|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
6-540 |
4.65e-161 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 470.80 E-value: 4.65e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 6 ENVMAILRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDLGALNSIVNDNISRdrGFRAFTEVFGTICILFTLSPQLAPVL 85
Cdd:COG1132 90 QRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQ--LVRSVVTLIGALVVLFVIDWRLALIV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 86 GLLMLAVSVLVAVYKRSTVPVYKSHGLAQATMSDCVSETFSAIRTVRSFSGEKRQMSIFGSQILAYKLSGLKLGTFKSIN 165
Cdd:COG1132 168 LLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALF 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 166 ESITRVAVYISLLALYCLGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDLRGTFAAIDRINSILNA-VDIDEA 244
Cdd:COG1132 248 FPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEpPEIPDP 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 245 layglERDIHTKKVQdenlklflsagpnvnirhldkyymsnlkstnnlrtltwaGDVCLDDVHFAYPlrPDVKVLDGLSL 324
Cdd:COG1132 328 -----PGAVPLPPVR---------------------------------------GEIEFENVSFSYP--GDRPVLKDISL 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 325 TLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVSIVNQEPVLFSLSVAENIAYGLPNe 404
Cdd:COG1132 362 TIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPD- 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 405 hVSKDDIIKAAKAANAHDFIISLPQGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEATSALDAVSERLVQSAL 484
Cdd:COG1132 441 -ATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEAL 519
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 145334131 485 NRLMKDRTTLVIAHRLSTVQSANQIAVCSDGKIIELGTHSELVAQKGSYASLVGTQ 540
Cdd:COG1132 520 ERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYRLQ 575
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
1-544 |
9.80e-122 |
|
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: 369.80 E-value: 9.80e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 1 MTAIWENVMAILRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDLGALNSIVNDNISRdrGFRAFTEVFGTICILFTLSPQ 80
Cdd:TIGR02204 82 VTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSM--ALRNALMCIGGLIMMFITSPK 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 81 LApvlGLLMLAVSVLVA---VYKRStvpVYKSHGLAQATMSDCVS---ETFSAIRTVRSFSGEKRQMSIFGSQILAYKLS 154
Cdd:TIGR02204 160 LT---SLVLLAVPLVLLpilLFGRR---VRKLSRESQDRIADAGSyagETLGAIRTVQAFGHEDAERSRFGGAVEKAYEA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 155 GLKLGTFKSINESITRVAVYISLLALYCLGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDLRGTFAAIDRINS 234
Cdd:TIGR02204 234 ARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIE 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 235 ILNAVDidealayglerDIHTKKVQDEnlklflsagPNVNIRhldkyymsnlkstnnlrtltwaGDVCLDDVHFAYPLRP 314
Cdd:TIGR02204 314 LLQAEP-----------DIKAPAHPKT---------LPVPLR----------------------GEIEFEQVNFAYPARP 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 315 DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVSIVNQEPVLFSLSVA 394
Cdd:TIGR02204 352 DQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVM 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 395 ENIAYGLPneHVSKDDIIKAAKAANAHDFIISLPQGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEATSALDA 474
Cdd:TIGR02204 432 ENIRYGRP--DATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDA 509
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 475 VSERLVQSALNRLMKDRTTLVIAHRLSTVQSANQIAVCSDGKIIELGTHSELVAQKGSYASLVgtqRLAF 544
Cdd:TIGR02204 510 ESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLA---RLQF 576
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
303-540 |
5.39e-121 |
|
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: 355.69 E-value: 5.39e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPLRPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVSIV 382
Cdd:cd03249 3 FKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 383 NQEPVLFSLSVAENIAYGLPNEHVSKDDIIKAAKAAnaHDFIISLPQGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPI 462
Cdd:cd03249 83 SQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANI--HDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145334131 463 LILDEATSALDAVSERLVQSALNRLMKDRTTLVIAHRLSTVQSANQIAVCSDGKIIELGTHSELVAQKGSYASLVGTQ 540
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
10-540 |
1.23e-115 |
|
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: 358.38 E-value: 1.23e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 10 AILRAQIFRRVLIQKAEFFDKYKVGELTG----------LLTSDLgaLNSIVNdnisrdrgfrAFTeVFGTICILFTLSP 79
Cdd:COG2274 229 LRLSSRFFRHLLRLPLSFFESRSVGDLASrfrdvesireFLTGSL--LTALLD----------LLF-VLIFLIVLFFYSP 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 80 QLApVLGLLMLAVSVLVAVY-----KRSTVPVYKSHGLAQATMSdcvsETFSAIRTVRSFSGEKRQMSIFGSQILAYKLS 154
Cdd:COG2274 296 PLA-LVVLLLIPLYVLLGLLfqprlRRLSREESEASAKRQSLLV----ETLRGIETIKALGAESRFRRRWENLLAKYLNA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 155 GLKLGTFKSINESITRVAVYISLLALYCLGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDLRGTFAAIDRINS 234
Cdd:COG2274 371 RFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDD 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 235 ILNAVDidealayglERDIHTKKVQDENLKlflsagpnvnirhldkyymsnlkstnnlrtltwaGDVCLDDVHFAYPlRP 314
Cdd:COG2274 451 ILDLPP---------EREEGRSKLSLPRLK----------------------------------GDIELENVSFRYP-GD 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 315 DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVSIVNQEPVLFSLSVA 394
Cdd:COG2274 487 SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIR 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 395 ENIAYGlpNEHVSKDDIIKAAKAANAHDFIISLPQGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEATSALDA 474
Cdd:COG2274 567 ENITLG--DPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDA 644
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145334131 475 VSERLVQSALNRLMKDRTTLVIAHRLSTVQSANQIAVCSDGKIIELGTHSELVAQKGSYASLVGTQ 540
Cdd:COG2274 645 ETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQ 710
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
12-537 |
2.88e-113 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 352.10 E-value: 2.88e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 12 LRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDLGALNSIVNDNISRdrGFRAFTEVFGTICILFTLSPQLAPV----LGL 87
Cdd:TIGR00958 236 IREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNV--LLRNLVMLLGLLGFMLWLSPRLTMVtlinLPL 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 88 LMLAVSVLVAVYKRSTVPVYKShgLAQATmsDCVSETFSAIRTVRSFSGEKRQMSIFGSQILayklSGLKLGTFKSINES 167
Cdd:TIGR00958 314 VFLAEKVFGKRYQLLSEELQEA--VAKAN--QVAEEALSGMRTVRSFAAEEGEASRFKEALE----ETLQLNKRKALAYA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 168 ----ITRV-AVYISLLALYClGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDLrgtfaaidrinsiLNAVDID 242
Cdd:TIGR00958 386 gylwTTSVlGMLIQVLVLYY-GGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGM-------------MQAVGAS 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 243 EalayglerdihtkkvqdenlKLFlsagpnvniRHLDKyyMSNLKSTNNLRTLTWAGDVCLDDVHFAYPLRPDVKVLDGL 322
Cdd:TIGR00958 452 E--------------------KVF---------EYLDR--KPNIPLTGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGL 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 323 SLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVSIVNQEPVLFSLSVAENIAYGLp 402
Cdd:TIGR00958 501 TFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGL- 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 403 nEHVSKDDIIKAAKAANAHDFIISLPQGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEATSALDAVSERLVQS 482
Cdd:TIGR00958 580 -TDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE 658
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 145334131 483 ALNRlmKDRTTLVIAHRLSTVQSANQIAVCSDGKIIELGTHSELVAQKGSYASLV 537
Cdd:TIGR00958 659 SRSR--ASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
301-536 |
1.31e-103 |
|
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: 311.09 E-value: 1.31e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 301 VCLDDVHFAYPLRPDvKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVS 380
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 381 IVNQEPVLFSLSVAENIAYGLPNEhvSKDDIIKAAKAANAHDFIISLPQGYDTLVGERGGLLSGGQRQRVAIARSLLKNA 460
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGA--TREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145334131 461 PILILDEATSALDAVSERLVQSALNRLMKDRTTLVIAHRLSTVQSANQIAVCSDGKIIELGTHSELVAQKGSYASL 536
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1-536 |
7.18e-102 |
|
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: 318.20 E-value: 7.18e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 1 MTAIWENVMAILRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDLGALNSIVNDNIS---RDRgfrafTEVFGTICILFTL 77
Cdd:TIGR02203 78 LSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIvlvRET-----LTVIGLFIVLLYY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 78 SPQLAPVLGLLMLAVSVLVAVYKRSTVPVYKSHGLAQATMSDCVSETFSAIRTVRSFSGEKRQMSIFGSQILAYKLSGLK 157
Cdd:TIGR02203 153 SWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMK 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 158 LGTFKSINESITRVAVYISLLALYCLGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDLRGTFAAIDRINSILN 237
Cdd:TIGR02203 233 MTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLD 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 238 AVDidealayglERDIHTkkvqdenlklflsagpnvniRHLDKYymsnlkstnnlrtltwAGDVCLDDVHFAYPLRpDVK 317
Cdd:TIGR02203 313 SPP---------EKDTGT--------------------RAIERA----------------RGDVEFRNVTFRYPGR-DRP 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 318 VLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVSIVNQEPVLFSLSVAENI 397
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNI 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 398 AYGLPNEhVSKDDIIKAAKAANAHDFIISLPQGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEATSALDAVSE 477
Cdd:TIGR02203 427 AYGRTEQ-ADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESE 505
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 145334131 478 RLVQSALNRLMKDRTTLVIAHRLSTVQSANQIAVCSDGKIIELGTHSELVAQKGSYASL 536
Cdd:TIGR02203 506 RLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQL 564
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
298-541 |
3.93e-100 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 314.84 E-value: 3.93e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 298 AGDVCLDDVHFAYplRPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAK 377
Cdd:COG5265 355 GGEVRFENVSFGY--DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 378 VVSIVNQEPVLFSLSVAENIAYGLPNehVSKDDIIKAAKAANAHDFIISLPQGYDTLVGERGGLLSGGQRQRVAIARSLL 457
Cdd:COG5265 433 AIGIVPQDTVLFNDTIAYNIAYGRPD--ASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLL 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 458 KNAPILILDEATSALDAVSERLVQSALNRLMKDRTTLVIAHRLSTVQSANQIAVCSDGKIIELGTHSELVAQKGSYASLV 537
Cdd:COG5265 511 KNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMW 590
|
....
gi 145334131 538 GTQR 541
Cdd:COG5265 591 ARQQ 594
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
301-536 |
1.54e-95 |
|
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: 290.29 E-value: 1.54e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 301 VCLDDVHFAYPlrPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVS 380
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 381 IVNQEPVLFSLSVAENIAYGLPNehVSKDDIIKAAKAANAHDFIISLPQGYDTLVGERGGLLSGGQRQRVAIARSLLKNA 460
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPD--ATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145334131 461 PILILDEATSALDAVSERLVQSALNRLMKDRTTLVIAHRLSTVQSANQIAVCSDGKIIELGTHSELVAQKGSYASL 536
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
293-531 |
3.01e-89 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 285.11 E-value: 3.01e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 293 RTLTWAG--DVCLDDVHFAYPlrPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMF 370
Cdd:COG4988 327 APLPAAGppSIELEDVSFSYP--GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 371 DKSEWAKVVSIVNQEPVLFSLSVAENIAYGLPNehVSKDDIIKAAKAANAHDFIISLPQGYDTLVGERGGLLSGGQRQRV 450
Cdd:COG4988 405 DPASWRRQIAWVPQNPYLFAGTIRENLRLGRPD--ASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 451 AIARSLLKNAPILILDEATSALDAVSERLVQSALNRLMKDRTTLVIAHRLSTVQSANQIAVCSDGKIIELGTHSELVAQK 530
Cdd:COG4988 483 ALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
.
gi 145334131 531 G 531
Cdd:COG4988 563 G 563
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
7-536 |
1.54e-88 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 283.83 E-value: 1.54e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 7 NVMAILRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDL--------GALNSIVNDNISrdrgfrafteVFGTICILFTLS 78
Cdd:PRK11176 95 KVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSeqvassssGALITVVREGAS----------IIGLFIMMFYYS 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 79 PQLAPVLGLLMLAVSVLVAVYKRSTVPVYKShglAQATMSDCVSETFSAI---RTVRSFSGEKRQMSIFGSQILAYKLSG 155
Cdd:PRK11176 165 WQLSLILIVIAPIVSIAIRVVSKRFRNISKN---MQNTMGQVTTSAEQMLkghKEVLIFGGQEVETKRFDKVSNRMRQQG 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 156 LKLGTFKSINESITRVAVYISLLA-LYCLGGSKVKtGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDLRGTFAAIDRINS 234
Cdd:PRK11176 242 MKMVSASSISDPIIQLIASLALAFvLYAASFPSVM-DTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 235 ILnavDIDEalayglERDIHTKKVQDENlklflsagpnvnirhldkyymsnlkstnnlrtltwaGDVCLDDVHFAYPLRp 314
Cdd:PRK11176 321 IL---DLEQ------EKDEGKRVIERAK------------------------------------GDIEFRNVTFTYPGK- 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 315 DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVSIVNQEPVLFSLSVA 394
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIA 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 395 ENIAYGlPNEHVSKDDIIKAAKAANAHDFIISLPQGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEATSALDA 474
Cdd:PRK11176 435 NNIAYA-RTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDT 513
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145334131 475 VSERLVQSALNRLMKDRTTLVIAHRLSTVQSANQIAVCSDGKIIELGTHSELVAQKGSYASL 536
Cdd:PRK11176 514 ESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQL 575
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
299-531 |
5.47e-88 |
|
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: 270.64 E-value: 5.47e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 299 GDVCLDDVHFAYplRPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKV 378
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 379 VSIVNQEPVLFSLSVAENIAYGLPNehVSKDDIIKAAKAANAHDFIISLPQGYDTLVGERGGLLSGGQRQRVAIARSLLK 458
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPN--ATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145334131 459 NAPILILDEATSALDAVSERLVQSALNRLMKDRTTLVIAHRLSTVQSANQIAVCSDGKIIELGTHSELVAQKG 531
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
8-536 |
4.52e-85 |
|
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: 274.34 E-value: 4.52e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 8 VMAILRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDLGALnsivnDN---------ISrdrgfrAFTEVFGTICILFTLS 78
Cdd:COG4987 86 LLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDAL-----DNlylrvllplLV------ALLVILAAVAFLAFFS 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 79 PQLAPVLGLLMLAVSVLV--AVYKRSTvPVYKSHGLAQATMSDCVSETFSAIRTVRSFSGEKRQMSIFGSQILAYKLSGL 156
Cdd:COG4987 155 PALALVLALGLLLAGLLLplLAARLGR-RAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQR 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 157 KLGTFKSINESITRVAVYISLLALYCLGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDLRGTFAAIDRINSIL 236
Cdd:COG4987 234 RLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 237 NAvdidealayglerdihTKKVQDENLKLFLSAGPnvnirhldkyymsnlkstnnlrtltwagDVCLDDVHFAYPLRPDv 316
Cdd:COG4987 314 DA----------------PPAVTEPAEPAPAPGGP----------------------------SLELEDVSFRYPGAGR- 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 317 KVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVSIVNQEPVLFSLSVAEN 396
Cdd:COG4987 349 PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLREN 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 397 IAYGLPNehVSKDDIIKAAKAANAHDFIISLPQGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEATSALDAVS 476
Cdd:COG4987 429 LRLARPD--ATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAAT 506
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 477 ERLVQSALNRLMKDRTTLVIAHRLSTVQSANQIAVCSDGKIIELGTHSELVAQKGSYASL 536
Cdd:COG4987 507 EQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQL 566
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
291-517 |
1.90e-84 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 261.64 E-value: 1.90e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 291 NLRTLTWAGDVCLDDVHFAYPLRPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMF 370
Cdd:cd03248 2 SLAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 371 DKSEWAKVVSIVNQEPVLFSLSVAENIAYGLPNehVSKDDIIKAAKAANAHDFIISLPQGYDTLVGERGGLLSGGQRQRV 450
Cdd:cd03248 82 EHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQS--CSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145334131 451 AIARSLLKNAPILILDEATSALDAVSERLVQSALNRLMKDRTTLVIAHRLSTVQSANQIAVCSDGKI 517
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
64-545 |
1.07e-83 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 271.45 E-value: 1.07e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 64 FTEVFGTICILFTLSP-------QLAPVLGLLMLAVSVLvavykrSTVPVYKSHGLAQA------TMSDCVSETFSAIRT 130
Cdd:PRK13657 134 MREHLATLVALVVLLPlalfmnwRLSLVLVVLGIVYTLI------TTLVMRKTKDGQAAveehyhDLFAHVSDAIGNVSV 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 131 VRSFS---GEKRQMSIFGSQILAYKLSGLKLGTFKSInesITRVAVYISLLALYCLGGSKVKTGELAVGTVVSFIGYTfT 207
Cdd:PRK13657 208 VQSYNrieAETQALRDIADNLLAAQMPVLSWWALASV---LNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVGFA-T 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 208 LTFAVQGLVNTFgdlrgtfaaidrINSILNAvdidealayglerdihTKKVQDenlkLF--LSAGPNVNIRhldkyymSN 285
Cdd:PRK13657 284 LLIGRLDQVVAF------------INQVFMA----------------APKLEE----FFevEDAVPDVRDP-------PG 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 286 LKSTNNLrtltwAGDVCLDDVHFAYPLRPdvKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGE 365
Cdd:PRK13657 325 AIDLGRV-----KGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGT 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 366 DVRMFDKSEWAKVVSIVNQEPVLFSLSVAENIAYGLPNehVSKDDIIKAAKAANAHDFIISLPQGYDTLVGERGGLLSGG 445
Cdd:PRK13657 398 DIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPD--ATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGG 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 446 QRQRVAIARSLLKNAPILILDEATSALDAVSERLVQSALNRLMKDRTTLVIAHRLSTVQSANQIAVCSDGKIIELGTHSE 525
Cdd:PRK13657 476 ERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDE 555
|
490 500
....*....|....*....|
gi 145334131 526 LVAQKGSYASLVGTQRLAFE 545
Cdd:PRK13657 556 LVARGGRFAALLRAQGMLQE 575
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
301-516 |
2.05e-78 |
|
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: 243.83 E-value: 2.05e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 301 VCLDDVHFAYPLRPdVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVS 380
Cdd:cd03228 1 IEFKNVSFSYPGRP-KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 381 IVNQEPVLFSLSVAENIayglpnehvskddiikaakaanahdfiislpqgydtlvgergglLSGGQRQRVAIARSLLKNA 460
Cdd:cd03228 80 YVPQDPFLFSGTIRENI--------------------------------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 145334131 461 PILILDEATSALDAVSERLVQSALNRLMKDRTTLVIAHRLSTVQSANQIAVCSDGK 516
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
301-540 |
4.61e-75 |
|
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: 237.77 E-value: 4.61e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 301 VCLDDVHFAYplRPDVK-VLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVV 379
Cdd:cd03252 1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 380 SIVNQEPVLFSLSVAENIAygLPNEHVSKDDIIKAAKAANAHDFIISLPQGYDTLVGERGGLLSGGQRQRVAIARSLLKN 459
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIA--LADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 460 APILILDEATSALDAVSERLVQSALNRLMKDRTTLVIAHRLSTVQSANQIAVCSDGKIIELGTHSELVAQKGSYASLVGT 539
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQL 236
|
.
