE 452
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGIAIIHQELNLVpNLSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 453 NIKYGRPDATDHDMQSAVHKAKAAEFIPQL---VDLkgrsgyEAQVGErgvkLSGGQRQRIAIARVFLKDAPILILDEAT 529
Cdd:COG1129 99 NIFLGREPRRGGLIDWRAMRRRARELLARLgldIDP------DTPVGD----LSVAQQQLVEIARALSRDARVLILDEPT 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 746197230 530 SAL-DSEVEAaiqssLNDLMVD-----KTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQG-----THEELIAK 589
Cdd:COG1129 169 ASLtEREVER-----LFRIIRRlkaqgVAIIYISHRLDEVFEIaDRVTVLRDGRLVGTGpvaelTEDELVRL 235
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
361-586 |
1.26e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 121.01 E-value: 1.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKN--VIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANIAL 438
Cdd:PRK13648 8 IVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 439 VTQ--DTSLLHRSVAENIKYGRPD-ATDHD-MQSAVHKAKAAefipqlVDLKGRSGYEAQvgergvKLSGGQRQRIAIAR 514
Cdd:PRK13648 88 VFQnpDNQFVGSIVKYDVAFGLENhAVPYDeMHRRVSEALKQ------VDMLERADYEPN------ALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 746197230 515 VFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDK--TVIAIAHRLSTIAQMDRLIVLDEGKIAEQGTHEEL 586
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
375-588 |
1.37e-30 |
|
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: 122.08 E-value: 1.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 375 VIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFY---HLKEGAILIDGQNIEDVTQDSLRA----NIALVTQD--TSL 445
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppGITSGEILFDGEDLLKLSEKELRKirgrEIQMIFQDpmTSL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 446 --LHR---SVAENIKYGRpdatdhDMQSAVHKAKAAEFIpQLVDLkgrSGYEAQVGERGVKLSGGQRQRIAIARVFLKDA 520
Cdd:COG0444 100 npVMTvgdQIAEPLRIHG------GLSKAEARERAIELL-ERVGL---PDPERRLDRYPHELSGGMRQRVMIARALALEP 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 746197230 521 PILILDEATSALDSEVEAAIqssLNdLMVD------KTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEELIA 588
Cdd:COG0444 170 KLLIADEPTTALDVTIQAQI---LN-LLKDlqrelgLAILFITHDLGVVAEIaDRVAVMYAGRIVEEGPVEELFE 240
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
361-577 |
1.87e-30 |
|
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: 118.66 E-value: 1.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAY-NNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDS---LRANI 436
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 437 ALVTQDTSLL-HRSVAENIKYGRpDATDHDMQSAVHKAKAAEfipQLVDLKGRS-GYEAQvgergvkLSGGQRQRIAIAR 514
Cdd:cd03292 81 GVVFQDFRLLpDRNVYENVAFAL-EVTGVPPREIRKRVPAAL---ELVGLSHKHrALPAE-------LSGGEQQRVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 746197230 515 VFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIA-HRLSTIAQMD-RLIVLDEGKI 577
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVAtHAKELVDTTRhRVIALERGKL 214
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
365-590 |
1.70e-29 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 116.61 E-value: 1.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 365 DVTFAYNNKNVidHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNiEDVTQDSLRAnIALVTQDTS 444
Cdd:PRK10771 6 DITWLYHHLPM--RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPSRRP-VSMLFQENN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 445 LL-HRSVAENIKYG-----RPDATDHDmqsavhkakaaefipQLVDLKGRSGYEAQVGERGVKLSGGQRQRIAIARVFLK 518
Cdd:PRK10771 82 LFsHLTVAQNIGLGlnpglKLNAAQRE---------------KLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 746197230 519 DAPILILDEATSALDSEVEAAIQSSLNDLMVDK--TVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEELIAKN 590
Cdd:PRK10771 147 EQPILLLDEPFSALDPALRQEMLTLVSQVCQERqlTLLMVSHSLEDAARIaPRSLVVADGRIAWDGPTDELLSGK 221
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
361-586 |
2.81e-29 |
|
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: 115.80 E-value: 2.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVtqDSLRANIALVT 440
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNL--PPHKRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 441 QDTSLL-HRSVAENIKYGrpdATDHDMQSAVHKAKAAEFIpQLVDLKG-RSGYEAQvgergvkLSGGQRQRIAIARVFLK 518
Cdd:cd03300 79 QNYALFpHLTVFENIAFG---LRLKKLPKAEIKERVAEAL-DLVQLEGyANRKPSQ-------LSGGQQQRVAIARALVN 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 746197230 519 DAPILILDEATSALDSEVEAAIQSSLNDL--MVDKTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEEL 586
Cdd:cd03300 148 EPKVLLLDEPLGALDLKLRKDMQLELKRLqkELGITFVFVTHDQEEALTMsDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
361-581 |
4.09e-29 |
|
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: 115.04 E-value: 4.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVtqDSLRANIALVT 440
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDL--PPKDRDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 441 QDTSLL-HRSVAENIKYG------RPDATDHDMQSAVHKAKaaefIPQLVDLKGRsgyeaqvgergvKLSGGQRQRIAIA 513
Cdd:cd03301 79 QNYALYpHMTVYDNIAFGlklrkvPKDEIDERVREVAELLQ----IEHLLDRKPK------------QLSGGQRQRVALG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 746197230 514 RVFLKDAPILILDEATSALDSEVEAAIQSSLNDLM--VDKTVIAIAH-RLSTIAQMDRLIVLDEGKIAEQG 581
Cdd:cd03301 143 RAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQqrLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
361-587 |
4.59e-29 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 115.58 E-value: 4.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIED--VTQDSLRANIAL 438
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 439 VTQDTSLL-HRSVAENIKYGrPdatdhdmqSAVHKAKAAEFIPQLVDLKGRSGYEAQVGERGVKLSGGQRQRIAIARVfL 517
Cdd:PRK09493 82 VFQQFYLFpHLTALENVMFG-P--------LRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARA-L 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 746197230 518 KDAPILIL-DEATSALDSEVEAAIQSSLNDL------MVDKT-VIAIAHRLSTiaqmdRLIVLDEGKIAEQGTHEELI 587
Cdd:PRK09493 152 AVKPKLMLfDEPTSALDPELRHEVLKVMQDLaeegmtMVIVThEIGFAEKVAS-----RLIFIDKGRIAEDGDPQVLI 224
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
361-590 |
9.44e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 115.88 E-value: 9.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNN--KNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANIAL 438
Cdd:PRK13635 6 IRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 439 VTQ--DTSLLHRSVAENIKYG-------RPDATDHdMQSAVHKAKAAEFIPQlvdlkgrsgyEAQvgergvKLSGGQRQR 509
Cdd:PRK13635 86 VFQnpDNQFVGATVQDDVAFGlenigvpREEMVER-VDQALRQVGMEDFLNR----------EPH------RLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 510 IAIARVFLKDAPILILDEATSALD----SEVEAAIQSSLNDLMVdkTVIAIAHRLSTIAQMDRLIVLDEGKIAEQGTHEE 585
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDprgrREVLETVRQLKEQKGI--TVLSITHDLDEAAQADRVIVMNKGEILEEGTPEE 226
|
....*
gi 746197230 586 LIAKN 590
Cdd:PRK13635 227 IFKSG 231
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
361-585 |
9.96e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 115.92 E-value: 9.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYN-----NKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIED--VTQDSLR 433
Cdd:PRK13637 3 IKIENLTHIYMegtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 434 ANIALVTQ--DTSLLHRSVAENIKYG--RPDATDHDMQSAVHKAKAAEFIPqLVDLKGRSGYEaqvgergvkLSGGQRQR 509
Cdd:PRK13637 83 KKVGLVFQypEYQLFEETIEKDIAFGpiNLGLSEEEIENRVKRAMNIVGLD-YEDYKDKSPFE---------LSGGQKRR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 746197230 510 IAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDK--TVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEE 585
Cdd:PRK13637 153 VAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKLaDRIIVMNKGKCELQGTPRE 231
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
361-586 |
1.02e-28 |
|
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: 114.59 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNN-KNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSL---RANI 436
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 437 ALVTQDTSLLHR-SVAENIKYGRPDATDH-----DMQSAVHKAKAAEfipqLVDLKGRSGYEAQvgeRGVKLSGGQRQRI 510
Cdd:cd03256 81 GMIFQQFNLIERlSVLENVLSGRLGRRSTwrslfGLFPKEEKQRALA----ALERVGLLDKAYQ---RADQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 746197230 511 AIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDK--TVIAIAHRLSTIAQ-MDRLIVLDEGKIAEQGTHEEL 586
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPAEL 232
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
361-589 |
1.29e-28 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 117.21 E-value: 1.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDV--TFAYNNKNVI--DHFNLHIKAGEKIGIVGRSGAGKSTLIQLLlhfyHLKE----GAILIDGQNIEDVTQDSL 432
Cdd:PRK11153 2 IELKNIskVFPQGGRTIHalNNVSLHIPAGEIFGVIGASGAGKSTLIRCI----NLLErptsGRVLVDGQDLTALSEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 433 RA---NIALVTQDTSLL-HRSVAENIKY-----GRPDATDhdmqsavhKAKAAEfipqLVDLKG----RSGYEAQvgerg 499
Cdd:PRK11153 78 RKarrQIGMIFQHFNLLsSRTVFDNVALplelaGTPKAEI--------KARVTE----LLELVGlsdkADRYPAQ----- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 500 vkLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDL--MVDKTVIAIAHRLSTIAQM-DRLIVLDEGK 576
Cdd:PRK11153 141 --LSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDInrELGLTIVLITHEMDVVKRIcDRVAVIDAGR 218
|
250
....*....|...
gi 746197230 577 IAEQGTHEELIAK 589
Cdd:PRK11153 219 LVEQGTVSEVFSH 231
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
377-589 |
1.73e-28 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 116.37 E-value: 1.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 377 DHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRA---NIALVTQD--TSL-----L 446
Cdd:COG4608 35 DGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPlrrRMQMVFQDpyASLnprmtV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 447 HRSVAENIKYgrpdatdHDMQSAV-HKAKAAEFIpQLVDLK----GRSGYEaqvgergvkLSGGQRQRIAIARVFLKDAP 521
Cdd:COG4608 115 GDIIAEPLRI-------HGLASKAeRRERVAELL-ELVGLRpehaDRYPHE---------FSGGQRQRIGIARALALNPK 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 746197230 522 ILILDEATSALDSEVEAAIqssLNdLMVD------KTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEELIAK 589
Cdd:COG4608 178 LIVCDEPVSALDVSIQAQV---LN-LLEDlqdelgLTYLFISHDLSVVRHIsDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
360-586 |
6.39e-28 |
|
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: 112.43 E-value: 6.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 360 EIVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGqniEDVTQDSLRA-NIAL 438
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG---EDATDVPVQErNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 439 VTQDTSLL-HRSVAENIKYG---RPDATDHDmqSAVHKAKAAEFIpQLVDLKG-RSGYEAQvgergvkLSGGQRQRIAIA 513
Cdd:cd03296 79 VFQHYALFrHMTVFDNVAFGlrvKPRSERPP--EAEIRAKVHELL-KLVQLDWlADRYPAQ-------LSGGQRQRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 746197230 514 RVFLKDAPILILDEATSALDSEVEAAIQSSLNDLM--VDKTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEEL 586
Cdd:cd03296 149 RALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHdeLHVTTVFVTHDQEEALEVaDRVVVMNKGRIEQVGTPDEV 224
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
350-585 |
8.81e-28 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 115.43 E-value: 8.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 350 EAKPLavkqgeIVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQ 429
Cdd:PRK09452 10 SLSPL------VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 430 DslRANIALVTQDTSLL-HRSVAENIKYG-RpdatdhdMQsavhKAKAAEFIP---------QLVDLKGRsgyeaqvgeR 498
Cdd:PRK09452 84 E--NRHVNTVFQSYALFpHMTVFENVAFGlR-------MQ----KTPAAEITPrvmealrmvQLEEFAQR---------K 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 499 GVKLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLM--VDKTVIAIAH-RLSTIAQMDRLIVLDEG 575
Cdd:PRK09452 142 PHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQrkLGITFVFVTHdQEEALTMSDRIVVMRDG 221
|
250
....*....|
gi 746197230 576 KIAEQGTHEE 585
Cdd:PRK09452 222 RIEQDGTPRE 231
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
361-586 |
2.84e-27 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 113.28 E-value: 2.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGqniEDVTQDSLRA-NIALV 439
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDG---EDVTHRSIQQrDICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 440 TQDTSLL-HRSVAENIKYGRpdatdhDMQsAVHKAKAAEFIPQ---LVDLkgrSGYEaqvgERGV-KLSGGQRQRIAIAR 514
Cdd:PRK11432 84 FQSYALFpHMSLGENVGYGL------KML-GVPKEERKQRVKEaleLVDL---AGFE----DRYVdQISGGQQQRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 746197230 515 VFLKDAPILILDEATSALDSEVEAAIQSSLNDLM--VDKTVIAIAHRLS-TIAQMDRLIVLDEGKIAEQGTHEEL 586
Cdd:PRK11432 150 ALILKPKVLLFDEPLSNLDANLRRSMREKIRELQqqFNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
347-596 |
2.84e-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: 118.12 E-value: 2.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 347 DKPEAKPlaVKQGE---IVFKDVTF--AYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDG 421
Cdd:TIGR00957 622 DSIERRT--IKPGEgnsITVHNATFtwARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 422 qniedvtqdslraNIALVTQDTSLLHRSVAENIKYGRPdatdhdMQSAVHKA--KAAEFIPQLVDLKGrsGYEAQVGERG 499
Cdd:TIGR00957 700 -------------SVAYVPQQAWIQNDSLRENILFGKA------LNEKYYQQvlEACALLPDLEILPS--GDRTEIGEKG 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 500 VKLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSL---NDLMVDKTVIAIAHRLSTIAQMDRLIVLDEGK 576
Cdd:TIGR00957 759 VNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGK 838
|
250 260
....*....|....*....|
gi 746197230 577 IAEQGTHEELIAKNGIYAQL 596
Cdd:TIGR00957 839 ISEMGSYQELLQRDGAFAEF 858
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
361-581 |
3.28e-27 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 109.59 E-value: 3.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGeKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDvTQDSLRANIALVT 440
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 441 QDTSLLHR-SVAENIKYGrpdATDHDMQSAVHKAKAAEFIpQLVDLKGRsgyeaqVGERGVKLSGGQRQRIAIARVFLKD 519
Cdd:cd03264 79 QEFGVYPNfTVREFLDYI---AWLKGIPSKEVKARVDEVL-ELVNLGDR------AKKKIGSLSGGMRRRVGIAQALVGD 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 746197230 520 APILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQG 581
Cdd:cd03264 149 PSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
361-596 |
3.57e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 111.36 E-value: 3.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYN---NKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANIA 437
Cdd:PRK13650 5 IEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 438 LVTQ--DTSLLHRSVAENIKYGRPD-ATDH-DMQSAVHKAkaaefipqlVDLKGRSGYEAQVGERgvkLSGGQRQRIAIA 513
Cdd:PRK13650 85 MVFQnpDNQFVGATVEDDVAFGLENkGIPHeEMKERVNEA---------LELVGMQDFKEREPAR---LSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 514 RVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDK--TVIAIAHRLSTIAQMDRLIVLDEGKIAEQGTHEELIAKNG 591
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGN 232
|
....*
gi 746197230 592 IYAQL 596
Cdd:PRK13650 233 DLLQL 237
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
361-595 |
3.58e-27 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 110.53 E-value: 3.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAY-NNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQnieDVTQDS------LR 433
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQ---DVTALRgralrrLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 434 ANIALVTQDTSLLHR-SVAENIKYGR------PDATDHdMQSAVHKAKAAEFIPQlVDLkgrsgyEAQVGERGVKLSGGQ 506
Cdd:COG3638 80 RRIGMIFQQFNLVPRlSVLTNVLAGRlgrtstWRSLLG-LFPPEDRERALEALER-VGL------ADKAYQRADQLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 507 RQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDK--TVIAIAHRLStIAQM--DRLIVLDEGKIAEQGT 582
Cdd:COG3638 152 QQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDgiTVVVNLHQVD-LARRyaDRIIGLRDGRVVFDGP 230
|
250
....*....|....*
gi 746197230 583 HEELIAK--NGIYAQ 595
Cdd:COG3638 231 PAELTDAvlREIYGG 245
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
360-586 |
1.64e-26 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 111.01 E-value: 1.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 360 EIVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIeDVTQDSLRANIALV 439
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL-FTNLPPRERRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 440 TQDTSLL-HRSVAENIKYG----RPDAtdhdmqsAVHKAKAAEFIpQLVDLKGRSG-YEAQvgergvkLSGGQRQRIAIA 513
Cdd:COG1118 81 FQHYALFpHMTVAENIAFGlrvrPPSK-------AEIRARVEELL-ELVQLEGLADrYPSQ-------LSGGQRQRVALA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 514 RVFLKDAPILILDEATSALDSEVEAAIQSSLNDLM--VDKTVIAIAH------RLStiaqmDRLIVLDEGKIAEQGTHEE 585
Cdd:COG1118 146 RALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHdeLGGTTVFVTHdqeealELA-----DRVVVMNQGRIEQVGTPDE 220
|
.
gi 746197230 586 L 586
Cdd:COG1118 221 V 221
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
361-581 |
4.94e-26 |
|
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: 106.15 E-value: 4.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANiALVT 440
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIG-ALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 441 QDTSLLHRSVAENIKYgrpdatdhdmqSAVHKAKAAEFIPQLVDLKGrsgyEAQVGERGVK-LSGGQRQRIAIARVFLKD 519
Cdd:cd03268 80 APGFYPNLTARENLRL-----------LARLLGIRKKRIDEVLDVVG----LKDSAKKKVKgFSLGMKQRLGIALALLGN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 746197230 520 APILILDEATSALDSEVEAAIQSSLNDLMVD-KTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQG 581
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELILSLRDQgITVLISSHLLSEIQKVaDRIGIINKGKLIEEG 208
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
370-581 |
7.55e-26 |
|
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: 105.71 E-value: 7.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 370 YNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIedVTQDSLRANIALVTQDTSLL-HR 448
Cdd:TIGR01277 8 YEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSH--TGLAPYQRPVSMLFQENNLFaHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 449 SVAENIKYG-RPDATdhdmQSAVHKAKAAEFIPQLvdlkGRSGYEAQVGErgvKLSGGQRQRIAIARVFLKDAPILILDE 527
Cdd:TIGR01277 86 TVRQNIGLGlHPGLK----LNAEQQEKVVDAAQQV----GIADYLDRLPE---QLSGGQRQRVALARCLVRPNPILLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 746197230 528 ATSALD----SEVEAAIQSSLNDLmvDKTVIAIAHRLS-TIAQMDRLIVLDEGKIAEQG 581
Cdd:TIGR01277 155 PFSALDpllrEEMLALVKQLCSER--QRTLLMVTHHLSdARAIASQIAVVSQGKIKVVS 211
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
361-587 |
7.87e-26 |
|
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: 106.71 E-value: 7.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGA-ILIDGQNIEDVTQDSLRANIALV 439
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRIGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 440 TQDtslLHRSVAENIK---------------YGRPDATDHDmqsavhKAKA--AEFipQLVDLKGRSgyeaqVGErgvkL 502
Cdd:COG1119 84 SPA---LQLRFPRDETvldvvlsgffdsiglYREPTDEQRE------RAREllELL--GLAHLADRP-----FGT----L 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 503 SGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVD--KTVIAIAHRLSTIAQ-MDRLIVLDEGKIAE 579
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHVEEIPPgITHVLLLKDGRVVA 223
|
....*...
gi 746197230 580 QGTHEELI 587
Cdd:COG1119 224 AGPKEEVL 231
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
88-615 |
7.88e-26 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 113.53 E-value: 7.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 88 ISVLFANILFVNIQSIIKHQILYSTFPMRLRWRFHNLLL----KQSLDFFH----NDFAGRLSAKVMQTALAIREFWIIL 159
Cdd:PLN03232 339 VGYVYAFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLVaaifHKSLRLTHearkNFASGKVTNMITTDANALQQIAEQL 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 160 GDMlaYVSIYFITVSIVL-------GAISPTLLIPLMVWLGLFLLSAwffIPRLSKVSQQQADARAVMTGRVTDAytnIQ 232
Cdd:PLN03232 419 HGL--WSAPFRIIVSMVLlyqqlgvASLFGSLILFLLIPLQTLIVRK---MRKLTKEGLQWTDKRVGIINEILAS---MD 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 233 TVKLFA-HAGRESQYAKASMKEFMTTVYAQMrlgtLFEVSINMLSAVlfvGVIGTAVWLWTQGLAALGVIAATTAMILKL 311
Cdd:PLN03232 491 TVKCYAwEKSFESRIQGIRNEELSWFRKAQL----LSAFNSFILNSI---PVVVTLVSFGVFVLLGGDLTPARAFTSLSL 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 312 NSMAEFMMWHMSALFENVGTIQDGMQTLGKKINIQDKPEAK--PLAVKQGEIVFKDVTFAYNNKN---VIDHFNLHIKAG 386
Cdd:PLN03232 564 FAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEERILAQnpPLQPGAPAISIKNGYFSWDSKTskpTLSDINLEIPVG 643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 387 EKIGIVGRSGAGKSTLIQLLL-HFYHLKEGAILIdgqniedvtqdslRANIALVTQDTSLLHRSVAENIKYGRpdatdhD 465
Cdd:PLN03232 644 SLVAIVGGTGEGKTSLISAMLgELSHAETSSVVI-------------RGSVAYVPQVSWIFNATVRENILFGS------D 704
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 466 MQSAVH-KAKAAEFIPQLVDL-KGRSGYEaqVGERGVKLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAI-QS 542
Cdd:PLN03232 705 FESERYwRAIDVTALQHDLDLlPGRDLTE--IGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVfDS 782
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 746197230 543 SLNDLMVDKTVIAIAHRLSTIAQMDRLIVLDEGKIAEQGTHEELiAKNGIYAQLWKRQTGGFLIEQKVVQGQD 615
Cdd:PLN03232 783 CMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL-SKSGSLFKKLMENAGKMDATQEVNTNDE 854
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
380-588 |
7.91e-26 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 105.98 E-value: 7.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 380 NLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDV-TQDSLRANIALVTQDTSLLHR-SVAENIKYG 457
Cdd:cd03224 20 SLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLpPHERARAGIGYVPEGRRIFPElTVEENLLLG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 458 RpdatdhdmqSAVHKAKAAEFIPQLVD----LKGRSGYEAQVgergvkLSGGQRQRIAIARVFLKDAPILILDEATSALD 533
Cdd:cd03224 100 A---------YARRRAKRKARLERVYElfprLKERRKQLAGT------LSGGEQQMLAIARALMSRPKLLLLDEPSEGLA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 534 ----SEVEAAIQsSLNDLMVdkTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEELIA 588
Cdd:cd03224 165 pkivEEIFEAIR-ELRDEGV--TILLVEQNARFALEIaDRAYVLERGRVVLEGTAAELLA 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
377-588 |
1.10e-25 |
|
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: 111.31 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 377 DHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHlKEGAILIDGQNIEDVTQD---SLRANIALVTQD--TSLLHR-SV 450
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRalrPLRRRMQVVFQDpfGSLSPRmTV 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 451 AENIKYG----RPDATDHDMQSAVHKAKAAefipqlVDLKGRSGY----EaqvgergvkLSGGQRQRIAIAR-VFLKdaP 521
Cdd:COG4172 382 GQIIAEGlrvhGPGLSAAERRARVAEALEE------VGLDPAARHryphE---------FSGGQRQRIAIARaLILE--P 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 746197230 522 -ILILDEATSALDSEVEAAIQSSLNDLMVDK--TVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEELIA 588
Cdd:COG4172 445 kLLVLDEPTSALDVSVQAQILDLLRDLQREHglAYLFISHDLAVVRALaHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
361-589 |
1.20e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 106.81 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNN--KNVIDHFNLHIKAGEKIGIVGRSGAGKST---LIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRAN 435
Cdd:PRK13640 6 VEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 436 IALVTQ--DTSLLHRSVAENIKYG-------RPDatdhdMQSAVHKAKAAefipqlVDLKGRSGYEAQvgergvKLSGGQ 506
Cdd:PRK13640 86 VGIVFQnpDNQFVGATVGDDVAFGlenravpRPE-----MIKIVRDVLAD------VGMLDYIDSEPA------NLSGGQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 507 RQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDK--TVIAIAHRLSTIAQMDRLIVLDEGKIAEQGTHE 584
Cdd:PRK13640 149 KQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPV 228
|
....*
gi 746197230 585 ELIAK 589
Cdd:PRK13640 229 EIFSK 233
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
353-596 |
1.28e-25 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 112.91 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 353 PLAVKQGEIVFKDVTFAYNNKN---VIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLhfyhlKEGAILIDGQNIedvtq 429
Cdd:PLN03130 607 PLEPGLPAISIKNGYFSWDSKAerpTLSNINLDVPVGSLVAIVGSTGEGKTSLISAML-----GELPPRSDASVV----- 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 430 dsLRANIALVTQDTSLLHRSVAENIKYGRP----------DAT--DHDMQSavhkakaaefipqlvdLKGrsGYEAQVGE 497
Cdd:PLN03130 677 --IRGTVAYVPQVSWIFNATVRDNILFGSPfdperyeraiDVTalQHDLDL----------------LPG--GDLTEIGE 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 498 RGVKLSGGQRQRIAIARVFLKDAPILILDEATSALDSEV-EAAIQSSLNDLMVDKTVIAIAHRLSTIAQMDRLIVLDEGK 576
Cdd:PLN03130 737 RGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVgRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGM 816
|
250 260
....*....|....*....|
gi 746197230 577 IAEQGTHEELIAKNGIYAQL 596
Cdd:PLN03130 817 IKEEGTYEELSNNGPLFQKL 836
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
361-576 |
1.29e-25 |
|
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: 104.87 E-value: 1.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTqDSLRANIALVT 440
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-EDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 441 QDTSL-LHRSVAENIkygrpdatdhDMQSAVHKAKAAEF-IPQLVDLKGRSGYEAQ-VGergvKLSGGQRQRIAIARVFL 517
Cdd:COG4133 82 HADGLkPELTVRENL----------RFWAALYGLRADREaIDEALEAVGLAGLADLpVR----QLSAGQKRRVALARLLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 746197230 518 KDAPILILDEATSALDSEVEAAiqssLNDLMVD-----KTVIAIAHRLSTIAQmDRLIVLDEGK 576
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVAL----LAELIAAhlargGAVLLTTHQPLELAA-ARVLDLGDFK 206
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
380-594 |
1.31e-25 |
|
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: 105.50 E-value: 1.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 380 NLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDslRANIALVTQDTSLL-HRSVAENIKYG- 457
Cdd:cd03299 19 SLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNIAYGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 458 ----RPDATDHdmqSAVHKAKAAEFIPQLVDLKGRSgyeaqvgergvkLSGGQRQRIAIARVFLKDAPILILDEATSALD 533
Cdd:cd03299 97 kkrkVDKKEIE---RKVLEIAEMLGIDHLLNRKPET------------LSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 746197230 534 SEVEAAIQSSLNDLM--VDKTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEELI--AKNGIYA 594
Cdd:cd03299 162 VRTKEKLREELKKIRkeFGVTVLHVTHDFEEAWALaDKVAIMLNGKLIQVGKPEEVFkkPKNEFVA 227
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
360-581 |
2.52e-25 |
|
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: 103.40 E-value: 2.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 360 EIVFKDVTFAYNNKN------VIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLL--LHFYHLKEGAILIDGQNIEDvtqDS 431
Cdd:cd03213 3 TLSFRNLTVTVKSSPsksgkqLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDK---RS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 432 LRANIALVTQDTSLL-HRSVAENIKYgrpdatdhdmqsavhkakAAEfipqlvdLKGrsgyeaqvgergvkLSGGQRQRI 510
Cdd:cd03213 80 FRKIIGYVPQDDILHpTLTVRETLMF------------------AAK-------LRG--------------LSGGERKRV 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 746197230 511 AIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVD-KTVIAIAHRLST--IAQMDRLIVLDEGKIAEQG 581
Cdd:cd03213 121 SIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTgRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
361-588 |
2.54e-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: 2.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTL---IQLLLH--FYHLKEGAILIDGQNIEDVTQD---SL 432
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLlrcINLLEQpeAGTIRVGDITIDTARSLSQQKGlirQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 433 RANIALVTQDTSLL-HRSVAENIKYGRPDATDHDMQSAVHKAKaaefipQLVDLKGRSGYEAQVGERgvkLSGGQRQRIA 511
Cdd:PRK11264 84 RQHVGFVFQNFNLFpHRTVLENIIEGPVIVKGEPKEEATARAR------ELLAKVGLAGKETSYPRR---LSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 746197230 512 IARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDK-TVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEELIA 588
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGPAKALFA 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
349-579 |
2.65e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 109.77 E-value: 2.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 349 PEAKPLavkqGEIVF--KDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIdGQNIEd 426
Cdd:COG0488 306 PPPERL----GKKVLelEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 427 vtqdslranIALVTQDTSLLH--RSVAENIKYGRPDATDhdmqsavhkakaaefiPQLVDLKGR---SGYEAQ--VGerg 499
Cdd:COG0488 380 ---------IGYFDQHQEELDpdKTVLDELRDGAPGGTE----------------QEVRGYLGRflfSGDDAFkpVG--- 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 500 vKLSGGQRQRIAIARVFLKDAPILILDEATSALDSE-VEAaiqssLNDLMVD--KTVIAIAH-R--LSTIAqmDRLIVLD 573
Cdd:COG0488 432 -VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIEtLEA-----LEEALDDfpGTVLLVSHdRyfLDRVA--TRILEFE 503
|
....*.