gi 145334131 540 Q 540
Cdd:cd03252 237 Q 237
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
64-536 |
1.59e-74 |
|
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: 250.04 E-value: 1.59e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 64 FTEVFgtICILFTLSPQLA-PVLGLLM--LAVSVLVAVYKRSTVP-VYKSHGLAQATMSDCVSetfsAIRTVRSFSGEKR 139
Cdd:TIGR01846 265 FVVVF--LAVMFFYSPTLTgVVIGSLVcyALLSVFVGPILRKRVEdKFERSAAATSFLVESVT----GIETIKATATEPQ 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 140 QMSIFGSQILAYKLSGLKLGTFKSINESITRVAVYISLLALYCLGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGLVNTF 219
Cdd:TIGR01846 339 FQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLW 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 220 GDLRGTFAAIDRINSILNAvdidealayglerdihtkkvQDENLKLFLSAGPNVNirhldkyymsnlkstnnlrtltwaG 299
Cdd:TIGR01846 419 QDFQQTGIALERLGDILNS--------------------PTEPRSAGLAALPELR------------------------G 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 300 DVCLDDVHFAYplRPDV-KVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKV 378
Cdd:TIGR01846 455 AITFENIRFRY--APDSpEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQ 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 379 VSIVNQEPVLFSLSVAENIAYGLPN---EHVskddiIKAAKAANAHDFIISLPQGYDTLVGERGGLLSGGQRQRVAIARS 455
Cdd:TIGR01846 533 MGVVLQENVLFSRSIRDNIALCNPGapfEHV-----IHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARA 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 456 LLKNAPILILDEATSALDAVSERLVQSALNRLMKDRTTLVIAHRLSTVQSANQIAVCSDGKIIELGTHSELVAQKGSYAS 535
Cdd:TIGR01846 608 LVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYAR 687
|
.
gi 145334131 536 L 536
Cdd:TIGR01846 688 L 688
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
1-232 |
2.30e-71 |
|
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: 229.75 E-value: 2.30e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 1 MTAIWENVMAILRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDLGALNSIVNDNISRdrGFRAFTEVFGTICILFTLSPQ 80
Cdd:cd18557 60 FNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQ--LLRNILQVIGGLIILFILSWK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 81 LAPVLGLLMLAVSVLVAVYKRSTVPVYKSHGLAQATMSDCVSETFSAIRTVRSFSGEKRQMSIFGSQILAYKLSGLKLGT 160
Cdd:cd18557 138 LTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKAL 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145334131 161 FKSINESITRVAVYISLLALYCLGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDLRGTFAAIDRI 232
Cdd:cd18557 218 ANALFQGITSLLIYLSLLLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
14-537 |
2.07e-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: 217.50 E-value: 2.07e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 14 AQIFRRVLIQKAEFFDKYKVGELTGLLTSdlgalnsivNDNISRDRGFRAFTEVFGTICILF--TLSPQLAPVLGLLMLA 91
Cdd:TIGR03796 231 ARFLWHILRLPVRFFAQRHAGDIASRVQL---------NDQVAEFLSGQLATTALDAVMLVFyaLLMLLYDPVLTLIGIA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 92 VSVLVAVYKR--STVPVYKSHGLAQ--ATMSDCVSETFSAIRTVRSFSGEkrqmSIFGSQILAYK-----------LSGL 156
Cdd:TIGR03796 302 FAAINVLALQlvSRRRVDANRRLQQdaGKLTGVAISGLQSIETLKASGLE----SDFFSRWAGYQakllnaqqelgVLTQ 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 157 KLGTFKSINESITRVAVYIsllalycLGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDLRGTFAAIDRINSIL 236
Cdd:TIGR03796 378 ILGVLPTLLTSLNSALILV-------VGGLRVMEGQLTIGMLVAFQSLMSSFLEPVNNLVGFGGTLQELEGDLNRLDDVL 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 237 -NAVDIDealaygLERDIHTKKVQDENLKLflsagpnvnirhldkyymsnlkstnnlrtltwAGDVCLDDVHFAY-PLRP 314
Cdd:TIGR03796 451 rNPVDPL------LEEPEGSAATSEPPRRL--------------------------------SGYVELRNITFGYsPLEP 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 315 dvKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVSIVNQEPVLFSLSVA 394
Cdd:TIGR03796 493 --PLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVR 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 395 ENIAygLPNEHVSKDDIIKAAKAANAHDFIISLPQGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEATSALDA 474
Cdd:TIGR03796 571 DNLT--LWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDP 648
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145334131 475 VSERLVQSALNRlmkdR--TTLVIAHRLSTVQSANQIAVCSDGKIIELGTHSELVAQKGSYASLV 537
Cdd:TIGR03796 649 ETEKIIDDNLRR----RgcTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARLI 709
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
12-542 |
2.72e-62 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 214.19 E-value: 2.72e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 12 LRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDLgalnsivndnisrDRGFRAFTE---------VFGtICILFTLSPQLA 82
Cdd:PRK10789 71 LREDFYRQLSRQHPEFYLRHRTGDLMARATNDV-------------DRVVFAAGEgvltlvdslVMG-CAVLIVMSTQIS 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 83 PVLGLL-MLAVSVLVAVYKRSTVPVYKSHGLAQATMS---DCVSETFSAIRTVRSFSGEKRQMSIFGSqilAYKLSGLKl 158
Cdd:PRK10789 137 WQLTLLaLLPMPVMAIMIKRYGDQLHERFKLAQAAFSslnDRTQESLTSIRMIKAFGLEDRQSALFAA---DAEDTGKK- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 159 gtfksiNESITRV------AVYIS-----LLALYclGGS-KVKTGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDL-RGT 225
Cdd:PRK10789 213 ------NMRVARIdarfdpTIYIAigmanLLAIG--GGSwMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVeRGS 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 226 fAAIDRINSILnavdiDEALAyglerdihtkkVQDENLKLFLSAGP-NVNIRhldkyymsnlkstnnlrtltwagdvcld 304
Cdd:PRK10789 285 -AAYSRIRAML-----AEAPV-----------VKDGSEPVPEGRGElDVNIR---------------------------- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 305 dvHFAYPlRPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVSIVNQ 384
Cdd:PRK10789 320 --QFTYP-QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 385 EPVLFSLSVAENIAYGLPNehVSKDDIIKAAKAANAHDFIISLPQGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILI 464
Cdd:PRK10789 397 TPFLFSDTVANNIALGRPD--ATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILI 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145334131 465 LDEATSALDAVSERLVQSALNRLMKDRTTLVIAHRLSTVQSANQIAVCSDGKIIELGTHSELVAQKGSYASLVGTQRL 542
Cdd:PRK10789 475 LDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQQL 552
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
121-545 |
1.43e-61 |
|
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: 212.83 E-value: 1.43e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 121 VSETFSAIRTVRSFS---GEKRQMSIFGSQILAYKLSGLKLGTFKSineSITRVAVYISLLALYCLGGSKVKTGELAVGT 197
Cdd:TIGR01192 198 VSDSISNVSVVHSYNrieAETSALKQFTNNLLSAQYPVLDWWALAS---GLNRMASTISMMCILVIGTVLVIKGELSVGE 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 198 VVSFIGYTFTLtfavqglvntfgdlrgtFAAIDRINSILNAvdIDEALAYGLERDIHTKKVQDENLKLFLSAGPNVnirh 277
Cdd:TIGR01192 275 VIAFIGFANLL-----------------IGRLDQMSGFITQ--IFEARAKLEDFFDLEDSVFQREEPADAPELPNV---- 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 278 ldkyymsnlkstnnlrtltwAGDVCLDDVHFAYPlRPDVKVLDgLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQ 357
Cdd:TIGR01192 332 --------------------KGAVEFRHITFEFA-NSSQGVFD-VSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTV 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 358 GRITVGGEDVRMFDKSEWAKVVSIVNQEPVLFSLSVAENIAYGlpNEHVSKDDIIKAAKAANAHDFIISLPQGYDTLVGE 437
Cdd:TIGR01192 390 GQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLG--REGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 438 RGGLLSGGQRQRVAIARSLLKNAPILILDEATSALDAVSERLVQSALNRLMKDRTTLVIAHRLSTVQSANQIAVCSDGKI 517
Cdd:TIGR01192 468 RGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRL 547
|
410 420
....*....|....*....|....*...
gi 145334131 518 IELGTHSELVAQKGSYASLVGTQRLAFE 545
Cdd:TIGR01192 548 IEKGSFQELIQKDGRFYKLLRRSGLLTN 575
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
299-518 |
4.25e-59 |
|
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: 195.50 E-value: 4.25e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 299 GDVCLDDVHFAYPLRPdVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKV 378
Cdd:cd03245 1 GRIEFRNVSFSYPNQE-IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 379 VSIVNQEPVLFSLSVAENIAYGLPneHVSKDDIIKAAKAANAHDFIISLPQGYDTLVGERGGLLSGGQRQRVAIARSLLK 458
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAP--LADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 459 NAPILILDEATSALDAVSERLVQSALNRLMKDRTTLVIAHRLSTVQSANQIAVCSDGKII 518
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
303-511 |
3.14e-58 |
|
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: 202.52 E-value: 3.14e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPLRPdvKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVSIV 382
Cdd:TIGR02857 324 FSGVSVAYPGRR--PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 383 NQEPVLFSLSVAENIAYGLPNehVSKDDIIKAAKAANAHDFIISLPQGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPI 462
Cdd:TIGR02857 402 PQHPFLFAGTIAENIRLARPD--ASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPL 479
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 145334131 463 LILDEATSALDAVSERLVQSALNRLMKDRTTLVIAHRLSTVQSANQIAV 511
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVV 528
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
312-536 |
4.96e-57 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 200.46 E-value: 4.96e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 312 LRPDVKVLDG-LSLTLNSGTVTALVGSSGAGKSTIVQLLARFYePTQGRITVGGEDVRMFDKSEWAKVVSIVNQEPVLFS 390
Cdd:PRK11174 358 LSPDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPH 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 391 LSVAENIAYGlpNEHVSKDDIIKAAKAANAHDFIISLPQGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEATS 470
Cdd:PRK11174 437 GTLRDNVLLG--NPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTA 514
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145334131 471 ALDAVSERLVQSALNRLMKDRTTLVIAHRLSTVQSANQIAVCSDGKIIELGTHSELVAQKGSYASL 536
Cdd:PRK11174 515 SLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
298-542 |
5.36e-57 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 200.05 E-value: 5.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 298 AGDVCLDDVHFAYPLRPDvKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAK 377
Cdd:PRK11160 336 QVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 378 VVSIVNQEPVLFSLSVAENIAYGLPNEHvskDDIIKAAKAANAHDFIISLPQGYDTLVGERGGLLSGGQRQRVAIARSLL 457
Cdd:PRK11160 415 AISVVSQRVHLFSATLRDNLLLAAPNAS---DEALIEVLQQVGLEKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALL 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 458 KNAPILILDEATSALDAVSERLVQSALNRLMKDRTTLVIAHRLSTVQSANQIAVCSDGKIIELGTHSELVAQKGSYASLv 537
Cdd:PRK11160 492 HDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL- 570
|
....*
gi 145334131 538 gTQRL 542
Cdd:PRK11160 571 -KQRL 574
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
299-522 |
8.33e-55 |
|
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: 184.23 E-value: 8.33e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 299 GDVCLDDVHFAYplRPDVK-VLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAK 377
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 378 VVSIVNQEPVLFSLSVAENIAyglPNEHVSKDDIIKAAKAANAHDFIISLPQGYDTLVGERGGLLSGGQRQRVAIARSLL 457
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLD---PFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145334131 458 KNAPILILDEATSALDAVSERLVQSALNRLMKDRTTLVIAHRLSTVQSANQIAVCSDGKIIELGT 522
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
113-537 |
1.10e-54 |
|
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: 196.11 E-value: 1.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 113 AQATMSDCVSETFSAIRTVRSFSGEKRQMSIFGSQILAYKLSGLKLGTFKSINESITRVAVYISLLALYCLGGSKVKTGE 192
Cdd:TIGR01193 329 ANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKADQGQQAIKAVTKLILNVVILWTGAYLVMRGK 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 193 LAVGTVVSFigytftltfavQGLVNTFgdlrgtfaaIDRINSILNavdidealaygLERDIHTKKVQDENL-KLFLsagp 271
Cdd:TIGR01193 409 LTLGQLITF-----------NALLSYF---------LTPLENIIN-----------LQPKLQAARVANNRLnEVYL---- 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 272 nVNIRHLDKYYMSNLKSTNnlrtltwaGDVCLDDVHFAYPLrpDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLAR 351
Cdd:TIGR01193 454 -VDSEFINKKKRTELNNLN--------GDIVINDVSYSYGY--GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVG 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 352 FYEPTQGRITVGGEDVRMFDKSEWAKVVSIVNQEPVLFSLSVAENIAYGlPNEHVSKDDIIKAAKAANAHDFIISLPQGY 431
Cdd:TIGR01193 523 FFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLG-AKENVSQDEIWAACEIAEIKDDIENMPLGY 601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 432 DTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEATSALDAVSE-RLVQSALNrlMKDRTTLVIAHRLSTVQSANQIA 510
Cdd:TIGR01193 602 QTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEkKIVNNLLN--LQDKTIIFVAHRLSVAKQSDKII 679
|
410 420
....*....|....*....|....*..
gi 145334131 511 VCSDGKIIELGTHSELVAQKGSYASLV 537
Cdd:TIGR01193 680 VLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
8-500 |
1.18e-50 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 181.79 E-value: 1.18e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 8 VMAILRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDLGALNSIVNDNISRdrGFRAFTEVFGTICILFTLSPQLAPVLgL 87
Cdd:TIGR02868 84 SLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVP--AGVALVVGAAAVAAIAVLSVPAALIL-A 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 88 LMLAVSVLVA------VYKRSTVPVYKSHG-LAQATMS--DCVSETfsairtvrSFSGEK----RQMSIFGSQILAYKLS 154
Cdd:TIGR02868 161 AGLLLAGFVAplvslrAARAAEQALARLRGeLAAQLTDalDGAAEL--------VASGALpaalAQVEEADRELTRAERR 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 155 GlklGTFKSINESITRVAVYISLLALYCLGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDLRGTFAAIDRINs 234
Cdd:TIGR02868 233 A---AAATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIV- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 235 ilnavdidEALAYGLERDIhtkkVQDENLKLFLSAGPnvnirhldkyymsnlkstnnlrtltwagDVCLDDVHFAYPlrP 314
Cdd:TIGR02868 309 --------EVLDAAGPVAE----GSAPAAGAVGLGKP----------------------------TLELRDLSAGYP--G 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 315 DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVSIVNQEPVLFSLSVA 394
Cdd:TIGR02868 347 APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVR 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 395 ENIAYGLPNehVSKDDIIKAAKAANAHDFIISLPQGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEATSALDA 474
Cdd:TIGR02868 427 ENLRLARPD--ATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDA 504
|
490 500
....*....|....*....|....*.