gi 746197230 574 EGKIAE 579
Cdd:COG0488 504 DGGVRE 509
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
361-578 |
3.46e-25 |
|
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: 102.12 E-value: 3.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIE-DVTQDSLRANIALV 439
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSfASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 440 TQdtsllhrsvaenikygrpdatdhdmqsavhkakaaefipqlvdlkgrsgyeaqvgergvkLSGGQRQRIAIARVFLKD 519
Cdd:cd03216 81 YQ------------------------------------------------------------LSVGERQMVEIARALARN 100
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 746197230 520 APILILDEATSAL-DSEVEAaiqssLNDLMVD-----KTVIAIAHRLSTIAQM-DRLIVLDEGKIA 578
Cdd:cd03216 101 ARLLILDEPTAALtPAEVER-----LFKVIRRlraqgVAVIFISHRLDEVFEIaDRVTVLRDGRVV 161
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
364-585 |
4.16e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 104.85 E-value: 4.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 364 KDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANIALVTQDT 443
Cdd:PRK13548 6 RNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 444 SLLHR-SVAENIKYGR---PDATDHDMQSAVHKAKAAEfipqLVDLKGRSgYEAqvgergvkLSGGQRQRIAIARVFL-- 517
Cdd:PRK13548 86 SLSFPfTVEEVVAMGRaphGLSRAEDDALVAAALAQVD----LAHLAGRD-YPQ--------LSGGEQQRVQLARVLAql 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 518 ----KDAPILILDEATSALDseveaaIQSSLNDLMVDK--------TVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHE 584
Cdd:PRK13548 153 wepdGPPRWLLLDEPTSALD------LAHQHHVLRLARqlaherglAVIVVLHDLNLAARYaDRIVLLHQGRLVADGTPA 226
|
.
gi 746197230 585 E 585
Cdd:PRK13548 227 E 227
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
360-587 |
7.96e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 103.94 E-value: 7.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 360 EIVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANIALV 439
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 440 TQdtsllHRSVAENIK------YGRP----------DATDHDMQSAVHKAKAAEFIPQLVDlkgrsgyeaqvgergvKLS 503
Cdd:PRK11231 82 PQ-----HHLTPEGITvrelvaYGRSpwlslwgrlsAEDNARVNQAMEQTRINHLADRRLT----------------DLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 504 GGQRQRIAIARVFLKDAPILILDEATSALD--SEVEaaiqssLNDLMVD-----KTVIAIAHRLSTIAQM-DRLIVLDEG 575
Cdd:PRK11231 141 GGQRQRAFLAMVLAQDTPVVLLDEPTTYLDinHQVE------LMRLMRElntqgKTVVTVLHDLNQASRYcDHLVVLANG 214
|
250
....*....|..
gi 746197230 576 KIAEQGTHEELI 587
Cdd:PRK11231 215 HVMAQGTPEEVM 226
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
364-577 |
9.50e-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: 102.34 E-value: 9.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 364 KDVTFAYN-NKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIedvTQDSLRANIALVTQD 442
Cdd:cd03226 3 ENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 443 TS--LLHRSVAENIKYGRPDATDhdmqsavhKAKAAEFIPQLVDLkgrsgYEAQvgERG-VKLSGGQRQRIAIARVFLKD 519
Cdd:cd03226 80 VDyqLFTDSVREELLLGLKELDA--------GNEQAETVLKDLDL-----YALK--ERHpLSLSGGQKQRLAIAAALLSG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 520 APILILDEATSALDSEVEAAIQSSLNDLM-VDKTVIAIAHRLSTIAQM-DRLIVLDEGKI 577
Cdd:cd03226 145 KDLLIFDEPTSGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLAKVcDRVLLLANGAI 204
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
379-581 |
1.13e-24 |
|
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: 102.37 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 379 FNLHIK---AGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDvTQDSL-----RANIALVTQDTSLL-HRS 449
Cdd:cd03297 13 FTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFD-SRKKInlppqQRKIGLVFQQYALFpHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 450 VAENIKYGRPDATDHDMQSAVHkakaaefipQLVDLKGRSgyeaQVGERGV-KLSGGQRQRIAIARVFLKDAPILILDEA 528
Cdd:cd03297 92 VRENLAFGLKRKRNREDRISVD---------ELLDLLGLD----HLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 746197230 529 TSALDSEVEAAIQSSLNDLMVD--KTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQG 581
Cdd:cd03297 159 FSALDRALRLQLLPELKQIKKNlnIPVIFVTHDLSEAEYLaDRIVVMEDGRLQYIG 214
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
158-595 |
1.28e-24 |
|
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: 109.61 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 158 ILGDMLAYVSIYFITVS-IVLGAI------SPTLL---IPLMVwlgLFLLSAWFFIPRLSKVSQQQADARAVMTGRVTDA 227
Cdd:TIGR01271 994 IIDDMLPLTLFDFIQLTlIVLGAIfvvsvlQPYIFiaaIPVAV---IFIMLRAYFLRTSQQLKQLESEARSPIFSHLITS 1070
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 228 YTNIQTVKLFahaGRESQYAKASMKEFMT-TVYAQMRLGTL--FEVSINMLSAVLFVGVIGTAVWLWTQGLAALGVIAAT 304
Cdd:TIGR01271 1071 LKGLWTIRAF---GRQSYFETLFHKALNLhTANWFLYLSTLrwFQMRIDIIFVFFFIAVTFIAIGTNQDGEGEVGIILTL 1147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 305 TAMILKLNSMA-------EFMMWHMSALFENVGTIQDGMQTLGK-------KINIQDKPEAKPLAVKQGEIVFKDVTFAY 370
Cdd:TIGR01271 1148 AMNILSTLQWAvnssidvDGLMRSVSRVFKFIDLPQEEPRPSGGggkyqlsTVLVIENPHAQKCWPSGGQMDVQGLTAKY 1227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 371 NN--KNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHlKEGAILIDGQNIEDVTQDSLRANIALVTQDTSLLHR 448
Cdd:TIGR01271 1228 TEagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSG 1306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 449 SVAENIK-YGRpdATDHDMQSAVHKAKAAEFIPQLVDlkgrsGYEAQVGERGVKLSGGQRQRIAIARVFLKDAPILILDE 527
Cdd:TIGR01271 1307 TFRKNLDpYEQ--WSDEEIWKVAEEVGLKSVIEQFPD-----KLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDE 1379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 746197230 528 ATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIAQMDRLIVLDEGKIAEQGTHEELIAKNGIYAQ 595
Cdd:TIGR01271 1380 PSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQ 1447
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
380-588 |
1.58e-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: 105.19 E-value: 1.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 380 NLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSL----RANIALVTQDTSLL-HRSVAENI 454
Cdd:TIGR02142 17 DFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFlppeKRRIGYVFQEARLFpHLSVRGNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 455 KYGRPDATDHDMQsavhkAKAAEFIPQLvdlkgrsGYEAQVGERGVKLSGGQRQRIAIARVFLKDAPILILDEATSALDS 534
Cdd:TIGR02142 97 RYGMKRARPSERR-----ISFERVIELL-------GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 746197230 535 EVEAAIQSSLNDLM--VDKTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEELIA 588
Cdd:TIGR02142 165 PRKYEILPYLERLHaeFGIPILYVSHSLQEVLRLaDRVVVLEDGRVAAAGPIAEVWA 221
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
361-588 |
1.60e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 104.12 E-value: 1.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSlRANIALVT 440
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 441 QDTSL-LHRSVAENIK-YGRpdatdhdmQSAVHKAKAAEFIPQLVDL-KGRSGYEAQVGErgvkLSGGQRQRIAIARVFL 517
Cdd:PRK13537 87 QFDNLdPDFTVRENLLvFGR--------YFGLSAAAARALVPPLLEFaKLENKADAKVGE----LSGGMKRRLTLARALV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 746197230 518 KDAPILILDEATSALDSEVEAAIQSSLNDLMV-DKTVIAIAHRLSTIAQM-DRLIVLDEG-KIAEqGTHEELIA 588
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARHLMWERLRSLLArGKTILLTTHFMEEAERLcDRLCVIEEGrKIAE-GAPHALIE 227
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
364-587 |
1.84e-24 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 102.89 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 364 KDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANIALVTQDT 443
Cdd:COG4559 5 ENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLPQHS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 444 SL-LHRSVAENIKYGR------PDATDHDMQSAVHKAkaaefipQLVDLKGRSgYEAqvgergvkLSGGQRQRIAIARVF 516
Cdd:COG4559 85 SLaFPFTVEEVVALGRaphgssAAQDRQIVREALALV-------GLAHLAGRS-YQT--------LSGGEQQRVQLARVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 517 L-----KDAP--ILILDEATSALDseveAAIQSSLNDL---MVDK--TVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTH 583
Cdd:COG4559 149 AqlwepVDGGprWLFLDEPTSALD----LAHQHAVLRLarqLARRggGVVAVLHDLNLAAQYaDRILLLHQGRLVAQGTP 224
|
....
gi 746197230 584 EELI 587
Cdd:COG4559 225 EEVL 228
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
391-586 |
3.57e-24 |
|
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: 103.73 E-value: 3.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 391 IVGRSGAGKSTLIQLLLHFYHLKEGAILIDGqniEDVTQ-DSLRANIALVTQDTSLL-HRSVAENIKYGRpdatdhDMQs 468
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDG---EDVTNvPPHLRHINMVFQSYALFpHMTVEENVAFGL------KMR- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 469 avhKAKAAEFIPQLVDLKGRSGYEAQVGERGVKLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLM 548
Cdd:TIGR01187 71 ---KVPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQ 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 746197230 549 --VDKTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEEL 586
Cdd:TIGR01187 148 eqLGITFVFVTHDQEEAMTMsDRIAIMRKGKIAQIGTPEEI 188
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
361-589 |
4.63e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 102.55 E-value: 4.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNN-----KNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQlllHFYHL---KEGAILIDGQNIEDVTQD-- 430
Cdd:PRK13646 3 IRFDNVSYTYQKgtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQ---NINALlkpTTGTVTVDDITITHKTKDky 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 431 --SLRANIALVTQ--DTSLLHRSVAENIKYGrPDATDHDMQSAvhKAKAAEFIPQLvdlkgrsGYEAQVGERG-VKLSGG 505
Cdd:PRK13646 80 irPVRKRIGMVFQfpESQLFEDTVEREIIFG-PKNFKMNLDEV--KNYAHRLLMDL-------GFSRDVMSQSpFQMSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 506 QRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVD--KTVIAIAHRLSTIAQ-MDRLIVLDEGKIAEQGT 582
Cdd:PRK13646 150 QMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDenKTIILVSHDMNEVARyADEVIVMKEGSIVSQTS 229
|
....*..
gi 746197230 583 HEELIAK 589
Cdd:PRK13646 230 PKELFKD 236
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
347-586 |
7.26e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 103.76 E-value: 7.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 347 DKPEAKPLAVKQGEIVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIED 426
Cdd:PRK11607 6 PRPQAKTRKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 427 VTqdSLRANIALVTQDTSLL-HRSVAENIKYG-------RPDATD--HDMQSAVHKAKAAEFIPQlvdlkgrsgyeaqvg 496
Cdd:PRK11607 86 VP--PYQRPINMMFQSYALFpHMTVEQNIAFGlkqdklpKAEIASrvNEMLGLVHMQEFAKRKPH--------------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 497 ergvKLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLM--VDKTVIAIAHRLSTIAQM-DRLIVLD 573
Cdd:PRK11607 149 ----QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILerVGVTCVMVTHDQEEAMTMaGRIAIMN 224
|
250
....*....|...
gi 746197230 574 EGKIAEQGTHEEL 586
Cdd:PRK11607 225 RGKFVQIGEPEEI 237
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
361-587 |
1.39e-23 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 100.16 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQL---LLhfyHLKEGAILIDGQNIEDVTQDSLRANIA 437
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMisrLL---PPDSGEVLVDGLDVATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 438 LVTQDTSLLHR-SVAENIKYGR-------PDATDHDmqsavHKAKAAEFIpQLVDLKGRsgyeaQVGErgvkLSGGQRQR 509
Cdd:COG4604 79 ILRQENHINSRlTVRELVAFGRfpyskgrLTAEDRE-----IIDEAIAYL-DLEDLADR-----YLDE----LSGGQRQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 510 IAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLmVD---KTVIAIAHRL---STIAqmDRLIVLDEGKIAEQGTH 583
Cdd:COG4604 144 AFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRL-ADelgKTVVIVLHDInfaSCYA--DHIVAMKDGRVVAQGTP 220
|
....
gi 746197230 584 EELI 587
Cdd:COG4604 221 EEII 224
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
361-577 |
1.45e-23 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 100.14 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDslranIALVT 440
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARED-----TRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 441 QDTSLLH-RSVAENIKYG-----RPDAtdhdmqsavHKAKAAefipqlVDLKGRSgyeaqvGERGVKLSGGQRQRIAIAR 514
Cdd:PRK11247 88 QDARLLPwKKVIDNVGLGlkgqwRDAA---------LQALAA------VGLADRA------NEWPAALSGGQKQRVALAR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 746197230 515 VFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDK--TVIAIAHRLS-TIAQMDRLIVLDEGKI 577
Cdd:PRK11247 147 ALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
361-586 |
1.68e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 100.55 E-value: 1.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAY------NNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQlllHFYHL---KEGAILIDGQNIEDVTQD- 430
Cdd:PRK13633 5 IKCKNVSYKYesneesTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAK---HMNALlipSEGKVYVDGLDTSDEENLw 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 431 SLRANIALVTQ--DTSLLHRSVAENIKYG------RPDATDHDMQSAVHKAKAAEF---IPQLvdlkgrsgyeaqvgerg 499
Cdd:PRK13633 82 DIRNKAGMVFQnpDNQIVATIVEEDVAFGpenlgiPPEEIRERVDESLKKVGMYEYrrhAPHL----------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 500 vkLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDK--TVIAIAHRLSTIAQMDRLIVLDEGKI 577
Cdd:PRK13633 145 --LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKV 222
|
....*....
gi 746197230 578 AEQGTHEEL 586
Cdd:PRK13633 223 VMEGTPKEI 231
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
375-581 |
2.51e-23 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 98.59 E-value: 2.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 375 VIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQnieDVTQDSL--RANIALVTQDTSLLHR-SVA 451
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGF---DVVKEPAeaRRRLGFVSDSTGLYDRlTAR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 452 ENIKY-GRpdatdhdmqsaVHKAKAAEFIPQLVDLKGRSGYEAQVGERGVKLSGGQRQRIAIARVFLKDAPILILDEATS 530
Cdd:cd03266 97 ENLEYfAG-----------LYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 746197230 531 ALDSEVEAAIQSSLNDLM-VDKTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQG 581
Cdd:cd03266 166 GLDVMATRALREFIRQLRaLGKCILFSTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
361-587 |
2.55e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 102.61 E-value: 2.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANIALVT 440
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 441 QDTSL-LHRSVAENIKYGRP----------DATDHDMQSAVHKAKAAEFIPQLVDlkgrsgyeaqvgergvKLSGGQRQR 509
Cdd:PRK09536 84 QDTSLsFEFDVRQVVEMGRTphrsrfdtwtETDRAAVERAMERTGVAQFADRPVT----------------SLSGGERQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 510 IAIARVFLKDAPILILDEATSALDseVEAAIQS--SLNDLMVD-KTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEE 585
Cdd:PRK09536 148 VLLARALAQATPVLLLDEPTASLD--INHQVRTleLVRRLVDDgKTAVAAIHDLDLAARYcDELVLLADGRVRAAGPPAD 225
|
..
gi 746197230 586 LI 587
Cdd:PRK09536 226 VL 227
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
346-584 |
3.20e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 101.06 E-value: 3.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 346 QDKPEAK---PLAVKQGEIVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQ 422
Cdd:PRK13536 24 QGISEAKasiPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 423 NIEDVTQdSLRANIALVTQ-DTSLLHRSVAEN-IKYGRpdatdhdmQSAVHKAKAAEFIPQLVDLkgrSGYEAQVGERGV 500
Cdd:PRK13536 104 PVPARAR-LARARIGVVPQfDNLDLEFTVRENlLVFGR--------YFGMSTREIEAVIPSLLEF---ARLESKADARVS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 501 KLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMV-DKTVIAIAHRLSTIAQM-DRLIVLDEG-KI 577
Cdd:PRK13536 172 DLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLArGKTILLTTHFMEEAERLcDRLCVLEAGrKI 251
|
....*..
gi 746197230 578 AEQGTHE 584
Cdd:PRK13536 252 AEGRPHA 258
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
364-588 |
3.44e-23 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 98.52 E-value: 3.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 364 KDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDV-TQDSLRANIALVTQD 442
Cdd:COG0410 7 ENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLpPHRIARLGIGYVPEG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 443 ----TSLlhrSVAENIK---YGRPDATDHDMQsavhKAKAAEFIPQLVDLKGRsgyeaqvgeRGVKLSGGQRQRIAIARV 515
Cdd:COG0410 87 rrifPSL---TVEENLLlgaYARRDRAEVRAD----LERVYELFPRLKERRRQ---------RAGTLSGGEQQMLAIGRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 516 FLKDAPILILDEATSALD----SEVEAAIQsSLND-----LMVDKTviaiAHRLSTIAqmDRLIVLDEGKIAEQGTHEEL 586
Cdd:COG0410 151 LMSRPKLLLLDEPSLGLAplivEEIFEIIR-RLNRegvtiLLVEQN----ARFALEIA--DRAYVLERGRIVLEGTAAEL 223
|
..
gi 746197230 587 IA 588
Cdd:COG0410 224 LA 225
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
373-580 |
5.10e-23 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 99.11 E-value: 5.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 373 KNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRA---NIALVTQDT--SLLH 447
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAfrrDVQLVFQDSpsAVNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 448 RSVAENIkYGRPDATDHDMQSAVHKAKAAEFIpQLVDLKgrsgyEAQVGERGVKLSGGQRQRIAIARVFLKDAPILILDE 527
Cdd:TIGR02769 104 RMTVRQI-IGEPLRHLTSLDESEQKARIAELL-DMVGLR-----SEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 746197230 528 ATSALDSEVEAAIQSSLNDLMVD--KTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQ 580
Cdd:TIGR02769 177 AVSNLDMVLQAVILELLRKLQQAfgTAYLFITHDLRLVQSFcQRVAVMDKGQIVEE 232
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
27-575 |
5.58e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 103.35 E-value: 5.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 27 PFvWQATEGVRPYLLLLVICT-AGAATFEALLFSKI-GQLVDWLSKSQPESFLSQhasnILILISVLFANILFVNIQsii 104
Cdd:COG4178 13 PY-WRSEEKWKAWGLLALLLLlTLASVGLNVLLNFWnRDFYDALQARDAAAFWQQ----LGVFALLAAISILLAVYQ--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 105 khqiLYSTFPMRLRWR--FHNLLLKQSLD---FFHNDFAG--------RLS--AKVMqTALAIRefwiiLGDMLAYVSIY 169
Cdd:COG4178 85 ----TYLRQRLQIRWRewLTERLLDRWLSnraYYRLQLSGgeidnpdqRIAedIRLF-TETTLS-----LSLGLLSSVVT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 170 FITVSIVLGAISPTLLIPL----------MVWLgLFL------LSAWFFIPRLSKVSQQQ----ADARAVMTgRVTDayt 229
Cdd:COG4178 155 LISFIGILWSLSGSLTFTLggysitipgyMVWA-ALIyaiigtLLTHLIGRPLIRLNFEQqrreADFRFALV-RVRE--- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 230 NIQTVKLFAHAGRESQYAKASMKE----FMTTVYAQMRLgTLFEVSINMLSAVL--FV------------GVIGTAVWLW 291
Cdd:COG4178 230 NAESIALYRGEAAERRRLRRRFDAvianWRRLIRRQRNL-TFFTTGYGQLAVIFpiLVaapryfageitlGGLMQAASAF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 292 TQGLAALGVIaattamILKLNSMAEFmmwhmSALFENVGTIQDGMQTLGKkiniQDKPEAKPLAVKQGEIVFKDVTFA-Y 370
Cdd:COG4178 309 GQVQGALSWF------VDNYQSLAEW-----RATVDRLAGFEEALEAADA----LPEAASRIETSEDGALALEDLTLRtP 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 371 NNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQniedvtqdslrANIALVTQDTSLLHRSV 450
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAG-----------ARVLFLPQRPYLPLGTL 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 451 AENIKYGRP--DATDHDMQSAVHKAKAAEFIPQLvdlkgrsgyeAQVGERGVKLSGGQRQRIAIARVFLKDAPILILDEA 528
Cdd:COG4178 443 REALLYPATaeAFSDAELREALEAVGLGHLAERL----------DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEA 512
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 746197230 529 TSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIAQMDRLIVLDEG 575
Cdd:COG4178 513 TSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
360-589 |
1.11e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 98.55 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 360 EIVFKDVTFAYNNKN-----VIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQD---- 430
Cdd:PRK13634 2 DITFQKVEHRYQYKTpferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkklk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 431 SLRANIALVTQ--DTSLLHRSVAENIKYGrpdATDHDMQSAVHKAKAAEFIpQLV----DLKGRSGYEaqvgergvkLSG 504
Cdd:PRK13634 82 PLRKKVGIVFQfpEHQLFEETVEKDICFG---PMNFGVSEEDAKQKAREMI-ELVglpeELLARSPFE---------LSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 505 GQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDK--TVIAIAHRLSTIAQ-MDRLIVLDEGKIAEQG 581
Cdd:PRK13634 149 GQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSMEDAARyADQIVVMHKGTVFLQG 228
|
....*...
gi 746197230 582 THEELIAK 589
Cdd:PRK13634 229 TPREIFAD 236
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
373-588 |
1.78e-22 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 101.30 E-value: 1.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 373 KNVIDHFNLHIKAGEKIGIVGRSGAGKS----TLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRA----NIALVTQD-- 442
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEpm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 443 TSL--LH---RSVAENIKYGRpdatdhdmqsAVHKAKAAEFIPQLVDlkgrsgyeaQVG----ERGVK-----LSGGQRQ 508
Cdd:COG4172 103 TSLnpLHtigKQIAEVLRLHR----------GLSGAAARARALELLE---------RVGipdpERRLDayphqLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 509 RIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDL-----MvdkTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGT 582
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqrelgM---ALLLITHDLGVVRRFaDRVAVMRQGEIVEQGP 240
|
....*.
gi 746197230 583 HEELIA 588
Cdd:COG4172 241 TAELFA 246
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
363-581 |
1.80e-22 |
|
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: 96.19 E-value: 1.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 363 FKDVTFAYNNKN----VIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLL---LHFYHLKEGAILIDGQnieDVTQDSLRAN 435
Cdd:cd03234 6 WWDVGLKAKNWNkyarILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNGQ---PRKPDQFQKC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 436 IALVTQDTSLL-HRSVAENIKYGRPDATDHDMQSAVHKAKAAEFIPQLVDLKgrsgyeaQVGERGVK-LSGGQRQRIAIA 513
Cdd:cd03234 83 VAYVRQDDILLpGLTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLALT-------RIGGNLVKgISGGERRRVSIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 746197230 514 RVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMV-DKTVIAIAHR-LSTIAQM-DRLIVLDEGKIAEQG 581
Cdd:cd03234 156 VQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARrNRIVILTIHQpRSDLFRLfDRILLLSSGEIVYSG 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
377-576 |
2.62e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 100.49 E-value: 2.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 377 DHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQ--NIEDvTQDSLRANIALVTQDTSLLHR-SVAEN 453
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRS-PRDAIALGIGMVHQHFMLVPNlTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 454 IKYGRPDATDH--DMQSAvhKAKAAEFIPQL---VDLkgrsgyEAQVGErgvkLSGGQRQRIAIARVFLKDAPILILDEA 528
Cdd:COG3845 101 IVLGLEPTKGGrlDRKAA--RARIRELSERYgldVDP------DAKVED----LSVGEQQRVEILKALYRGARILILDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 746197230 529 TSAL-DSEVE---AAIQSslndlMVD--KTVIAIAHRLSTIAQM-DRLIVLDEGK 576
Cdd:COG3845 169 TAVLtPQEADelfEILRR-----LAAegKSIIFITHKLREVMAIaDRVTVLRRGK 218
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
361-588 |
2.94e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 96.98 E-value: 2.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAY-NNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQ-DSLRANIAL 438
Cdd:PRK13644 2 IRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 439 VTQ--DTSLLHRSVAENIKYGRPDATDHDMQsavhkakaaefIPQLVDLK-GRSGYEAQVGERGVKLSGGQRQRIAIARV 515
Cdd:PRK13644 82 VFQnpETQFVGRTVEEDLAFGPENLCLPPIE-----------IRKRVDRAlAEIGLEKYRHRSPKTLSGGQGQCVALAGI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 746197230 516 FLKDAPILILDEATSALDSEVEAAIQSSLNDLMVD-KTVIAIAHRLSTIAQMDRLIVLDEGKIAEQGTHEELIA 588
Cdd:PRK13644 151 LTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
170-579 |
3.90e-22 |
|
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: 100.26 E-value: 3.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 170 FITVSIVLGA------ISPTLLIPLMVWLGLFLLSAWFFIPRLSKVSQQQADARAVMTGRVTDAYTNIQTVKLfaHAGRE 243
Cdd:COG4615 129 LQSVALVLGClaylawLSPPLFLLTLVLLGLGVAGYRLLVRRARRHLRRAREAEDRLFKHFRALLEGFKELKL--NRRRR 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 244 SQYAKASMKEFMTTVYAQMRLGTLFEVSINMLSAVLFVGVIGTAVWLWTQ-GLAALGVIAATTAMILklnsmaeFMMWHM 322
Cdd:COG4615 207 RAFFDEDLQPTAERYRDLRIRADTIFALANNWGNLLFFALIGLILFLLPAlGWADPAVLSGFVLVLL-------FLRGPL 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 323 SALFENVGTIQDG------MQTLGKKINIQDKPEAKPLAVKQ----GEIVFKDVTFAYNNKNVIDHF-----NLHIKAGE 387
Cdd:COG4615 280 SQLVGALPTLSRAnvalrkIEELELALAAAEPAAADAAAPPApadfQTLELRGVTYRYPGEDGDEGFtlgpiDLTIRRGE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 388 KIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANIALVTQDTSLLHRSvaenikYGRPDATDHdmq 467
Cdd:COG4615 360 LVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDRL------LGLDGEADP--- 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 468 savhkAKAAEFIPQLvDLKGRSGYEAQVGERgVKLSGGQRQRIAIARVFLKDAPILILDEAtsaldseveAAIQsslndl 547
Cdd:COG4615 431 -----ARARELLERL-ELDHKVSVEDGRFST-TDLSQGQRKRLALLVALLEDRPILVFDEW---------AADQ------ 488
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 746197230 548 mvD-------------------KTVIAIAH--RLSTIAqmDRLIVLDEGKIAE 579
Cdd:COG4615 489 --DpefrrvfytellpelkargKTVIAISHddRYFDLA--DRVLKMDYGKLVE 537
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
361-586 |
4.67e-22 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 95.87 E-value: 4.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLiqlllhfyhLK--------------EGAILIDGQNIED 426
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTL---------LRclnrmndlipgarvEGEILLDGEDIYD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 427 VTQD--SLRANIALVTQDTSLLHRSVAENIKYG---RPDATDHDMQSAVHKA--KAAefipqLVD-LKGRsgyeaqVGER 498
Cdd:COG1117 83 PDVDvvELRRRVGMVFQKPNPFPKSIYDNVAYGlrlHGIKSKSELDEIVEESlrKAA-----LWDeVKDR------LKKS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 499 GVKLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAH------RLStiaqmDRLIVL 572
Cdd:COG1117 152 ALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHnmqqaaRVS-----DYTAFF 226
|
250
....*....|....
gi 746197230 573 DEGKIAEQGTHEEL 586
Cdd:COG1117 227 YLGELVEFGPTEQI 240
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
375-590 |
5.09e-22 |
|
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: 95.20 E-value: 5.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 375 VIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSL-RANIALVTQDTSLLHR-SVAE 452
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIaRLGIGRTFQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 453 NIKYGRPDATDHDMQSAVHKAKAAEFIPQLVDLKGRSGYEAQVGERGVKLSGGQRQRIAIARVFLKDAPILILDEATSAL 532
Cdd:cd03219 95 NVMVAAQARTGSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 746197230 533 -DSEVEAAIQ--SSLNDLmvDKTVIAIAHRLSTIAQM-DRLIVLDEG-KIAEqGTHEElIAKN 590
Cdd:cd03219 175 nPEETEELAEliRELRER--GITVLLVEHDMDVVMSLaDRVTVLDQGrVIAE-GTPDE-VRNN 233
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
380-579 |
9.17e-22 |
|
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: 94.42 E-value: 9.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 380 NLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSL----RANIALVTQDTSLL-HRSVAENI 454
Cdd:COG4181 32 SLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarlrARHVGFVFQSFQLLpTLTALENV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 455 KY-----GRPDAtdhdmqsavhKAKAAEFIPQlVDLKGRSG-YEAQvgergvkLSGGQRQRIAIARVFLKDAPILILDEA 528
Cdd:COG4181 112 MLplelaGRRDA----------RARARALLER-VGLGHRLDhYPAQ-------LSGGEQQRVALARAFATEPAILFADEP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 746197230 529 TSALDSEVEAAIQsslnDLMVDK------TVIAIAHRLSTIAQMDRLIVLDEGKIAE 579
Cdd:COG4181 174 TGNLDAATGEQII----DLLFELnrergtTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
380-588 |
1.45e-21 |
|
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: 96.71 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 380 NLHIKAGEKIGIVGRSGAGKSTLIQLL--LHfyHLKEGAILIDGQniedVTQDSLRA--------NIALVTQDTSLL-HR 448
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIagLE--RPDSGRIRLGGE----VLQDSARGiflpphrrRIGYVFQEARLFpHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 449 SVAENIKYGRPDATDHDMQSAVHkakaaefipQLVDLKGrsgyeaqVG---ERGV-KLSGGQRQRIAIARVFLKDAPILI 524
Cdd:COG4148 93 SVRGNLLYGRKRAPRAERRISFD---------EVVELLG-------IGhllDRRPaTLSGGERQRVAIGRALLSSPRLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 746197230 525 LDEATSALDSEVEAAIQSSLNDLmVDKT---VIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEELIA 588
Cdd:COG4148 157 MDEPLAALDLARKAEILPYLERL-RDELdipILYVSHSLDEVARLaDHVVLLEQGRVVASGPLAEVLS 223
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
376-575 |
1.65e-21 |
|
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: 93.16 E-value: 1.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 376 IDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAI-----LIDGQNIEDVTQDSlRANIALVTQDTSLLHRSV 450
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnkNESEPSFEATRSRN-RYSVAYAAQKPWLLNATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 451 AENIKYGRPdatdHDMQSAVHKAKAAEFIPQLVDLKgrSGYEAQVGERGVKLSGGQRQRIAIARVFLKDAPILILDEATS 530
Cdd:cd03290 96 EENITFGSP----FNKQRYKAVTDACSLQPDIDLLP--FGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 746197230 531 ALDSEV-EAAIQSSLNDLMVD--KTVIAIAHRLSTIAQMDRLIVLDEG 575
Cdd:cd03290 170 ALDIHLsDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
364-588 |
1.73e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 94.77 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 364 KDVTFAYNNKNVIDHFN---LHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANIALVT 440
Cdd:PRK13642 8 ENLVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 441 Q--DTSLLHRSVAENIKYGRPDaTDHDMQSAVHKAKAAEFIPQLVDLKGRsgyeaqvgeRGVKLSGGQRQRIAIARVFLK 518
Cdd:PRK13642 88 QnpDNQFVGATVEDDVAFGMEN-QGIPREEMIKRVDEALLAVNMLDFKTR---------EPARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 746197230 519 DAPILILDEATSALDSEVEAAIQSSLNDLMvDK---TVIAIAHRLSTIAQMDRLIVLDEGKIAEQGTHEELIA 588
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIHEIK-EKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
370-588 |
2.17e-21 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 93.88 E-value: 2.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 370 YNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQD-------------SLRANI 436
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadknqlrLLRTRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 437 ALVTQDTSLL-HRSVAENIkygrpdatdhdMQSAVH-----KAKAAEFIPQLVDLKGRSgyEAQVGERGVKLSGGQRQRI 510
Cdd:PRK10619 95 TMVFQHFNLWsHMTVLENV-----------MEAPIQvlglsKQEARERAVKYLAKVGID--ERAQGKYPVHLSGGQQQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 511 AIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVD-KTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEELIA 588
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
379-589 |
3.03e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 95.03 E-value: 3.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 379 FNLHikAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIED---VTQDSLRANIALVTQD--TSLLHRSVAEN 453
Cdd:PRK11308 36 FTLE--RGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadpEAQKLLRQKIQIVFQNpyGSLNPRKKVGQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 454 IkYGRPDATDHDMQSAVHKAKAAEFIpqlvdlkgrsgyeAQVGERGVK-------LSGGQRQRIAIARVFLKDAPILILD 526
Cdd:PRK11308 114 I-LEEPLLINTSLSAAERREKALAMM-------------AKVGLRPEHydryphmFSGGQRQRIAIARALMLDPDVVVAD 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 746197230 527 EATSALDSEVEAAIqssLNdLMVD------KTVIAIAHRLST---IAqmDRLIVLDEGKIAEQGTHEELIAK 589
Cdd:PRK11308 180 EPVSALDVSVQAQV---LN-LMMDlqqelgLSYVFISHDLSVvehIA--DEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
361-586 |
3.56e-21 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 95.48 E-value: 3.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVtQDSLRaNIALVT 440
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDV-PPAER-GVGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 441 QDTSLL-HRSVAENIKYGrpdatdhdMQSAvhKAKAAEfIPQLVDLKGRSGYEAQVGERGVK-LSGGQRQRIAIARVFLK 518
Cdd:PRK11000 82 QSYALYpHLSVAENMSFG--------LKLA--GAKKEE-INQRVNQVAEVLQLAHLLDRKPKaLSGGQRQRVAIGRTLVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 746197230 519 DAPILILDEATSALDS--EVEAAIQSSLNDLMVDKTVIAIAH---RLSTIAqmDRLIVLDEGKIAEQGTHEEL 586
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAalRVQMRIEISRLHKRLGRTMIYVTHdqvEAMTLA--DKIVVLDAGRVAQVGKPLEL 221
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
358-586 |
6.52e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 92.28 E-value: 6.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 358 QGEIVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLK-----EGAILIDGQNIEDVTQDSL 432
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 433 RANIALVTQ-DTSLLHRSVAENIKYG----RPDATDHDMQSAVHKA--KAaefipQLVD-LKGRSGYEAQvgergvKLSG 504
Cdd:PRK14247 81 RRRVQMVFQiPNPIPNLSIFENVALGlklnRLVKSKKELQERVRWAleKA-----QLWDeVKDRLDAPAG------KLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 505 GQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTH 583
Cdd:PRK14247 150 GQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARIsDYVAFLYKGQIVEWGPT 229
|
...
gi 746197230 584 EEL 586
Cdd:PRK14247 230 REV 232
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
370-586 |
6.57e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 94.38 E-value: 6.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 370 YNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQnieDVTQDSLR-ANIALVTQDTSLL-H 447
Cdd:PRK10851 12 FGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT---DVSRLHARdRKVGFVFQHYALFrH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 448 RSVAENIKYG--------RPDAtdhdmqsAVHKAKAAEFIP--QLVDLKGRsgYEAQvgergvkLSGGQRQRIAIARVFL 517
Cdd:PRK10851 89 MTVFDNIAFGltvlprreRPNA-------AAIKAKVTQLLEmvQLAHLADR--YPAQ-------LSGGQKQRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 746197230 518 KDAPILILDEATSALDSEVEAAIQSSLNDLM--VDKTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEEL 586
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHeeLKFTSVFVTHDQEEAMEVaDRVVVMSQGNIEQAGTPDQV 224
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
376-586 |
7.99e-21 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 94.00 E-value: 7.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 376 IDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRA---NIALVTQD--TSLLHRS- 449
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAvrsDIQMIFQDplASLNPRMt 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 450 ----VAENIKYGRPDATDHDMQSAVhKAKAAE--FIPQLVDlkgRSGYEaqvgergvkLSGGQRQRIAIARVFLKDAPIL 523
Cdd:PRK15079 117 igeiIAEPLRTYHPKLSRQEVKDRV-KAMMLKvgLLPNLIN---RYPHE---------FSGGQCQRIGIARALILEPKLI 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 746197230 524 ILDEATSALDSEVEAAIQSSLNDLM--VDKTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEEL 586
Cdd:PRK15079 184 ICDEPVSALDVSIQAQVVNLLQQLQreMGLSLIFIAHDLAVVKHIsDRVLVMYLGHAVELGTYDEV 249
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
371-577 |
8.38e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 92.46 E-value: 8.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 371 NNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQnieDVTQDSL--RAN-IALVTQD----- 442
Cdd:COG1101 17 NEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGK---DVTKLPEykRAKyIGRVFQDpmmgt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 443 -TSLlhrSVAEN--IKYGRpdATDHDMQSAVHKAKAAEFIPQLVDLKgrSGYE----AQVGergvKLSGGQRQRIAIARV 515
Cdd:COG1101 94 aPSM---TIEENlaLAYRR--GKRRGLRRGLTKKRRELFRELLATLG--LGLEnrldTKVG----LLSGGQRQALSLLMA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 746197230 516 FLKDAPILILDEATSALDSEVeAAIQSSLNDLMVDK---TVIAIAHRLS-TIAQMDRLIVLDEGKI 577
Cdd:COG1101 163 TLTKPKLLLLDEHTAALDPKT-AALVLELTEKIVEEnnlTTLMVTHNMEqALDYGNRLIMMHEGRI 227
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
364-586 |
9.65e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 92.15 E-value: 9.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 364 KDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLK-----EGAILIDGQNIEDVTQDS--LRANI 436
Cdd:PRK14239 9 SDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYSPRTDTvdLRKEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 437 ALVTQDTSLLHRSVAENIKYGRPDATDHDMQ---SAVHKAkaaefipqlvdLKGRSGYEaQVGER----GVKLSGGQRQR 509
Cdd:PRK14239 89 GMVFQQPNPFPMSIYENVVYGLRLKGIKDKQvldEAVEKS-----------LKGASIWD-EVKDRlhdsALGLSGGQQQR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 746197230 510 IAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEEL 586
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRIsDRTGFFLDGDLIEYNDTKQM 234
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
375-590 |
1.54e-20 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 91.25 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 375 VIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSL-RANIALVTQDTSLLHR-SVAE 452
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIaRLGIARTFQNPRLFPElTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 453 NIKYGRPDATDHDMQSAV------------HKAKAAEFIpQLVDLKGRSgyEAQVGErgvkLSGGQRQRIAIARVFLKDA 520
Cdd:COG0411 99 NVLVAAHARLGRGLLAALlrlprarreereARERAEELL-ERVGLADRA--DEPAGN----LSYGQQRRLEIARALATEP 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 746197230 521 PILILDEATSAL-DSEVEAAIQ--SSLNDLMvDKTVIAIAHRLSTIAQM-DRLIVLDEG-KIAEqGTHEElIAKN 590
Cdd:COG0411 172 KLLLLDEPAAGLnPEETEELAEliRRLRDER-GITILLIEHDMDLVMGLaDRIVVLDFGrVIAE-GTPAE-VRAD 243
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
364-595 |
1.57e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 91.79 E-value: 1.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 364 KDVTFAYN-NKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANIALVTQ- 441
Cdd:PRK13652 7 RDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQn 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 442 -DTSLLHRSVAENIKYGrPDATDHDMQSAVHKAKAAEFIPQLVDLKGRSGYEaqvgergvkLSGGQRQRIAIARVFLKDA 520
Cdd:PRK13652 87 pDDQIFSPTVEQDIAFG-PINLGLDEETVAHRVSSALHMLGLEELRDRVPHH---------LSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 746197230 521 PILILDEATSALDSEVEAAIQSSLNDLMVD--KTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEELIAKNGIYAQ 595
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEMaDYIYVMDKGRIVAYGTVEEIFLQPDLLAR 234
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
361-576 |
1.59e-20 |
|
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: 88.27 E-value: 1.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGaILIDGQNIEdvtqdslranIALVT 440
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG-IVTWGSTVK----------IGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 441 QdtsllhrsvaenikygrpdatdhdmqsavhkakaaefipqlvdlkgrsgyeaqvgergvkLSGGQRQRIAIARVFLKDA 520
Cdd:cd03221 70 Q------------------------------------------------------------LSGGEKMRLALAKLLLENP 89
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 746197230 521 PILILDEATSALDSEVEAAIQSSLNDLmvDKTVIAIAH-R--LSTIAqmDRLIVLDEGK 576
Cdd:cd03221 90 NLLLLDEPTNHLDLESIEALEEALKEY--PGTVILVSHdRyfLDQVA--TKIIELEDGK 144
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
356-588 |
2.14e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 94.77 E-value: 2.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 356 VKQGeiVFKDVTfayNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHlKEGAILIDGQNIEDVTQDSL--- 432
Cdd:PRK15134 287 IRKG--ILKRTV---DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNRRQLlpv 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 433 RANIALVTQD--TSLLHR-----SVAENIKYGRPDATDHDMQSAVHKAKAAEFIpqlvDLKGRSGYEAQvgergvkLSGG 505
Cdd:PRK15134 361 RHRIQVVFQDpnSSLNPRlnvlqIIEEGLRVHQPTLSAAQREQQVIAVMEEVGL----DPETRHRYPAE-------FSGG 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 506 QRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDKTV--IAIAHRLSTIAQM-DRLIVLDEGKIAEQGT 582
Cdd:PRK15134 430 QRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRALcHQVIVLRQGEVVEQGD 509
|
....*.
gi 746197230 583 HEELIA 588
Cdd:PRK15134 510 CERVFA 515
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
380-587 |
2.57e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 93.56 E-value: 2.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 380 NLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLR----ANIALVTQDTSLL-HRSVAENI 454
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMpHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 455 KYGRPDAtdhDMQSAVHKAKAAEFIPQLVDLKGRSGYEAQvgergvkLSGGQRQRIAIARVFLKDAPILILDEATSALDS 534
Cdd:PRK10070 128 AFGMELA---GINAEERREKALDALRQVGLENYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 746197230 535 EVEAAIQSSLNDLMV--DKTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEELI 587
Cdd:PRK10070 198 LIRTEMQDELVKLQAkhQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEIL 253
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
364-586 |
6.93e-20 |
|
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: 88.74 E-value: 6.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 364 KDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDV-TQDSLRANIALVTQD 442
Cdd:TIGR03410 4 SNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLpPHERARAGIAYVPQG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 443 TSLLHR-SVAENIKYG---RPDAtdhdmqsavhKAKAAEFI----PQLVDLKGRsgyeaqvgeRGVKLSGGQRQRIAIAR 514
Cdd:TIGR03410 84 REIFPRlTVEENLLTGlaaLPRR----------SRKIPDEIyelfPVLKEMLGR---------RGGDLSGGQQQQLAIAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 746197230 515 VFLKDAPILILDEATSALDSEVEAAIQSSLNDL--MVDKTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEEL 586
Cdd:TIGR03410 145 ALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLraEGGMAILLVEQYLDFARELaDRYYVMERGRVVASGAGDEL 219
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
361-586 |
7.13e-20 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 88.58 E-value: 7.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQnieDVTQDS--LRANIAL 438
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGH---DVVREPreVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 439 VTQDTSLlhrsvaENIKYGRPDATDHDMQSAVHKAKAAEFIPQLVDLKGRsgyeAQVGERGVK-LSGGQRQRIAIARVFL 517
Cdd:cd03265 78 VFQDLSV------DDELTGWENLYIHARLYGVPGAERRERIDELLDFVGL----LEAADRLVKtYSGGMRRRLEIARSLV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 746197230 518 KDAPILILDEATSALDSEVEAAIQSSLNDLM--VDKTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEEL 586
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKeeFGMTILLTTHYMEEAEQLcDRVAIIDHGRIIAEGTPEEL 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
373-579 |
7.80e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 89.75 E-value: 7.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 373 KNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRA---NIALVTQDT------ 443
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAfrrDIQMVFQDSisavnp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 444 -SLLHRSVAENIKygrpdatdH--DMQSAVHKAKAAEFIpQLVDLKgrsgyEAQVGERGVKLSGGQRQRIAIARVFLKDA 520
Cdd:PRK10419 105 rKTVREIIREPLR--------HllSLDKAERLARASEML-RAVDLD-----DSVLDKRPPQLSGGQLQRVCLARALAVEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 746197230 521 PILILDEATSALDSEVEAAIQSSLNDLMvDKTVIA---IAHRLSTIAQM-DRLIVLDEGKIAE 579
Cdd:PRK10419 171 KLLILDEAVSNLDLVLQAGVIRLLKKLQ-QQFGTAclfITHDLRLVERFcQRVMVMDNGQIVE 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
361-589 |
1.01e-19 |
|
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: 92.94 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLL--LHFYHLKEGAIL-------------------- 418
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 419 -------------IDGQNIEDVTQDSLRANIALVTQDTSLLH--RSVAENIKYGRPDAtDHDMQSAVHKAkaAEFIPQlV 483
Cdd:TIGR03269 81 pcpvcggtlepeeVDFWNLSDKLRRRIRKRIAIMLQRTFALYgdDTVLDNVLEALEEI-GYEGKEAVGRA--VDLIEM-V 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 484 DLKGRSGYEAQvgergvKLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDK--TVIAIAHRLS 561
Cdd:TIGR03269 157 QLSHRITHIAR------DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPE 230
|
250 260
....*....|....*....|....*....
gi 746197230 562 TIAQM-DRLIVLDEGKIAEQGTHEELIAK 589
Cdd:TIGR03269 231 VIEDLsDKAIWLENGEIKEEGTPDEVVAV 259
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
375-604 |
1.04e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 93.25 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 375 VIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSL----RANIALVTQDTSLL-HRS 449
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHLLsHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 450 VAENIKYgrpdatdhdmqSAVHKAKA-AEFIPQLVDLKGRSGYEAQVGERGVKLSGGQRQRIAIARVFLKDAPILILDEA 528
Cdd:PRK10535 103 AAQNVEV-----------PAVYAGLErKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 529 TSALDS----EVeAAIQSSLNDLmvDKTVIAIAHRLSTIAQMDRLIVLDEGKI-AEQGTHEELIAKNGIYAQL-----WK 598
Cdd:PRK10535 172 TGALDShsgeEV-MAILHQLRDR--GHTVIIVTHDPQVAAQAERVIEIRDGEIvRNPPAQEKVNVAGGTEPVVntasgWR 248
|
....*.
gi 746197230 599 RQTGGF 604
Cdd:PRK10535 249 QFVSGF 254
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
364-589 |
1.16e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 89.52 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 364 KDVTFAY-NNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQD--SLRANIALVT 440
Cdd:PRK13636 9 EELNYNYsDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlmKLRESVGMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 441 Q--DTSLLHRSVAENIKYGRPDAT--DHDMQSAVHKAKAaefipqlvdlkgRSGYEAQVGERGVKLSGGQRQRIAIARVF 516
Cdd:PRK13636 89 QdpDNQLFSASVYQDVSFGAVNLKlpEDEVRKRVDNALK------------RTGIEHLKDKPTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 746197230 517 LKDAPILILDEATSALD----SEVEAAIQSSLNDLmvDKTVIAIAHRLSTIA-QMDRLIVLDEGKIAEQGTHEELIAK 589
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKEL--GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
361-588 |
1.32e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 89.50 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYN-----NKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQlllHFYHL---KEGAILIDGQNIEDVTQD-- 430
Cdd:PRK13641 3 IKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQ---HFNALlkpSSGTITIAGYHITPETGNkn 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 431 --SLRANIALVTQ--DTSLLHRSVAENIKYGrPDATDHDMQSAvhKAKAAEFIPQL---VDLKGRSGYEaqvgergvkLS 503
Cdd:PRK13641 80 lkKLRKKVSLVFQfpEAQLFENTVLKDVEFG-PKNFGFSEDEA--KEKALKWLKKVglsEDLISKSPFE---------LS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 504 GGQRQRIAIARVFLKDAPILILDEATSALDSEVeaaiQSSLNDLMVD-----KTVIAIAHRLSTIAQ-MDRLIVLDEGKI 577
Cdd:PRK13641 148 GGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG----RKEMMQLFKDyqkagHTVILVTHNMDDVAEyADDVLVLEHGKL 223
|
250
....*....|.
gi 746197230 578 AEQGTHEELIA 588
Cdd:PRK13641 224 IKHASPKEIFS 234
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
361-599 |
1.67e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 89.02 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKN-VIDHFNLHIKAGEKIGIVGRSGAGKSTliqLLLHF---YHLKEGAILIDGQNIEDVTQDSLRANI 436
Cdd:PRK13647 5 IEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKST---LLLHLngiYLPQRGRVKVMGREVNAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 437 ALVTQ--DTSLLHRSVAENIKYGrPDATDHDMQSAVHKAKAAEFIPQLVDLKGRSGYEaqvgergvkLSGGQRQRIAIAR 514
Cdd:PRK13647 82 GLVFQdpDDQVFSSTVWDDVAFG-PVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYH---------LSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 515 VFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVD-KTVIAIAHRLSTIAQ-MDRLIVLDEGKIAEQG-----THEELI 587
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQgKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGdksllTDEDIV 231
|
250
....*....|....*.
gi 746197230 588 AKNG----IYAQLWKR 599
Cdd:PRK13647 232 EQAGlrlpLVAQIFED 247
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
361-589 |
2.43e-19 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 89.90 E-value: 2.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKN-VIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVtQDSLRaNIALV 439
Cdd:PRK11650 4 LKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNEL-EPADR-DIAMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 440 TQDTSLL-HRSVAENIKYG---RPDATDHDMQSAVHKAKAAEfIPQLVDLKGRsgyeaqvgergvKLSGGQRQRIAIARV 515
Cdd:PRK11650 82 FQNYALYpHMSVRENMAYGlkiRGMPKAEIEERVAEAARILE-LEPLLDRKPR------------ELSGGQRQRVAMGRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 516 FLKDAPILILDEATSALDSEVEAAIQSSLNDLmvdktviaiaHR-LSTIA------QM------DRLIVLDEGKIaEQ-G 581
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLDAKLRVQMRLEIQRL----------HRrLKTTSlyvthdQVeamtlaDRVVVMNGGVA-EQiG 217
|
....*...