gi 145334131 475 VSERLVQSALNRLMKDRTTLVIAHRL 500
Cdd:TIGR02868 505 ETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
12-533 |
1.05e-47 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 174.91 E-value: 1.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 12 LRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDLGALNSIVNDNISRDrgFRAFTEVFGTICILFTLSPQLAPVLGLLMLA 91
Cdd:PRK10790 100 LRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATV--LRSAALIGAMLVAMFSLDWRMALVAIMIFPA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 92 VSVLVAVYKRSTVPVYKSHGLAQATMSDCVSETFSAIRTVRSFsgekRQMSIFGSQIL------------AYKLSGLKLG 159
Cdd:PRK10790 178 VLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQF----RQQARFGERMGeasrshymarmqTLRLDGFLLR 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 160 TFKSINESItrvaVYISLLALYCLGGSkvktGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDLRGTFAAIDRINSILNAv 239
Cdd:PRK10790 254 PLLSLFSAL----ILCGLLMLFGFSAS----GTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELMDG- 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 240 didEALAYGlerdihtkkvqdenlklflsagpnvnirhldkyymsnlkstNNLRTLTwAGDVCLDDVHFAYplRPDVKVL 319
Cdd:PRK10790 325 ---PRQQYG-----------------------------------------NDDRPLQ-SGRIDIDNVSFAY--RDDNLVL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 320 DGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVSIVNQEPVLFSLSVAENIAY 399
Cdd:PRK10790 358 QNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTL 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 400 GlpnEHVSKDDIIKAAKAANAHDFIISLPQGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEATSALDAVSERL 479
Cdd:PRK10790 438 G---RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQA 514
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 145334131 480 VQSALnRLMKDRTTL-VIAHRLSTVQSANQIAVCSDGKIIELGTHSELVAQKGSY 533
Cdd:PRK10790 515 IQQAL-AAVREHTTLvVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRY 568
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
298-529 |
1.83e-47 |
|
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: 173.78 E-value: 1.83e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 298 AGDVCLDDVHFAYPLRpDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAK 377
Cdd:COG4618 328 KGRLSVENLTVVPPGS-KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 378 VVSIVNQEPVLFSLSVAENIAyGLPNehVSKDDIIKAAKAANAHDFIISLPQGYDTLVGERGGLLSGGQRQRVAIARSLL 457
Cdd:COG4618 407 HIGYLPQDVELFDGTIAENIA-RFGD--ADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALY 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145334131 458 KNAPILILDEATSALDAVSERLVQSALnRLMKDR--TTLVIAHRLSTVQSANQIAVCSDGKIIELGTHSELVAQ 529
Cdd:COG4618 484 GDPRLVVLDEPNSNLDDEGEAALAAAI-RALKARgaTVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
282-514 |
2.72e-47 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 177.53 E-value: 2.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 282 YMSNLKSTNNL----------------RTLTWAGDVCLDDVHFAYPLRPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTI 345
Cdd:PTZ00265 348 YMKSLEATNSLyeiinrkplvennddgKKLKDIKKIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTI 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 346 VQLLARFYEPTQGRITVG-GEDVRMFDKSEWAKVVSIVNQEPVLFSLSVAENIAYGL------------PNE-------- 404
Cdd:PTZ00265 428 LKLIERLYDPTEGDIIINdSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSLyslkdlealsnyYNEdgndsqen 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 405 ----------------------------HVSKD-------DIIKAAKAANAHDFIISLPQGYDTLVGERGGLLSGGQRQR 449
Cdd:PTZ00265 508 knkrnscrakcagdlndmsnttdsneliEMRKNyqtikdsEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQR 587
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145334131 450 VAIARSLLKNAPILILDEATSALDAVSERLVQSALNRLM--KDRTTLVIAHRLSTVQSANQIAVCSD 514
Cdd:PTZ00265 588 ISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLSN 654
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
6-540 |
3.15e-46 |
|
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: 172.06 E-value: 3.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 6 ENVM-AILRAQIFRRVLIQKAEFFDKYKVGELTglltSDLGALNSIvnDNISRDRGFRA-FTEVFG--TICILFTLSPQL 81
Cdd:TIGR03797 204 ETRMdASLQAAVWDRLLRLPVSFFRQYSTGDLA----SRAMGISQI--RRILSGSTLTTlLSGIFAllNLGLMFYYSWKL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 82 ApVLGLLMLAVSVLVAVYKrSTVPVYKSHGL--AQATMSDCVSETFSAIRTVRSFSGEKRQMSIFGSQILAYKLSGLKLG 159
Cdd:TIGR03797 278 A-LVAVALALVAIAVTLVL-GLLQVRKERRLleLSGKISGLTVQLINGISKLRVAGAENRAFARWAKLFSRQRKLELSAQ 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 160 TFKSINESITRVAVYISLLALYCLGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDLRGTFAAIDRINSILNAV 239
Cdd:TIGR03797 356 RIENLLTVFNAVLPVLTSAALFAAAISLLGGAGLSLGSFLAFNTAFGSFSGAVTQLSNTLISILAVIPLWERAKPILEAL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 240 -DIDEAlayglerdihtkKVQDENLklflsagpnvnirhldkyymsnlkstnnlrtltwAGDVCLDDVHFAYplRPD-VK 317
Cdd:TIGR03797 436 pEVDEA------------KTDPGKL----------------------------------SGAIEVDRVTFRY--RPDgPL 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 318 VLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVSIVNQEPVLFSLSVAENI 397
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENI 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 398 AYGLPnehVSKDDIIKAAKAANAHDFIISLPQGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEATSALDAVSE 477
Cdd:TIGR03797 548 AGGAP---LTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQ 624
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145334131 478 RLVQSALNRLMKDRttLVIAHRLSTVQSANQIAVCSDGKIIELGTHSELVAQKGSYASLVGTQ 540
Cdd:TIGR03797 625 AIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLARRQ 685
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-537 |
5.98e-46 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 173.68 E-value: 5.98e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 4 IWENVMAILRAQIFRRVLIQKAEFFD--KYKVGELTGLLTSDLGALNSIVNDNISRdrgFRAFTEVFGTICIL-FTLSPQ 80
Cdd:PTZ00265 893 IGEKVEKTMKRRLFENILYQEISFFDqdKHAPGLLSAHINRDVHLLKTGLVNNIVI---FTHFIVLFLVSMVMsFYFCPI 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 81 LAPVLGLLMLAVSVLVAVYKR---------------STVPVYKSHGLAQATMSDCVSETFSAIRTVRSFSGEKRQMSIFG 145
Cdd:PTZ00265 970 VAAVLTGTYFIFMRVFAIRARltankdvekkeinqpGTVFAYNSDDEIFKDPSFLIQEAFYNMNTVIIYGLEDYFCNLIE 1049
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 146 SQIlAYKLSGLKLGTFksINESI----TRVAVYISLLAlYCLGGSKVKTGELAVGtvvSFIGYTFTLTFAvqglvntfgd 221
Cdd:PTZ00265 1050 KAI-DYSNKGQKRKTL--VNSMLwgfsQSAQLFINSFA-YWFGSFLIRRGTILVD---DFMKSLFTFLFT---------- 1112
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 222 lrGTFAAidRINSilnavdidealaygLERDIHTKKVQDENLKLFLSAGPNVNIRHLDKYymsNLKSTNNLRtltwaGDV 301
Cdd:PTZ00265 1113 --GSYAG--KLMS--------------LKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGI---RIKNKNDIK-----GKI 1166
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 302 CLDDVHFAYPLRPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYE--------------------------- 354
Cdd:PTZ00265 1167 EIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgde 1246
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 355 ---------------------------PTQGRITVGGEDVRMFDKSEWAKVVSIVNQEPVLFSLSVAENIAYGlpNEHVS 407
Cdd:PTZ00265 1247 eqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFG--KEDAT 1324
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 408 KDDIIKAAKAANAHDFIISLPQGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEATSALDAVSERLVQSALNRL 487
Cdd:PTZ00265 1325 REDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDI 1404
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 145334131 488 MK--DRTTLVIAHRLSTVQSANQIAVCSD----GKIIEL-GTHSELV-AQKGSYASLV 537
Cdd:PTZ00265 1405 KDkaDKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQAhGTHEELLsVQDGVYKKYV 1462
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
303-530 |
4.84e-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: 155.95 E-value: 4.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPlrPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVSIV 382
Cdd:COG1122 3 LENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 383 NQEPV--LFSLSVAENIAYGLPNEHVSKDDIIKAAKaanahdfiislpqgyDTLvgERGGL----------LSGGQRQRV 450
Cdd:COG1122 81 FQNPDdqLFAPTVEEDVAFGPENLGLPREEIRERVE---------------EAL--ELVGLehladrppheLSGGQKQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 451 AIARSLLKNAPILILDEATSALDAVSERLVQSALNRLMKDRTTLVIA-HRLSTV-QSANQIAVCSDGKIIELGTHSELVA 528
Cdd:COG1122 144 AIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVaELADRVIVLDDGRIVADGTPREVFS 223
|
..
gi 145334131 529 QK 530
Cdd:COG1122 224 DY 225
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
303-529 |
3.88e-43 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 153.68 E-value: 3.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPlrpDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRmFDKSEWAKVVSIV 382
Cdd:COG1131 3 VRGLTKRYG---DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA-RDPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 383 NQEPVLF-SLSVAENI-----AYGLPNEHVSKDdiikaakaanAHDFI--ISLPQGYDTLVGErgglLSGGQRQRVAIAR 454
Cdd:COG1131 79 PQEPALYpDLTVRENLrffarLYGLPRKEARER----------IDELLelFGLTDAADRKVGT----LSGGMKQRLGLAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145334131 455 SLLKNAPILILDEATSALDAVSERLVQSALNRLMKDRTTLVIA-HRLSTVQS-ANQIAVCSDGKIIELGTHSELVAQ 529
Cdd:COG1131 145 ALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
303-516 |
4.09e-43 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 152.62 E-value: 4.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPlRPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVSIV 382
Cdd:cd03225 2 LKNLSFSYP-DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 383 NQEP--VLFSLSVAENIAYGLPNEHVSKDDIIKAAKAANahdfiislpqgydtlvgERGGL----------LSGGQRQRV 450
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAFGLENLGLPEEEIEERVEEAL-----------------ELVGLeglrdrspftLSGGQKQRV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145334131 451 AIARSLLKNAPILILDEATSALDAVSERLVQSALNRLMKDRTTLVIA-HRLSTVQS-ANQIAVCSDGK 516
Cdd:cd03225 144 AIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
319-470 |
4.44e-43 |
|
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: 150.49 E-value: 4.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 319 LDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVSIVNQEPVLFS-LSVAENI 397
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPrLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145334131 398 AYGLPNEHVSKDDiikaaKAANAHDFIISLPQGY--DTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEATS 470
Cdd:pfam00005 81 RLGLLLKGLSKRE-----KDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
303-521 |
5.83e-43 |
|
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: 151.31 E-value: 5.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPlRPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKsEWAKVVSIV 382
Cdd:cd03247 3 INNVSFSYP-EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK-ALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 383 NQEPVLFSLSVAENIayglpnehvskddiikaakaanahdfiislpqgydtlvGERgglLSGGQRQRVAIARSLLKNAPI 462
Cdd:cd03247 81 NQRPYLFDTTLRNNL--------------------------------------GRR---FSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 145334131 463 LILDEATSALDAVSERLVQSALNRLMKDRTTLVIAHRLSTVQSANQIAVCSDGKIIELG 521
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
299-529 |
6.12e-43 |
|
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: 160.98 E-value: 6.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 299 GDVCLDDVHFAYPlRPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKV 378
Cdd:TIGR01842 315 GHLSVENVTIVPP-GGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKH 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 379 VSIVNQEPVLFSLSVAENIA-YGlpnEHVSKDDIIKAAKAANAHDFIISLPQGYDTLVGERGGLLSGGQRQRVAIARSLL 457
Cdd:TIGR01842 394 IGYLPQDVELFPGTVAENIArFG---ENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALY 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145334131 458 KNAPILILDEATSALDAVSERLVQSALNRLMKDR-TTLVIAHRLSTVQSANQIAVCSDGKIIELGTHSELVAQ 529
Cdd:TIGR01842 471 GDPKLVVLDEPNSNLDEEGEQALANAIKALKARGiTVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
303-517 |
6.85e-42 |
|
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: 148.13 E-value: 6.85e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYP--LRPdvkVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVS 380
Cdd:cd03246 3 VENVSFRYPgaEPP---VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 381 IVNQEPVLFSLSVAENIayglpnehvskddiikaakaanahdfiislpqgydtlvgergglLSGGQRQRVAIARSLLKNA 460
Cdd:cd03246 80 YLPQDDELFSGSIAENI--------------------------------------------LSGGQRQRLGLARALYGNP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 145334131 461 PILILDEATSALDAVSERLVQSALNRL-MKDRTTLVIAHRLSTVQSANQIAVCSDGKI 517
Cdd:cd03246 116 RILVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
303-526 |
1.13e-41 |
|
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: 156.60 E-value: 1.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPLRP--DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKS---EWAK 377
Cdd:COG1123 263 VRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRslrELRR 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 378 VVSIVNQEPV--LF-SLSVAENIAYGLPNEHVSKDDIIKAAKAANAHDFiiSLPQGY-DTLVGErgglLSGGQRQRVAIA 453
Cdd:COG1123 343 RVQMVFQDPYssLNpRMTVGDIIAEPLRLHGLLSRAERRERVAELLERV--GLPPDLaDRYPHE----LSGGQRQRVAIA 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 454 RSLLKNAPILILDEATSALDaVSerlVQSALNRLMKD------RTTLVIAHRLSTVQS-ANQIAVCSDGKIIELGTHSEL 526
Cdd:COG1123 417 RALALEPKLLILDEPTSALD-VS---VQAQILNLLRDlqrelgLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEV 492
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
303-521 |
2.42e-39 |
|
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: 142.66 E-value: 2.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPlrpDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVrmFDKSEWAKVVSIV 382
Cdd:cd03259 3 LKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV--TGVPPERRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 383 NQEPVLF-SLSVAENIAYGLPNEHVSKDDIIKAAKAANAhdfiislpqgydtLVGERGGL------LSGGQRQRVAIARS 455
Cdd:cd03259 78 FQDYALFpHLTVAENIAFGLKLRGVPKAEIRARVRELLE-------------LVGLEGLLnrypheLSGGQQQRVALARA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145334131 456 LLKNAPILILDEATSALDAVSERLVQSALNRLMKDR--TTLVIAHRLSTVQS-ANQIAVCSDGKIIELG 521
Cdd:cd03259 145 LAREPSLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
303-521 |
4.04e-39 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 142.64 E-value: 4.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPLRPD-VKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDK---SEWAKV 378
Cdd:cd03257 4 VKNLSVSFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRrlrKIRRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 379 VSIVNQEPVL---FSLSVAENIAYGLpNEHVSKDDIIKAAKAANAHDFIISLPqgyDTLVGERGGLLSGGQRQRVAIARS 455
Cdd:cd03257 84 IQMVFQDPMSslnPRMTIGEQIAEPL-RIHGKLSKKEARKEAVLLLLVGVGLP---EEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145334131 456 LLKNAPILILDEATSALDAVSERLVQSALNRLMKDR--TTLVIAHRLSTVQS-ANQIAVCSDGKIIELG 521
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
303-531 |
4.91e-39 |
|
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: 142.69 E-value: 4.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPlrpDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRmFDKSEWAKVVSIV 382
Cdd:COG4555 4 VENLSKKYG---KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR-KEPREARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 383 NQEPVLFS-LSVAENIAYgLPNEHVSKDDIIKAAKAANAHDFIISLPQgyDTLVGErgglLSGGQRQRVAIARSLLKNAP 461
Cdd:COG4555 80 PDERGLYDrLTVRENIRY-FAELYGLFDEELKKRIEELIELLGLEEFL--DRRVGE----LSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145334131 462 ILILDEATSALDAVSERLVQSALNRLMKDRTTLVIA-HRLSTVQS-ANQIAVCSDGKIIELGTHSELVAQKG 531
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
303-520 |
1.13e-38 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 140.72 E-value: 1.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPLRPdvkVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVSIV 382
Cdd:COG4619 3 LEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 383 NQEPVLFSLSVAENIAYGLPNEHVSKDDIIKAAKAANahdfiISLPQGY-DTLVGErgglLSGGQRQRVAIARSLLKNAP 461
Cdd:COG4619 80 PQEPALWGGTVRDNLPFPFQLRERKFDRERALELLER-----LGLPPDIlDKPVER----LSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145334131 462 ILILDEATSALDAVSERLVQSALNRLM--KDRTTLVIAHrlstvqSANQIAVCSDgKIIEL 520
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYLaeEGRAVLWVSH------DPEQIERVAD-RVLTL 204
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
11-536 |
3.82e-38 |
|
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: 150.48 E-value: 3.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 11 ILRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDLGALNSIVNDNISRDRGfrAFTEVFGTICILFTLSPQLA---PVLGL 87
Cdd:TIGR00957 1039 VLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMG--SLFNVIGALIVILLATPIAAviiPPLGL 1116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 88 LMLAVSVLVAVYKR--------STVPVYkSHglaqatmsdcVSETFSAIRTVRSFSGEKRQMSIFGSQILAYKLSglklg 159
Cdd:TIGR00957 1117 LYFFVQRFYVASSRqlkrlesvSRSPVY-SH----------FNETLLGVSVIRAFEEQERFIHQSDLKVDENQKA----- 1180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 160 TFKSI--NESIT-RVAVYISLLALYCLGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDLRGTFAAIDRINSil 236
Cdd:TIGR00957 1181 YYPSIvaNRWLAvRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKE-- 1258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 237 navdidealayglerdiHTKKVQDENLKLFLSAGPNvnirhldkyymsnlkstnnlrtlTW--AGDVCLDDVHFAYplRP 314
Cdd:TIGR00957 1259 -----------------YSETEKEAPWQIQETAPPS-----------------------GWppRGRVEFRNYCLRY--RE 1296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 315 DVK-VLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVSIVNQEPVLFSLSV 393
Cdd:TIGR00957 1297 DLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSL 1376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 394 AENIAyglPNEHVSKDDIIKAAKAANAHDFIISLPQGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEATSALD 473
Cdd:TIGR00957 1377 RMNLD---PFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145334131 474 AVSERLVQSALNRLMKDRTTLVIAHRLSTVQSANQIAVCSDGKIIELGTHSELVAQKGSYASL 536
Cdd:TIGR00957 1454 LETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
303-528 |
6.01e-38 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 139.56 E-value: 6.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPLRPdvkVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKV---V 379
Cdd:cd03261 3 LRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrrrM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 380 SIVNQEPVLF-SLSVAENIAYGLpNEHVSKDDIIKAAKAANAHDFiISLPQGYDTLVGErgglLSGGQRQRVAIARSLLK 458
Cdd:cd03261 80 GMLFQSGALFdSLTVFENVAFPL-REHTRLSEEEIREIVLEKLEA-VGLRGAEDLYPAE----LSGGMKKRVALARALAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145334131 459 NAPILILDEATSALDAVSERLVQSALNRL--MKDRTTLVIAHRLSTVQS-ANQIAVCSDGKIIELGTHSELVA 528
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
299-522 |
1.30e-37 |
|
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: 137.54 E-value: 1.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 299 GDVCLDDVHFAYplRPDV-KVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAK 377
Cdd:cd03369 5 GEIEVENLSVRY--APDLpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 378 VVSIVNQEPVLFSLSVAENIAyglPNEHVSKDDIikaakaanahdfiislpqgYDTLVGERGGL-LSGGQRQRVAIARSL 456
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLD---PFDEYSDEEI-------------------YGALRVSEGGLnLSQGQRQLLCLARAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145334131 457 LKNAPILILDEATSALDAVSERLVQSALNRLMKDRTTLVIAHRLSTVQSANQIAVCSDGKIIELGT 522
Cdd:cd03369 141 LKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
303-529 |
2.08e-37 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 144.66 E-value: 2.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPLRpDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPT---QGRITVGGEDVRMFDKSEWAKVV 379
Cdd:COG1123 7 VRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRRI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 380 SIVNQEP--VLFSLSVAENIAYGLPNEHVSKDDIikaakaanaHDFIISLPQ--GYDTLVGERGGLLSGGQRQRVAIARS 455
Cdd:COG1123 86 GMVFQDPmtQLNPVTVGDQIAEALENLGLSRAEA---------RARVLELLEavGLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145334131 456 LLKNAPILILDEATSALDAVSERLVQSALNRLMKDR--TTLVIAHRLSTV-QSANQIAVCSDGKIIELGTHSELVAQ 529
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
290-532 |
7.27e-37 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 146.27 E-value: 7.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 290 NNLRTLTW--AGDVCLDDVHFAYplRPDVK-VLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGED 366
Cdd:PLN03232 1222 NNRPVSGWpsRGSIKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCD 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 367 VRMFDKSEWAKVVSIVNQEPVLFSLSVAENIAyglPNEHVSKDDIIKAAKAANAHDFIISLPQGYDTLVGERGGLLSGGQ 446
Cdd:PLN03232 1300 VAKFGLTDLRRVLSIIPQSPVLFSGTVRFNID---PFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQ 1376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 447 RQRVAIARSLLKNAPILILDEATSALDAVSERLVQSALNRLMKDRTTLVIAHRLSTVQSANQIAVCSDGKIIELGTHSEL 526
Cdd:PLN03232 1377 RQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQEL 1456
|
....*.