gi 746197230 582 THEELIAK 589
Cdd:PRK11650 218 TPVEVYEK 225
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
366-587 |
2.43e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 88.12 E-value: 2.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 366 VTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANIALVTQD-TS 444
Cdd:PRK10253 13 LTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNaTT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 445 LLHRSVAENIKYGR----PDAT--DHDMQSAVHKAKAAEFIPQLVDLKGRSgyeaqvgergvkLSGGQRQRIAIARVFLK 518
Cdd:PRK10253 93 PGDITVQELVARGRyphqPLFTrwRKEDEEAVTKAMQATGITHLADQSVDT------------LSGGQRQRAWIAMVLAQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 746197230 519 DAPILILDEATSALDSEVEAAIQSSLNDLMVDK--TVIAIAHRLSTIAQ-MDRLIVLDEGKIAEQGTHEELI 587
Cdd:PRK10253 161 ETAIMLLDEPTTWLDISHQIDLLELLSELNREKgyTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIV 232
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
359-595 |
2.49e-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: 88.37 E-value: 2.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 359 GEIVFKDVTFAYNNKN--VIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLkEGAILIDGQNIEDVTQDSLRANI 436
Cdd:cd03289 1 GQMTVKDLTAKYTEGGnaVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 437 ALVTQDTSLLHRSVAENIK-YGRpdATDHDMQSAVHKAKAAEFIPQLVDlkgrsGYEAQVGERGVKLSGGQRQRIAIARV 515
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDpYGK--WSDEEIWKVAEEVGLKSVIEQFPG-----QLDFVLVDGGCVLSHGHKQLMCLARS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 516 FLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIAQMDRLIVLDEGKIAEQGTHEELIAKNGIYAQ 595
Cdd:cd03289 153 VLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQ 232
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
364-588 |
2.58e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 88.21 E-value: 2.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 364 KDVTFAYNN-KNVIDHFNLHIKAGEKIGIVGRSGAGKSTLiqlLLHF---YHLKEGAILIDGQNIeDVTQDSL---RANI 436
Cdd:PRK13639 5 RDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTL---FLHFngiLKPTSGEVLIKGEPI-KYDKKSLlevRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 437 ALVTQ--DTSLLHRSVAENIKYGrPDATDHDMQSAVHKAKAAefipqlvdLK--GRSGYEAQVGERgvkLSGGQRQRIAI 512
Cdd:PRK13639 81 GIVFQnpDDQLFAPTVEEDVAFG-PLNLGLSKEEVEKRVKEA--------LKavGMEGFENKPPHH---LSGGQKKRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 746197230 513 ARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIA-HRLSTIA-QMDRLIVLDEGKIAEQGTHEELIA 588
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVPvYADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
376-581 |
5.88e-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: 86.37 E-value: 5.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 376 IDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLraniaLVTQDTSLLH-RSVAENI 454
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 455 kYGRPDATDHDMQSAVHKAKAAEFIpQLVDLKgrsgyEAQvGERGVKLSGGQRQRIAIARVFLKDAPILILDEATSALDS 534
Cdd:TIGR01184 76 -ALAVDRVLPDLSKSERRAIVEEHI-ALVGLT-----EAA-DKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 746197230 535 EVEAAIQSSLNDLMVDK--TVIAIAHRL-STIAQMDRLIVLDEGKIAEQG 581
Cdd:TIGR01184 148 LTRGNLQEELMQIWEEHrvTVLMVTHDVdEALLLSDRVVMLTNGPAANIG 197
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
360-586 |
6.72e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 87.83 E-value: 6.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 360 EIVFKDVTFAYNNK-----NVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQ----LLL-------HFY---HLKEGAILID 420
Cdd:PRK13651 2 QIKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEhlnaLLLpdtgtieWIFkdeKNKKKTKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 421 GQNIEDVTQDS----------LRANIALVTQ--DTSLLHRSVAENIKYGrpdATDHDMQSAVHKAKAAEFIpQLVDLK-- 486
Cdd:PRK13651 82 KVLEKLVIQKTrfkkikkikeIRRRVGVVFQfaEYQLFEQTIEKDIIFG---PVSMGVSKEEAKKRAAKYI-ELVGLDes 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 487 --GRSGYEaqvgergvkLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVD-KTVIAIAHRLSTI 563
Cdd:PRK13651 158 ylQRSPFE---------LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNV 228
|
250 260
....*....|....*....|....*
gi 746197230 564 AQ-MDRLIVLDEGKIAEQG-THEEL 586
Cdd:PRK13651 229 LEwTKRTIFFKDGKIIKDGdTYDIL 253
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
364-576 |
7.21e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 89.99 E-value: 7.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 364 KDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLL--LHFYHLKEGAILIDGQNIEDVT-QDSLRANIALVT 440
Cdd:PRK13549 9 KNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLsgVYPHGTYEGEIIFEGEELQASNiRDTERAGIAIIH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 441 QDTSLL-HRSVAENIKYGRPDATDHDMQSAVHKAKAAEFIPQL-----VDLKgrsgyeaqVGErgvkLSGGQRQRIAIAR 514
Cdd:PRK13549 89 QELALVkELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLkldinPATP--------VGN----LGLGQQQLVEIAK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 746197230 515 VFLKDAPILILDEATSALdSEVEAAIqssLNDLMVD-----KTVIAIAHRLSTIAQM-DRLIVLDEGK 576
Cdd:PRK13549 157 ALNKQARLLILDEPTASL-TESETAV---LLDIIRDlkahgIACIYISHKLNEVKAIsDTICVIRDGR 220
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
359-588 |
8.25e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 86.99 E-value: 8.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 359 GEIVFKDVTFAYNNKN-----VIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDG----QNIEDVTQ 429
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 430 -DSLRANIALVTQ--DTSLLHRSVAENIKYGrPDATDHDMQSAVHKakaaefIPQLVDLKgrSGYEAQVGERGVKLSGGQ 506
Cdd:PRK13645 85 vKRLRKEIGLVFQfpEYQLFQETIEKDIAFG-PVNLGENKQEAYKK------VPELLKLV--QLPEDYVKRSPFELSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 507 RQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVD--KTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTH 583
Cdd:PRK13645 156 KRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVLRIaDEVIVMHEGKVISIGSP 235
|
....*
gi 746197230 584 EELIA 588
Cdd:PRK13645 236 FEIFS 240
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
363-558 |
1.18e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.35 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 363 FKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGqniedvtqdslRANIALVTQD 442
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 443 TSLL-HRSVAENIKYGRPDATD--HDMQSAVHK--------AKAAEFIPQLVDLKGRSgYEAQVGE-------------R 498
Cdd:COG0488 70 PPLDdDLTVLDTVLDGDAELRAleAELEELEAKlaepdedlERLAELQEEFEALGGWE-AEARAEEilsglgfpeedldR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 746197230 499 GVK-LSGGQRQRIAIARVFLKDAPILILDEATSALDSEveaAIQ---SSLNDLmvDKTVIAIAH 558
Cdd:COG0488 149 PVSeLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLE---SIEwleEFLKNY--PGTVLVVSH 207
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
375-580 |
1.22e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 86.07 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 375 VIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQnieDVTQDSlrANIALVTQDTSLLH-RSVAEN 453
Cdd:COG4525 22 ALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV---PVTGPG--ADRGVVFQKDALLPwLNVLDN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 454 IKY-----GRPDATDHdmqsavhkAKAAEFIpQLVDLKGrsgyeaqVGERGV-KLSGGQRQRIAIARVFLKDAPILILDE 527
Cdd:COG4525 97 VAFglrlrGVPKAERR--------ARAEELL-ALVGLAD-------FARRRIwQLSGGMRQRVGIARALAADPRFLLMDE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 746197230 528 ATSALDSEVEAAIQSSLNDLMVD--KTVIAIAHR------LSTiaqmdRLIVLD--EGKIAEQ 580
Cdd:COG4525 161 PFGALDALTREQMQELLLDVWQRtgKGVFLITHSveealfLAT-----RLVVMSpgPGRIVER 218
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
360-584 |
1.36e-18 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 85.45 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 360 EIVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDG------QNIEDVTQDSLR 433
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 434 ANIALVTQDTSLL-HRSVAENIKYGRPDATDHDMQSAVHKAKAAEFIPQLVDLKGRsgYEAQvgergvkLSGGQRQRIAI 512
Cdd:COG4161 82 QKVGMVFQQYNLWpHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADR--FPLH-------LSGGQQQRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 746197230 513 ARVFLKDAPILILDEATSALDSEVEAAIQSSLNDL-MVDKTVIAIAHRLS---TIAQmdRLIVLDEGKIAEQGTHE 584
Cdd:COG4161 153 ARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELsQTGITQVIVTHEVEfarKVAS--QVVYMEKGRIIEQGDAS 226
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
359-577 |
2.27e-18 |
|
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: 83.25 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 359 GEIVF--KDVTfaynNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIE-DVTQDSLRAN 435
Cdd:cd03215 1 GEPVLevRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTrRSPRDAIRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 436 IALVTQDTS----LLHRSVAENIkygrpdatdhdmqsavhkakaaeFIPQLvdlkgrsgyeaqvgergvkLSGGQRQRIA 511
Cdd:cd03215 77 IAYVPEDRKreglVLDLSVAENI-----------------------ALSSL-------------------LSGGNQQKVV 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 746197230 512 IARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVD-KTVIAIAHRLSTIAQM-DRLIVLDEGKI 577
Cdd:cd03215 115 LARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAgKAVLLISSELDELLGLcDRILVMYEGRI 182
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
369-572 |
2.76e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 83.05 E-value: 2.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 369 AYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGqniedvtqdslRANIALVTQDTSL--- 445
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEVpds 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 446 LHRSVAENIKYG---------RPDATDHdmqSAVHKAKAAefiPQLVDLKGRsgyeaQVGErgvkLSGGQRQRIAIARVF 516
Cdd:NF040873 70 LPLTVRDLVAMGrwarrglwrRLTRDDR---AAVDDALER---VGLADLAGR-----QLGE----LSGGQRQRALLAQGL 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 746197230 517 LKDAPILILDEATSALDSEVEAAIQSSLNDLMVDK-TVIAIAHRLSTIAQMDRLIVL 572
Cdd:NF040873 135 AQEADLLLLDEPTTGLDAESRERIIALLAEEHARGaTVVVVTHDLELVRRADPCVLL 191
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
354-586 |
2.99e-18 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 86.32 E-value: 2.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 354 LAVKQGEIVFK----DVTfAYNNKNvidhFNLHikAGEKIGIVGRSGAGKS-TLIQL--LLHFYHLKEGAILIDGQNIED 426
Cdd:PRK09473 13 LDVKDLRVTFStpdgDVT-AVNDLN----FSLR--AGETLGIVGESGSGKSqTAFALmgLLAANGRIGGSATFNGREILN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 427 VTQ---DSLRA-NIALVTQD--TSL---------------LHRsvaeniKYGRPDATDHD--MQSAVHkakaaefIPQLV 483
Cdd:PRK09473 86 LPEkelNKLRAeQISMIFQDpmTSLnpymrvgeqlmevlmLHK------GMSKAEAFEESvrMLDAVK-------MPEAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 484 DLKGRSGYEaqvgergvkLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVD--KTVIAIAHRLS 561
Cdd:PRK09473 153 KRMKMYPHE---------FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfnTAIIMITHDLG 223
|
250 260
....*....|....*....|....*.
gi 746197230 562 TIAQM-DRLIVLDEGKIAEQGTHEEL 586
Cdd:PRK09473 224 VVAGIcDKVLVMYAGRTMEYGNARDV 249
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
40-311 |
3.82e-18 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 85.29 E-value: 3.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 40 LLLLVICTAGAATFEALLFSKIGQLVDWLSKSQPESFLsqhASNILILISVLFANILFVNIQSII----KHQILYstfpm 115
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLL---LWIALLLLLLALLRALLSYLRRYLaarlGQRVVF----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 116 RLRWRFHNLLLKQSLDFFHNDFAGRLSAKVMQTALAIREFwiILGDMLAYVS--IYFITVSIVLGAISPTLLIPLMVWLG 193
Cdd:cd07346 73 DLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNL--VSSGLLQLLSdvLTLIGALVILFYLNWKLTLVALLLLP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 194 LFLLSAWFFIPRLSKVSQQQADARAVMTGRVTDAYTNIQTVKLFAHAGRESQYAKASMKEFMTTVYAQMRLGTLFEVSIN 273
Cdd:cd07346 151 LYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIG 230
|
250 260 270
....*....|....*....|....*....|....*...
gi 746197230 274 MLSAVLFVGVIGTAVWLWTQGLAALGVIAATTAMILKL 311
Cdd:cd07346 231 LLTALGTALVLLYGGYLVLQGSLTIGELVAFLAYLGML 268
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
355-588 |
4.33e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 87.38 E-value: 4.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 355 AVKQGEIVF--KDVTfaynNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIE-DVTQDS 431
Cdd:COG1129 249 AAAPGEVVLevEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRiRSPRDA 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 432 LRANIALVTQD---TSL-LHRSVAENI------KYGRPDATDHDMQSAVhkakAAEFIPQLvDLKGRSGyEAQVGErgvk 501
Cdd:COG1129 325 IRAGIAYVPEDrkgEGLvLDLSIRENItlasldRLSRGGLLDRRRERAL----AEEYIKRL-RIKTPSP-EQPVGN---- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 502 LSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLmVD--KTVIAIAHRLSTIAQM-DRLIVLDEGKIA 578
Cdd:COG1129 395 LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIREL-AAegKAVIVISSELPELLGLsDRILVMREGRIV 473
|
250
....*....|....*
gi 746197230 579 -----EQGTHEELIA 588
Cdd:COG1129 474 geldrEEATEEAIMA 488
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
361-566 |
4.89e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 84.32 E-value: 4.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLK-----EGAILIDGQNIED--VTQDSLR 433
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIYErrVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 434 ANIALVTQDTSLLHRSVAENIKYG------RPDAT-DHDMQSAVhkaKAAEFIPQLvdlkgrsgyEAQVGERGVKLSGGQ 506
Cdd:PRK14258 88 RQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEiDDIVESAL---KDADLWDEI---------KHKIHKSALDLSGGQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 746197230 507 RQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMV--DKTVIAIAHRLSTIAQM 566
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLrsELTMVIVSHNLHQVSRL 217
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
361-584 |
5.20e-18 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 83.91 E-value: 5.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIeDVTQD-------SLR 433
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHF-DFSKTpsdkairELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 434 ANIALVTQDTSLL-HRSVAENIKYGRPDATDHDMQSAVHKAKAAEFIPQLVDLKGRsgYEAQvgergvkLSGGQRQRIAI 512
Cdd:PRK11124 82 RNVGMVFQQYNLWpHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADR--FPLH-------LSGGQQQRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 746197230 513 ARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDK-TVIAIAHRLStIAQ--MDRLIVLDEGKIAEQGTHE 584
Cdd:PRK11124 153 ARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGiTQVIVTHEVE-VARktASRVVYMENGHIVEQGDAS 226
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
375-575 |
6.61e-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: 83.25 E-value: 6.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 375 VIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILI--DGQNIeDVTQDSLRANIAL-------VTQ---- 441
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWV-DLAQASPREILALrrrtigyVSQflrv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 442 -------DT---SLLHRSVAEnikygrpdatdhdmqsAVHKAKAAEFIPQLvdlkgrsgyeaQVGERgvkL--------S 503
Cdd:COG4778 105 iprvsalDVvaePLLERGVDR----------------EEARARARELLARL-----------NLPER---LwdlppatfS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 746197230 504 GGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDKT-VIAIAHRLSTIAQM-DRLIVLDEG 575
Cdd:COG4778 155 GGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTaIIGIFHDEEVREAVaDRVVDVTPF 228
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
363-581 |
8.17e-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: 82.33 E-value: 8.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 363 FKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIedvtQDSLRANIALVTQD 442
Cdd:cd03269 3 VENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL----DIAARNRIGYLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 443 TSL-LHRSVAENIKYGrpdATDHDMQsavhKAKAAEFIPQLVDLKGRSGYEAQVGErgvKLSGGQRQRIAIARVFLKDAP 521
Cdd:cd03269 79 RGLyPKMKVIDQLVYL---AQLKGLK----KEEARRRIDEWLERLELSEYANKRVE---ELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 746197230 522 ILILDEATSALDSEVEAAIQSSLNDLMVD-KTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQG 581
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVEELcDRVLLLNKGRAVLYG 210
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
375-586 |
8.55e-18 |
|
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: 84.14 E-value: 8.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 375 VIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQniedvtqdslranIALVTQDTSLLHRSVAENI 454
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 455 KYGRpDATDHDMQSAVHKAKAAEFIPQLVDLKgrsgyEAQVGERGVKLSGGQRQRIAIARVFLKDAPILILDEATSALDS 534
Cdd:cd03291 119 IFGV-SYDEYRYKSVVKACQLEEDITKFPEKD-----NTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 746197230 535 EVEAAI-QSSLNDLMVDKTVIAIAHRLSTIAQMDRLIVLDEGKIAEQGTHEEL 586
Cdd:cd03291 193 FTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
370-588 |
1.30e-17 |
|
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: 82.21 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 370 YNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQnieDVTQDSL----RANIALVTQDTSL 445
Cdd:cd03218 10 YGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQ---DITKLPMhkraRLGIGYLPQEASI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 446 LHR-SVAENIK-----YGRPDATDHdmqsavHKAKA--AEFipQLVDLKGRSGYeaqvgergvKLSGGQRQRIAIARVFL 517
Cdd:cd03218 87 FRKlTVEENILavleiRGLSKKERE------EKLEEllEEF--HITHLRKSKAS---------SLSGGERRRVEIARALA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 746197230 518 KDAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIA-HRLS-TIAQMDRLIVLDEGKIAEQGTHEELIA 588
Cdd:cd03218 150 TNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
364-587 |
1.97e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 82.53 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 364 KDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANIALVTQDT 443
Cdd:PRK10575 15 RNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 444 SLLH-RSVAENIKYGR-PDATDHDMQSAVHKAKAAEFIpQLVDLKgrsgyeaQVGERGV-KLSGGQRQRIAIARVFLKDA 520
Cdd:PRK10575 95 PAAEgMTVRELVAIGRyPWHGALGRFGAADREKVEEAI-SLVGLK-------PLAHRLVdSLSGGERQRAWIAMLVAQDS 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 746197230 521 PILILDEATSALD----SEVEAAIQ--SSLNDLmvdkTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEELI 587
Cdd:PRK10575 167 RCLLLDEPTSALDiahqVDVLALVHrlSQERGL----TVIAVLHDINMAARYcDYLVALRGGEMIAQGTPAELM 236
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
361-573 |
3.58e-17 |
|
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: 79.12 E-value: 3.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAY-NNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAIlidgqniedvtqdslranialv 439
Cdd:cd03223 1 IELENLSLATpDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 440 tqdtsllhrsvaenikyGRPDATDHdmqsavhkakaaEFIPQLvdlkgrsGYEAQVGERGV-------KLSGGQRQRIAI 512
Cdd:cd03223 59 -----------------GMPEGEDL------------LFLPQR-------PYLPLGTLREQliypwddVLSGGEQQRLAF 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 746197230 513 ARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVdkTVIAIAHRLSTIAQMDRLIVLD 573
Cdd:cd03223 103 ARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGI--TVISVGHRPSLWKFHDRVLDLD 161
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
350-535 |
9.30e-17 |
|
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: 78.94 E-value: 9.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 350 EAKPLAVKQGE-IVFKDVTFaynnknvidhfnlHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDvT 428
Cdd:TIGR01189 2 AARNLACSRGErMLFEGLSF-------------TLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE-Q 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 429 QDSLRANIALvtqdtsLLHR-------SVAENIKYGRPDATDHdmQSAVHKAKAAefipqlVDLKGRSGYEAQvgergvK 501
Cdd:TIGR01189 68 RDEPHENILY------LGHLpglkpelSALENLHFWAAIHGGA--QRTIEDALAA------VGLTGFEDLPAA------Q 127
|
170 180 190
....*....|....*....|....*....|....
gi 746197230 502 LSGGQRQRIAIARVFLKDAPILILDEATSALDSE 535
Cdd:TIGR01189 128 LSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
377-614 |
1.11e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.04 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 377 DHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIE-DVTQDSLRANIALVTQDTSLL-HRSVAENI 454
Cdd:PRK11288 21 DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGVAIIYQELHLVpEMTVAENL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 455 KYGRPDATDHDMQSAVHKAKAAEfipQLVDLKGRSGYEAQVGErgvkLSGGQRQRIAIARVFLKDAPILILDEATSALDS 534
Cdd:PRK11288 101 YLGQLPHKGGIVNRRLLNYEARE---QLEHLGVDIDPDTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTSSLSA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 535 EVEAAIQSSLNDLMVD-KTVIAIAHRLSTIAQM-DRLIVLDEGKIAE------QGTHEELIAK------NGIYAqlWK-R 599
Cdd:PRK11288 174 REIEQLFRVIRELRAEgRVILYVSHRMEEIFALcDAITVFKDGRYVAtfddmaQVDRDQLVQAmvgreiGDIYG--YRpR 251
|
250
....*....|....*
gi 746197230 600 QTGGFLIEQKVVQGQ 614
Cdd:PRK11288 252 PLGEVRLRLDGLKGP 266
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
375-589 |
1.44e-16 |
|
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: 83.81 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 375 VIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQniedvtqdslranIALVTQDTSLLHRSVAENI 454
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 455 KYGRpdATDHDMQSAVHKAKAAEFIPQLVDLKGRSgyeaQVGERGVKLSGGQRQRIAIARVFLKDAPILILDEATSALDS 534
Cdd:TIGR01271 508 IFGL--SYDEYRYTSVIKACQLEEDIALFPEKDKT----VLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 746197230 535 EVEAAI-QSSLNDLMVDKTVIAIAHRLSTIAQMDRLIVLDEGKIAEQGTHEELIAK 589
Cdd:TIGR01271 582 VTEKEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAK 637
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
353-594 |
1.64e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 81.05 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 353 PLAVKQGEIV-FKDVTFAYNNKN-----VIDHFNLHIKAGEKIGIVGRSGAGKSTLIQlllHFYHL---KEGAILID--- 420
Cdd:PRK13631 13 PNPLSDDIILrVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVT---HFNGLiksKYGTIQVGdiy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 421 -GQNIEDVTQDS------------LRANIALVTQ--DTSLLHRSVAENIKYGrPDATDhdmQSAVHKAKAAEFIPQLVDL 485
Cdd:PRK13631 90 iGDKKNNHELITnpyskkiknfkeLRRRVSMVFQfpEYQLFKDTIEKDIMFG-PVALG---VKKSEAKKLAKFYLNKMGL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 486 KG----RSGYEaqvgergvkLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEaaiqSSLNDLMVD-----KTVIAI 556
Cdd:PRK13631 166 DDsyleRSPFG---------LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGE----HEMMQLILDakannKTVFVI 232
|
250 260 270
....*....|....*....|....*....|....*....
gi 746197230 557 AHRLSTIAQM-DRLIVLDEGKIAEQGTHEELIAKNGIYA 594
Cdd:PRK13631 233 THTMEHVLEVaDEVIVMDKGKILKTGTPYEIFTDQHIIN 271
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
370-579 |
1.69e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 79.74 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 370 YNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTqdslrANIALVTQDTSLLH-R 448
Cdd:PRK11248 11 YGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-----AERGVVFQNEGLLPwR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 449 SVAENIKYGRPDAtdhDMQSAVHKAKAAEFIpQLVDLKGrsgyeaqVGERGV-KLSGGQRQRIAIARVFLKDAPILILDE 527
Cdd:PRK11248 86 NVQDNVAFGLQLA---GVEKMQRLEIAHQML-KKVGLEG-------AEKRYIwQLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 746197230 528 ATSALDSEVEAAIQSSLNDLMVD--KTVIAIAHRLSTIAQMDRLIVL---DEGKIAE 579
Cdd:PRK11248 155 PFGALDAFTREQMQTLLLKLWQEtgKQVLLITHDIEEAVFMATELVLlspGPGRVVE 211
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
367-586 |
2.55e-16 |
|
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: 78.32 E-value: 2.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 367 TFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDvTQDSLRANIALVTQDTSLL 446
Cdd:cd03263 9 TYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 447 HR-SVAENIKY-----GRPdatDHDMQSAVHKAKaaefipQLVDLKgrsgyeaQVGERGVK-LSGGQRQRIAIARVFLKD 519
Cdd:cd03263 88 DElTVREHLRFyarlkGLP---KSEIKEEVELLL------RVLGLT-------DKANKRARtLSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 746197230 520 APILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEEL 586
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALcDRIAIMSDGKLRCIGSPQEL 219
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
382-586 |
2.82e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 82.40 E-value: 2.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 382 HIKAGEKIGIVGRSGAGKSTLIQLLLhFYHLK----EGAILIDGQNIEdvtQDSLRANIALVTQDTSLL-HRSVAENIKY 456
Cdd:TIGR00955 47 VAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMPID---AKEMRAISAYVQQDDLFIpTLTVREHLMF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 457 grpdaTDH-DMQSAVHKAKAAEFIPQLV-DLKGRSGYEAQVGERGVK--LSGGQRQRIAIARVFLKDAPILILDEATSAL 532
Cdd:TIGR00955 123 -----QAHlRMPRRVTKKEKRERVDEVLqALGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGL 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 746197230 533 DSEVEAAIQSSLNDL-MVDKTVIAIAHRLST--IAQMDRLIVLDEGKIAEQGTHEEL 586
Cdd:TIGR00955 198 DSFMAYSVVQVLKGLaQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
361-586 |
4.23e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 79.38 E-value: 4.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTqdslRANIALVT 440
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 441 QDTSLLHR-SVAENIKY-GRPdatdHDMQSAVHKAKAAEFIPQLvDLKGRSGYEAQvgergvKLSGGQRQRIAIARVFLK 518
Cdd:COG4152 78 EERGLYPKmKVGEQLVYlARL----KGLSKAEAKRRADEWLERL-GLGDRANKKVE------ELSKGNQQKVQLIAALLH 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 746197230 519 DAPILILDEATSALDseveaaiqsSLN-DLMVD---------KTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEEL 586
Cdd:COG4152 147 DPELLILDEPFSGLD---------PVNvELLKDvirelaakgTTVIFSSHQMELVEELcDRIVIINKGRKVLSGSVDEI 216
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
380-596 |
4.26e-16 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 82.52 E-value: 4.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 380 NLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDgqniedvtqdslrANIALVTQDTSLLHRSVAENIKYGRP 459
Cdd:PTZ00243 680 SVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRGNILFFDE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 460 DATDhDMQSAVHKAKAAEFIPQLvdlkgRSGYEAQVGERGVKLSGGQRQRIAIARVFLKDAPILILDEATSALDSEV-EA 538
Cdd:PTZ00243 747 EDAA-RLADAVRVSQLEADLAQL-----GGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgER 820
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 746197230 539 AIQSSLNDLMVDKTVIAIAHRLSTIAQMDRLIVLDEGKIAEQGTHEELiAKNGIYAQL 596
Cdd:PTZ00243 821 VVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADF-MRTSLYATL 877
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
350-540 |
4.53e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.22 E-value: 4.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 350 EAKPLAVKQGE-IVFKDVTFaynnknvidhfnlHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDvt 428
Cdd:PRK13539 4 EGEDLACVRGGrVLFSGLSF-------------TLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDD-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 429 qDSLRANIA-LVTQDTSLLHRSVAENIK-----YGRPDatdhdmqSAVHKAKAAEFIPQLVDLKGrsGYeaqvgergvkL 502
Cdd:PRK13539 69 -PDVAEACHyLGHRNAMKPALTVAENLEfwaafLGGEE-------LDIAAALEAVGLAPLAHLPF--GY----------L 128
|
170 180 190
....*....|....*....|....*....|....*...
gi 746197230 503 SGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAI 540
Cdd:PRK13539 129 SAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALF 166
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
370-589 |
5.56e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 79.36 E-value: 5.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 370 YNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNI-EDvtQDSLRANIALV----TQ--- 441
Cdd:COG4586 32 YREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPfKR--RKEFARRIGVVfgqrSQlww 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 442 -----DTSLLHRSVaenikYGRPDAtdhdmqsaVHKAKAAEFIpQLVDLKG------RsgyeaqvgergvKLSGGQRQRI 510
Cdd:COG4586 110 dlpaiDSFRLLKAI-----YRIPDA--------EYKKRLDELV-ELLDLGElldtpvR------------QLSLGQRMRC 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 511 AIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDK--TVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEELI 587
Cdd:COG4586 164 ELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMDDIEALcDRVIVIDHGRIIYDGSLEELK 243
|
..
gi 746197230 588 AK 589
Cdd:COG4586 244 ER 245
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
380-585 |
5.93e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 79.53 E-value: 5.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 380 NLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQD-SL---RANIALVTQDTSLL-HRSVAENI 454
Cdd:PRK11144 18 NLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGiCLppeKRRIGYVFQDARLFpHYKVRGNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 455 KYGrpdatdhdmqsaVHKAKAAEFiPQLVDLKGrsgYEAQVGERGVKLSGGQRQRIAIARVFLKDAPILILDEATSALD- 533
Cdd:PRK11144 98 RYG------------MAKSMVAQF-DKIVALLG---IEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDl 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 746197230 534 ---SEVEAAIQSSLNDlmVDKTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEE 585
Cdd:PRK11144 162 prkRELLPYLERLARE--INIPILYVSHSLDEILRLaDRVVVLEQGKVKAFGPLEE 215
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
364-533 |
6.43e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 76.75 E-value: 6.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 364 KDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLK---EGAILIDGQNIEDVtqDSLRANIALVT 440
Cdd:COG4136 5 ENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTAL--PAEQRRIGILF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 441 QDtSLL--HRSVAENIKYGRPDATDHdmqsAVHKAKAAEFIPQlVDLKGRsgyeaqvGERGVK-LSGGQRQRIAIARVFL 517
Cdd:COG4136 83 QD-DLLfpHLSVGENLAFALPPTIGR----AQRRARVEQALEE-AGLAGF-------ADRDPAtLSGGQRARVALLRALL 149
|
170
....*....|....*.
gi 746197230 518 KDAPILILDEATSALD 533
Cdd:COG4136 150 AEPRALLLDEPFSKLD 165
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
375-589 |
7.91e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 77.43 E-value: 7.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 375 VIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGqniedvtqdslraNIAlvtqdtSLL------HR 448
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-------------RVS------ALLelgagfHP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 449 --SVAENIK-----YGrpdATDHDMQSAVhkAKAAEFipqlvdlkgrsgyeAQVGE---RGVK-LSGGQRQRIAIARVFL 517
Cdd:COG1134 102 elTGRENIYlngrlLG---LSRKEIDEKF--DEIVEF--------------AELGDfidQPVKtYSSGMRARLAFAVATA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 746197230 518 KDAPILILDEATSALDSE----VEAAIQSSLNDlmvDKTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEELIAK 589
Cdd:COG1134 163 VDPDILLVDEVLAVGDAAfqkkCLARIRELRES---GRTVIFVSHSMGAVRRLcDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
364-591 |
7.93e-16 |
|
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: 76.41 E-value: 7.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 364 KDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHF--YHLKEGAILIDGQNIEDV-TQDSLRANIALVT 440
Cdd:cd03217 4 KDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLpPEERARLGIFLAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 441 QdtsllhrsvaenikygRPdatdhdmqSAVHKAKAAEFIpqlvdlkgrsgyeaqvgeRGV--KLSGGQRQRIAIARVFLK 518
Cdd:cd03217 84 Q----------------YP--------PEIPGVKNADFL------------------RYVneGFSGGEKKRNEILQLLLL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 519 DAPILILDEATSALD----SEVEAAIQSSLNDlmvDKTVIAIAH--RLSTIAQMDRLIVLDEGKIAEQGTHE--ELIAKN 590
Cdd:cd03217 122 EPDLAILDEPDSGLDidalRLVAEVINKLREE---GKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKElaLEIEKK 198
|
.
gi 746197230 591 G 591
Cdd:cd03217 199 G 199
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
355-586 |
8.15e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 77.78 E-value: 8.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 355 AVKQGEIVFkDVTFAY---NNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLL---LHFYHLK---EGAILIDGQNIE 425
Cdd:PRK14246 3 AGKSAEDVF-NISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLnrlIEIYDSKikvDGKVLYFGKDIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 426 DVTQDSLRANIALVTQDTSLL-HRSVAENIKYgrpdatdhDMQSavHKAKAAEFIPQLVDLKGRS-GYEAQVGER----G 499
Cdd:PRK14246 82 QIDAIKLRKEVGMVFQQPNPFpHLSIYDNIAY--------PLKS--HGIKEKREIKKIVEECLRKvGLWKEVYDRlnspA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 500 VKLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIAQM-DRLIVLDEGKIA 578
Cdd:PRK14246 152 SQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVaDYVAFLYNGELV 231
|
....*...
gi 746197230 579 EQGTHEEL 586
Cdd:PRK14246 232 EWGSSNEI 239
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
364-596 |
9.83e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 77.03 E-value: 9.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 364 KDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLL-H-FYHLKEGAILIDGQNIEDVTQDSlRAN--IALV 439
Cdd:COG0396 4 KNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMgHpKYEVTSGSILLDGEDILELSPDE-RARagIFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 440 TQD---------TSLLHRsvAENIKYGRPdatdhdmqsavhkAKAAEFIPQLVDLKGRSGYEAQVGERGV--KLSGGQRQ 508
Cdd:COG0396 83 FQYpveipgvsvSNFLRT--ALNARRGEE-------------LSAREFLKLLKEKMKELGLDEDFLDRYVneGFSGGEKK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 509 RIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMV-DKTVIAIAH--RLSTIAQMDRLIVLDEGKIAEQGTHE- 584
Cdd:COG0396 148 RNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSpDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGKEl 227
|
250
....*....|...
gi 746197230 585 -ELIAKNGiYAQL 596
Cdd:COG0396 228 aLELEEEG-YDWL 239
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
379-588 |
9.98e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 80.05 E-value: 9.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 379 FNLHikAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVT-QDSLRANIALVTQDTS----LLHRSVAEN 453
Cdd:PRK10762 273 FTLR--KGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpQDGLANGIVYISEDRKrdglVLGMSVKEN 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 454 IKYGRPDATDHDMQSAVHKAK---AAEFIpQLVDLKGRSgYEAQVGergvKLSGGQRQRIAIARVFLKDAPILILDEATS 530
Cdd:PRK10762 351 MSLTALRYFSRAGGSLKHADEqqaVSDFI-RLFNIKTPS-MEQAIG----LLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 746197230 531 ALDSEVEAAIQSSLNDLMVDK-TVIAIAHRLSTIAQM-DRLIVLDEGKI-----AEQGTHEELIA 588
Cdd:PRK10762 425 GVDVGAKKEIYQLINQFKAEGlSIILVSSEMPEVLGMsDRILVMHEGRIsgeftREQATQEKLMA 489
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
376-588 |
1.01e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 80.23 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 376 IDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILID-GQNIEDVTQDSL----RAN--IALVTQDTSLL-H 447
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGPdgrgRAKryIGILHQEYDLYpH 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 448 RSVAEN----IKYGRPDatDHDMQSAVHKAKAAEFipqlVDLKGRSGYEAQVGErgvkLSGGQRQRIAIARVFLKDAPIL 523
Cdd:TIGR03269 380 RTVLDNlteaIGLELPD--ELARMKAVITLKMVGF----DEEKAEEILDKYPDE----LSEGERHRVALAQVLIKEPRIV 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 524 ILDEATSALDS----EVEAAIQSSLNDLmvDKTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEELIA 588
Cdd:TIGR03269 450 ILDEPTGTMDPitkvDVTHSILKAREEM--EQTFIIVSHDMDFVLDVcDRAALMRDGKIVKIGDPEEIVE 517
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
376-576 |
1.20e-15 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 79.77 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 376 IDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIE-DVTQDSLRANIALVTQDTSL-LHRSVAEN 453
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQELNLvLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 454 IKYGR-PDA---TDHDmqsAVHKAKAAEFIPQLVDLKGRsgyeaqvgERGVKLSGGQRQRIAIARVFLKDAPILILDEAT 529
Cdd:PRK10982 94 MWLGRyPTKgmfVDQD---KMYRDTKAIFDELDIDIDPR--------AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 746197230 530 SAL-DSEVEA--AIQSSLNDLMVdkTVIAIAHRLSTIAQM-DRLIVLDEGK 576
Cdd:PRK10982 163 SSLtEKEVNHlfTIIRKLKERGC--GIVYISHKMEEIFQLcDEITILRDGQ 211
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
163-592 |
1.21e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 80.02 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 163 LAYVSIYFITVSIVLGAISPTLLIPLMVWLGLFLLSAWFFIprlSKVSQQQADARavmtgRVTDA-YTNIQTV-----KL 236
Cdd:PRK10522 128 LVQGIILTLGSAAYLAWLSPKMLLVTAIWMAVTIWGGFVLV---ARVYKHMATLR-----ETEDKlYNDYQTVlegrkEL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 237 FAHAGRESQYAKASMKEFMTTVYAQMRLGTLFEVSINMLSAVLFVGVIGTAVWLW-TQGLAALGViAATTAM-ILKLNSM 314
Cdd:PRK10522 200 TLNRERAEYVFENEYEPDAQEYRHHIIRADTFHLSAVNWSNIMMLGAIGLVFYMAnSLGWADTNV-AATYSLtLLFLRTP 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 315 AEFMMWHMSALFenvgTIQDGMQTLgKKINIQD-KPEAKPLAVKQG--EIVFKDVTFAYNNKNV-IDHFNLHIKAGEKIG 390
Cdd:PRK10522 279 LLSAVGALPTLL----SAQVAFNKL-NKLALAPyKAEFPRPQAFPDwqTLELRNVTFAYQDNGFsVGPINLTIKRGELLF 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 391 IVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRANIALVTQDTSLLhrsvaenikygrpdatDHDMQSAV 470
Cdd:PRK10522 354 LIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLF----------------DQLLGPEG 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 471 HKAKAAEFIPQLVDLKGRSGYEAQVGE-RGVKLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMV 549
Cdd:PRK10522 418 KPANPALVEKWLERLKMAHKLELEDGRiSNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQ 497
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 746197230 550 D--KTVIAIAHRLSTIAQMDRLIVLDEGKIAE-QGTHEELIAKNGI 592
Cdd:PRK10522 498 EmgKTIFAISHDDHYFIHADRLLEMRNGQLSElTGEERDAASRDAV 543
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
375-581 |
1.45e-15 |
|
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: 76.03 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 375 VIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGqniedvtQDS--LRANIALvtqDTSLlhrSVAE 452
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-------RVSslLGLGGGF---NPEL---TGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 453 NIK-----YGRPDATDHDMqsavhkakaAEFIPQLVDLKgrsgyeaQVGERGVK-LSGGQRQRIAIARVFLKDAPILILD 526
Cdd:cd03220 104 NIYlngrlLGLSRKEIDEK---------IDEIIEFSELG-------DFIDLPVKtYSSGMKARLAFAIATALEPDILLID 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 746197230 527 EATSALDSEVEAAIQSSLNDLMVD-KTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQG 581
Cdd:cd03220 168 EVLAVGDAAFQEKCQRRLRELLKQgKTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
361-577 |
1.67e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 76.07 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAY-NNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDS---LRANI 436
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 437 ALVTQDTSLL-HRSVAENIKYGR--PDATDHDMQSAVHKAkaaefipqlVDlkgRSGYEAQVGERGVKLSGGQRQRIAIA 513
Cdd:PRK10908 82 GMIFQDHHLLmDRTVYDNVAIPLiiAGASGDDIRRRVSAA---------LD---KVGLLDKAKNFPIQLSGGEQQRVGIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 746197230 514 RVFLKDAPILILDEATSALDSEVEAAIQSSLNDL-MVDKTVIAIAHRLSTIAQMD-RLIVLDEGKI 577
Cdd:PRK10908 150 RAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFnRVGVTVLMATHDIGLISRRSyRMLTLSDGHL 215
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
370-581 |
4.38e-15 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 75.06 E-value: 4.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 370 YNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGqNIEDVTQDSLRANIALV----TQ---- 441
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-LVPWKRRKKFLRRIGVVfgqkTQlwwd 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 442 ----DTSLLHRSVaenikYGRPDAtdhdmqsavhkaKAAEFIPQLVDLkgrsgyeAQVGE------RgvKLSGGQRQRIA 511
Cdd:cd03267 110 lpviDSFYLLAAI-----YDLPPA------------RFKKRLDELSEL-------LDLEElldtpvR--QLSLGQRMRAE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 746197230 512 IARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDK--TVIAIAHRLSTIAQM-DRLIVLDEGKIAEQG 581
Cdd:cd03267 164 IAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALaRRVLVIDKGRLLYDG 236
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
356-584 |
6.70e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 75.30 E-value: 6.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 356 VKQGEIVFKDVTFAYNNKNV-IDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNiedvTQDSLRA 434
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRNGHTaLRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP----TRQALQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 435 N-IALVTQ----DTS--LLHRSVAENIKYG------RPDATDHDMQSAvhkakAAEFIpQLVDLKGRsgyeaQVGErgvk 501
Cdd:PRK15056 78 NlVAYVPQseevDWSfpVLVEDVVMMGRYGhmgwlrRAKKRDRQIVTA-----ALARV-DMVEFRHR-----QIGE---- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 502 LSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVD-KTVIAIAHRLSTIAQMDRLIVLDEGKIAEQ 580
Cdd:PRK15056 143 LSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVKGTVLAS 222
|
....
gi 746197230 581 GTHE 584
Cdd:PRK15056 223 GPTE 226
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
350-572 |
7.86e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 73.98 E-value: 7.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 350 EAKPLavkqgeIVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQ 429
Cdd:PRK10247 3 ENSPL------LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 430 DSLRANIALVTQDTSLLHRSVAENIKYG---RPDATDHDmqsavhkakaaefipQLVDLKGRSGYEAQVGERGV-KLSGG 505
Cdd:PRK10247 77 EIYRQQVSYCAQTPTLFGDTVYDNLIFPwqiRNQQPDPA---------------IFLDDLERFALPDTILTKNIaELSGG 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 746197230 506 QRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDK--TVIAIAHRLSTIAQMDRLIVL 572
Cdd:PRK10247 142 EKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQniAVLWVTHDKDEINHADKVITL 210
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
363-592 |
8.59e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 74.15 E-value: 8.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 363 FKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIED-VTQDSLRANIALVTQ 441
Cdd:PRK11614 8 FDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKIMREAVAIVPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 442 DTSLLHR-SVAENIKYGRPDATDHDMQSAVhkAKAAEFIPQLvdlkgrsgYEAQVgERGVKLSGGQRQRIAIARVFLKDA 520
Cdd:PRK11614 88 GRRVFSRmTVEENLAMGGFFAERDQFQERI--KWVYELFPRL--------HERRI-QRAGTMSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 746197230 521 PILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIA--QMDRLIVLDEGKIAEQGTHEELIAKNGI 592
Cdd:PRK11614 157 RLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQAlkLADRGYVLENGHVVLEDTGDALLANEAV 230
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
358-582 |
1.04e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 74.43 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 358 QGEIVFK--DVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHL-----KEGAILIDGQNI--EDVT 428
Cdd:PRK14243 6 GTETVLRteNLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLyaPDVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 429 QDSLRANIALVTQDTSLLHRSVAENIKYG-RPDATDHDMQSAVHKA-KAAEFIPQLVDlkgrsgyeaQVGERGVKLSGGQ 506
Cdd:PRK14243 86 PVEVRRRIGMVFQKPNPFPKSIYDNIAYGaRINGYKGDMDELVERSlRQAALWDEVKD---------KLKQSGLSLSGGQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 746197230 507 RQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIAQMDRLIVLDEGKIAEQGT 582
Cdd:PRK14243 157 QQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGG 232
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
359-586 |
1.40e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 76.51 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 359 GEIVF--KDVTfAYN----NKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYH-LKEGAILIDGQNIEDVT-QD 430
Cdd:PRK13549 256 GEVILevRNLT-AWDpvnpHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNpQQ 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 431 SLRANIALVTQDTS----LLHRSVAENI------KYGRPDATDHDmqsavHKAKAAEFIPQLVDLKGRSGyEAQVGergv 500
Cdd:PRK13549 335 AIAQGIAMVPEDRKrdgiVPVMGVGKNItlaaldRFTGGSRIDDA-----AELKTILESIQRLKVKTASP-ELAIA---- 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 501 KLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLmVDK--TVIAIAHRLSTIAQM-DRLIVLDEGKI 577
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQL-VQQgvAIIVISSELPEVLGLsDRVLVMHEGKL 483
|
....*....
gi 746197230 578 AEQGTHEEL 586
Cdd:PRK13549 484 KGDLINHNL 492
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
386-581 |
1.59e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 76.82 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 386 GEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQ---DSLRANIALVTQD--TSLLHR-----SVAENIK 455
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPgklQALRRDIQFIFQDpyASLDPRqtvgdSIMEPLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 456 ygrpdatdhdMQSAVHKAKAAEFIPQLVDlkgRSGYEAQVGER-GVKLSGGQRQRIAIARVFLKDAPILILDEATSALDS 534
Cdd:PRK10261 430 ----------VHGLLPGKAAAARVAWLLE---RVGLLPEHAWRyPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 746197230 535 EVEAAIQSSLNDLMVDKTV--IAIAHRLSTIAQMD-RLIVLDEGKIAEQG 581
Cdd:PRK10261 497 SIRGQIINLLLDLQRDFGIayLFISHDMAVVERIShRVAVMYLGQIVEIG 546
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
379-585 |
2.07e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 73.34 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 379 FNLHIKAGEKIGIVGRSGAGKSTLIQL---LLHFyhlkEGAILIDGQNIEDVTQDSL---RAniALVTQDTSLLHRSVAE 452
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARmagLLPG----QGEILLNGRPLSDWSAAELarhRA--YLSQQQSPPFAMPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 453 NIKYGRPDATDHDMQSAVHKAKAAEFipQLVDLKGRsgyeaQVGergvKLSGGQRQRIAIARVFLK-------DAPILIL 525
Cdd:COG4138 89 YLALHQPAGASSEAVEQLLAQLAEAL--GLEDKLSR-----PLT----QLSGGEWQRVRLAAVLLQvwptinpEGQLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 746197230 526 DEATSALDseveAAIQSSLNDLMVD-----KTVIAIAHRLS-TIAQMDRLIVLDEGKIAEQGTHEE 585
Cdd:COG4138 158 DEPMNSLD----VAQQAALDRLLRElcqqgITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAE 219
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
368-599 |
2.40e-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: 76.98 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 368 FAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEdVTQDSLRANIALVTQDTSLLH 447
Cdd:TIGR01257 938 FEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE-TNLDAVRQSLGMCPQHNILFH 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 448 R-SVAENIKYgrpdatdhdmqsavhkakaaefipqLVDLKGRSGYEAQV---------------GERGVKLSGGQRQRIA 511
Cdd:TIGR01257 1017 HlTVAEHILF-------------------------YAQLKGRSWEEAQLemeamledtglhhkrNEEAQDLSGGMQRKLS 1071
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 512 IARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTheELIAKN 590
Cdd:TIGR01257 1072 VAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLgDRIAIISQGRLYCSGT--PLFLKN 1149
|
250
....*....|...
gi 746197230 591 ----GIYAQLWKR 599
Cdd:TIGR01257 1150 cfgtGFYLTLVRK 1162
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
369-588 |
2.74e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 73.00 E-value: 2.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 369 AYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVT-QDSLRANIALVTQDTSLLH 447
Cdd:PRK10895 12 AYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYLPQEASIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 448 R-SVAENIKYGRpdATDHDMQSAVHKAKAAEF-----IPQLVDLKGRSgyeaqvgergvkLSGGQRQRIAIARVFLKDAP 521
Cdd:PRK10895 92 RlSVYDNLMAVL--QIRDDLSAEQREDRANELmeefhIEHLRDSMGQS------------LSGGERRRVEIARALAANPK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 746197230 522 ILILDEATSALDS----EVEAAIQ----SSLNDLMVDKTViaiahrLSTIAQMDRLIVLDEGKIAEQGTHEELIA 588
Cdd:PRK10895 158 FILLDEPFAGVDPisviDIKRIIEhlrdSGLGVLITDHNV------RETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
375-588 |
2.82e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.90 E-value: 2.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 375 VIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYH-----LKEGAILIDGQNIEDVTQDSLRA----NIALVTQD--T 443
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPsppvvYPSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQEpmV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 444 SL--LH---RSVAENIKYGRpdatdhDMQsavHKAKAAEFIpQLVDLKGRSGYEAQVGERGVKLSGGQRQRIAIARVFLK 518
Cdd:PRK15134 104 SLnpLHtleKQLYEVLSLHR------GMR---REAARGEIL-NCLDRVGIRQAAKRLTDYPHQLSGGERQRVMIAMALLT 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 746197230 519 DAPILILDEATSALDSEVEAAIQSSLNDLM--VDKTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEELIA 588
Cdd:PRK15134 174 RPELLIADEPTTALDVSVQAQILQLLRELQqeLNMGLLFITHNLSIVRKLaDRVAVMQNGRCVEQNRAATLFS 246
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
350-544 |
3.27e-14 |
|
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: 71.76 E-value: 3.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 350 EAKPLAVKQGE-IVFKDVTFAYNnknvidhfnlhikAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIeDVT 428
Cdd:cd03231 2 EADELTCERDGrALFSGLSFTLA-------------AGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-DFQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 429 QDSLRANIALVTQDTSLLHR-SVAENIKYGRPDATDHDMQSAVhkakaaefipqlvdlkgrsgyeAQVGERGVK------ 501
Cdd:cd03231 68 RDSIARGLLYLGHAPGIKTTlSVLENLRFWHADHSDEQVEEAL----------------------ARVGLNGFEdrpvaq 125
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 746197230 502 LSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSL 544
Cdd:cd03231 126 LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAM 168
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
381-580 |
4.61e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.04 E-value: 4.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 381 LHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIE-DVTQDSLRANIALVTQDTSLL-HRSVAENIKYGR 458
Cdd:PRK10762 25 LNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEAGIGIIHQELNLIpQLTIAENIFLGR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 459 PDATDhdMQSAVHKAKAAEFIPQLVDLKGRSGYEAQVGErgvkLSGGQRQRIAIARVFLKDAPILILDEATSAL-DSEVE 537
Cdd:PRK10762 105 EFVNR--FGRIDWKKMYAEADKLLARLNLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 746197230 538 aAIQSSLNDLMVDKTVIA-IAHRLSTIAQM-DRLIVLDEGK-IAEQ 580
Cdd:PRK10762 179 -SLFRVIRELKSQGRGIVyISHRLKEIFEIcDDVTVFRDGQfIAER 223
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
370-586 |
4.77e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 72.18 E-value: 4.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 370 YNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLK-----EGAILIDGQNI--EDVTQDSLRANIALVTQ- 441
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDPIEVRREVGMVFQy 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 442 DTSLLHRSVAENIKYG--------RPDATDHDMQSAVHKAKAAEfipqlvDLKGR-SGYEAQvgergvkLSGGQRQRIAI 512
Cdd:PRK14267 94 PNPFPHLTIYDNVAIGvklnglvkSKKELDERVEWALKKAALWD------EVKDRlNDYPSN-------LSGGQRQRLVI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 746197230 513 ARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEEL 586
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVsDYVAFLYLGKLIEVGPTRKV 235
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
365-588 |
6.82e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 72.44 E-value: 6.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 365 DVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFY-----HLKEGAILIDGQNI---EDVTQdsLRANI 436
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdkvsgYRYSGDVLLGGRSIfnyRDVLE--FRRRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 437 ALVTQDTSLLHRSVAENIKYGrpdATDHDMQSAVHKAKAAEfiPQLVDLKGRSGYEAQVGERGVKLSGGQRQRIAIARVF 516
Cdd:PRK14271 104 GMLFQRPNPFPMSIMDNVLAG---VRAHKLVPRKEFRGVAQ--ARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 746197230 517 LKDAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEELIA 588
Cdd:PRK14271 179 AVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARIsDRAALFFDGRLVEEGPTEQLFS 251
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
379-582 |
8.85e-14 |
|
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: 71.29 E-value: 8.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 379 FNLHIKAG-----EKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDG-------QNIEDVTQDSLRANIALVTQDTsll 446
Cdd:cd03237 13 FTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdtvsykpQYIKADYEGTVRDLLSSITKDF--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 447 hrsvaenikygrpdATDHDMQSAVHKakaaefiP-QLVDLkgrsgYEAQVGErgvkLSGGQRQRIAIARVFLKDAPILIL 525
Cdd:cd03237 90 --------------YTHPYFKTEIAK-------PlQIEQI-----LDREVPE----LSGGELQRVAIAACLSKDADIYLL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 526 DEATSALDSEVEAAIQSSLNDLMV--DKTVIAIAHRLSTIAQM-DRLIVLDeGKIAEQGT 582
Cdd:cd03237 140 DEPSAYLDVEQRLMASKVIRRFAEnnEKTAFVVEHDIIMIDYLaDRLIVFE-GEPSVNGV 198
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
361-575 |
1.03e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.05 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVT-QDSLRANIALV 439
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhKLAAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 440 TQDTSLLHR-SVAENIKYGRpdatdhdmqsavHKAKAAEFIPqLVDLKG----------RSGYEAQVGERGVKLSGGQRQ 508
Cdd:PRK09700 86 YQELSVIDElTVLENLYIGR------------HLTKKVCGVN-IIDWREmrvraammllRVGLKVDLDEKVANLSISHKQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 746197230 509 RIAIARVFLKDAPILILDEATSAL-DSEVEA--AIqssLNDLMVD-KTVIAIAHRLSTIAQM-DRLIVLDEG 575
Cdd:PRK09700 153 MLEIAKTLMLDAKVIIMDEPTSSLtNKEVDYlfLI---MNQLRKEgTAIVYISHKLAEIRRIcDRYTVMKDG 221
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
362-582 |
1.10e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 71.00 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 362 VFKDVTFAynnknvidhfnlhIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIedvTQDSLRANIALVTQ 441
Cdd:PRK11629 24 VLHNVSFS-------------IGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPM---SKLSSAAKAELRNQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 442 DTSLLHRsvaenIKYGRPDATDHD---MQSAVHKAKAAEFIPQLVDLKGRSGYEAQVGERGVKLSGGQRQRIAIARVFLK 518
Cdd:PRK11629 88 KLGFIYQ-----FHHLLPDFTALEnvaMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 746197230 519 DAPILILDEATSALDSEVEAAIQSSLNDLMVDK--TVIAIAHRLSTIAQMDRLIVLDEGKIAEQGT 582
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELNRLQgtAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
381-580 |
1.17e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 70.58 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 381 LHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQD---SLRA-NIALVTQDTSLLHRSVA-ENIK 455
Cdd:PRK10584 31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRAkHVGFVFQSFMLIPTLNAlENVE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 456 YGRPDATDHDMQSavhKAKAAEFIPQLvdlkgrsGYEAQVGERGVKLSGGQRQRIAIARVFLKDAPILILDEATSALDSE 535
Cdd:PRK10584 111 LPALLRGESSRQS---RNGAKALLEQL-------GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQ 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 746197230 536 VEAAIQSSLNDLMVD--KTVIAIAHRLSTIAQMDRLIVLDEGKIAEQ 580
Cdd:PRK10584 181 TGDKIADLLFSLNREhgTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
364-576 |
1.18e-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: 73.71 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 364 KDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLL--LHFYHLKEGAILIDGQNIE-DVTQDSLRANIALVT 440
Cdd:TIGR02633 5 KGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILsgVYPHGTWDGEIYWSGSPLKaSNIRDTERAGIVIIH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 441 QDTSLLHR-SVAENIKYGR----PDATDHDmQSAVHKAKaaEFIPQL-VDLKGRSgyeAQVGERGvklsGGQRQRIAIAR 514
Cdd:TIGR02633 85 QELTLVPElSVAENIFLGNeitlPGGRMAY-NAMYLRAK--NLLRELqLDADNVT---RPVGDYG----GGQQQLVEIAK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 746197230 515 VFLKDAPILILDEATSALdSEVEAAIqssLNDLMVD-----KTVIAIAHRLSTIAQM-DRLIVLDEGK 576
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSL-TEKETEI---LLDIIRDlkahgVACVYISHKLNEVKAVcDTICVIRDGQ 218
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
365-535 |
1.31e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 70.26 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 365 DVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEdvTQDSLR-----ANIALV 439
Cdd:PRK13543 16 ALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT--RGDRSRfmaylGHLPGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 440 TQDTSLLhrsvaENIKYgrpdatdhdmQSAVHKAKAAEFIPQLVDLKGRSGYEAQVGErgvKLSGGQRQRIAIARVFLKD 519
Cdd:PRK13543 94 KADLSTL-----ENLHF----------LCGLHGRRAKQMPGSALAIVGLAGYEDTLVR---QLSAGQKKRLALARLWLSP 155
|
170
....*....|....*.