gi 145334131 527 VAQKGS 532
Cdd:PLN03232 1457 LSRDTS 1462
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
303-528 |
1.19e-36 |
|
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: 136.47 E-value: 1.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPLRP-DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVSI 381
Cdd:COG1124 4 VRNLSVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 382 VNQEPVLfSL----SVAENIAYGLPNEHVSKDDIIkaakaanahdfIISLPQgydtLVGERGGL-------LSGGQRQRV 450
Cdd:COG1124 84 VFQDPYA-SLhprhTVDRILAEPLRIHGLPDREER-----------IAELLE----QVGLPPSFldryphqLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 451 AIARSLLKNAPILILDEATSALDAVSERLVQSALNRLMKDR--TTLVIAHRLSTVQS-ANQIAVCSDGKIIELGTHSELV 527
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLL 227
|
.
gi 145334131 528 A 528
Cdd:COG1124 228 A 228
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
298-532 |
1.53e-36 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 145.65 E-value: 1.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 298 AGDVCLDDVHFAYplRPDVK-VLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWA 376
Cdd:PLN03130 1235 SGSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLR 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 377 KVVSIVNQEPVLFSLSVAENIAyglP-NEHvSKDDIIKAAKAANAHDFIISLPQGYDTLVGERGGLLSGGQRQRVAIARS 455
Cdd:PLN03130 1313 KVLGIIPQAPVLFSGTVRFNLD---PfNEH-NDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARA 1388
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145334131 456 LLKNAPILILDEATSALDAVSERLVQSALNRLMKDRTTLVIAHRLSTVQSANQIAVCSDGKIIELGTHSELVAQKGS 532
Cdd:PLN03130 1389 LLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGS 1465
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
303-526 |
2.46e-36 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 138.31 E-value: 2.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPlrpDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVrmfdksewAKV---- 378
Cdd:COG3842 8 LENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV--------TGLppek 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 379 --VSIVNQEPVLFS-LSVAENIAYGLPNEHVSKDDIikaakaanahdfiislpqgyDTLVGE---RGGL----------L 442
Cdd:COG3842 77 rnVGMVFQDYALFPhLTVAENVAFGLRMRGVPKAEI--------------------RARVAElleLVGLegladryphqL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 443 SGGQRQRVAIARSLLKNAPILILDEATSALDAvseRL---VQSALNRLMKDR--TTLVIAHRlstvQS-----ANQIAVC 512
Cdd:COG3842 137 SGGQQQRVALARALAPEPRVLLLDEPLSALDA---KLreeMREELRRLQRELgiTFIYVTHD----QEealalADRIAVM 209
|
250
....*....|....
gi 145334131 513 SDGKIIELGTHSEL 526
Cdd:COG3842 210 NDGRIEQVGTPEEI 223
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
303-527 |
3.03e-36 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 135.56 E-value: 3.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPLRPdvkVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVSIV 382
Cdd:COG1120 4 AENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 383 NQEPVL-FSLSVAENIAYGL-----PNEHVSKDDIIkaakaanahdfIIslpqgYDTLvgERGGL----------LSGGQ 446
Cdd:COG1120 81 PQEPPApFGLTVRELVALGRyphlgLFGRPSAEDRE-----------AV-----EEAL--ERTGLehladrpvdeLSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 447 RQRVAIARSLLKNAPILILDEATSALDAVSERLVQSALNRL--MKDRTTLVIAHRLS-TVQSANQIAVCSDGKIIELGTH 523
Cdd:COG1120 143 RQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPP 222
|
....
gi 145334131 524 SELV 527
Cdd:COG1120 223 EEVL 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
303-528 |
5.50e-36 |
|
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: 134.34 E-value: 5.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPlrpDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKV---V 379
Cdd:COG1127 8 VRNLTKSFG---DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrrrI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 380 SIVNQEPVLF-SLSVAENIAYGLpNEHVSKDDiikaakaanahDFIIS----------LPQGYDTLVGErgglLSGGQRQ 448
Cdd:COG1127 85 GMLFQGGALFdSLTVFENVAFPL-REHTDLSE-----------AEIRElvleklelvgLPGAADKMPSE----LSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 449 RVAIARSLLKNAPILILDEATSALDAVSERlvqsALNRLMKDR------TTLVIAHRLSTVQS-ANQIAVCSDGKIIELG 521
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDPITSA----VIDELIRELrdelglTSVVVTHDLDSAFAiADRVAVLADGKIIAEG 224
|
....*..
gi 145334131 522 THSELVA 528
Cdd:COG1127 225 TPEELLA 231
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
302-516 |
8.67e-36 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 130.83 E-value: 8.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 302 CLDDVHFAYPlrpDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVSI 381
Cdd:cd00267 1 EIENLSFRYG---GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 382 VNQepvlfslsvaeniayglpnehvskddiikaakaanahdfiislpqgydtlvgergglLSGGQRQRVAIARSLLKNAP 461
Cdd:cd00267 78 VPQ---------------------------------------------------------LSGGQRQRVALARALLLNPD 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 145334131 462 ILILDEATSALDAVSERLVQSALNRLMKD-RTTLVIAHRLSTVQ-SANQIAVCSDGK 516
Cdd:cd00267 101 LLLLDEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAElAADRVIVLKDGK 157
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
303-529 |
9.01e-36 |
|
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: 133.48 E-value: 9.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPLRP-DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKV--- 378
Cdd:cd03258 4 LKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKArrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 379 VSIVNQEPVLF-SLSVAENIAYGLPNEHVSKDDIIKAAKAANahdfiislpqgydTLVG--ERG----GLLSGGQRQRVA 451
Cdd:cd03258 84 IGMIFQHFNLLsSRTVFENVALPLEIAGVPKAEIEERVLELL-------------ELVGleDKAdaypAQLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 452 IARSLLKNAPILILDEATSALDAVSERLVQSALNRLMKDR--TTLVIAHRLSTVQS-ANQIAVCSDGKIIELGTHSELVA 528
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFA 230
|
.
gi 145334131 529 Q 529
Cdd:cd03258 231 N 231
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
303-498 |
1.12e-35 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 134.06 E-value: 1.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPLRP-DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSewakvVSI 381
Cdd:COG1116 10 LRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----RGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 382 VNQEPVLFS-LSVAENIAYGLPNEHVSKDDIIKAAkaanaHDFIislpqgydTLVGerggL----------LSGGQRQRV 450
Cdd:COG1116 85 VFQEPALLPwLTVLDNVALGLELRGVPKAERRERA-----RELL--------ELVG----LagfedayphqLSGGMRQRV 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 145334131 451 AIARSLLKNAPILILDEATSALDAVSERLVQSALNRLMKDR--TTLVIAH 498
Cdd:COG1116 148 AIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETgkTVLFVTH 197
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
303-519 |
8.65e-35 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 130.55 E-value: 8.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPL-RPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKV--- 378
Cdd:COG1136 7 LRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARLrrr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 379 -VSIVNQEPVLF-SLSVAENIAYGLPNEHVSKDDIIkaakaanahdfiislPQGYDTLvgERGGL----------LSGGQ 446
Cdd:COG1136 87 hIGFVFQFFNLLpELTALENVALPLLLAGVSRKERR---------------ERARELL--ERVGLgdrldhrpsqLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145334131 447 RQRVAIARSLLKNAPILILDEATSALDAVSERLVQSALNRLMKDR-TTLVIA-HRLSTVQSANQIAVCSDGKIIE 519
Cdd:COG1136 150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELgTTIVMVtHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
303-516 |
9.72e-35 |
|
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: 128.84 E-value: 9.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPlrpDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWA--KVVS 380
Cdd:cd03229 3 LKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPlrRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 381 IVNQEPVLFS-LSVAENIAYGlpnehvskddiikaakaanahdfiislpqgydtlvgergglLSGGQRQRVAIARSLLKN 459
Cdd:cd03229 80 MVFQDFALFPhLTVLENIALG-----------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 460 APILILDEATSALDAVSERLVQSALNRL--MKDRTTLVIAHRLSTVQS-ANQIAVCSDGK 516
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
303-526 |
1.59e-34 |
|
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: 129.99 E-value: 1.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPlrpDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYE-----PTQGRITVGGEDVRM--FDKSEW 375
Cdd:cd03260 3 LRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDldVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 376 AKVVSIVNQEPVLFSLSVAENIAYGlPNEHVSKDDIIKaakaanahdfiislpqgyDTLVGE---RGGL----------- 441
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYG-LRLHGIKLKEEL------------------DERVEEalrKAALwdevkdrlhal 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 442 -LSGGQRQRVAIARSLLKNAPILILDEATSALDAVSERLVQSALNRLMKDRTTLVIAHRLSTVQS-ANQIAVCSDGKIIE 519
Cdd:cd03260 141 gLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVE 220
|
....*..
gi 145334131 520 LGTHSEL 526
Cdd:cd03260 221 FGPTEQI 227
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
315-517 |
1.71e-34 |
|
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: 127.90 E-value: 1.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 315 DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRmFDKSEWAKVVSIVNQEPVLFS-LSV 393
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK-KEPEEVKRRIGYLPEEPSLYEnLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 394 AENIayglpnehvskddiikaakaanahdfiislpqgydtlvgerggLLSGGQRQRVAIARSLLKNAPILILDEATSALD 473
Cdd:cd03230 91 RENL-------------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLD 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 145334131 474 AVSERLVQSALNRLMKDRTTLVIA-HRLSTVQS-ANQIAVCSDGKI 517
Cdd:cd03230 128 PESRREFWELLRELKKEGKTILLSsHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
303-519 |
4.57e-34 |
|
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: 128.36 E-value: 4.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPLR-PDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRmfdksEWAKVVSI 381
Cdd:cd03293 3 VRNVSKTYGGGgGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT-----GPGPDRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 382 VNQEPVLFS-LSVAENIAYGLPNEHVSKDDiikaakaanahdfIISLPQGYDTLVGERGGL------LSGGQRQRVAIAR 454
Cdd:cd03293 78 VFQQDALLPwLTVLDNVALGLELQGVPKAE-------------ARERAEELLELVGLSGFEnayphqLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 455 SLLKNAPILILDEATSALDAVSERLVQSALNRLMKDR--TTLVIAHRLS-TVQSANQIAVCS--DGKIIE 519
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDIDeAVFLADRVVVLSarPGRIVA 214
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
301-516 |
4.76e-34 |
|
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: 127.97 E-value: 4.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 301 VCLDDVHFAYPLRPDV--KVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEdvrmfdksewakv 378
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 379 VSIVNQEPVLFSLSVAENIAYGLPNEH-----------VSKDdiikaakaanahdfIISLPQGYDTLVGERGGLLSGGQR 447
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPFDEeryekvikacaLEPD--------------LEILPDGDLTEIGEKGINLSGGQK 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145334131 448 QRVAIARSLLKNAPILILDEATSALDA-VSERLVQSALN-RLMKDRTTLVIAHRLSTVQSANQIAVCSDGK 516
Cdd:cd03250 134 QRISLARAVYSDADIYLLDDPLSAVDAhVGRHIFENCILgLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
303-529 |
1.18e-33 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 127.56 E-value: 1.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAY---PLRpdvkvldgLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEwaKVV 379
Cdd:COG3840 4 LDDLTYRYgdfPLR--------FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 380 SIVNQEPVLFS-LSVAENIAYGL-PNEHVSKDDiikaakaanaHDFIISLPQ--GYDTLVGERGGLLSGGQRQRVAIARS 455
Cdd:COG3840 74 SMLFQENNLFPhLTVAQNIGLGLrPGLKLTAEQ----------RAQVEQALErvGLAGLLDRLPGQLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145334131 456 LLKNAPILILDEATSALDAV--SERLvqSALNRLMKDR--TTLVIAHRLSTVQS-ANQIAVCSDGKIIELGTHSELVAQ 529
Cdd:COG3840 144 LVRKRPILLLDEPFSALDPAlrQEML--DLVDELCRERglTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDG 220
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
1-232 |
9.40e-33 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 126.86 E-value: 9.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 1 MTAIWENVMAILRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDLGALNSIVNDNISrdRGFRAFTEVFGTICILFTLSPQ 80
Cdd:cd18573 65 LRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLS--DGLRSLVSGVGGIGMMLYISPK 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 81 LAPVLGLLMLAVSVLVAVYKRSTVPVYKSHGLAQATMSDCVSETFSAIRTVRSFSGEKRQMSIFGSQI-LAYKLsGLKLG 159
Cdd:cd18573 143 LTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVdEVFDL-AKKEA 221
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145334131 160 TFKSINESITRVAVYISLLALYCLGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDLRGTFAAIDRI 232
Cdd:cd18573 222 LASGLFFGSTGFSGNLSLLSVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
303-532 |
2.61e-32 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 126.73 E-value: 2.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPLRP-DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKV--- 378
Cdd:COG1135 4 LENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAArrk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 379 VSIVNQEPVLF-SLSVAENIAYGLPNEHVSKDDIikaakaanahdfiislpqgyDTLVGE---RGGL----------LSG 444
Cdd:COG1135 84 IGMIFQHFNLLsSRTVAENVALPLEIAGVPKAEI--------------------RKRVAElleLVGLsdkadaypsqLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 445 GQRQRVAIARSLLKNAPILILDEATSALD-----AVSERLVQsaLNRLMKdRTTLVIAHRLSTVQS-ANQIAVCSDGKII 518
Cdd:COG1135 144 GQKQRVGIARALANNPKVLLCDEATSALDpettrSILDLLKD--INRELG-LTIVLITHEMDVVRRiCDRVAVLENGRIV 220
|
250
....*....|....