gi 746197230 520 APILILDEATSALDSE 535
Cdd:PRK13543 156 APLWLLDEPYANLDLE 171
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
361-582 |
3.46e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 70.16 E-value: 3.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYN-----NKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNI--EDVTQD--S 431
Cdd:PRK13649 3 INLQNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItsTSKNKDikQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 432 LRANIALVTQ--DTSLLHRSVAENIKYGrpdatdhDMQSAVHKAKAAEFIPQLVDLKGRSgyEAQVGERGVKLSGGQRQR 509
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFG-------PQNFGVSQEEAEALAREKLALVGIS--ESLFEKNPFELSGGQMRR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 746197230 510 IAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVD-KTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGT 582
Cdd:PRK13649 154 VAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSgMTIVLVTHLMDDVANYaDFVYVLEKGKLVLSGK 228
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
377-576 |
3.62e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 72.13 E-value: 3.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 377 DHFNLHIKAGEKIGIVGRSGAGKSTLIQLL--LHFYHLKEGAILIDGQ-----NIedvtQDSLRANIALVTQDTSLL-HR 448
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKSTLMKVLsgVYPHGSYEGEILFDGEvcrfkDI----RDSEALGIVIIHQELALIpYL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 449 SVAENIKYGRPDATDHDMQSAVHKAKAAEFIPQlVDLKGRSgyEAQVGERGVklsgGQRQRIAIARVFLKDAPILILDEA 528
Cdd:NF040905 94 SIAENIFLGNERAKRGVIDWNETNRRARELLAK-VGLDESP--DTLVTDIGV----GKQQLVEIAKALSKDVKLLILDEP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 746197230 529 TSAL---DSEveaaiqsSLNDLMVD-----KTVIAIAHRLSTIAQM-DRLIVLDEGK 576
Cdd:NF040905 167 TAALneeDSA-------ALLDLLLElkaqgITSIIISHKLNEIRRVaDSITVLRDGR 216
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
355-535 |
4.64e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 72.29 E-value: 4.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 355 AVKQGEIVF--KDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIdGQNIEDVTQDSL 432
Cdd:PRK11147 312 ASRSGKIVFemENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLEVAYFDQH 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 433 RANIalvtqDtslLHRSVAENIKYGRpdatdhdmqsavhkakaaefipQLVDLKGRS----GY---------EAQVgerG 499
Cdd:PRK11147 391 RAEL-----D---PEKTVMDNLAEGK----------------------QEVMVNGRPrhvlGYlqdflfhpkRAMT---P 437
|
170 180 190
....*....|....*....|....*....|....*..
gi 746197230 500 VK-LSGGQRQRIAIARVFLKDAPILILDEATSALDSE 535
Cdd:PRK11147 438 VKaLSGGERNRLLLARLFLKPSNLLILDEPTNDLDVE 474
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
361-582 |
9.77e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 68.99 E-value: 9.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYN------NKNVIDhFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDS--- 431
Cdd:PRK13643 2 IKFEKVNYTYQpnspfaSRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeik 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 432 -LRANIALVTQ--DTSLLHRSVAENIKYGrpdatdhDMQSAVHKAKAAEFIPQLVDLKGRSgyeAQVGERG-VKLSGGQR 507
Cdd:PRK13643 81 pVRKKVGVVFQfpESQLFEETVLKDVAFG-------PQNFGIPKEKAEKIAAEKLEMVGLA---DEFWEKSpFELSGGQM 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 746197230 508 QRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDL-MVDKTVIAIAHRLSTIAQ-MDRLIVLDEGKIAEQGT 582
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT 227
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
370-586 |
1.14e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 68.50 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 370 YNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQlllHFYHLKEG-------------AILIDGQNIEDVTQDslRANI 436
Cdd:PRK09984 14 FNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLR---HLSGLITGdksagshiellgrTVQREGRLARDIRKS--RANT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 437 ALVTQDTSLLHR-SVAENIKYGRPDATDH-----DMQSAVHKAKAAEFIPqlvdlkgRSGYEAQVGERGVKLSGGQRQRI 510
Cdd:PRK09984 89 GYIFQQFNLVNRlSVLENVLIGALGSTPFwrtcfSWFTREQKQRALQALT-------RVGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 746197230 511 AIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDK--TVIAIAHRLS-TIAQMDRLIVLDEGKIAEQGTHEEL 586
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
364-584 |
1.35e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 68.13 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 364 KDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLL-H-FYHLKEGAILIDGQNIEDVTQDsLRAN------ 435
Cdd:CHL00131 11 KNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAgHpAYKILEGDILFKGESILDLEPE-ERAHlgifla 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 436 ------IALVTQDTSLLHRSVAENIKYGRPDatdhdmqsaVHKAKAAEFIPQLVDLkgrSGYEAQVGERGVK--LSGGQR 507
Cdd:CHL00131 90 fqypieIPGVSNADFLRLAYNSKRKFQGLPE---------LDPLEFLEIINEKLKL---VGMDPSFLSRNVNegFSGGEK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 508 QRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLM-VDKTVIAIAH--RLSTIAQMDRLIVLDEGKIAEQGTHE 584
Cdd:CHL00131 158 KRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGDAE 237
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
378-588 |
2.07e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 69.69 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 378 HFNLHikAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLRA-NIALVTQDTSLL-HRSVAENIK 455
Cdd:PRK15439 31 DFTLH--AGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQlGIYLVPQEPLLFpNLSVKENIL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 456 YGRPdatdhdmQSAVHKAKAAEFIPQL---VDLkgrsgyEAQVGergvKLSGGQRQRIAIARVFLKDAPILILDEATSAL 532
Cdd:PRK15439 109 FGLP-------KRQASMQKMKQLLAALgcqLDL------DSSAG----SLEVADRQIVEILRGLMRDSRILILDEPTASL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 746197230 533 D-SEVEAAIQ--SSLNDLMVDktVIAIAHRLSTIAQM-DRLIVLDEGKIAEQG-----THEELIA 588
Cdd:PRK15439 172 TpAETERLFSriRELLAQGVG--IVFISHKLPEIRQLaDRISVMRDGTIALSGktadlSTDDIIQ 234
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
361-592 |
2.11e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 69.92 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAIlidgqniedvtQDSLRANIALVT 440
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-----------KWSENANIGYYA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 441 QDtsllHRSVAENikygrpDATDHDMQSAVHKAKAAEfipQLV-DLKGRSGYEAQVGERGVK-LSGGQRQRIAIARVFLK 518
Cdd:PRK15064 389 QD----HAYDFEN------DLTLFDWMSQWRQEGDDE---QAVrGTLGRLLFSQDDIKKSVKvLSGGEKGRMLFGKLMMQ 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 746197230 519 DAPILILDEATSALDSEVEAAIQSSLNdlMVDKTVIAIAH-R--LSTIAQmdRLIVLDEGKIAE-QGTHEELIAKNGI 592
Cdd:PRK15064 456 KPNVLVMDEPTNHMDMESIESLNMALE--KYEGTLIFVSHdRefVSSLAT--RIIEITPDGVVDfSGTYEEYLRSQGI 529
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
354-586 |
2.57e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.88 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 354 LAVKQGEIVFKDvtfAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDG--------QNIE 425
Cdd:PRK10261 13 LAVENLNIAFMQ---EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrQVIE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 426 --DVTQDSLR----ANIALVTQD--TSL-----LHRSVAENIKYGRPDATDHDMQSAVHKAKAAEfIPQLVDLKGRsgYE 492
Cdd:PRK10261 90 lsEQSAAQMRhvrgADMAMIFQEpmTSLnpvftVGEQIAESIRLHQGASREEAMVEAKRMLDQVR-IPEAQTILSR--YP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 493 AQvgergvkLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDKT--VIAIAHRLSTIAQM-DRL 569
Cdd:PRK10261 167 HQ-------LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIaDRV 239
|
250
....*....|....*..
gi 746197230 570 IVLDEGKIAEQGTHEEL 586
Cdd:PRK10261 240 LVMYQGEAVETGSVEQI 256
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
376-588 |
2.64e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 67.03 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 376 IDHFNLHIKAGEKIGIVGRSGAGKS----TLIQLLLHFYHLKEGAILIDGQNIEdvtQDSLRA-NIALVTQDTsllhRSV 450
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVA---PCALRGrKIATIMQNP----RSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 451 AENIKYGRPDATDHDMQSAVHKAKAAefIPQLVDLKGRSGYEAQVGERGVKLSGGQRQRIAIARVFLKDAPILILDEATS 530
Cdd:PRK10418 92 FNPLHTMHTHARETCLALGKPADDAT--LTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 746197230 531 ALDSEVEAAIQSSLNDLMVDKT--VIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEELIA 588
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARLaDDVAVMSHGRIVEQGDVETLFN 230
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
376-577 |
4.63e-12 |
|
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: 68.70 E-value: 4.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 376 IDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLK-EGAILIDGQNIEDVT-QDSLRANIALVTQDTS----LLHRS 449
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNpAQAIRAGIAMVPEDRKrhgiVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 450 VAENI---------KYGRPDATDHD--MQSAVHKAKAAEFIPQLvdlkgrsgyeaQVGergvKLSGGQRQRIAIARVFLK 518
Cdd:TIGR02633 356 VGKNItlsvlksfcFKMRIDAAAELqiIGSAIQRLKVKTASPFL-----------PIG----RLSGGNQQKAVLAKMLLT 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 746197230 519 DAPILILDEATSALDSEVEAAIQSSLNDLMVDK-TVIAIAHRLSTIAQM-DRLIVLDEGKI 577
Cdd:TIGR02633 421 NPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGvAIIVVSSELAEVLGLsDRVLVIGEGKL 481
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
383-581 |
5.16e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 69.37 E-value: 5.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 383 IKAGEKIGIVGRSGAGKSTLIQLL---LHFYHL-KEGAILIDGQNIEDVTQdSLRANIALVTQ-DTSLLHRSVAENIKYG 457
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIasnTDGFHIgVEGVITYDGITPEEIKK-HYRGDVVYNAEtDVHFPHLTVGETLDFA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 458 --------RPDATDHDmqsaVHKAKAAEFIPQLVDLkgRSGYEAQVGE---RGVklSGGQRQRIAIARVFLKDAPILILD 526
Cdd:TIGR00956 163 arcktpqnRPDGVSRE----EYAKHIADVYMATYGL--SHTRNTKVGNdfvRGV--SGGERKRVSIAEASLGGAKIQCWD 234
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 746197230 527 EATSALDS----EVEAAIQSSLNdlMVDKTVIAIAHRLS--TIAQMDRLIVLDEGKIAEQG 581
Cdd:TIGR00956 235 NATRGLDSatalEFIRALKTSAN--ILDTTPLVAIYQCSqdAYELFDKVIVLYEGYQIYFG 293
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
347-586 |
7.24e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 68.13 E-value: 7.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 347 DKPEAKPlavkqGEIVF--KDVTFA-YNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQN 423
Cdd:COG3845 247 EKAPAEP-----GEVVLevENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGED 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 424 IEDVT-QDSLRANIALVTQDTslLHR------SVAENI---KYGRPDATDHDMqsaVHKAKAAEFIPQLV---DLKGRSG 490
Cdd:COG3845 322 ITGLSpRERRRLGVAYIPEDR--LGRglvpdmSVAENLilgRYRRPPFSRGGF---LDRKAIRAFAEELIeefDVRTPGP 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 491 yEAQVGergvKLSGGQRQRIAIARVFLKDAPILILDEATSALDseVEAA--IQSSLNDLMvD--KTVIAIAHRLSTIAQM 566
Cdd:COG3845 397 -DTPAR----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLD--VGAIefIHQRLLELR-DagAAVLLISEDLDEILAL 468
|
250 260
....*....|....*....|....*.
gi 746197230 567 -DRLIVLDEGKI-----AEQGTHEEL 586
Cdd:COG3845 469 sDRIAVMYEGRIvgevpAAEATREEI 494
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
350-533 |
9.32e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.44 E-value: 9.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 350 EAKPLAVKQGE-IVFkdvtfaynnknviDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVt 428
Cdd:PRK13538 3 EARNLACERDErILF-------------SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQ- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 429 QDSLRANIALVTQDT---SLLhrSVAENIKYGrpdATDHDMQS--AVHKAKAAefipqlVDLKGRSgyEAQVGErgvkLS 503
Cdd:PRK13538 69 RDEYHQDLLYLGHQPgikTEL--TALENLRFY---QRLHGPGDdeALWEALAQ------VGLAGFE--DVPVRQ----LS 131
|
170 180 190
....*....|....*....|....*....|
gi 746197230 504 GGQRQRIAIARVFLKDAPILILDEATSALD 533
Cdd:PRK13538 132 AGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
39-309 |
1.11e-11 |
|
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: 65.74 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 39 YLLLLVICTAGAATFEALLFskiGQLVDWLSKSQPESFLSQhASNILILISVLFANILFVNIQSIIKHqILYSTFPMRLR 118
Cdd:pfam00664 3 LAILLAILSGAISPAFPLVL---GRILDVLLPDGDPETQAL-NVYSLALLLLGLAQFILSFLQSYLLN-HTGERLSRRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 119 WRFHNLLLKQSLDFFHNDFAGRLSAKVMQTALAIREFW-IILGDMLAYVSIyFITVSIVLGAISPTLLIPLMVWLGLFLL 197
Cdd:pfam00664 78 RKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLgEKLGLLFQSLAT-IVGGIIVMFYYGWKLTLVLLAVLPLYIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 198 SAWFFIPRLSKVSQQQADARAVMTGRVTDAYTNIQTVKLFahaGRESQYAKASMKEFMTTVYAQMRLGT---LFEVSINM 274
Cdd:pfam00664 157 VSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAF---GREEYELEKYDKALEEALKAGIKKAVangLSFGITQF 233
|
250 260 270
....*....|....*....|....*....|....*
gi 746197230 275 LSAVLFVGVIGTAVWLWTQGLAALGVIAATTAMIL 309
Cdd:pfam00664 234 IGYLSYALALWFGAYLVISGELSVGDLVAFLSLFA 268
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
386-574 |
1.22e-11 |
|
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: 62.78 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 386 GEKIGIVGRSGAGKSTLIQLLLHFYHLKE-GAILIDGQNIEDVTQDSLRANIalvtqdtsllhrsvaenikygrpdatdh 464
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGgGVIYIDGEDILEEVLDQLLLII---------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 465 dmqsavhkakaaefipqlvdlkgrsgyeaqVGERGVKLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSL 544
Cdd:smart00382 54 ------------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLE 103
|
170 180 190
....*....|....*....|....*....|....*..
gi 746197230 545 NDLM-------VDKTVIAIAHRLSTIAQMDRLIVLDE 574
Cdd:smart00382 104 ELRLllllkseKNLTVILTTNDEKDLGPALLRRRFDR 140
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
379-585 |
1.37e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.95 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 379 FNLHIKAGEKIGIVGRSGAGKSTLIQLL--LHFYhlkEGAILIDGQNIEDVTQDSL---RAniALVTQDTSLLHRSVAEN 453
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMagLLPG---SGSIQFAGQPLEAWSAAELarhRA--YLSQQQTPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 454 IKYGRPDATD-HDMQSAVHkaKAAEFIpQLVDLKGRSgyeaqVGErgvkLSGGQRQRIAIARVFLKDAP-------ILIL 525
Cdd:PRK03695 90 LTLHQPDKTRtEAVASALN--EVAEAL-GLDDKLGRS-----VNQ----LSGGEWQRVRLAAVVLQVWPdinpagqLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 746197230 526 DEATSALDSEVEAAIQSSLNDL-MVDKTVIAIAHRLS-TIAQMDRLIVLDEGKIAEQGTHEE 585
Cdd:PRK03695 158 DEPMNSLDVAQQAALDRLLSELcQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
360-558 |
1.40e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 67.27 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 360 EIVF--KDVTFAYN-NKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEG-AILIDGQNIEDVTQD----- 430
Cdd:TIGR03719 2 QYIYtmNRVSKVVPpKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGeARPQPGIKVGYLPQEpqldp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 431 --SLRANIALVTQDT-SLLHRSVAENIKYGRPD------------------ATD-HDMQSAVHKAKAAEFIPQlvdlkgr 488
Cdd:TIGR03719 82 tkTVRENVEEGVAEIkDALDRFNEISAKYAEPDadfdklaaeqaelqeiidAADaWDLDSQLEIAMDALRCPP------- 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 489 sgYEAQVGergvKLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLmvDKTVIAIAH 558
Cdd:TIGR03719 155 --WDADVT----KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY--PGTVVAVTH 216
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
365-589 |
2.16e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 64.64 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 365 DVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQD--SLRANIALVTQD 442
Cdd:PRK13638 6 DLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGllALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 443 TSllhrsvaENIKYgrpdaTDHDMQSA-------VHKAKAAEFIPQLVDLKGRSGYEAQVGErgvKLSGGQRQRIAIARV 515
Cdd:PRK13638 86 PE-------QQIFY-----TDIDSDIAfslrnlgVPEAEITRRVDEALTLVDAQHFRHQPIQ---CLSHGQKKRVAIAGA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 746197230 516 FLKDAPILILDEATSALDSEVEAAIQSSLNDLMVD-KTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEELIAK 589
Cdd:PRK13638 151 LVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQgNHVIISSHDIDLIYEIsDAVYVLRQGQILTHGAPGEVFAC 226
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
376-586 |
4.07e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 64.76 E-value: 4.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 376 IDHFNLHIKAGEKIGIVGRSGAGKS----TLIQLLLHFYHLKEGAILIDGQNIEDVTQDSLR----ANIALVTQD--TSL 445
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRnlvgAEVAMIFQDpmTSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 446 -----LHRSVAENIKYgrpdatdHdmQSAVHKAKAAEFIpQLVDLKGRSGYEAQVGERGVKLSGGQRQRIAIARVFLKDA 520
Cdd:PRK11022 103 npcytVGFQIMEAIKV-------H--QGGNKKTRRQRAI-DLLNQVGIPDPASRLDVYPHQLSGGMSQRVMIAMAIACRP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 746197230 521 PILILDEATSALDSEVEAAIQSSLNDLMVDK--TVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEEL 586
Cdd:PRK11022 173 KLLIADEPTTALDVTIQAQIIELLLELQQKEnmALVLITHDLALVAEAaHKIIVMYAGQVVETGKAHDI 241
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
361-591 |
6.36e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.21 E-value: 6.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAIlidgqniedVTQDSLRanIALVT 440
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---------KRNGKLR--IGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 441 QDTSL---LHRSVAENIKYgRPDATDHDMQSAVHKAKAAEFIPQLVDlkgrsgyeaqvgergvKLSGGQRQRIAIARVFL 517
Cdd:PRK09544 74 QKLYLdttLPLTVNRFLRL-RPGTKKEDILPALKRVQAGHLIDAPMQ----------------KLSGGETQRVLLARALL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 518 KDAPILILDEATSALDSEVEAAIQSSLNDLM--VDKTVIAIAHRLSTI-AQMDRLIVLDEgKIAEQGT------HEELIA 588
Cdd:PRK09544 137 NRPQLLVLDEPTQGVDVNGQVALYDLIDQLRreLDCAVLMVSHDLHLVmAKTDEVLCLNH-HICCSGTpevvslHPEFIS 215
|
...
gi 746197230 589 KNG 591
Cdd:PRK09544 216 MFG 218
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
379-585 |
6.54e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.93 E-value: 6.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 379 FNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIE-DVTQDSLRANIALVTQDTS----LLHRSVAEN 453
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRDAIRAGIMLCPEDRKaegiIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 454 IkygrpdatdhDMQSAVHKAKAAEFIpqlvdlkgRSGYEAQVGERGVK---------------LSGGQRQRIAIARVFLK 518
Cdd:PRK11288 352 I----------NISARRHHLRAGCLI--------NNRWEAENADRFIRslniktpsreqlimnLSGGNQQKAILGRWLSE 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 746197230 519 DAPILILDEATSALDSEVEAAIQSSLNDLMVDK-TVIAIAHRL-STIAQMDRLIVLDEGKIAEQGTHEE 585
Cdd:PRK11288 414 DMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGvAVLFVSSDLpEVLGVADRIVVMREGRIAGELAREQ 482
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
359-579 |
6.81e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.81 E-value: 6.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 359 GEIVF--KDVTfAYNNKNVIDhFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQ-DSLRAN 435
Cdd:PRK09700 262 HETVFevRNVT-SRDRKKVRD-ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAVKKG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 436 IALVTQ---DTSLLHR-SVAENI------KYGRPDATdHDMQSAVHKAKAAEFIPQLVDLKGRSgYEAQVGErgvkLSGG 505
Cdd:PRK09700 340 MAYITEsrrDNGFFPNfSIAQNMaisrslKDGGYKGA-MGLFHEVDEQRTAENQRELLALKCHS-VNQNITE----LSGG 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 746197230 506 QRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVD-KTVIAIAHRLSTI-AQMDRLIVLDEGKIAE 579
Cdd:PRK09700 414 NQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIiTVCDRIAVFCEGRLTQ 489
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
371-561 |
7.09e-11 |
|
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: 65.16 E-value: 7.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 371 NNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNiedvtqdslraNIALVTQDTSLLHRSV 450
Cdd:TIGR00954 463 NGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKG-----------KLFYVPQRPYMTLGTL 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 451 AENIKYgrPDATDhDMQSAVHKAKAAEFIPQLVDL----KGRSGYEAQVGERGVkLSGGQRQRIAIARVFLKDAPILILD 526
Cdd:TIGR00954 532 RDQIIY--PDSSE-DMKRRGLSDKDLEQILDNVQLthilEREGGWSAVQDWMDV-LSGGEKQRIAMARLFYHKPQFAILD 607
|
170 180 190
....*....|....*....|....*....|....*
gi 746197230 527 EATSALDSEVEAAIQSSLNDLMVdkTVIAIAHRLS 561
Cdd:TIGR00954 608 ECTSAVSVDVEGYMYRLCREFGI--TLFSVSHRKS 640
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
365-576 |
8.47e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.90 E-value: 8.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 365 DVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLL---LHFYHLKeGAILIDGQNIedvTQDSLRaNIALVTQ 441
Cdd:PLN03211 73 DETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALagrIQGNNFT-GTILANNRKP---TKQILK-RTGFVTQ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 442 DTSLL-HRSVAENIKYGRPDATDHDMQSAVHKAKAAEFIPQLVDLKGRSGYEAQVGERGVklSGGQRQRIAIARVFLKDA 520
Cdd:PLN03211 148 DDILYpHLTVRETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFIRGI--SGGERKRVSIAHEMLINP 225
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 746197230 521 PILILDEATSALDSEVEAAIQSSLNDLMVD-KTVIAIAHRLST-IAQM-DRLIVLDEGK 576
Cdd:PLN03211 226 SLLILDEPTSGLDATAAYRLVLTLGSLAQKgKTIVTSMHQPSSrVYQMfDSVLVLSEGR 284
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
371-577 |
1.17e-10 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 61.12 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 371 NNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLL---LHFYHLKEGAILIDGQNIeDVTQDSLRANIALVTQDTSLLH 447
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPY-KEFAEKYPGEIIYVSEEDVHFP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 448 R-SVAENIKYgrpdatdhdmqsaVHKAKAAEFIpqlvdlkgrsgyeaqvgeRGVklSGGQRQRIAIARVFLKDAPILILD 526
Cdd:cd03233 97 TlTVRETLDF-------------ALRCKGNEFV------------------RGI--SGGERKRVSIAEALVSRASVLCWD 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 746197230 527 EATSALDSEVEAAIQSSLNdLMVDK---TVIAIAHRLS--TIAQMDRLIVLDEGKI 577
Cdd:cd03233 144 NSTRGLDSSTALEILKCIR-TMADVlktTTFVSLYQASdeIYDLFDKVLVLYEGRQ 198
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
343-582 |
2.90e-10 |
|
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: 63.26 E-value: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 343 INIQDKP----EAKPLAVKQGEIVFK--DVTFAYNNknvidhFNLH-----IKAGEKIGIVGRSGAGKSTLIQLLlhfyh 411
Cdd:COG1245 318 VRIRDEPiefeVHAPRREKEEETLVEypDLTKSYGG------FSLEveggeIREGEVLGIVGPNGIGKTTFAKIL----- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 412 lkEGAILIDGQNIEdvtqdsLRANIAL----VTQDTSLlhrSVAENIKYGRPDatdhDMQSAVHKAKAAEfiP-QLVDLk 486
Cdd:COG1245 387 --AGVLKPDEGEVD------EDLKISYkpqyISPDYDG---TVEEFLRSANTD----DFGSSYYKTEIIK--PlGLEKL- 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 487 grsgYEAQVGErgvkLSGGQRQRIAIARVFLKDAPILILDEATSALDSE--VEAA--IQSslndlMV---DKTVIAIAHR 559
Cdd:COG1245 449 ----LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrLAVAkaIRR-----FAenrGKTAMVVDHD 515
|
250 260
....*....|....*....|....
gi 746197230 560 LSTIAQM-DRLIVLdEGKIAEQGT 582
Cdd:COG1245 516 IYLIDYIsDRLMVF-EGEPGVHGH 538
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
359-546 |
4.95e-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: 62.26 E-value: 4.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 359 GEIV--FKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIdGQNIE----DVTQDSL 432
Cdd:TIGR03719 319 GDKVieAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKlayvDQSRDAL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 433 RANialvtqdtsllhRSVAENIKygrpDATDH------DMQSavhKAKAAEFipqlvDLKGrSGYEAQVGErgvkLSGGQ 506
Cdd:TIGR03719 398 DPN------------KTVWEEIS----GGLDIiklgkrEIPS---RAYVGRF-----NFKG-SDQQKKVGQ----LSGGE 448
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 746197230 507 RQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLND 546
Cdd:TIGR03719 449 RNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLN 488
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
379-573 |
5.74e-10 |
|
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: 62.11 E-value: 5.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 379 FNLHI-KAGEKIGIVGRSGAGKSTLIQLLlhfyhlkeGAILID--GQNIEDVTQDS-LRAnialvTQDTSL---LHRSVA 451
Cdd:COG1245 91 YGLPVpKKGKVTGILGPNGIGKSTALKIL--------SGELKPnlGDYDEEPSWDEvLKR-----FRGTELqdyFKKLAN 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 452 ENIKygrpdatdhdmqsAVHKAKAAEFIPQLVDLKGRSGYEaQVGERGV-------------------KLSGGQRQRIAI 512
Cdd:COG1245 158 GEIK-------------VAHKPQYVDLIPKVFKGTVRELLE-KVDERGKldelaeklglenildrdisELSGGELQRVAI 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 746197230 513 ARVFLKDAPILILDEATSALD----SEVEAAIQSSLNDlmvDKTVIAIAHrlstiaqmDrLIVLD 573
Cdd:COG1245 224 AAALLRDADFYFFDEPSSYLDiyqrLNVARLIRELAEE---GKYVLVVEH--------D-LAILD 276
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
40-284 |
7.00e-10 |
|
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: 60.27 E-value: 7.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 40 LLLLVICTAGaatfEALLFSKIGQLVDWLSKSQPESFLSQhasNILILISVLFANILFVNIQSIIkHQILYSTFPMRLRW 119
Cdd:cd18557 2 LLFLLISSAA----QLLLPYLIGRLIDTIIKGGDLDVLNE---LALILLAIYLLQSVFTFVRYYL-FNIAGERIVARLRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 120 RFHNLLLKQSLDFFHNDFAGRLSAKVMQTALAIREfwiILGDMLAYVSIYFITVSIVLG---AISPTLLIPLMVWLGLFL 196
Cdd:cd18557 74 DLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQS---AVTDNLSQLLRNILQVIGGLIilfILSWKLTLVLLLVIPLLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 197 LSAWFFIPRLSKVSQQQADARAVMTGRVTDAYTNIQTVKLFAHAGRESQYAKASMKEFMTTVYAQMRLGTLFEVSINMLS 276
Cdd:cd18557 151 IASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLI 230
|
....*...