gi 145334131 519 ELGTHSELVAQKGS 532
Cdd:COG1135 221 EQGPVLDVFANPQS 234
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
303-517 |
4.16e-32 |
|
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: 122.98 E-value: 4.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPLRPD-VKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKV--- 378
Cdd:cd03255 3 LKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFrrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 379 -VSIVNQEPVLFS-LSVAENIAYGLPNEHVSKDDIIKAAKAANAHdfiISLPQGYDTLVGErgglLSGGQRQRVAIARSL 456
Cdd:cd03255 83 hIGFVFQSFNLLPdLTALENVELPLLLAGVPKKERRERAEELLER---VGLGDRLNHYPSE----LSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145334131 457 LKNAPILILDEATSALDAVSERLVQSALNRLMKDR-TTLVIA-HRLSTVQSANQIAVCSDGKI 517
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
1-232 |
4.51e-32 |
|
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: 124.97 E-value: 4.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 1 MTAIWENVMAILRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDLGALNSIVNDNISRdrGFRAFTEVFGTICILFTLSPQ 80
Cdd:cd07346 63 AARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQ--LLSDVLTLIGALVILFYLNWK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 81 LAPVLGLLMLAVSVLVAVYKRSTVPVYKSHGLAQATMSDCVSETFSAIRTVRSFSGEKRQMSIFGSQILAYKLSGLKLGT 160
Cdd:cd07346 141 LTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAAR 220
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145334131 161 FKSINESITRVAVYISLLALYCLGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDLRGTFAAIDRI 232
Cdd:cd07346 221 LSALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
318-542 |
5.02e-32 |
|
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: 123.21 E-value: 5.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 318 VLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEwaKVVSIVNQEPVLF-SLSVAEN 396
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVPQNYALFpHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 397 IAYGLPNEHVSKDDIIKAAKAanahdfiISLPQGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEATSALDavs 476
Cdd:cd03299 92 IAYGLKKRKVDKKEIERKVLE-------IAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALD--- 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145334131 477 eRLVQSALNRLMK------DRTTLVIAHRLSTVQS-ANQIAVCSDGKIIELGTHSELV--AQKGSYASLVGTQRL 542
Cdd:cd03299 162 -VRTKEKLREELKkirkefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFkkPKNEFVAEFLGFNNI 235
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
301-521 |
5.59e-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: 122.22 E-value: 5.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 301 VCLDDVHFAY---PLRpdvkvldgLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEwaK 377
Cdd:cd03298 1 VRLDKIRFSYgeqPMH--------FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--R 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 378 VVSIVNQEPVLFS-LSVAENIAYGL-PNEHVSKDDIIKAAKaanahdfiISLPQGYDTLVGERGGLLSGGQRQRVAIARS 455
Cdd:cd03298 71 PVSMLFQENNLFAhLTVEQNVGLGLsPGLKLTAEDRQAIEV--------ALARVGLAGLEKRLPGELSGGERQRVALARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145334131 456 LLKNAPILILDEATSALDAVSERLVQSALNRLMKDR--TTLVIAHRLSTVQS-ANQIAVCSDGKIIELG 521
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
323-529 |
1.15e-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: 123.14 E-value: 1.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 323 SLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKV----VSIVNQEPVLF-SLSVAENI 397
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLpHRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 398 AYGLPNEHVSKDDIIKAAKAANA----HDFIISLPqgydtlvgergGLLSGGQRQRVAIARSLLKNAPILILDEATSALD 473
Cdd:cd03294 124 AFGLEVQGVPRAEREERAAEALElvglEGWEHKYP-----------DELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 145334131 474 AVSERLVQSALNRLMKD--RTTLVIAHRLS-TVQSANQIAVCSDGKIIELGTHSELVAQ 529
Cdd:cd03294 193 PLIRREMQDELLRLQAElqKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
303-542 |
1.16e-31 |
|
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: 122.41 E-value: 1.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPLRPdvKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVSIV 382
Cdd:cd03295 3 FENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 383 NQEPVLFS-LSVAENIAYGLPNEHVSKDDIIKAAKAANAhdfIISLPQGydTLVGERGGLLSGGQRQRVAIARSLLKNAP 461
Cdd:cd03295 81 IQQIGLFPhMTVEENIALVPKLLKWPKEKIRERADELLA---LVGLDPA--EFADRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 462 ILILDEATSALDAVSERLVQSALNRLMKD--RTTLVIAHRL-STVQSANQIAVCSDGKIIELGTHSELVAQKGS--YASL 536
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQElgKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRSPANdfVAEF 235
|
....*.
gi 145334131 537 VGTQRL 542
Cdd:cd03295 236 VGADRL 241
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
303-521 |
1.74e-31 |
|
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: 119.85 E-value: 1.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPLRPdvkVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVSIV 382
Cdd:cd03214 2 VENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 383 NQepVLFSLSVAeniayglpnehvskddiikaakaanahDFiisLPQGYDTLvgerggllSGGQRQRVAIARSLLKNAPI 462
Cdd:cd03214 79 PQ--ALELLGLA---------------------------HL---ADRPFNEL--------SGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145334131 463 LILDEATSALDAVSERLVQSALNRLMKDR--TTLVIAHRLS-TVQSANQIAVCSDGKIIELG 521
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLELLRRLARERgkTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
306-529 |
2.46e-31 |
|
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: 123.62 E-value: 2.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 306 VHFAYPlRPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEP---TQGRITVGGEDVRMFDKSEWAKV---- 378
Cdd:COG0444 9 VYFPTR-RGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKIrgre 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 379 VSIVNQEPVLfSL--------SVAENIAYglpNEHVSKDDIikaakaanaHDFIISLPQgydtLVG-----ERGGL---- 441
Cdd:COG0444 88 IQMIFQDPMT-SLnpvmtvgdQIAEPLRI---HGGLSKAEA---------RERAIELLE----RVGlpdpeRRLDRyphe 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 442 LSGGQRQRVAIARSLLKNAPILILDEATSALDAVSERLVQSALNRLMKDR--TTLVIAHRLSTV-QSANQIAVCSDGKII 518
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELglAILFITHDLGVVaEIADRVAVMYAGRIV 230
|
250
....*....|.
gi 145334131 519 ELGTHSELVAQ 529
Cdd:COG0444 231 EEGPVEELFEN 241
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
299-526 |
2.67e-31 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 124.42 E-value: 2.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 299 GDVCLDDVHFAYPlrpDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDV-------RMfd 371
Cdd:COG3839 2 ASLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVtdlppkdRN-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 372 ksewakvVSIVNQEPVLF-SLSVAENIAYGLPNEHVSKDDIikaakaanahdfiislpqgyDTLVGE------------- 437
Cdd:COG3839 77 -------IAMVFQSYALYpHMTVYENIAFPLKLRKVPKAEI--------------------DRRVREaaellgledlldr 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 438 RGGLLSGGQRQRVAIARSLLKNAPILILDEATSALDAvseRL-VQ--SALNRLMKD-RTTLVIA-HRlstvQS-----AN 507
Cdd:COG3839 130 KPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDA---KLrVEmrAEIKRLHRRlGTTTIYVtHD----QVeamtlAD 202
|
250
....*....|....*....
gi 145334131 508 QIAVCSDGKIIELGTHSEL 526
Cdd:COG3839 203 RIAVMNDGRIQQVGTPEEL 221
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
323-521 |
3.81e-31 |
|
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: 119.97 E-value: 3.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 323 SLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEwaKVVSIVNQEPVLFS-LSVAENIAYGL 401
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQ--RPVSMLFQENNLFAhLTVRQNIGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 402 -PN---EHVSKDDIIKAAKAANAHDFIISLPqgydtlvgergGLLSGGQRQRVAIARSLLKNAPILILDEATSALDAV-- 475
Cdd:TIGR01277 96 hPGlklNAEQQEKVVDAAQQVGIADYLDRLP-----------EQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLlr 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 145334131 476 SERLVQSALNRLMKDRTTLVIAHRLS-TVQSANQIAVCSDGKIIELG 521
Cdd:TIGR01277 165 EEMLALVKQLCSERQRTLLMVTHHLSdARAIASQIAVVSQGKIKVVS 211
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
300-541 |
4.34e-31 |
|
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: 121.17 E-value: 4.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 300 DVClddVHFAYPLRPdvkVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVV 379
Cdd:cd03288 24 DLC---VRYENNLKP---VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 380 SIVNQEPVLFSLSVAENIAyglPNEHVSKDDIIKAAKAANAHDFIISLPQGYDTLVGERGGLLSGGQRQRVAIARSLLKN 459
Cdd:cd03288 98 SIILQDPILFSGSIRFNLD---PECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 460 APILILDEATSALDAVSERLVQSALNRLMKDRTTLVIAHRLSTVQSANQIAVCSDGKIIELGTHSELVAQK-GSYASLVG 538
Cdd:cd03288 175 SSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVFASLVR 254
|
...
gi 145334131 539 TQR 541
Cdd:cd03288 255 TDK 257
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
314-526 |
9.17e-31 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 125.52 E-value: 9.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 314 PDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSE-WAKVVSIVNQEPVLF-SL 391
Cdd:COG1129 15 GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAAGIAIIHQELNLVpNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 392 SVAENIAygLPNEhvskddiikaakaANAHDFI-------------------ISLpqgyDTLVGErgglLSGGQRQRVAI 452
Cdd:COG1129 95 SVAENIF--LGRE-------------PRRGGLIdwramrrrarellarlgldIDP----DTPVGD----LSVAQQQLVEI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145334131 453 ARSLLKNAPILILDEATSALDAV-SERLVQsALNRLMKDRTTLV-IAHRLSTVQS-ANQIAVCSDGKIIELGTHSEL 526
Cdd:COG1129 152 ARALSRDARVLILDEPTASLTEReVERLFR-IIRRLKAQGVAIIyISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
315-526 |
1.18e-30 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 119.33 E-value: 1.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 315 DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVrMFDKSEWAKV---VSIVNQEPVLFS- 390
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKLrrkVGMVFQQFNLFPh 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 391 LSVAENIAYGLpnEHV---SKDDIIKaakaanahdfiislpQGYDTLvgERGGL----------LSGGQRQRVAIARSLL 457
Cdd:COG1126 92 LTVLENVTLAP--IKVkkmSKAEAEE---------------RAMELL--ERVGLadkadaypaqLSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145334131 458 KNAPILILDEATSALD--AVSErlVQSALNRLMKDRTTLVIA-HRLS---TVqsANQIAVCSDGKIIELGTHSEL 526
Cdd:COG1126 153 MEPKVMLFDEPTSALDpeLVGE--VLDVMRDLAKEGMTMVVVtHEMGfarEV--ADRVVFMDGGRIVEEGPPEEF 223
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
303-538 |
1.91e-30 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 118.92 E-value: 1.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAY---PLRpdvkvldgLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEwaKVV 379
Cdd:PRK10771 4 LTDITWLYhhlPMR--------FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR--RPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 380 SIVNQEPVLFS-LSVAENIAYGL-PN---EHVSKDDIIKAAKAANAHDFIISLPqgydtlvgergGLLSGGQRQRVAIAR 454
Cdd:PRK10771 74 SMLFQENNLFShLTVAQNIGLGLnPGlklNAAQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALAR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 455 SLLKNAPILILDEATSALDAVserLVQSALNRL-----MKDRTTLVIAHRLstvQSANQIA----VCSDGKIIELGTHSE 525
Cdd:PRK10771 143 CLVREQPILLLDEPFSALDPA---LRQEMLTLVsqvcqERQLTLLMVSHSL---EDAARIAprslVVADGRIAWDGPTDE 216
|
250
....*....|...
gi 145334131 526 LVAQKGSYASLVG 538
Cdd:PRK10771 217 LLSGKASASALLG 229
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
316-529 |
2.31e-30 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 120.99 E-value: 2.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 316 VKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKV---VSIVNQEPvlFS-- 390
Cdd:COG4608 31 VKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLrrrMQMVFQDP--YAsl 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 391 ---LSVAENIAYGLP-NEHVSKDDIIkaakaanahDFIISLpqgydtLvgERGGL-----------LSGGQRQRVAIARS 455
Cdd:COG4608 109 nprMTVGDIIAEPLRiHGLASKAERR---------ERVAEL------L--ELVGLrpehadrypheFSGGQRQRIGIARA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 456 LLKNAPILILDEATSALDaVSerlVQS-ALNRLM--KDR---TTLVIAHRLSTVQS-ANQIAVCSDGKIIELGTHSELVA 528
Cdd:COG4608 172 LALNPKLIVCDEPVSALD-VS---IQAqVLNLLEdlQDElglTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYA 247
|
.
gi 145334131 529 Q 529
Cdd:COG4608 248 R 248
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
303-519 |
3.41e-30 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 117.85 E-value: 3.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPlrPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKV---V 379
Cdd:COG2884 4 FENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLrrrI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 380 SIVNQE-PVLFSLSVAENIAYGLpneHVskddiikaakaanahdfiislpQGYD------------TLVG--ERGGL--- 441
Cdd:COG2884 82 GVVFQDfRLLPDRTVYENVALPL---RV----------------------TGKSrkeirrrvrevlDLVGlsDKAKAlph 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 442 -LSGGQRQRVAIARSLLKNAPILILDEATSALD-AVSERLVQsALNRLMKDRTTLVIA-HRLSTVQSANQ-IAVCSDGKI 517
Cdd:COG2884 137 eLSGGEQQRVAIARALVNRPELLLADEPTGNLDpETSWEIME-LLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRL 215
|
..
gi 145334131 518 IE 519
Cdd:COG2884 216 VR 217
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
301-525 |
5.51e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 117.88 E-value: 5.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 301 VCLDDVHFAYPLRPdvkVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRmfdkSEWAKV-- 378
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR----RARRRIgy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 379 ---VSIVNQEpvlFSLSVAENIAYGLPNEH-----VSKDDIIKAAKAANA---HDFIislpqgyDTLVGErgglLSGGQR 447
Cdd:COG1121 80 vpqRAEVDWD---FPITVRDVVLMGRYGRRglfrrPSRADREAVDEALERvglEDLA-------DRPIGE----LSGGQQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 448 QRVAIARSLLKNAPILILDEATSALDAVSERLVQSALNRL-MKDRTTLVIAHRLSTVQS-ANQIaVCSDGKIIELGTHSE 525
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREyFDRV-LLLNRGLVAHGPPEE 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
314-521 |
1.02e-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: 116.20 E-value: 1.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 314 PDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEwaKVVSIVNQEPVLF-SLS 392
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVFQNYALYpHMT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 393 VAENIAYGLPNEHVSKDDiikaaKAANAHDFIISLpqGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEATSAL 472
Cdd:cd03301 89 VYDNIAFGLKLRKVPKDE-----IDERVREVAELL--QIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 145334131 473 DAVSERLVQSALNRLMK--DRTTLVIAH-RLSTVQSANQIAVCSDGKIIELG 521
Cdd:cd03301 162 DAKLRVQMRAELKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
303-518 |
1.27e-29 |
|
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: 115.43 E-value: 1.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYplRPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRmfdKSEWAKVVSIV 382
Cdd:cd03226 2 IENISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK---AKERRKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 383 NQEP--VLFSLSVAENIAYGLPNEHVSKDDIIKAAKAANAHDFIISLPQGydtlvgergglLSGGQRQRVAIARSLLKNA 460
Cdd:cd03226 77 MQDVdyQLFTDSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLS-----------LSGGQKQRLAIAAALLSGK 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 461 PILILDEATSALDAVSERLVQSALNRLMK-DRTTLVIAHRLSTVQS-ANQIAVCSDGKII 518
Cdd:cd03226 146 DLLIFDEPTSGLDYKNMERVGELIRELAAqGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
303-530 |
1.34e-29 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 117.53 E-value: 1.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPlRPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMfDKSEWA--KVVS 380
Cdd:TIGR04520 3 VENVSFSYP-ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLD-EENLWEirKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 381 IVNQEP--VLFSLSVAENIAYGLPNEHVSKDDiikaakaanahdfIISLPQGYDTLVG-----ERG-GLLSGGQRQRVAI 452
Cdd:TIGR04520 81 MVFQNPdnQFVGATVEDDVAFGLENLGVPREE-------------MRKRVDEALKLVGmedfrDREpHLLSGGQKQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 453 ARSLLKNAPILILDEATSALDAVSERLVQSALNRLMKDR--TTLVIAHRLSTVQSANQIAVCSDGKIIELGTHSELVAQK 530
Cdd:TIGR04520 148 AGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQV 227
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
2-232 |
2.99e-29 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 116.97 E-value: 2.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 2 TAIWENVMAILRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDLGALNSIVNDNISrdRGFRAFTEVFGTICILFTLSPQL 81
Cdd:cd18780 67 TLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLS--MLLRYLVQIIGGLVFMFTTSWKL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 82 ApvlgLLMLAV----SVLVAVYKRSTVPVYKSHGLAQATMSDCVSETFSAIRTVRSFSGEKRQMSIFGSQI-LAYKLsGL 156
Cdd:cd18780 145 T----LVMLSVvpplSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKInESYLL-GK 219
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145334131 157 KLGTFKSINESITRVAVYISLLALYCLGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDLRGTFAAIDRI 232
Cdd:cd18780 220 KLARASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
313-526 |
5.07e-29 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 114.52 E-value: 5.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 313 RPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMfDKSEWAKVVSIVNQEPVLFS-L 391
Cdd:cd03263 12 KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALFDeL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 392 SVAENIAY-----GLPNEHVSKDDIIKAAkaanahdfIISLPQGYDTLVGErgglLSGGQRQRVAIARSLLKNAPILILD 466
Cdd:cd03263 91 TVREHLRFyarlkGLPKSEIKEEVELLLR--------VLGLTDKANKRART----LSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145334131 467 EATSALDAVSERLVQSALNRLMKDRTTLVIAHRLSTVQS-ANQIAVCSDGKIIELGTHSEL 526
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
303-530 |
5.27e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 115.86 E-value: 5.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPlrPDVK-VLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVSI 381
Cdd:PRK13632 10 VENVSFSYP--NSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 382 VNQEP--VLFSLSVAENIAYGLPNEHVSKDDIIkaakaanahDFIISLPQ--GYDTLVGERGGLLSGGQRQRVAIARSLL 457
Cdd:PRK13632 88 IFQNPdnQFIGATVEDDIAFGLENKKVPPKKMK---------DIIDDLAKkvGMEDYLDKEPQNLSGGQKQRVAIASVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145334131 458 KNAPILILDEATSALDAVSERLVQSALNRLMKDRT-TLV-IAHRLSTVQSANQIAVCSDGKIIELGTHSELVAQK 530
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLIsITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
303-518 |
5.50e-29 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 115.15 E-value: 5.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPlrPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKV---V 379
Cdd:COG3638 5 LRNLSKRYP--GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrrrI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 380 SIVNQEPVLFS-LSVAENIAYGLPNEH---------VSKDDiikaakaanahdfiisLPQGYDTL--VG------ERGGL 441
Cdd:COG3638 83 GMIFQQFNLVPrLSVLTNVLAGRLGRTstwrsllglFPPED----------------RERALEALerVGladkayQRADQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 442 LSGGQRQRVAIARSLLKNAPILILDEATSALDAVSERLVQSALNRLMKDR--TTLVIAHRLSTVQS-ANQIAVCSDGKII 518
Cdd:COG3638 147 LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDgiTVVVNLHQVDLARRyADRIIGLRDGRVV 226
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
315-526 |
1.05e-28 |
|
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: 113.87 E-value: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 315 DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEwaKVVSIVNQEPVLFS-LSV 393
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK--RPVNTVFQNYALFPhLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 394 AENIAYGLPNEHVSKDDIIKAAKAanahdfIISLPQgYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEATSALD 473
Cdd:cd03300 90 FENIAFGLRLKKLPKAEIKERVAE------ALDLVQ-LEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 145334131 474 AVSERLVQSALNRLMKDR--TTLVIAHRLSTVQS-ANQIAVCSDGKIIELGTHSEL 526
Cdd:cd03300 163 LKLRKDMQLELKRLQKELgiTFVFVTHDQEEALTmSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
6-232 |
1.35e-28 |
|
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: 115.27 E-value: 1.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 6 ENVMAILRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDLGALNSIVNDNISRdrGFRAFTEVFGTICILFTLSPQLAPVL 85
Cdd:cd18576 65 ERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAE--FLRQILTLIGGVVLLFFISWKLTLLM 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 86 GLLMLAVSVLVAVYKRSTVPVYKS--HGLAQATMSdcVSETFSAIRTVRSFSGEKRQMSIFGSQILAYKLSGLKLGTFKS 163
Cdd:cd18576 143 LATVPVVVLVAVLFGRRIRKLSKKvqDELAEANTI--VEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRA 220
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145334131 164 INESITRVAVYISLLALYCLGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDLRGTFAAIDRI 232
Cdd:cd18576 221 LFSSFIIFLLFGAIVAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
314-518 |
1.76e-28 |
|
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: 110.98 E-value: 1.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 314 PDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSE-WAKVVSIVNQepvlfsls 392
Cdd:cd03216 11 GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAMVYQ-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 393 vaeniayglpnehvskddiikaakaanahdfiislpqgydtlvgergglLSGGQRQRVAIARSLLKNAPILILDEATSAL 472
Cdd:cd03216 83 -------------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAAL 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 145334131 473 DAVSERLVQSALNRLMKD-RTTLVIAHRLSTVQS-ANQIAVCSDGKII 518
Cdd:cd03216 114 TPAEVERLFKVIRRLRAQgVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
303-521 |
3.67e-28 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 111.86 E-value: 3.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPLRPdvkVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSewakvVSIV 382
Cdd:cd03235 2 VEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR-----IGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 383 NQEPVL---FSLSVAENIAYGL-----PNEHVSKDDIIKAAKAanaHDFIislpqGYDTLVGERGGLLSGGQRQRVAIAR 454
Cdd:cd03235 74 PQRRSIdrdFPISVRDVVLMGLyghkgLFRRLSKADKAKVDEA---LERV-----GLSELADRQIGELSGGQQQRVLLAR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145334131 455 SLLKNAPILILDEATSALDAVSERLVQSALNRL-MKDRTTLVIAHRLSTVQSANQIAVCSDGKIIELG 521
Cdd:cd03235 146 ALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEYFDRVLLLNRTVVASG 213
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
303-529 |
3.98e-28 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 114.90 E-value: 3.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPL-RPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWA----K 377
Cdd:PRK11153 4 LKNISKVFPQgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRkarrQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 378 VVSIVNQEPVLFSLSVAENIAYGLPNEHVSKDDIikaakaanahdfiislpqgyDTLVGE---RGGL----------LSG 444
Cdd:PRK11153 84 IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEI--------------------KARVTElleLVGLsdkadrypaqLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 445 GQRQRVAIARSLLKNAPILILDEATSALDAVSERLVQSAL---NRLMKdRTTLVIAHRLSTVQS-ANQIAVCSDGKIIEL 520
Cdd:PRK11153 144 GQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLkdiNRELG-LTIVLITHEMDVVKRiCDRVAVIDAGRLVEQ 222
|
....*....
gi 145334131 521 GTHSELVAQ 529
Cdd:PRK11153 223 GTVSEVFSH 231
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
303-526 |
4.72e-28 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 114.86 E-value: 4.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPlrpDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMfdkseWAKV---- 378
Cdd:COG1118 5 VRNISKRFG---SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFT-----NLPPrerr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 379 VSIVNQEPVLF-SLSVAENIAYGLPNEHVSKDDIIKAAkaanaHDFIIslpqgydtLVGeRGGL-------LSGGQRQRV 450
Cdd:COG1118 77 VGFVFQHYALFpHMTVAENIAFGLRVRPPSKAEIRARV-----EELLE--------LVQ-LEGLadrypsqLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 451 AIARSLLKNAPILILDEATSALDAVSERLVQSALNRLMKD--RTTLVIAH------RLstvqsANQIAVCSDGKIIELGT 522
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDElgGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGT 217
|
....
gi 145334131 523 HSEL 526
Cdd:COG1118 218 PDEV 221
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
313-497 |
6.05e-28 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 111.03 E-value: 6.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 313 RPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMfDKSEWAKVVSIVNQEPVLF-SL 391
Cdd:COG4133 12 RGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYLGHADGLKpEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 392 SVAENIAY--GLPNEHVSKDDIikaakaanaHDFIISLpqGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEAT 469
Cdd:COG4133 91 TVRENLRFwaALYGLRADREAI---------DEALEAV--GLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180
....*....|....*....|....*...
gi 145334131 470 SALDAVSERLVQSALNRLMKDRTTLVIA 497
Cdd:COG4133 160 TALDAAGVALLAELIAAHLARGGAVLLT 187
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
303-521 |
6.23e-28 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 111.13 E-value: 6.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPLRpdvKVLDGLSLTLNSGtVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMfDKSEWAKVVSIV 382
Cdd:cd03264 3 LENLTKRYGKK---RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 383 NQEPVLF-SLSVAENIAY-----GLPNEHVSKddiikaakaanAHDFIISLPQGYDTLvGERGGLLSGGQRQRVAIARSL 456
Cdd:cd03264 78 PQEFGVYpNFTVREFLDYiawlkGIPSKEVKA-----------RVDEVLELVNLGDRA-KKKIGSLSGGMRRRVGIAQAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145334131 457 LKNAPILILDEATSALDaVSERL-VQSALNRLMKDRTTLVIAHRLSTVQS-ANQIAVCSDGKIIELG 521
Cdd:cd03264 146 VGDPSILIVDEPTAGLD-PEERIrFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
303-529 |
9.87e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 112.42 E-value: 9.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPlRPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGedVRMFDKSEWA--KVVS 380
Cdd:PRK13635 8 VEHISFRYP-DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG--MVLSEETVWDvrRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 381 IVNQEP--VLFSLSVAENIAYGLPNEHVSKDDII----KAAKAANAHDFIISLPQGydtlvgergglLSGGQRQRVAIAR 454
Cdd:PRK13635 85 MVFQNPdnQFVGATVQDDVAFGLENIGVPREEMVervdQALRQVGMEDFLNREPHR-----------LSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145334131 455 SLLKNAPILILDEATSALDAVSERLVQSALnRLMKDR---TTLVIAHRLSTVQSANQIAVCSDGKIIELGTHSELVAQ 529
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETV-RQLKEQkgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
317-521 |
2.28e-27 |
|
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: 109.69 E-value: 2.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 317 KVLDGLSLTLN---SGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGedVRMFDKSEWA------KVVSIVNQEPV 387
Cdd:cd03297 8 KRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG--TVLFDSRKKInlppqqRKIGLVFQQYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 388 LFS-LSVAENIAYGLPNEHVSKDdiikaakAANAHDFIISLpqGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILILD 466
Cdd:cd03297 86 LFPhLNVRENLAFGLKRKRNRED-------RISVDELLDLL--GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 145334131 467 EATSALDAVSERLVQSALNRLMKD--RTTLVIAHRLSTVQS-ANQIAVCSDGKIIELG 521
Cdd:cd03297 157 EPFSALDRALRLQLLPELKQIKKNlnIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
315-517 |
2.54e-27 |
|
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: 109.54 E-value: 2.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 315 DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVrMFDKSEWAKV---VSIVNQEPVLFS- 390
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINELrqkVGMVFQQFNLFPh 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 391 LSVAENIAYGLPN-EHVSKDDIIKAakaanahdfiislpqGYDTLvgERGGL----------LSGGQRQRVAIARSLLKN 459
Cdd:cd03262 91 LTVLENITLAPIKvKGMSKAEAEER---------------ALELL--EKVGLadkadaypaqLSGGQQQRVAIARALAMN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145334131 460 APILILDEATSALDA--VSErlVQSALNRLMKDRTTLVIA-HRLSTVQS-ANQIAVCSDGKI 517
Cdd:cd03262 154 PKVMLFDEPTSALDPelVGE--VLDVMKDLAEEGMTMVVVtHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
6-232 |
2.74e-27 |
|
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: 111.37 E-value: 2.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 6 ENVMAILRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDLGALNSIVNDNISRdrGFRAFTEVFGTICILFTLSPQLAPVL 85
Cdd:cd18551 65 ERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQ--LVTGVLTVVGAVVLMFLLDWVLTLVT 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 86 GLLMLAVSVLVAVYKRSTVPVYKSHGLAQATMSDCVSETFSAIRTVRSFSGEKRQMSIFGSQILAYKLSGLKLGTFKSIN 165
Cdd:cd18551 143 LAVVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALI 222
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145334131 166 ESITRVAVYISLLALYCLGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDLRGTFAAIDRI 232
Cdd:cd18551 223 GPLMGLAVQLALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
317-521 |
3.53e-27 |
|
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: 108.41 E-value: 3.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 317 KVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLA--RFYEPTQGRITVGGedvRMFDKSEWAKVVSIVNQEPVLFS-LSV 393
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLING---RPLDKRSFRKIIGYVPQDDILHPtLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 394 AENIayglpnehvskddiikaakaanahDFIISLpqgydtlvgeRGglLSGGQRQRVAIARSLLKNAPILILDEATSALD 473
Cdd:cd03213 100 RETL------------------------MFAAKL----------RG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 145334131 474 AVSERLVQSALNRLMKD-RTTLVIAHRLST--VQSANQIAVCSDGKIIELG 521
Cdd:cd03213 144 SSSALQVMSLLRRLADTgRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
305-530 |
1.37e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 109.01 E-value: 1.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 305 DVHFAYPlrPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKS--EWAKVVSIV 382
Cdd:PRK13639 6 DLKYSYP--DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllEVRKTVGIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 383 NQEP--VLFSLSVAENIAYGLPNEHVSKDDIIKAAKAANAHdfiISLpQGYDTLVGERgglLSGGQRQRVAIARSLLKNA 460
Cdd:PRK13639 84 FQNPddQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKA---VGM-EGFENKPPHH---LSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145334131 461 PILILDEATSALDAVSERLVQSALNRLMKDRTTLVIA-HRLSTVQS-ANQIAVCSDGKIIELGTHSELVAQK 530
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVPVyADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
314-526 |
1.47e-26 |
|
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: 108.20 E-value: 1.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 314 PDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEwaKVVSIVNQEPVLFS-LS 392
Cdd:cd03296 13 GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVFQHYALFRhMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 393 VAENIAYGLPNEHVSKDDIIKAAKAANAHdfIISLPQgYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEATSAL 472
Cdd:cd03296 91 VFDNVAFGLRVKPRSERPPEAEIRAKVHE--LLKLVQ-LDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 145334131 473 DAVSERLVQSALNRLMKDR--TTLVIAHRLS-TVQSANQIAVCSDGKIIELGTHSEL 526
Cdd:cd03296 168 DAKVRKELRRWLRRLHDELhvTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
6-212 |
2.16e-26 |
|
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: 108.50 E-value: 2.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 6 ENVMAILRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDLGALNSIVNDNISRdrGFRAFTEVFGTICILFTLSPQLAPVL 85
Cdd:pfam00664 70 ERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGL--LFQSLATIVGGIIVMFYYGWKLTLVL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 86 GLLMLAVSVLVAVYKRSTVPVYKSHGLAQATMSDCVSETFSAIRTVRSFSGEKRQMSIFGSQILAYKLSGLKLGTFKSIN 165
Cdd:pfam00664 148 LAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLS 227
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 145334131 166 ESITRVAVYISLLALYCLGGSKVKTGELAVGTVVSFIGYTFTLTFAV 212
Cdd:pfam00664 228 FGITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
301-526 |
2.25e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 108.73 E-value: 2.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 301 VCLDDVHFAYPLRPdVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEP---TQGRITVGGedVRMFDKSEW-- 375
Cdd:PRK13640 6 VEFKHVSFTYPDSK-KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDG--ITLTAKTVWdi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 376 AKVVSIVNQEP--VLFSLSVAENIAYGLPNEHVSKDDIIKAAKAANAH----DFIISLPQGydtlvgergglLSGGQRQR 449
Cdd:PRK13640 83 REKVGIVFQNPdnQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADvgmlDYIDSEPAN-----------LSGGQKQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145334131 450 VAIARSLLKNAPILILDEATSALDAVSERLVQSALNRLMKDR--TTLVIAHRLSTVQSANQIAVCSDGKIIELGTHSEL 526
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
315-530 |
3.47e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 107.41 E-value: 3.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 315 DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVSIVNQEPVL-FSLSV 393
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGITV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 394 AENIAYGlPNEHVS-------KDDIIKAAKAANAHdfiislpqgYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILILD 466
Cdd:PRK11231 94 RELVAYG-RSPWLSlwgrlsaEDNARVNQAMEQTR---------INHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 467 EATSALDaVSErlvQSALNRLMKD-----RTTLVIAHRLSTV-QSANQIAVCSDGKIIELGTHSELVAQK 530
Cdd:PRK11231 164 EPTTYLD-INH---QVELMRLMRElntqgKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
315-530 |
6.10e-26 |
|
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: 106.50 E-value: 6.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 315 DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKV---VSIVNQEPVLFS- 390
Cdd:cd03256 13 GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrqIGMIFQQFNLIEr 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 391 LSVAENIAYGLPNEH---------VSKDDIIKAAKaanahdfiiSLPQ-GYDTLVGERGGLLSGGQRQRVAIARSLLKNA 460
Cdd:cd03256 93 LSVLENVLSGRLGRRstwrslfglFPKEEKQRALA---------ALERvGLLDKAYQRADQLSGGQQQRVAIARALMQQP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145334131 461 PILILDEATSALDAVSERLVQSALNRLMKDR--TTLVIAHRLSTVQS-ANQIAVCSDGKIIELGTHSELVAQK 530
Cdd:cd03256 164 KLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPAELTDEV 236
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
304-522 |
8.66e-26 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 110.93 E-value: 8.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 304 DDVHFAYPLR--------PDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFyEPTQGRITVGGEDVRMFDKSEW 375
Cdd:COG4172 279 RDLKVWFPIKrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRAL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 376 AKV---VSIVNQEPvlFS-----LSVAENIAYGLpnehvskddiikaakaaNAHDFIISlPQGYDTLVG---ERGGL--- 441
Cdd:COG4172 358 RPLrrrMQVVFQDP--FGslsprMTVGQIIAEGL-----------------RVHGPGLS-AAERRARVAealEEVGLdpa 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 442 --------LSGGQRQRVAIARSLLKNAPILILDEATSALDavseRLVQSA----LNRLMKDR--TTLVIAHRLSTVQS-A 506
Cdd:COG4172 418 arhrypheFSGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQAQildlLRDLQREHglAYLFISHDLAVVRAlA 493
|
250
....*....|....*.