gi 746197230 277 AVLFVGVI 284
Cdd:cd18557 231 YLSLLLVL 238
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
383-588 |
9.01e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 59.80 E-value: 9.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 383 IKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIE--DVTQDSLRanIALVTQD--TSLLHRSVAENIkYGR 458
Cdd:PRK15112 36 LREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQR--IRMIFQDpsTSLNPRQRISQI-LDF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 459 PDATDHDMQSAVHKAKAAEFIPQLVDLKGRSGYEAQVgergvkLSGGQRQRIAIARVFLKDAPILILDEATSALDseveA 538
Cdd:PRK15112 113 PLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHM------LAPGQKQRLGLARALILRPKVIIADEALASLD----M 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 746197230 539 AIQSSLNDLMV---DKTVIAIAHRLSTIAQM----DRLIVLDEGKIAEQGTHEELIA 588
Cdd:PRK15112 183 SMRSQLINLMLelqEKQGISYIYVTQHLGMMkhisDQVLVMHQGEVVERGSTADVLA 239
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
343-582 |
9.90e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.36 E-value: 9.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 343 INIQDKP---EAKPLAVKQGE---IVFKDVTFAYNNknvidhFNLH-----IKAGEKIGIVGRSGAGKSTLIQLLLHFYH 411
Cdd:PRK13409 317 MRIRPEPiefEERPPRDESERetlVEYPDLTKKLGD------FSLEveggeIYEGEVIGIVGPNGIGKTTFAKLLAGVLK 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 412 LKEGAILID------GQNIEDVTQDSLRANIalvtqdtsllhRSVAENIkygrpdatdhdmQSAVHKAkaaEFI-P-QLV 483
Cdd:PRK13409 391 PDEGEVDPElkisykPQYIKPDYDGTVEDLL-----------RSITDDL------------GSSYYKS---EIIkPlQLE 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 484 DLkgrsgYEAQVGErgvkLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLM--VDKTVIAIAHRLS 561
Cdd:PRK13409 445 RL-----LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAeeREATALVVDHDIY 515
|
250 260
....*....|....*....|..
gi 746197230 562 TIAQM-DRLIVLdEGKIAEQGT 582
Cdd:PRK13409 516 MIDYIsDRLMVF-EGEPGKHGH 536
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
306-575 |
1.19e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 61.66 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 306 AMILKLNSMAEFMMWHMSALFENVGTIQDGMQTlgKKINIQDKPEA----KPLAVKQGEIVF--KDVTFAYNNKN----V 375
Cdd:TIGR00956 701 EILVFRRGSLKRAKKAGETSASNKNDIEAGEVL--GSTDLTDESDDvndeKDMEKESGEDIFhwRNLTYEVKIKKekrvI 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 376 IDHFNLHIKAGEKIGIVGRSGAGKSTLIQLL---LHFYHLKEGAILIDGQNIedvtQDSLRANIALVTQ-DTSLLHRSVA 451
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLaerVTTGVITGGDRLVNGRPL----DSSFQRSIGYVQQqDLHLPTSTVR 854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 452 ENIKYG----RPdatdhdmqSAVHKAKAAEFIPQLVDLKGRSGY-EAQVGERGVKLSGGQRQRIAIArVFL--KDAPILI 524
Cdd:TIGR00956 855 ESLRFSaylrQP--------KSVSKSEKMEYVEEVIKLLEMESYaDAVVGVPGEGLNVEQRKRLTIG-VELvaKPKLLLF 925
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 746197230 525 LDEATSALDSEVEAAIQSSLNDLmVD--KTVIAIAHRLSTI--AQMDRLIVLDEG 575
Cdd:TIGR00956 926 LDEPTSGLDSQTAWSICKLMRKL-ADhgQAILCTIHQPSAIlfEEFDRLLLLQKG 979
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
347-533 |
1.64e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.41 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 347 DKPEAKP-LAVKQGEIVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLL-----------LHFYHLKE 414
Cdd:PRK10938 246 DEPSARHaLPANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpqgysndLTLFGRRR 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 415 GAilidGQNIEDVTQdslraNIALVTQDTSLLHR---SVAENIKYGRPDA-------TDHDMQSAVhkakaaefipQLVD 484
Cdd:PRK10938 326 GS----GETIWDIKK-----HIGYVSSSLHLDYRvstSVRNVILSGFFDSigiyqavSDRQQKLAQ----------QWLD 386
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 746197230 485 LKGRSGYEAQVGERGvkLSGGQrQRIA-IARVFLKDAPILILDEATSALD 533
Cdd:PRK10938 387 ILGIDKRTADAPFHS--LSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLD 433
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
383-573 |
1.89e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.59 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 383 IKAGEKIGIVGRSGAGKSTLIQLLlhfyhlkeGAILID--GQNIEDVTQDS-LRANIALVTQDtsLLHRSVAENIKygrp 459
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKIL--------SGELIPnlGDYEEEPSWDEvLKRFRGTELQN--YFKKLYNGEIK---- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 460 datdhdmqsAVHKAKAAEFIPQLVDLKGRSGYEaQVGERGV-------------------KLSGGQRQRIAIARVFLKDA 520
Cdd:PRK13409 162 ---------VVHKPQYVDLIPKVFKGKVRELLK-KVDERGKldevverlglenildrdisELSGGELQRVAIAAALLRDA 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 746197230 521 PILILDEATSALD--SEVEAA--IQsslnDLMVDKTVIAIAHrlstiaqmDrLIVLD 573
Cdd:PRK13409 232 DFYFFDEPTSYLDirQRLNVArlIR----ELAEGKYVLVVEH--------D-LAVLD 275
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
369-577 |
2.92e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.96 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 369 AYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGqnieDVT-----QDSLRANIALVTQDT 443
Cdd:PRK11147 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ----DLIvarlqQDPPRNVEGTVYDFV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 444 SLLHRSVAENIKygRPDATDHDM---QSAVHKAKAAEF---------------IPQLVDLKGRSGyEAQVGErgvkLSGG 505
Cdd:PRK11147 88 AEGIEEQAEYLK--RYHDISHLVetdPSEKNLNELAKLqeqldhhnlwqlenrINEVLAQLGLDP-DAALSS----LSGG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 746197230 506 QRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLmvDKTVIAIAHRLSTIAQMDRLIV-LDEGKI 577
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF--QGSIIFISHDRSFIRNMATRIVdLDRGKL 231
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
41-336 |
3.48e-09 |
|
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: 58.21 E-value: 3.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 41 LLLVICTAGAATFEALLfskIGQLVDWLSKSQPesflsqHASNILILISVLFANILFVNIQ----SIIKHQILYstfpmR 116
Cdd:cd18551 5 LLLSLLGTAASLAQPLL---VKNLIDALSAGGS------SGGLLALLVALFLLQAVLSALSsyllGRTGERVVL-----D 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 117 LRWRFHNLLLKQSLDFFHNDFAGRLSAKVMQTALAIREFwiiLGDMLAYVSIYFITVS---IVLGAISPTLLIPLMVWLG 193
Cdd:cd18551 71 LRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLREL---ITSGLPQLVTGVLTVVgavVLMFLLDWVLTLVTLAVVP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 194 LFLLSAWFFIPRLSKVSQQQADARAVMTGRVTDAYTNIQTVKLFAHAGRESQYAKASMKEFMTTVYAQMRLGTLFEVSIN 273
Cdd:cd18551 148 LAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMG 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 746197230 274 MLSAVLFVGVIGTAVWLWTQGLAALGviaATTAMILKLNSMAEfmmwHMSALFENVGTIQDGM 336
Cdd:cd18551 228 LAVQLALLVVLGVGGARVASGALTVG---TLVAFLLYLFQLIT----PLSQLSSFFTQLQKAL 283
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
379-581 |
3.63e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 58.01 E-value: 3.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 379 FNLHikAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIE--DVTQDS-------LRANIALVTQDTSLLHR- 448
Cdd:PRK11701 27 FDLY--PGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQlrDLYALSeaerrrlLRTEWGFVHQHPRDGLRm 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 449 --SVAENI----------KYGRPDATDHDMQSAVhkakaaEFIPQLVDLKGRSgyeaqvgergvkLSGGQRQRIAIARVf 516
Cdd:PRK11701 105 qvSAGGNIgerlmavgarHYGDIRATAGDWLERV------EIDAARIDDLPTT------------FSGGMQQRLQIARN- 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 517 LKDAPILIL-DEATSALDSEVEAAIQSSLNDLMVDK--TVIAIAHRLStIAQM--DRLIVLDEGKIAEQG 581
Cdd:PRK11701 166 LVTHPRLVFmDEPTGGLDVSVQARLLDLLRGLVRELglAVVIVTHDLA-VARLlaHRLLVMKQGRVVESG 234
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
366-577 |
6.07e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.03 E-value: 6.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 366 VTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAI-LIDGQNIEDVTQDSLranialvtqdts 444
Cdd:PRK10636 318 VSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQL------------ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 445 llhrsvaeniKYGRPDATdhDMQsavHKAKAA--EFIPQLVDLKGRSGYEA-QVGERGVKLSGGQRQRIAIARVFLKDAP 521
Cdd:PRK10636 386 ----------EFLRADES--PLQ---HLARLApqELEQKLRDYLGGFGFQGdKVTEETRRFSGGEKARLVLALIVWQRPN 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 746197230 522 ILILDEATSALDSEVEAAIQSSLNDLmvDKTVIAIAHRLSTI-AQMDRLIVLDEGKI 577
Cdd:PRK10636 451 LLLLDEPTNHLDLDMRQALTEALIDF--EGALVVVSHDRHLLrSTTDDLYLVHDGKV 505
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
365-533 |
8.59e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 55.73 E-value: 8.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 365 DVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIeDVTQDSLRANIALVTQDTS 444
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI-KKDLCTYQKQLCFVGHRSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 445 L-LHRSVAENIKYGrpdatdhdmqsaVHKAKAAEFIPQLVDLKGRSGY-EAQVGergvKLSGGQRQRIAIARVFLKDAPI 522
Cdd:PRK13540 85 InPYLTLRENCLYD------------IHFSPGAVGITELCRLFSLEHLiDYPCG----LLSSGQKRQVALLRLWMSKAKL 148
|
170
....*....|.
gi 746197230 523 LILDEATSALD 533
Cdd:PRK13540 149 WLLDEPLVALD 159
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
375-586 |
1.22e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 57.88 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 375 VIDHFNLHIKAGEKIGIVGRSGAGKSTL-IQLLLHFYHLK-EGAILIDGQNIEDVT-QDSLRANIALVTQDTS----LLH 447
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYGRNiSGTVFKDGKEVDVSTvSDAIDAGLAYVTEDRKgyglNLI 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 448 RSVAENI------KYGRPDATDHDMQSAVhkakAAEFipqLVDLKGRSgyeAQVGERGVKLSGGQRQRIAIARVFLKDAP 521
Cdd:NF040905 355 DDIKRNItlanlgKVSRRGVIDENEEIKV----AEEY---RKKMNIKT---PSVFQKVGNLSGGNQQKVVLSKWLFTDPD 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 746197230 522 ILILDEATSALDSEVEAAIQSSLNDLMVD-KTVIAIAHRLSTIAQM-DRLIVLDEGKI-----AEQGTHEEL 586
Cdd:NF040905 425 VLILDEPTRGIDVGAKYEIYTIINELAAEgKGVIVISSELPELLGMcDRIYVMNEGRItgelpREEASQERI 496
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
378-578 |
1.42e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.37 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 378 HFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNI-EDVTQDSLRANIALVTQDTS----LLHRSVAE 452
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEInALSTAQRLARGLVYLPEDRQssglYLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 453 NIKygrpDATDHDMQSAVHKAKAAEFIPQlvdlkgrsgYEAQVG------ERGVK-LSGGQRQRIAIARVFLKDAPILIL 525
Cdd:PRK15439 361 NVC----ALTHNRRGFWIKPARENAVLER---------YRRALNikfnhaEQAARtLSGGNQQKVLIAKCLEASPQLLIV 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 746197230 526 DEATSALDSEVEAAIQSSLNDLMVDKT-VIAIAHRLSTIAQM-DRLIVLDEGKIA 578
Cdd:PRK15439 428 DEPTRGVDVSARNDIYQLIRSIAAQNVaVLFISSDLEEIEQMaDRVLVMHQGEIS 482
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
40-309 |
1.55e-08 |
|
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: 56.28 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 40 LLLLVICTAGAATFEALLFSKIGQLVDWLSKSQPESFLSQHAsnILILISVLFANI-LFVN--IQSIIKHQILystfpMR 116
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVP--LAIIGLFLLRGLaSYLQtyLMAYVGQRVV-----RD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 117 LRWRFHNLLLKQSLDFFHNDFAGRLSAKVMQTALAIREFWIILGDMLAYVSIYFITVSIVLGAISPTL------LIPLMV 190
Cdd:cd18552 74 LRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLtlialvVLPLAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 191 WLglfllsAWFFIPRLSKVSQQQADARAVMTGRVTDAYTNIQTVKLFAHAGRESQYAKASMKEFMTTVYAQMRLGTLFEV 270
Cdd:cd18552 154 LP------IRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSP 227
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 746197230 271 SINMLSAVLFVGVIGTAVWLWTQGLAALGVIAA-TTAMIL 309
Cdd:cd18552 228 LMELLGAIAIALVLWYGGYQVISGELTPGEFISfITALLL 267
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
376-586 |
1.58e-08 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 55.77 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 376 IDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVT-QDSLRANIALVTQDTSLLHR-SVAEN 453
Cdd:PRK11300 21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPgHQIARMGVVRTFQHVRLFREmTVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 454 ikygrpdatdhdMQSAVHKAKAAEFIPQLVDLKG--RSGYEA---------QVGERGV------KLSGGQRQRIAIARVF 516
Cdd:PRK11300 101 ------------LLVAQHQQLKTGLFSGLLKTPAfrRAESEAldraatwleRVGLLEHanrqagNLAYGQQRRLEIARCM 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 746197230 517 LKDAPILILDEATSALD----SEVEAAIQSSLNDLMVdkTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEEL 586
Cdd:PRK11300 169 VTQPEILMLDEPAAGLNpketKELDELIAELRNEHNV--TVLLIEHDMKLVMGIsDRIYVVNQGTPLANGTPEEI 241
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
364-586 |
1.91e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 55.93 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 364 KDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVTQDSL---RANIALVT 440
Cdd:PRK11831 11 RGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSMLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 441 QDTSLL-HRSVAENIKYGRPDatdhdmqsavHKAKAAEFIPQLVDLKgrsgYEAqVGERGV------KLSGGQRQRIAIA 513
Cdd:PRK11831 91 QSGALFtDMNVFDNVAYPLRE----------HTQLPAPLLHSTVMMK----LEA-VGLRGAaklmpsELSGGMARRAALA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 746197230 514 RVFLKDAPILILDEATSALDS---EVEAAIQSSLNDLMvDKTVIAIAHRLSTIAQM-DRLIVLDEGKIAEQGTHEEL 586
Cdd:PRK11831 156 RAIALEPDLIMFDEPFVGQDPitmGVLVKLISELNSAL-GVTCVVVSHDVPEVLSIaDHAYIVADKKIVAHGSAQAL 231
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
61-298 |
2.49e-08 |
|
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: 55.56 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 61 IGQLVDW-LSKSQPESFLsqHASNILILISVLFA----------NILFVNIQSIIKHQILYStfpmrlrwrfhnlLLKQS 129
Cdd:cd18589 19 TGRMTDWiMNKDAPEAFT--AAITVMSLLTIASAvsefvcdliyNITMSRIHSRLQGLVFAA-------------VLRQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 130 LDFFHNDFAGRLSAKVMQTALAIREfwiILGDMLAYVSIYFITVSIVLGAI---SPTLLipLMVWLGLFLLsawFFIPRL 206
Cdd:cd18589 84 IAFFDSNQTGDIVSRVTTDTEDMSE---SLSENLSLLMWYLARGLFLFIFMlwlSPKLA--LLTALGLPLL---LLVPKF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 207 S---------KVSQQQADARAVmtgrVTDAYTNIQTVKLFAHAGRESQYAKASMKEFMTtvyaqmrlgtlfevsINMLSA 277
Cdd:cd18589 156 VgkfqqslavQVQKSLARANQV----AVETFSAMKTVRSFANEEGEAQRYRQRLQKTYR---------------LNKKEA 216
|
250 260
....*....|....*....|.
gi 746197230 278 VLFvgvigtAVWLWTQGLAAL 298
Cdd:cd18589 217 AAY------AVSMWTSSFSGL 231
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
360-558 |
3.31e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.28 E-value: 3.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 360 EIVF--KDVTFAYN-NKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLiqlllhfyhLK---------EG-AILIDGQNI-- 424
Cdd:PRK11819 4 QYIYtmNRVSKVVPpKKQILKDISLSFFPGAKIGVLGLNGAGKSTL---------LRimagvdkefEGeARPAPGIKVgy 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 425 ---E---DVTQDsLRANIALVTQDT-SLLHRSVAENIKYGRP------------------DATD-HDMQSAVHKAKAAEF 478
Cdd:PRK11819 75 lpqEpqlDPEKT-VRENVEEGVAEVkAALDRFNEIYAAYAEPdadfdalaaeqgelqeiiDAADaWDLDSQLEIAMDALR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 479 IPQlvdlkgrsgYEAQVGergvKLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLmvDKTVIAIAH 558
Cdd:PRK11819 154 CPP---------WDAKVT----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDY--PGTVVAVTH 218
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
373-575 |
5.73e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.81 E-value: 5.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 373 KNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEdvtqdslranialVTQDTSLLhrsvaE 452
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQ-------------FGREASLI-----D 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 453 NIkYGRPDATDhdmqsavhkakAAEFIpqlvdlkGRSGY-EAQVGERGVK-LSGGQRQRIAIARVFLKDAPILILDEATS 530
Cdd:COG2401 105 AI-GRKGDFKD-----------AVELL-------NAVGLsDAVLWLRRFKeLSTGQKFRFRLALLLAERPKLLVIDEFCS 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 746197230 531 ALDSEVEAAIQSSLNDLM--VDKTVIAIAHRLSTIA--QMDRLIVLDEG 575
Cdd:COG2401 166 HLDRQTAKRVARNLQKLArrAGITLVVATHHYDVIDdlQPDLLIFVGYG 214
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
78-292 |
1.18e-07 |
|
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: 53.75 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 78 SQHASNILILISVLFANILFVNIQSIIKHQILYST---FPMRLRWRFHNLLLKQSLDFFHNDFAGRLSAKVMQTALaIRE 154
Cdd:cd18782 35 QQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTanrIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRISELDT-IRG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 155 FwiILGDMLAY-VSIYFITVSI-VLGAISPTLLIPLMVWLGLFLLSAWFFIPRLSKVSQQQADARAVMTGRVTDAYTNIQ 232
Cdd:cd18782 114 F--LTGTALTTlLDVLFSVIYIaVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQ 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 746197230 233 TVKlfahagreSQYAKASMKEFMTTVYAQMrLGTLFEVS-INMLSAVL--FVGVIGTAVWLWT 292
Cdd:cd18782 192 TVK--------AQNAELKARWRWQNRYARS-LGEGFKLTvLGTTSGSLsqFLNKLSSLLVLWV 245
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
366-582 |
1.27e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 53.29 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 366 VTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLL---LHFYHLKEGA-----ILIDGQNIEDVTQDSL-RANI 436
Cdd:PRK13547 7 LHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALagdLTGGGAPRGArvtgdVTLNGEPLAAIDAPRLaRLRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 437 ALVTQDTSLLHRSVAENIKYGRpdaTDHDMQSAVHKAKAAEFIPQLVDlkgRSGYEAQVGERGVKLSGGQRQRIAIARVF 516
Cdd:PRK13547 87 VLPQAAQPAFAFSAREIVLLGR---YPHARRAGALTHRDGEIAWQALA---LAGATALVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 746197230 517 LK---------DAPILILDEATSALDSEVEAAIQSSLNDLMVD--KTVIAIAHRLSTIAQ-MDRLIVLDEGKIAEQGT 582
Cdd:PRK13547 161 AQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwnLGVLAIVHDPNLAARhADRIAMLADGAIVAHGA 238
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
85-303 |
1.52e-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: 53.24 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 85 LILISVLFANILFVN---------IQSIIKHQILYstfpmRLRWRFHNLLLKQSLDFFHNDFAGRLSAKVMQTALAIREF 155
Cdd:cd18545 39 LLIIALLFLALNLVNwvasrlriyLMAKVGQRILY-----DLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 156 WI-----ILGDMLayvSIYFITvsIVLGAISPTLLIPLMVWLGLFLLSAWFFIPRLSKVSQQQADARAVMTGRVTDAYTN 230
Cdd:cd18545 114 LSnglinLIPDLL---TLVGIV--IIMFSLNVRLALVTLAVLPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISG 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 746197230 231 IQTVKLFAHAGRESQY----AKASMKEFMTTVyaqmRLGTLFEVSINMLSAVLFVGVIGTAVWLWTQGLAALGVIAA 303
Cdd:cd18545 189 IRVIQSFAREDENEEIfdelNRENRKANMRAV----RLNALFWPLVELISALGTALVYWYGGKLVLGGAITVGVLVA 261
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
361-575 |
1.62e-07 |
|
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: 51.86 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNV----IDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYH--LKEGAILIDGQNIEDvtqdSLRA 434
Cdd:cd03232 4 LTWKNLNYTVPVKGGkrqlLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLDK----NFQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 435 NIALVTQ-DTSLLHRSVAENIKYgrpdatdhdmqSAVhkakaaefipqlvdLKGrsgyeaqvgergvkLSGGQRQRIAIA 513
Cdd:cd03232 80 STGYVEQqDVHSPNLTVREALRF-----------SAL--------------LRG--------------LSVEQRKRLTIG 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 746197230 514 rVFLKDAP-ILILDEATSALDSEVEAAIQSSLNDL-MVDKTVIAIAHRLS--TIAQMDRLIVLDEG 575
Cdd:cd03232 121 -VELAAKPsILFLDEPTSGLDSQAAYNIVRFLKKLaDSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
500-582 |
1.90e-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: 51.42 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 500 VKLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMV--DKTVIAIAHRLSTIAQM-DRLIVLdEGK 576
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYLsDRIHVF-EGE 148
|
....*.
gi 746197230 577 IAEQGT 582
Cdd:cd03222 149 PGVYGI 154
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
104-313 |
2.05e-07 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). 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. 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: 349998 [Multi-domain] Cd Length: 299 Bit Score: 52.81 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 104 IKHQILYStfpmrLRWRFHNLLLKQSLDFFHNDFAGRLSAKVMQTALAIREFWII-LGDMLAYVSIYFITVSIVLgAISP 182
Cdd:cd18554 73 IANKILYD-----IRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTgLMNIWLDMITIIIAICIML-VLNP 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 183 TLLIPLMVWLGLFLLSAWFFIPRLSKVSQQQADARAVMTGRVTDAYTNIQTVKLFAHAGRESQYAKASMKEFMTTVYAQM 262
Cdd:cd18554 147 KLTFVSLVIFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHT 226
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 746197230 263 RLGTLFEVSINMLSAVLFVGVIGTAVWLWTQGLAALGVIAATTAMILKLNS 313
Cdd:cd18554 227 RWNAKTFSAVNTITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYS 277
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
84-303 |
3.74e-07 |
|
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: 52.00 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 84 ILILISVLFANILFVNIQSIIKHQILYstfpmRLRWRFHNLLLKQSLDFFHNDFAGRLSAKVMQTALAIREFWI-----I 158
Cdd:cd18544 48 LGLLLLSFLLQYLQTYLLQKLGQRIIY-----DLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTsglvtL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 159 LGDMLayvsiYFITVSIVLGAISPTLLIPLMVWLGLFLLSAWFFIPRLSKVSQQQADARAVMTGRVTDAYTNIQTVKLFa 238
Cdd:cd18544 123 IGDLL-----LLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLF- 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 746197230 239 haGREsqyaKASMKEF-------MTTVYAQMRLGTLFEVSINMLSAVLFVGVIGTAVWLWTQGLAALGVIAA 303
Cdd:cd18544 197 --NRE----KREFEEFdeinqeyRKANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVLSGAVTLGVLYA 262
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
115-325 |
5.45e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 51.74 E-value: 5.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 115 MRLRWRFHNLLLKQSLDFFHNDFAGRLSAKVMQTALAIREF--WIILGdmLAYVSIYFITVSIVLGAISPTL------LI 186
Cdd:cd18563 76 ADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFlsDGLPD--FLTNILMIIGIGVVLFSLNWKLallvliPV 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 187 PLMVWLglfllsAWFFIPRLSKVSQQQADARAVMTGRVTDAYTNIQTVKLFAHAGRESQ-YAKASMKEFMTTVYAQMRLG 265
Cdd:cd18563 154 PLVVWG------SYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKrFDEANQELLDANIRAEKLWA 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 746197230 266 TLFEVsINMLSAVLFVGVIGTAVWLWTQGLAALGVIAATTAMILK----LNSMAEFMMWHMSAL 325
Cdd:cd18563 228 TFFPL-LTFLTSLGTLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMfygpLQWLSRLNNWITRAL 290
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
364-609 |
5.55e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 51.33 E-value: 5.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 364 KDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLL--HFYHLKEGAILIDGQNIEDVT-QDSLRANIALVT 440
Cdd:PRK09580 5 KDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSpEDRAGEGIFMAF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 441 Q---------DTSLLHRSVAENIKYGRPDATDH-DMQSAVHKAKAAEFIPQlvDLKGRSgyeAQVGergvkLSGGQRQRI 510
Cdd:PRK09580 85 QypveipgvsNQFFLQTALNAVRSYRGQEPLDRfDFQDLMEEKIALLKMPE--DLLTRS---VNVG-----FSGGEKKRN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 511 AIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDK-TVIAIAH--RLSTIAQMDRLIVLDEGKIAEQGTHEeli 587
Cdd:PRK09580 155 DILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKrSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFT--- 231
|
250 260
....*....|....*....|..
gi 746197230 588 akngiYAQLWKRQTGGFLIEQK 609
Cdd:PRK09580 232 -----LVKQLEEQGYGWLTEQQ 248
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
40-312 |
9.38e-07 |
|
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: 50.89 E-value: 9.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 40 LLLLVICTAGAATFEALLFSKIGQLVDwlsksqpeSFLSQHASNILILISVLFanILFVNIQSIIK--HQILYSTFP--- 114
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIID--------SVIGGGLRELLWLLALLI--LGVALLRGVFRylQGYLAEKASqkv 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 115 -MRLRWRFHNLLLKQSLDFFHNDFAGRLSAKVMQTALAIREF--WIILgdMLAYVSIYFITVSIVLGAISPTL-LIPLMV 190
Cdd:cd18542 71 aYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFlaFGLV--ELVRAVLLFIGALIIMFSINWKLtLISLAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 191 WLGLFLLSAWFFIpRLSKVSQQQADARAVMTGRVTDAYTNIQTVKLFAHAGRESQ-YAKASmKEFMTTVYAQMRLGTLFE 269
Cdd:cd18542 149 IPFIALFSYVFFK-KVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEkFDKEN-EEYRDLNIKLAKLLAKYW 226
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 746197230 270 VSINMLSAVLFVGVIGTAVWLWTQGLAALGVIAATTAMILKLN 312
Cdd:cd18542 227 PLMDFLSGLQIVLVLWVGGYLVINGEITLGELVAFISYLWMLI 269
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
41-285 |
1.39e-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: 50.23 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 41 LLLVICTAGAATFEALLFSK-IGQLVDWLSksQPESFLSQHASNILILISVLFANILFVNIQSIIKH----QILYStfpm 115
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWlIRELVDLVT--IGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHvaeqKVVAD---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 116 rLRWRFHNLLLKQSLDFFHNDFAGRLSAKVMQTAlaiREFWIILGDMLAYVSIYFIT---VSIVLGAISPTL----LIPL 188
Cdd:cd18778 75 -LRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDV---ANVERLIADGIPQGITNVLTlvgVAIILFSINPKLalltLIPI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 189 MvwlgLFLLSAWFFIPRLSKVSQQQADARAVMTGRVTDAYTNIQTVKLFAHAGRES-QYAKASMKEFMTTVYAqMRLGTL 267
Cdd:cd18778 151 P----FLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAkRFEALSRRYRKAQLRA-MKLWAI 225
|
250
....*....|....*...