gi 145334131 507 NQIAVCSDGKIIELGT 522
Cdd:COG4172 494 HRVMVMKDGKVVEQGP 509
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
12-232 |
1.07e-25 |
|
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: 106.86 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 12 LRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDLGALNSIVNDNISRdrGFRAFTEVFGTICILFTLSPQLA-------PV 84
Cdd:cd18572 71 LRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNV--FLRNLVQLVGGLAFMFSLSWRLTllafitvPV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 85 LGLLMLAVSvlvAVYKRSTVPVYKShgLAQAtmSDCVSETFSAIRTVRSFSGEKRQMSIFGSQILAYKLSGLKLGTFKSI 164
Cdd:cd18572 149 IALITKVYG---RYYRKLSKEIQDA--LAEA--NQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAG 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145334131 165 NESITRVAVYISLLALYCLGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDLRGTFAAIDRI 232
Cdd:cd18572 222 YVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
303-521 |
1.38e-25 |
|
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: 104.76 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAY-PLRPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMfDKSEWAKVVSI 381
Cdd:cd03266 4 ADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 382 VNQEPVLFS-LSVAENIAY--GLpneHVSKDDIIKAAKaanahDFIISLPQGYDTLvGERGGLLSGGQRQRVAIARSLLK 458
Cdd:cd03266 83 VSDSTGLYDrLTARENLEYfaGL---YGLKGDELTARL-----EELADRLGMEELL-DRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145334131 459 NAPILILDEATSALDAVSERLVQSALNRLMKDRTTLVIA-HRLSTVQS-ANQIAVCSDGKIIELG 521
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
294-539 |
4.19e-25 |
|
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: 110.42 E-value: 4.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 294 TLTWAgdvclddvhfayplRPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEdvrmfdks 373
Cdd:TIGR00957 643 TFTWA--------------RDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------- 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 374 ewakvVSIVNQEPVLFSLSVAENIAYGLP-NEHVSKddiIKAAKAANAHDFIIsLPQGYDTLVGERGGLLSGGQRQRVAI 452
Cdd:TIGR00957 701 -----VAYVPQQAWIQNDSLRENILFGKAlNEKYYQ---QVLEACALLPDLEI-LPSGDRTEIGEKGVNLSGGQKQRVSL 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 453 ARSLLKNAPILILDEATSALDA-VSERLVQSALNR--LMKDRTTLVIAHRLSTVQSANQIAVCSDGKIIELGTHSELVAQ 529
Cdd:TIGR00957 772 ARAVYSNADIYLFDDPLSAVDAhVGKHIFEHVIGPegVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQR 851
|
250
....*....|
gi 145334131 530 KGSYASLVGT 539
Cdd:TIGR00957 852 DGAFAEFLRT 861
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
318-526 |
5.16e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 106.84 E-value: 5.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 318 VLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDvrMFDKSEWAKVVSIVNQEPVLFS-LSVAEN 396
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD--LSHVPPYQRPINMMFQSYALFPhMTVEQN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 397 IAYGLPNEHVSKDDIIKAAKAanahdfIISLPQGYDtLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEATSALD-AV 475
Cdd:PRK11607 112 IAFGLKQDKLPKAEIASRVNE------MLGLVHMQE-FAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDkKL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 145334131 476 SERLVQSALNRLMKDRTTLV-IAH-RLSTVQSANQIAVCSDGKIIELGTHSEL 526
Cdd:PRK11607 185 RDRMQLEVVDILERVGVTCVmVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
318-538 |
6.17e-25 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 105.96 E-value: 6.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 318 VLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRmfDKSEWAKVVSIVNQEPVLFS-LSVAEN 396
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT--HRSIQQRDICMVFQSYALFPhMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 397 IAYGLPNEHVSKDDIIKAAKAANAhdfIISLPQGYDTLVGErgglLSGGQRQRVAIARSLLKNAPILILDEATSALDAVS 476
Cdd:PRK11432 99 VGYGLKMLGVPKEERKQRVKEALE---LVDLAGFEDRYVDQ----ISGGQQQRVALARALILKPKVLLFDEPLSNLDANL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145334131 477 ERLVQSALNRLMK--DRTTLVIAHRLSTVQS-ANQIAVCSDGKIIELGTHSELVAQKGS--YASLVG 538
Cdd:PRK11432 172 RRSMREKIRELQQqfNITSLYVTHDQSEAFAvSDTVIVMNKGKIMQIGSPQELYRQPASrfMASFMG 238
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
303-521 |
6.45e-25 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 103.96 E-value: 6.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPlrpDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYE--P---TQGRITVGGEDVrmFDKS---- 373
Cdd:COG1117 14 VRNLNVYYG---DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDI--YDPDvdvv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 374 EWAKVVSIVNQEPVLFSLSVAENIAYGLP-NEHVSKDDIikaakaanahDFII--SLPQG------YDTLvGERGGLLSG 444
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNVAYGLRlHGIKSKSEL----------DEIVeeSLRKAalwdevKDRL-KKSALGLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 445 GQRQRVAIARSLLKNAPILILDEATSALDAVSERLVQSALNRLmKDRTTLVIA-HRLStvqsanQIAVCSD-------GK 516
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL-KKDYTIVIVtHNMQ------QAARVSDytaffylGE 230
|
....*
gi 145334131 517 IIELG 521
Cdd:COG1117 231 LVEFG 235
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
313-519 |
9.44e-25 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 103.61 E-value: 9.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 313 RPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWA---KVVSIVNQ----- 384
Cdd:PRK10419 22 HQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKafrRDIQMVFQdsisa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 385 ------------EPV--LFSLSVAENIA--------YGLPNEHVSKddiikaakaanahdfiisLPQGydtlvgergglL 442
Cdd:PRK10419 102 vnprktvreiirEPLrhLLSLDKAERLArasemlraVDLDDSVLDK------------------RPPQ-----------L 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 443 SGGQRQRVAIARSLLKNAPILILDEATSALDAVSERLVQSALNRLMKDRTT--LVIAHRLSTVQS-ANQIAVCSDGKIIE 519
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
305-497 |
1.11e-24 |
|
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: 102.10 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 305 DVHFAYPlrPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKV---VSI 381
Cdd:cd03292 5 NVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLrrkIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 382 VNQE-PVLFSLSVAENIAYGLPNEHVSKDDIIKAAKAANAhdfIISLPQGYDTLVGErgglLSGGQRQRVAIARSLLKNA 460
Cdd:cd03292 83 VFQDfRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALE---LVGLSHKHRALPAE----LSGGEQQRVAIARAIVNSP 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 145334131 461 PILILDEATSALDAVSERLVQSALNRLMKDRTTLVIA 497
Cdd:cd03292 156 TILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
303-537 |
1.16e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 103.66 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYplRPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVSIV 382
Cdd:PRK13647 7 VEDLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 383 NQEP--VLFSLSVAENIAYGLPNEHVSKDDII----KAAKAANAHDFIISLPQGydtlvgergglLSGGQRQRVAIARSL 456
Cdd:PRK13647 85 FQDPddQVFSSTVWDDVAFGPVNMGLDKDEVErrveEALKAVRMWDFRDKPPYH-----------LSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 457 LKNAPILILDEATSALDAVSERLVQSALNRLMKDRTTLVIA-HRLS-TVQSANQIAVCSDGKII-----ELGTHSELVAQ 529
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDlAAEWADQVIVLKEGRVLaegdkSLLTDEDIVEQ 233
|
....*...
gi 145334131 530 KGSYASLV 537
Cdd:PRK13647 234 AGLRLPLV 241
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
318-525 |
1.20e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 102.93 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 318 VLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVSIVNQEPVL-FSLSVAEN 396
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 397 IAYGL-PNEHVSKDDIikaakaanahdfiiSLPQGYDTLVGeRGGL-------LSGGQRQRVAIARSLL------KNAPI 462
Cdd:PRK13548 97 VAMGRaPHGLSRAEDD--------------ALVAAALAQVD-LAHLagrdypqLSGGEQQRVQLARVLAqlwepdGPPRW 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145334131 463 LILDEATSALDAVSERLVQSALNRLMKDRTTLVIA--HRLS-TVQSANQIAVCSDGKIIELGTHSE 525
Cdd:PRK13548 162 LLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVvlHDLNlAARYADRIVLLHQGRLVADGTPAE 227
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
334-526 |
2.03e-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: 104.11 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 334 LVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRmfDKSEWAKVVSIVNQEPVLFS-LSVAENIAYGLPNEHVSKDDII 412
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVT--NVPPHLRHINMVFQSYALFPhMTVEENVAFGLKMRKVPRAEIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 413 KAAKAanahdfIISLPQgydtlVGERGGL----LSGGQRQRVAIARSLLKNAPILILDEATSALDAVSERLVQSALNRLM 488
Cdd:TIGR01187 79 PRVLE------ALRLVQ-----LEEFADRkphqLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQ 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 145334131 489 KDR--TTLVIAHRLSTVQS-ANQIAVCSDGKIIELGTHSEL 526
Cdd:TIGR01187 148 EQLgiTFVFVTHDQEEAMTmSDRIAIMRKGKIAQIGTPEEI 188
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
303-526 |
2.17e-24 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 101.36 E-value: 2.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPlrpDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRmfDKSEWAKV---V 379
Cdd:cd03224 3 VENLNAGYG---KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT--GLPPHERAragI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 380 SIVNQEPVLF-SLSVAENI---AYGLPNEHVSKDDiikaakaanahDFIISL-PQGYDTLvGERGGLLSGGQRQRVAIAR 454
Cdd:cd03224 78 GYVPEGRRIFpELTVEENLllgAYARRRAKRKARL-----------ERVYELfPRLKERR-KQLAGTLSGGEQQMLAIAR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145334131 455 SLLKNAPILILDEATSALDAVSERLVQSALNRLMKDRTT-LVIAHRLSTVQS-ANQIAVCSDGKIIELGTHSEL 526
Cdd:cd03224 146 ALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTiLLVEQNARFALEiADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
315-526 |
2.61e-24 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 101.61 E-value: 2.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 315 DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSE---WAKVVSIVNQEPVLFS- 390
Cdd:TIGR02315 14 GKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrkLRRRIGMIFQHYNLIEr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 391 LSVAENIAYGLPNehvSKDDIIKAAKAANAHDFIISLPQ----GYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILILD 466
Cdd:TIGR02315 94 LTVLENVLHGRLG---YKPTWRSLLGRFSEEDKERALSAlervGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILAD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145334131 467 EATSALDAVSERLVQSALNRLMKDR--TTLVIAHRLSTVQS-ANQIAVCSDGKIIELGTHSEL 526
Cdd:TIGR02315 171 EPIASLDPKTSKQVMDYLKRINKEDgiTVIINLHQVDLAKKyADRIVGLKAGEIVFDGAPSEL 233
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
317-526 |
3.32e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 101.78 E-value: 3.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 317 KVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYE-----PTQGRITVGGEDV--RMFDKSEWAKVVSIVNQEPVLF 389
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 390 SLSVAENIAYGLPNEHVsKDDIIKAAKAANahdfiiSLPQG----------YDTLVGergglLSGGQRQRVAIARSLLKN 459
Cdd:PRK14239 99 PMSIYENVVYGLRLKGI-KDKQVLDEAVEK------SLKGAsiwdevkdrlHDSALG-----LSGGQQQRVCIARVLATS 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145334131 460 APILILDEATSALDAVSERLVQSALNRLMKDRTTLVIAHRLstvQSANQI----AVCSDGKIIELGTHSEL 526
Cdd:PRK14239 167 PKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM---QQASRIsdrtGFFLDGDLIEYNDTKQM 234
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
316-529 |
3.79e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 103.12 E-value: 3.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 316 VKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWA---KVVSIVNQ-------- 384
Cdd:PRK11308 28 VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKllrQKIQIVFQnpygslnp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 385 ---------EPVLF--SLSVAENIA--------YGLPNEHVSKddiikaakaaNAHDFiislpqgydtlvgerggllSGG 445
Cdd:PRK11308 108 rkkvgqileEPLLIntSLSAAERREkalammakVGLRPEHYDR----------YPHMF-------------------SGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 446 QRQRVAIARSLLKNAPILILDEATSALDaVSerlVQSALNRLMKD-----RTTLV-IAHRLSTVQS-ANQIAVCSDGKII 518
Cdd:PRK11308 159 QRQRIAIARALMLDPDVVVADEPVSALD-VS---VQAQVLNLMMDlqqelGLSYVfISHDLSVVEHiADEVMVMYLGRCV 234
|
250
....*....|.
gi 145334131 519 ELGTHSELVAQ 529
Cdd:PRK11308 235 EKGTKEQIFNN 245
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
302-523 |
7.22e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 100.17 E-value: 7.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 302 CLDDVHFaypLRPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVSI 381
Cdd:PRK10247 9 QLQNVGY---LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 382 VNQEPVLFSLSVAENIA--YGLPNEHVSKDDIIKAAKAanahdfiISLPqgyDTLVGERGGLLSGGQRQRVAIARSLLKN 459
Cdd:PRK10247 86 CAQTPTLFGDTVYDNLIfpWQIRNQQPDPAIFLDDLER-------FALP---DTILTKNIAELSGGEKQRISLIRNLQFM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145334131 460 APILILDEATSALDAVSERLVQSALNRLMKDRTTLViahrLSTVQSANQIAVCSDgkIIELGTH 523
Cdd:PRK10247 156 PKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAV----LWVTHDKDEINHADK--VITLQPH 213
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
314-518 |
8.47e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 104.72 E-value: 8.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 314 PDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKV-VSIVNQEPVLF-SL 391
Cdd:COG3845 16 GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALgIGMVHQHFMLVpNL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 392 SVAENIAYGLPNEHVSKDDIIKAAKAanahdfIISLPQGY------DTLVGErgglLSGGQRQRVAIARSLLKNAPILIL 465
Cdd:COG3845 96 TVAENIVLGLEPTKGGRLDRKAARAR------IRELSERYgldvdpDAKVED----LSVGEQQRVEILKALYRGARILIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 145334131 466 DEATSAL-DAVSERLVQsALNRLMKDRTTLV-IAHRLSTVQS-ANQIAVCSDGKII 518
Cdd:COG3845 166 DEPTAVLtPQEADELFE-ILRRLAAEGKSIIfITHKLREVMAiADRVTVLRRGKVV 220
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
316-518 |
9.33e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 100.55 E-value: 9.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 316 VKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDV-RMfdkSEW--AKVVSIVNQEPVL---F 389
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtKL---PEYkrAKYIGRVFQDPMMgtaP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 390 SLSVAEN--IAY------GLpNEHVSKDDiikaakAANAHDFIISLPQGYDTLVGERGGLLSGGQRQRVAIARSLLKNAP 461
Cdd:COG1101 96 SMTIEENlaLAYrrgkrrGL-RRGLTKKR------RELFRELLATLGLGLENRLDTKVGLLSGGQRQALSLLMATLTKPK 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145334131 462 ILILDEATSALDAVSERLVQSALNRLMKDR--TTLVIAHRLstvQSA----NQIAVCSDGKII 518
Cdd:COG1101 169 LLLLDEHTAALDPKTAALVLELTEKIVEENnlTTLMVTHNM---EQAldygNRLIMMHEGRII 228
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
322-530 |
9.49e-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: 102.50 E-value: 9.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 322 LSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEdvRMFDKSEWA------KVVSIVNQEPVLFS-LSVA 394
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGR--TLFDSRKGIflppekRRIGYVFQEARLFPhLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 395 ENIAYGLPNEHVSkddiikaaKAANAHDFIISLpQGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEATSALDA 474
Cdd:TIGR02142 94 GNLRYGMKRARPS--------ERRISFERVIEL-LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 145334131 475 VSERLVQSALNRLMK--DRTTLVIAHRLSTVQS-ANQIAVCSDGKIIELGTHSELVAQK 530
Cdd:TIGR02142 165 PRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
317-525 |
1.18e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 100.89 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 317 KVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRmfDK----SEWAKVVSIVNQEP--VLFS 390
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDIT--DKkvklSDIRKKVGLVFQYPeyQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 391 LSVAENIAYGLPNEHVSKDDIIKAAKAANAhdfIISLPqgYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEATS 470
Cdd:PRK13637 99 ETIEKDIAFGPINLGLSEEEIENRVKRAMN---IVGLD--YEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 145334131 471 ALDAVSERLVQSALNRLMKDR--TTLVIAHRLSTVQS-ANQIAVCSDGKIIELGTHSE 525
Cdd:PRK13637 174 GLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
303-498 |
1.50e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 99.94 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYP-LRPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDV------Rmfdksew 375
Cdd:COG4525 6 VRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgpgadR------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 376 akvvSIVNQEPVLFS-LSVAENIAYGLPNEHVSKDDIIKAAkaanaHDFIislpqgydTLVGERGGL------LSGGQRQ 448
Cdd:COG4525 79 ----GVVFQKDALLPwLNVLDNVAFGLRLRGVPKAERRARA-----EELL--------ALVGLADFArrriwqLSGGMRQ 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 145334131 449 RVAIARSLLKNAPILILDEATSALDAVSERLVQSALNRLMKD--RTTLVIAH 498
Cdd:COG4525 142 RVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRtgKGVFLITH 193
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
1-232 |
1.88e-23 |
|
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: 100.57 E-value: 1.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 1 MTAIWENVMAILRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDLGALNSIVNDNISRdrGFRAFTEVFGTICILFTLSPQ 80
Cdd:cd18552 63 MAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTV--LVRDPLTVIGLLGVLFYLDWK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 81 LApVLGLLMLAVSVLVAVY--KRstvpVYKSHGLAQATMSDC---VSETFSAIRTVRSFSGEKRQMSIFGSQILAYKLSG 155
Cdd:cd18552 141 LT-LIALVVLPLAALPIRRigKR----LRKISRRSQESMGDLtsvLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLS 215
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145334131 156 LKLGTFKSINESITRVAVYISLLALYCLGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDLRGTFAAIDRI 232
Cdd:cd18552 216 MKIARARALSSPLMELLGAIAIALVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
316-526 |
2.17e-23 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 103.59 E-value: 2.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 316 VKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGedvRMFDKSEWAKV----VSIVNQEPVLF-S 390
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGG---NPCARLTPAKAhqlgIYLVPQEPLLFpN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 391 LSVAENIAYGLPNEHVSKDDIIKAAKAANAHdfiISLPQgydtlvgeRGGLLSGGQRQRVAIARSLLKNAPILILDEATS 470
Cdd:PRK15439 101 LSVKENILFGLPKRQASMQKMKQLLAALGCQ---LDLDS--------SAGSLEVADRQIVEILRGLMRDSRILILDEPTA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 145334131 471 ALDAV-SERLVQSALNRLMKDRTTLVIAHRLSTV-QSANQIAVCSDGKIIELGTHSEL 526
Cdd:PRK15439 170 SLTPAeTERLFSRIRELLAQGVGIVFISHKLPEIrQLADRISVMRDGTIALSGKTADL 227
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
315-522 |
2.20e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 101.95 E-value: 2.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 315 DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRmfDKSEWAKVVSIVNQEPVLFS-LSV 393
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT--HVPAENRHVNTVFQSYALFPhMTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 394 AENIAYGLPNEHVSKDDIIkaakaanahdfiislPQGYDTL-------VGERGGL-LSGGQRQRVAIARSLLKNAPILIL 465
Cdd:PRK09452 104 FENVAFGLRMQKTPAAEIT---------------PRVMEALrmvqleeFAQRKPHqLSGGQQQRVAIARAVVNKPKVLLL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145334131 466 DEATSALDAVSERLVQSALNRLMKDR--TTLVIAH----RLSTvqsANQIAVCSDGKIIELGT 522
Cdd:PRK09452 169 DESLSALDYKLRKQMQNELKALQRKLgiTFVFVTHdqeeALTM---SDRIVVMRDGRIEQDGT 228
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
314-515 |
2.21e-23 |
|
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: 98.56 E-value: 2.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 314 PDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRI--------TVGGEDVRMFDKSEwakvVSIVNQE 385
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesEPSFEATRSRNRYS----VAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 386 PVLFSLSVAENIAYGLPnehVSKDDIIKAAKAANAHDFIISLPQGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILIL 465
Cdd:cd03290 88 PWLLNATVEENITFGSP---FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 145334131 466 DEATSALDA-VSERLVQSALNRLMKD--RTTLVIAHRLSTVQSANQIAVCSDG 515
Cdd:cd03290 165 DDPFSALDIhLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
303-526 |
2.64e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 99.44 E-value: 2.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYplRPDVK-VLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVSI 381
Cdd:PRK13648 10 FKNVSFQY--QSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 382 VNQEP--VLFSLSVAENIAYGLPNEHVSKDDIIKAAKAANAH----DFIISLPQGydtlvgergglLSGGQRQRVAIARS 455
Cdd:PRK13648 88 VFQNPdnQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQvdmlERADYEPNA-----------LSGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145334131 456 LLKNAPILILDEATSALDAVSERLVQSALNRLM--KDRTTLVIAHRLSTVQSANQIAVCSDGKIIELGTHSEL 526
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKseHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
298-537 |
2.92e-23 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 104.86 E-value: 2.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 298 AGDVCLDDVHFAY----PLrpdvkVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKS 373
Cdd:PTZ00243 1306 AGSLVFEGVQMRYreglPL-----VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLR 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 374 EWAKVVSIVNQEPVLFSLSVAENIAyglPNEHVSKDDIIKAAKAANAHDFIISLPQGYDTLVGERGGLLSGGQRQRVAIA 453
Cdd:PTZ00243 1381 ELRRQFSMIPQDPVLFDGTVRQNVD---PFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMA 1457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 454 RSLLKNAPILIL-DEATSALDAVSERLVQSALNRLMKDRTTLVIAHRLSTVQSANQIAVCSDGKIIELGTHSELVAQKGS 532
Cdd:PTZ00243 1458 RALLKKGSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQS 1537
|
....*.