gi 746197230 268 FEVSINMLSAVLFVGVIG 285
Cdd:cd18778 226 FHPLMEFLTSLGTVLVLG 243
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
349-578 |
1.56e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.40 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 349 PEAKPlavkQGEIV-FKDVTFAYNNKNVI-DHFNLHIKAGEKIGIVGRSGAGKSTLIQLllhfyhlkegaILIDGQNIED 426
Cdd:PLN03073 500 PDDRP----GPPIIsFSDASFGYPGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKL-----------ISGELQPSSG 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 427 VTQDSLRANIALVTQdtsllHRSvaenikygrpDATDHDMQSAVHKAKAaefIPQLVDLKGRsgyeAQVGERGVK----- 501
Cdd:PLN03073 565 TVFRSAKVRMAVFSQ-----HHV----------DGLDLSSNPLLYMMRC---FPGVPEQKLR----AHLGSFGVTgnlal 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 502 -----LSGGQRQRIAIARVFLKDAPILILDEATSALDSE-VEAAIQSSlndLMVDKTVIAIAHRLSTIA-QMDRLIVLDE 574
Cdd:PLN03073 623 qpmytLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDaVEALIQGL---VLFQGGVLMVSHDEHLISgSVDELWVVSE 699
|
....
gi 746197230 575 GKIA 578
Cdd:PLN03073 700 GKVT 703
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
40-285 |
1.76e-06 |
|
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: 50.17 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 40 LLLLVICTAGAATFEALlfskIGQLVDwlsksqpeSFLSQHASNILILISVLFANILFVniQSIIK--HQILYSTFPMR- 116
Cdd:cd18576 2 LILLLLSSAIGLVFPLL----AGQLID--------AALGGGDTASLNQIALLLLGLFLL--QAVFSffRIYLFARVGERv 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 117 ---LRWRFHNLLLKQSLDFFHN----DFAGRLSAKVMQtalaIREFwiiLGDMLAYVSIYFITVS---IVLGAISPTLLI 186
Cdd:cd18576 68 vadLRKDLYRHLQRLPLSFFHErrvgELTSRLSNDVTQ----IQDT---LTTTLAEFLRQILTLIggvVLLFFISWKLTL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 187 PLMVWLGLFLLSAWFFIPRLSKVSQQQADARAVMTGRVTDAYTNIQTVKLFAHAGRESQYAKASMKEFMTTVYAQMRLGT 266
Cdd:cd18576 141 LMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRA 220
|
250
....*....|....*....
gi 746197230 267 LFEVSInmlSAVLFVGVIG 285
Cdd:cd18576 221 LFSSFI---IFLLFGAIVA 236
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
361-533 |
1.89e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.94 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLlhfyhlkEGAILIDGQNIedvtqdSLRANIAL-- 438
Cdd:PRK10636 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALL-------KNEISADGGSY------TFPGNWQLaw 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 439 VTQDTSLLHRS--------------------VAENIKYGRPDATDHDMQSAVH----KAKAAEFIPQLvdlkgrsGYEAQ 494
Cdd:PRK10636 69 VNQETPALPQPaleyvidgdreyrqleaqlhDANERNDGHAIATIHGKLDAIDawtiRSRAASLLHGL-------GFSNE 141
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 746197230 495 VGERGVK-LSGGQRQRIAIARVFLKDAPILILDEATSALD 533
Cdd:PRK10636 142 QLERPVSdFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD 181
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
379-578 |
2.16e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.50 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 379 FNLHikAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNIEDVT-QDSLRANIALVTQDtsllHRSVAeniKYG 457
Cdd:PRK10982 269 FDLH--KGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaNEAINHGFALVTEE----RRSTG---IYA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 458 RPDATDHDMQSAVHKAKAAefIPQLVDLKGRSGYEAQVGERGVK----------LSGGQRQRIAIARVFLKDAPILILDE 527
Cdd:PRK10982 340 YLDIGFNSLISNIRNYKNK--VGLLDNSRMKSDTQWVIDSMRVKtpghrtqigsLSGGNQQKVIIGRWLLTQPEILMLDE 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 746197230 528 ATSALDSEVEAAIQSSLNDLM-VDKTVIAIAHRLSTIAQM-DRLIVLDEGKIA 578
Cdd:PRK10982 418 PTRGIDVGAKFEIYQLIAELAkKDKGIIIISSEMPELLGItDRILVMSNGLVA 470
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
379-561 |
2.38e-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: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 379 FNLH----IKAGEKIGIVGRSGAGKSTLIQLL--------------------LHFYhlkEGAILidgQN-IEDVTQDSLR 433
Cdd:cd03236 15 FKLHrlpvPREGQVLGLVGPNGIGKSTALKILagklkpnlgkfddppdwdeiLDEF---RGSEL---QNyFTKLLEGDVK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 434 ANIAlvTQDTSLLHRSVAENIKygrpdatdhDMQSAVHKAKAAEFIPQLVDLKGrsgyeaqVGERGV-KLSGGQRQRIAI 512
Cdd:cd03236 89 VIVK--PQYVDLIPKAVKGKVG---------ELLKKKDERGKLDELVDQLELRH-------VLDRNIdQLSGGELQRVAI 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 746197230 513 ARVFLKDAPILILDEATSALD--SEVEAA--IQSSLNDlmvDKTVIAIAHRLS 561
Cdd:cd03236 151 AAALARDADFYFFDEPSSYLDikQRLNAArlIRELAED---DNYVLVVEHDLA 200
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
371-572 |
5.52e-06 |
|
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: 48.38 E-value: 5.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 371 NN-KNVidhfNLHIKAGEKIGIVGRSGAGKSTLIQLLLH-----FYHLK----------EGAILIDgqNIEDVTQD---- 430
Cdd:cd03271 9 NNlKNI----DVDIPLGVLTCVTGVSGSGKSSLINDTLYpalarRLHLKkeqpgnhdriEGLEHID--KVIVIDQSpigr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 431 SLRANIALVTQDTSLL-------------HRSVAEnIKY-GRPDATDHDMQSAvhkaKAAEF---IPQ-------LVDLk 486
Cdd:cd03271 83 TPRSNPATYTGVFDEIrelfcevckgkryNRETLE-VRYkGKSIADVLDMTVE----EALEFfenIPKiarklqtLCDV- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 487 gRSGYeAQVGERGVKLSGGQRQRIAIARVFLKDAP---ILILDEATSALDSEVEAAIQSSLNDLmVDK--TVIAIAHRLS 561
Cdd:cd03271 157 -GLGY-IKLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRL-VDKgnTVVVIEHNLD 233
|
250
....*....|.
gi 746197230 562 TIAQMDRLIVL 572
Cdd:cd03271 234 VIKCADWIIDL 244
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
361-535 |
1.01e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.58 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 361 IVFKDVTFAYNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIdGQNIE----DVTQDSLRANi 436
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVKlayvDQSRDALDPN- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 437 ALVTQDTSllhrSVAENIKYGrpdatDHDMQSavhKAKAAEFipqlvdlkGRSGYEAQ--VGErgvkLSGGQRQRIAIAR 514
Cdd:PRK11819 403 KTVWEEIS----GGLDIIKVG-----NREIPS---RAYVGRF--------NFKGGDQQkkVGV----LSGGERNRLHLAK 458
|
170 180
....*....|....*....|.
gi 746197230 515 VFLKDAPILILDEATSALDSE 535
Cdd:PRK11819 459 TLKQGGNVLLLDEPTNDLDVE 479
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
57-290 |
1.05e-05 |
|
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: 47.83 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 57 LFSKIgqLVDwlsksqpeSFLSQHASNILILISVLFANILFV-NIQSIIKHQILYST---FPMRLRWRFHNLLLKQSLDF 132
Cdd:cd18570 23 FFFQI--LID--------DIIPSGDINLLNIISIGLILLYLFqSLLSYIRSYLLLKLsqkLDIRLILGYFKHLLKLPLSF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 133 FHNDFAGRLSAKVMQtALAIREFW--IILGDMLAyvSIYFITVSIVLGAISPTLLIPLMVWLGLFLLSAWFFIPRLSKVS 210
Cdd:cd18570 93 FETRKTGEIISRFND-ANKIREAIssTTISLFLD--LLMVIISGIILFFYNWKLFLITLLIIPLYILIILLFNKPFKKKN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 211 QQQADARAVMTGRVTDAYTNIQTVKLFahaGRESQYAK---ASMKEFMTTVYAQMRLGTLFEVSINMLSAVLFVGVIGTA 287
Cdd:cd18570 170 REVMESNAELNSYLIESLKGIETIKSL---NAEEQFLKkieKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIG 246
|
...
gi 746197230 288 VWL 290
Cdd:cd18570 247 SYL 249
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
375-588 |
1.25e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.49 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 375 VIDHFNLHIKAGEKIGIVGRSGAGKStLIqlllhfyhlkegAILIDGQNIED--VTQDSLRANialvtqDTSLLHRSVAE 452
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKS-LI------------AKAICGVTKDNwrVTADRMRFD------DIDLLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 453 nikygRPDATDHDM-------QSAVHKAKA-----AEFIP---------QLVDLKGRSGYEA--QVGERGVK-------- 501
Cdd:PRK15093 83 -----RRKLVGHNVsmifqepQSCLDPSERvgrqlMQNIPgwtykgrwwQRFGWRKRRAIELlhRVGIKDHKdamrsfpy 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 502 -LSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVDK--TVIAIAHRLSTIAQM-DRLIVLDEGKI 577
Cdd:PRK15093 158 eLTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNntTILLISHDLQMLSQWaDKINVLYCGQT 237
|
250
....*....|.
gi 746197230 578 AEQGTHEELIA 588
Cdd:PRK15093 238 VETAPSKELVT 248
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
380-596 |
1.45e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.70 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 380 NLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILIDGQNI---------EDVTQDSLRANIALVTQDTSLLHRSV 450
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHItrlsfeqlqKLVSDEWQRNNTDMLSPGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 451 AENIkygrpdatdhdmQSAVHKAKAAEFIPQLVdlkgrsGYEAQVGERGVKLSGGQRQRIAIARVFLKDAPILILDEATS 530
Cdd:PRK10938 103 AEII------------QDEVKDPARCEQLAQQF------GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 746197230 531 ALDSEVEAAIQSSLNDLMVDK-TVIAIAHRLSTI-AQMDRLIVLDEGKIAEQGTHEELIAKnGIYAQL 596
Cdd:PRK10938 165 GLDVASRQQLAELLASLHQSGiTLVLVLNRFDEIpDFVQFAGVLADCTLAETGEREEILQQ-ALVAQL 231
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
500-570 |
2.35e-05 |
|
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: 45.04 E-value: 2.35e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 746197230 500 VKLSGGQRQRIAIARVF----LKDAPILILDEATSALDSEVEAAIQSSLNDLMVDK-TVIAIAHRLSTIAQMDRLI 570
Cdd:cd03227 76 LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGaQVIVITHLPELAELADKLI 151
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
502-570 |
3.20e-05 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 45.15 E-value: 3.20e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 746197230 502 LSGGQRQRIAIARVF----LKDAPILILDEATSALDsEVEAAIQSSLNDLMVDKT-VIAIAHRLSTIAQMDRLI 570
Cdd:cd03278 114 LSGGEKALTALALLFaifrVRPSPFCVLDEVDAALD-DANVERFARLLKEFSKETqFIVITHRKGTMEAADRLY 186
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
502-587 |
3.24e-05 |
|
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: 46.93 E-value: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 502 LSGGQRQRIAIARVFLKDA---PILILDEATSALDSEVEAAIQSSLNDLmVDK--TVIAIAHRLSTIAQMDRLIVLDE-- 574
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRStgrTLYILDEPTTGLHFDDIKKLLEVLQRL-VDKgnTVVVIEHNLDVIKTADYIIDLGPeg 908
|
90
....*....|....*..
gi 746197230 575 ----GKIAEQGTHEELI 587
Cdd:TIGR00630 909 gdggGTVVASGTPEEVA 925
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
116-304 |
4.58e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 45.58 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 116 RLRWRFHNLLLKQSLDFFHNDFAGRLSAKVMQTALAIREFwiiLGDMLAYVSIYFITVSIVLGA---ISPTL-LIPLMVw 191
Cdd:cd18564 88 DLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDL---LVSGVLPLLTNLLTLVGMLGVmfwLDWQLaLIALAV- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 192 LGLFLLSAWFFIPRLSKVSQQQADARAVMTGRVTDAYTNIQTVKLFA----HAGRESQYAKASMKEFMTTVyaqmRLGTL 267
Cdd:cd18564 164 APLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGreehEERRFARENRKSLRAGLRAA----RLQAL 239
|
170 180 190
....*....|....*....|....*....|....*..
gi 746197230 268 FEVSINMLSAVlfvgviGTAVWLWtqgLAALGVIAAT 304
Cdd:cd18564 240 LSPVVDVLVAV------GTALVLW---FGAWLVLAGR 267
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
391-548 |
5.37e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 44.52 E-value: 5.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 391 IVGRSGAGKSTLIQLLL------HFYHLKEGAILIDgqnieDVTQDSLRANIALVTQDtsllhrsvaenikygrpdATDH 464
Cdd:cd03240 27 IVGQNGAGKTTIIEALKyaltgeLPPNSKGGAHDPK-----LIREGEVRAQVKLAFEN------------------ANGK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 465 DMQ--SAVHKAKAAEFIPQ------LVDLKGRsgyeaqvgergvkLSGGQRQ------RIAIARVFLKDAPILILDEATS 530
Cdd:cd03240 84 KYTitRSLAILENVIFCHQgesnwpLLDMRGR-------------CSGGEKVlasliiRLALAETFGSNCGILALDEPTT 150
|
170
....*....|....*...
gi 746197230 531 ALDSEveaAIQSSLNDLM 548
Cdd:cd03240 151 NLDEE---NIEESLAEII 165
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
496-591 |
8.59e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.11 E-value: 8.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 496 GERGVKLSGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLNDLMVD-KTVIAIAHRLSTIAQM-DRLIVLD 573
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMEEAEQLaHELTVID 218
|
90
....*....|....*...
gi 746197230 574 EGKIAEQGTHEELIAKNG 591
Cdd:NF000106 219 RGRVIADGKVDELKTKVG 236
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
502-581 |
1.03e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 43.47 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 502 LSGGQRQRIAIAR-VFLKDAPIL-ILDEATSALDSEVEAAIQSSLNDLmVDK--TVIAIAHRLSTIAQMDRLIVL----- 572
Cdd:cd03238 88 LSGGELQRVKLASeLFSEPPGTLfILDEPSTGLHQQDINQLLEVIKGL-IDLgnTVILIEHNLDVLSSADWIIDFgpgsg 166
|
90
....*....|
gi 746197230 573 -DEGKIAEQG 581
Cdd:cd03238 167 kSGGKVVFSG 176
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
386-558 |
1.67e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.85 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 386 GEKIGIVGRSGAGKSTLIQLL--------------LHFYH-----------------------LKEGAILIDGQ---NIE 425
Cdd:PLN03073 203 GRHYGLVGRNGTGKTTFLRYMamhaidgipkncqiLHVEQevvgddttalqcvlntdiertqlLEEEAQLVAQQrelEFE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 426 DVTQDSLRANIALVTQDtsllhrSVAENIK--YGRPDATDHDmqSAvhKAKAAEFIPQLvdlkgrsGYEAQVGERGVK-L 502
Cdd:PLN03073 283 TETGKGKGANKDGVDKD------AVSQRLEeiYKRLELIDAY--TA--EARAASILAGL-------SFTPEMQVKATKtF 345
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 746197230 503 SGGQRQRIAIARVFLKDAPILILDEATSALDSEVEAAIQSSLndLMVDKTVIAIAH 558
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSH 399
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
171-303 |
2.40e-04 |
|
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: 43.55 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 171 ITVSIVLGAISpTLLIPLMVWLglfllsAWFFIPRLSKVSQQQADARAVMTGRVTDAYTNIQTVKLFahaGREsqyaKAS 250
Cdd:cd18547 141 LYISPLLTLIV-LVTVPLSLLV------TKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAF---NRE----EEA 206
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 746197230 251 MKEFM--------TTVYAQMrLGTLFEVSINMLSAVLFVGVIGTAVWLWTQGLAALGVIAA 303
Cdd:cd18547 207 IEEFDeineelykASFKAQF-YSGLLMPIMNFINNLGYVLVAVVGGLLVINGALTVGVIQA 266
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
61-282 |
3.56e-04 |
|
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: 42.89 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 61 IGQLVDWLSKS--QPESFLSQHASNILILISVL----FANILFVNIQSIIKHQILystfpMRLRWRFHNLLLKQSLDFFH 134
Cdd:cd18573 19 IGKLIDVASKEsgDIEIFGLSLKTFALALLGVFvvgaAANFGRVYLLRIAGERIV-----ARLRKRLFKSILRQDAAFFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 135 N----DFAGRLSAKVMQTALAirefwiiLGDMLAYVSIYFITVSIVLGA---ISPTLLIPLMVWLGLFLLSAWFFIPRLS 207
Cdd:cd18573 94 KnktgELVSRLSSDTSVVGKS-------LTQNLSDGLRSLVSGVGGIGMmlyISPKLTLVMLLVVPPIAVGAVFYGRYVR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 208 KVSQQQADARAVMTGRVTDAYTNIQTVKLFAHAGRESQ-YAKA-------SMKE-FMTTVYaqmrLGTLFeVSINM-LSA 277
Cdd:cd18573 167 KLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVErYAKKvdevfdlAKKEaLASGLF----FGSTG-FSGNLsLLS 241
|
....*
gi 746197230 278 VLFVG 282
Cdd:cd18573 242 VLYYG 246
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
40-303 |
3.79e-04 |
|
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: 42.86 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 40 LLLLVICTAGAATFEALlfskIGQLVDwlsksqpeSFLSQHASNILILISVLF---------ANILFVNIQSIIKHQILY 110
Cdd:cd18546 5 LLLVVVDTAASLAGPLL----VRYGID--------SGVRAGDLGVLLLAAAAYlavvlagwvAQRAQTRLTGRTGERLLY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 111 StfpMRLRWRFHnlLLKQSLDFFHNDFAGRLSAKvMQTAL-AIREFwiiLGDML--AYVSI-YFITVSIVLGAISPTL-L 185
Cdd:cd18546 73 D---LRLRVFAH--LQRLSLDFHERETSGRIMTR-MTSDIdALSEL---LQTGLvqLVVSLlTLVGIAVVLLVLDPRLaL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 186 IPLMVWLGLFLLSAWFfiPRLSKVSQQQA-DARAVMTGRVTDAYTNIQTVKLFAHAGR-ESQYAKASMKEFMTTVYAQmR 263
Cdd:cd18546 144 VALAALPPLALATRWF--RRRSSRAYRRArERIAAVNADLQETLAGIRVVQAFRRERRnAERFAELSDDYRDARLRAQ-R 220
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 746197230 264 LGTLFEVSINMLSAVLFVGVIGTAVWLWTQGLAALGVIAA 303
Cdd:cd18546 221 LVAIYFPGVELLGNLATAAVLLVGAWRVAAGTLTVGVLVA 260
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
44-238 |
3.93e-04 |
|
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: 42.92 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 44 VICTAGAATFEALLFSKIGQLVDWLSKSQPESFlSQHASNI------LILISVLFANILFVNIQSIikhQILYSTFPMRL 117
Cdd:cd18574 2 VLSALAAALVNIQIPLLLGDLVNVISRSLKETN-GDFIEDLkkpalkLLGLYLLQSLLTFAYISLL---SVVGERVAARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 118 RWRFHNLLLKQSLDFF--HN--DFAGRLSAKV--------MQTALAIREFWIILGDMlayVSIYFI--TVSIVLGAIspt 183
Cdd:cd18574 78 RNDLFSSLLRQDIAFFdtHRtgELVNRLTADVqefkssfkQCVSQGLRSVTQTVGCV---VSLYLIspKLTLLLLVI--- 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 746197230 184 llIPLMVWLGLFLLSawfFIPRLSKVSQQQaDARAvmTGRVTDAYTNIQTVKLFA 238
Cdd:cd18574 152 --VPVVVLVGTLYGS---FLRKLSRRAQAQ-VAKA--TGVADEALGNIRTVRAFA 198
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
502-570 |
3.99e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 3.99e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 746197230 502 LSGGQRQRIAIARVF----LKDAPILILDEATSALDsevEAAIQ--SSLNDLMVDKT-VIAIAHRLSTIAQMDRLI 570
Cdd:TIGR02168 1090 LSGGEKALTALALLFaifkVKPAPFCILDEVDAPLD---DANVErfANLLKEFSKNTqFIVITHNKGTMEVADQLY 1162
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
502-558 |
6.03e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 6.03e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 746197230 502 LSGGQRQ------RIAIARVFLKDAPILILDEATSALDSE----VEAAIQSSLNDLMVDKTVIAIAH 558
Cdd:PRK01156 802 LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDrrtnLKDIIEYSLKDSSDIPQVIMISH 868
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
37-244 |
1.02e-03 |
|
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: 41.67 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 37 RPYLLLLVICT--AGAAT-FEALLFSKigqLVDWLSKSQPESFLSQ--HASNILILISV--LFANILFVNIQSIIKHQIL 109
Cdd:cd18578 8 WPLLLLGLIGAiiAGAVFpVFAILFSK---LISVFSLPDDDELRSEanFWALMFLVLAIvaGIAYFLQGYLFGIAGERLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 110 ystfpMRLRWRFHNLLLKQSLDFF----HNdfAGRLSAKVMQTALAIREfwiILGDMLAYVSIYFITV--SIVLG-AISP 182
Cdd:cd18578 85 -----RRLRKLAFRAILRQDIAWFddpeNS--TGALTSRLSTDASDVRG---LVGDRLGLILQAIVTLvaGLIIAfVYGW 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 746197230 183 TLLIPLMVWLGLFLLSAWFFIPRLSKVSQQQADARAVMTGRVTDAYTNIQTVKLFahaGRES 244
Cdd:cd18578 155 KLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASL---TLED 213
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
40-249 |
1.75e-03 |
|
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: 40.92 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 40 LLLLVICTAGAATFEALLFSKIGQLVD-----WLSKSQPESFLSQHASNILILISVLFANILFVNIQSII-----KHQIl 109
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDaftdfGSGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACwtitgERQA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 110 ystfpMRLRWRFHNLLLKQSLDFFHNDFAGRLSAKVMQTALAIREfwII---LGDMLAYVSiYFITvSIVLG-AISPTL- 184
Cdd:cd18577 80 -----RRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQD--GIgekLGLLIQSLS-TFIA-GFIIAfIYSWKLt 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 746197230 185 -----LIPLMVwlglflLSAWFFIPRLSKVSQQQADARAVMTGRVTDAYTNIQTVKLFAHAGRESQ-YAKA 249
Cdd:cd18577 151 lvllaTLPLIA------IVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKrYSKA 215
|
|
| YqeH |
cd01855 |
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ... |
370-420 |
1.92e-03 |
|
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH induces an excess initiation of DNA replication, suggesting that it negatively controls initiation of chromosome replication. The YqeH subfamily is common in eukaryotes and sporadically present in bacteria with probable acquisition by plants from chloroplasts. Proteins of the YqeH family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases.
Pssm-ID: 206748 [Multi-domain] Cd Length: 191 Bit Score: 39.94 E-value: 1.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 746197230 370 YNNKNVIDHFNLHIKAGEKIGIVGRSGAGKSTLIQLLLHFYHLKEGAILID 420
Cdd:cd01855 109 WGVEELIEEIKKLAKYRGDVYVVGATNVGKSTLINALLKSNGGKVQAQALV 159
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
46-330 |
4.37e-03 |
|
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: 39.45 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 46 CTAGAATFEALLFSKIGQLVDWLSKS-QPESFlsqhASNILILISVLFANILFVNIQSIIKHqILYSTFPMRLRWRFHNL 124
Cdd:cd18572 4 FLVVAALSELAIPHYTGAVIDAVVADgSREAF----YRAVLLLLLLSVLSGLFSGLRGGCFS-YAGTRLVRRLRRDLFRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 125 LLKQSLDFFH----NDFAGRLSAKVMQTALAIRefwIILGDMLAYVsIYFITVSIVLGAISPTL-LIPLMVWLGLFLLSA 199
Cdd:cd18572 79 LLRQDIAFFDatktGELTSRLTSDCQKVSDPLS---TNLNVFLRNL-VQLVGGLAFMFSLSWRLtLLAFITVPVIALITK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 200 WF--FIPRLSKVSQQQ-ADARAVmtgrVTDAYTNIQTVKLFAHAGRESQYAKASMKEFMTTVYAQMRLGTLFEVSINMLS 276
Cdd:cd18572 155 VYgrYYRKLSKEIQDAlAEANQV----AEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQ 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 277 AVLFVGVigtavwLWTQGLAAL-GVIAA---TTAMI--LKLNSMAEFMMWHMSALFENVG 330
Cdd:cd18572 231 NGTQVLV------LFYGGHLVLsGRMSAgqlVTFMLyqQQLGEAFQSLGDVFSSLMQAVG 284
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
502-570 |
4.91e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 39.95 E-value: 4.91e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 746197230 502 LSGGQRQRIAIARVF----LKDAPILILDEATSALDSEVEAAIQSSLNDLMVDKTVIAIAHRLSTIAQMDRLI 570
Cdd:pfam02463 1078 LSGGEKTLVALALIFaiqkYKPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLV 1150
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
475-605 |
6.99e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.67 E-value: 6.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 475 AAEF---IPQ-------LVD--LkgrsGYeAQVGERGVKLSGGQRQRIAIARVFLKDA---PILILDEATSALDSEVEAA 539
Cdd:PRK00349 797 ALEFfeaIPKiarklqtLVDvgL----GY-IKLGQPATTLSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLHFEDIRK 871
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 746197230 540 IQSSLNDLmVDK--TVIAIAHRLSTIAQMDRLIVL-----DE-GKIAEQGTHEELIAKNGIYaqlwkrqTGGFL 605
Cdd:PRK00349 872 LLEVLHRL-VDKgnTVVVIEHNLDVIKTADWIIDLgpeggDGgGEIVATGTPEEVAKVEASY-------TGRYL 937
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
502-590 |
8.35e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.24 E-value: 8.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746197230 502 LSGGQRQRIAIARVFLKDAP---ILILDEATSAL---DseveaaIQ---SSLNDLmVDK--TVIAIAHRLSTIAQMDRLI 570
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTgktLYILDEPTTGLhfhD------IRkllEVLHRL-VDKgnTVVVIEHNLDVIKTADWII 899
|
90 100
....*....|....*....|....*.
gi 746197230 571 VL-----DE-GKIAEQGTHEElIAKN 590
Cdd:COG0178 900 DLgpeggDGgGEIVAEGTPEE-VAKV 924
|
|
| |