gi 145334131 533 -YASLV 537
Cdd:PTZ00243 1538 iFHSMV 1543
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
315-526 |
3.86e-23 |
|
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: 97.83 E-value: 3.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 315 DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMfDKSEWAKVVSIVNQEPVL-FSLSV 393
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVdDELTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 394 AENIA-----YGLPNEHVSKddiikaaKAANAHDFiISLPQGYDTLVGErgglLSGGQRQRVAIARSLLKNAPILILDEA 468
Cdd:cd03265 91 WENLYiharlYGVPGAERRE-------RIDELLDF-VGLLEAADRLVKT----YSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145334131 469 TSALDAVSERLVQSALNRLMK--DRTTLVIAHRLSTV-QSANQIAVCSDGKIIELGTHSEL 526
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKLKEefGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
315-526 |
3.93e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 98.45 E-value: 3.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 315 DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYE-----PTQGRITVGGEDVRMFDKSEWAKVVSIVNQEP-VL 388
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 389 FSLSVAENIAYGLPNEHVSKDDIIKAAKAANAhdfiISLPQGYDTL---VGERGGLLSGGQRQRVAIARSLLKNAPILIL 465
Cdd:PRK14247 95 PNLSIFENVALGLKLNRLVKSKKELQERVRWA----LEKAQLWDEVkdrLDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145334131 466 DEATSALDAVSERLVQSALNRLMKDRTTLVIAH-RLSTVQSANQIAVCSDGKIIELGTHSEL 526
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
303-530 |
5.84e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 98.77 E-value: 5.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPlrPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKS--EWAKVVS 380
Cdd:PRK13636 8 VEELNYNYS--DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlmKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 381 IVNQEP--VLFSLSVAENIAYGLPNEHVSKDDIIKAAKAANAHdfiislpQGYDTLVGERGGLLSGGQRQRVAIARSLLK 458
Cdd:PRK13636 86 MVFQDPdnQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKR-------TGIEHLKDKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145334131 459 NAPILILDEATSALD--AVSE--RLVQSALNRLmkDRTTLVIAHRLSTVQ-SANQIAVCSDGKIIELGTHSELVAQK 530
Cdd:PRK13636 159 EPKVLVLDEPTAGLDpmGVSEimKLLVEMQKEL--GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
318-543 |
8.03e-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: 97.95 E-value: 8.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 318 VLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKV---VSIVNQE---PVLFSL 391
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFrrdVQLVFQDspsAVNPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 392 SVAENIayGLPNEHVSKDDIIKAAKAANAHDFIISLPqgyDTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEATSA 471
Cdd:TIGR02769 106 TVRQII--GEPLRHLTSLDESEQKARIAELLDMVGLR---SEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSN 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145334131 472 LDAVSERLVQSALNRLMKDRTT--LVIAHRLSTVQS-ANQIAVCSDGKIIElgthSELVAQKGSYASLVGTQRLA 543
Cdd:TIGR02769 181 LDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSfCQRVAVMDKGQIVE----ECDVAQLLSFKHPAGRNLQS 251
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
309-512 |
9.06e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 95.76 E-value: 9.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 309 AYPLRPdvkVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGedvrmfdksewAKVVSIVNQ---E 385
Cdd:NF040873 1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQrseV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 386 PVLFSLSVAENIAYGL-----PNEHVSKDDIIKAAkaanahDFIISLpqGYDTLVGERGGLLSGGQRQRVAIARSLLKNA 460
Cdd:NF040873 67 PDSLPLTVRDLVAMGRwarrgLWRRLTRDDRAAVD------DALERV--GLADLAGRQLGELSGGQRQRALLAQGLAQEA 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 145334131 461 PILILDEATSALDAVSERLVQSALNRLMKD-RTTLVIAHRLSTVQSANQIAVC 512
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLAEEHARgATVVVVTHDLELVRRADPCVLL 191
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
197-537 |
1.31e-22 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 102.68 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 197 TVVSF-IGYTFTLTFAVQGLVNTFGDlrgTFAAIDRINSILNAvdiDEALAygLERDIHTKKVQDENLKLFLSAGpnvnI 275
Cdd:TIGR01271 339 TTISYcIVLRMTVTRQFPGAIQTWYD---SLGAITKIQDFLCK---EEYKT--LEYNLTTTEVEMVNVTASWDEG----I 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 276 RHLdkyyMSNLKSTNNLRTLTwAGDVCLDDVHFAYPLRPdvkVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEP 355
Cdd:TIGR01271 407 GEL----FEKIKQNNKARKQP-NGDDGLFFSNFSLYVTP---VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEP 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 356 TQGRITVGGEdvrmfdksewakvVSIVNQEPVLFSLSVAENIAYGLpnehvSKDDIIKAAKAAN--AHDFIISLPQGYDT 433
Cdd:TIGR01271 479 SEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNIIFGL-----SYDEYRYTSVIKAcqLEEDIALFPEKDKT 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 434 LVGERGGLLSGGQRQRVAIARSLLKNAPILILDEATSALDAVSER-LVQSALNRLMKDRTTLVIAHRLSTVQSANQIAVC 512
Cdd:TIGR01271 541 VLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKeIFESCLCKLMSNKTRILVTSKLEHLKKADKILLL 620
|
330 340
....*....|....*....|....*
gi 145334131 513 SDGKIIELGTHSELVAQKGSYASLV 537
Cdd:TIGR01271 621 HEGVCYFYGTFSELQAKRPDFSSLL 645
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
318-522 |
1.88e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 96.72 E-value: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 318 VLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVSIVNQEPVL-FSLSVAEN 396
Cdd:COG4559 16 LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLPQHSSLaFPFTVEEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 397 IAYGL-PNEHVSKDDiikaakaanahdfiislpqgyDTLVGE---RGGL----------LSGGQRQRVAIARSL--LKNA 460
Cdd:COG4559 96 VALGRaPHGSSAAQD---------------------RQIVREalaLVGLahlagrsyqtLSGGEQQRVQLARVLaqLWEP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145334131 461 P-----ILILDEATSALDavserLV-QSALNRLMKDRTT-----LVIAHRLS-TVQSANQIAVCSDGKIIELGT 522
Cdd:COG4559 155 VdggprWLFLDEPTSALD-----LAhQHAVLRLARQLARrgggvVAVLHDLNlAAQYADRILLLHQGRLVAQGT 223
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
12-232 |
2.38e-22 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 97.10 E-value: 2.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 12 LRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDLGA--------LNSIVNdnisrdrgfrAFTEVFGTICILFTLSPQLAP 83
Cdd:cd18541 75 LRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAvrmalgpgILYLVD----------ALFLGVLVLVMMFTISPKLTL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 84 VLGLLMLAVSVLVAVYKRStvpVYKSHGLAQ---ATMSDCVSETFSAIRTVRSFSGEKRQMSIFGSQILAYKLSGLKLGT 160
Cdd:cd18541 145 IALLPLPLLALLVYRLGKK---IHKRFRKVQeafSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLAR 221
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145334131 161 FKSINESITRVAVYISLLALYCLGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGL---VNTFGdlRGTfAAIDRI 232
Cdd:cd18541 222 VDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTITLGDLVAFNSYLGMLIWPMMALgwvINLIQ--RGA-ASLKRI 293
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
314-526 |
2.83e-22 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 99.99 E-value: 2.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 314 PDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFD-KSEWAKVVSIVNQEPVLF-SL 391
Cdd:PRK11288 15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAStTAALAAGVAIIYQELHLVpEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 392 SVAENIAYG-LPNEH--VSKDDIIKAAKAANAH---DFIISLPQGYdtlvgergglLSGGQRQRVAIARSLLKNAPILIL 465
Cdd:PRK11288 95 TVAENLYLGqLPHKGgiVNRRLLNYEAREQLEHlgvDIDPDTPLKY----------LSIGQRQMVEIAKALARNARVIAF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145334131 466 DEATSALDA-VSERLVqSALNRLMKD-RTTLVIAHRLSTV-QSANQIAVCSDGKIIElgTHSEL 526
Cdd:PRK11288 165 DEPTSSLSArEIEQLF-RVIRELRAEgRVILYVSHRMEEIfALCDAITVFKDGRYVA--TFDDM 225
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
315-519 |
3.26e-22 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 94.59 E-value: 3.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 315 DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMfDKSEWAKVVSIVnQEPVLF-SLSV 393
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-NIEALRRIGALI-EAPGFYpNLTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 394 AENI-----AYGLPNEHVskddiikaakaanahDFIISLpQGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEA 468
Cdd:cd03268 90 RENLrllarLLGIRKKRI---------------DEVLDV-VGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 145334131 469 TSALDAVSERLVQSALNRLMKDRTTLVIA-HRLSTVQS-ANQIAVCSDGKIIE 519
Cdd:cd03268 154 TNGLDPDGIKELRELILSLRDQGITVLISsHLLSEIQKvADRIGIINKGKLIE 206
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
323-529 |
6.08e-22 |
|
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: 97.48 E-value: 6.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 323 SLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVrmFD--KSEWAKV----VSIVNQEPVLFS-LSVAE 395
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL--QDsaRGIFLPPhrrrIGYVFQEARLFPhLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 396 NIAYGLPNEHVSKDdiikaakaANAHDFIISLpQGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEATSALDAV 475
Cdd:COG4148 97 NLLYGRKRAPRAER--------RISFDEVVEL-LGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 145334131 476 SERLVQSALNRLmKDRTTLVI---AHRLSTVQS-ANQIAVCSDGKIIELGTHSELVAQ 529
Cdd:COG4148 168 RKAEILPYLERL-RDELDIPIlyvSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
317-528 |
6.41e-22 |
|
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: 94.53 E-value: 6.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 317 KVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKV-VSIVNQEPVLF-SLSVA 394
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYLPQEASIFrKLTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 395 ENIAYGLPNEHVSKdDIIKAAKAANAHDFIISlpqgydTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEATSALD- 473
Cdd:cd03218 94 ENILAVLEIRGLSK-KEREEKLEELLEEFHIT------HLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDp 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145334131 474 -AVSE------RLVQSALNRLMKD---RTTLVIAHRlstvqsanqIAVCSDGKIIELGTHSELVA 528
Cdd:cd03218 167 iAVQDiqkiikILKDRGIGVLITDhnvRETLSITDR---------AYIIYEGKVLAEGTPEEIAA 222
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
316-522 |
7.11e-22 |
|
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: 95.11 E-value: 7.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 316 VKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDV--------------RMFdksewakvvsi 381
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItglpphriarlgiaRTF----------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 382 vnQEPVLF-SLSVAENIAYGLPNEHVSKDDIIKAAKAANAHDFIISLPQGYDTL--VG------ERGGLLSGGQRQRVAI 452
Cdd:COG0411 86 --QNPRLFpELTVLENVLVAAHARLGRGLLAALLRLPRARREEREARERAEELLerVGladradEPAGNLSYGQQRRLEI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145334131 453 ARSLLKNAPILILDEATSALDAV-SERLVQsALNRLMKDR--TTLVIAHRLSTVQS-ANQIAVCSDGKIIELGT 522
Cdd:COG0411 164 ARALATEPKLLLLDEPAAGLNPEeTEELAE-LIRRLRDERgiTILLIEHDMDLVMGlADRIVVLDFGRVIAEGT 236
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
317-526 |
7.74e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 97.08 E-value: 7.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 317 KVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDV-RMFDKSewaKVVSIVNQEPVLFS-LSVA 394
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVsRLHARD---RKVGFVFQHYALFRhMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 395 ENIAYGL--------PNEHVSKDDIIKAAKaanahdfIISLPQgydtLVGERGGLLSGGQRQRVAIARSLLKNAPILILD 466
Cdd:PRK10851 93 DNIAFGLtvlprrerPNAAAIKAKVTQLLE-------MVQLAH----LADRYPAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145334131 467 EATSALDAVSERLVQSALNRLMKDR--TTLVIAH-RLSTVQSANQIAVCSDGKIIELGTHSEL 526
Cdd:PRK10851 162 EPFGALDAQVRKELRRWLRQLHEELkfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
316-528 |
9.10e-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: 94.04 E-value: 9.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 316 VKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKV-VSIVNQEPVLF-SLSV 393
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIGRTFQIPRLFpELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 394 AENIAYGLPNEHVSKDDIIKAAKAANAH--------DFIislpqGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILIL 465
Cdd:cd03219 93 LENVMVAAQARTGSGLLLARARREEREAreraeellERV-----GLADLADRPAGELSYGQQRRLEIARALATDPKLLLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145334131 466 DEATSALDAV-SERLVQ--SALNRlmKDRTTLVIAHRLSTVQS-ANQIAVCSDGKIIELGTHSELVA 528
Cdd:cd03219 168 DEPAAGLNPEeTEELAEliRELRE--RGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
1-232 |
1.19e-21 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 95.24 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 1 MTAIWENVMAILRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDLGALNSIVNDNISrdRGFRAFTEVFGTICILFTLSPQ 80
Cdd:cd18575 60 VSWLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLS--IALRNLLLLIGGLVMLFITSPK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 81 LAPVLGLLMLAVSVLVAVYKRStvpVYKSHGLAQATMSDC---VSETFSAIRTVRSFSGEKRQMSIFGSQILAYKLSGLK 157
Cdd:cd18575 138 LTLLVLLVIPLVVLPIILFGRR---VRRLSRASQDRLADLsafAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALR 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145334131 158 LGTFKSINESITRVAVYISLLALYCLGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDLRGTFAAIDRI 232
Cdd:cd18575 215 RIRARALLTALVIFLVFGAIVFVLWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
323-527 |
2.15e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 96.26 E-value: 2.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 323 SLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKV----VSIVNQEPVLFS-LSVAENI 397
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMPhMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 398 AYGLPNEHVSKDDIIKAAKAANAHDFIISLPQGYDTlvgerggLLSGGQRQRVAIARSLLKNAPILILDEATSALDAVSE 477
Cdd:PRK10070 128 AFGMELAGINAEERREKALDALRQVGLENYAHSYPD-------ELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 145334131 478 RLVQSALNRLM--KDRTTLVIAHRL-STVQSANQIAVCSDGKIIELGTHSELV 527
Cdd:PRK10070 201 TEMQDELVKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
303-498 |
2.26e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 93.61 E-value: 2.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPLRPdvkVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVrmfdKSEWAKVVSIV 382
Cdd:PRK11248 4 ISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV----EGPGAERGVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 383 NQEPVLFSLSVAENIAYGLPNEHVSKDDIIKAAKAANAhdfiislpqgydtLVGERGG------LLSGGQRQRVAIARSL 456
Cdd:PRK11248 77 QNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLK-------------KVGLEGAekryiwQLSGGQRQRVGIARAL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 145334131 457 LKNAPILILDEATSALDAVSERLVQSALNRLMKD--RTTLVIAH 498
Cdd:PRK11248 144 AANPQLLLLDEPFGALDAFTREQMQTLLLKLWQEtgKQVLLITH 187
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
295-528 |
4.31e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 93.53 E-value: 4.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 295 LTWAGDVCLDDVHFAYPLRP--DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDV----- 367
Cdd:PRK13645 1 FDFSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 368 RMFDKSEWAKVVSIVNQEP--VLFSLSVAENIAYGLPNEHVSKDDIIKAAKAANAhdfIISLPQGYdtlVGERGGLLSGG 445
Cdd:PRK13645 81 KIKEVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLK---LVQLPEDY---VKRSPFELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 446 QRQRVAIARSLLKNAPILILDEATSALDAVSERLVQSALNRLMKD--RTTLVIAHRLSTV-QSANQIAVCSDGKIIELGT 522
Cdd:PRK13645 155 QKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGS 234
|
....*.
gi 145334131 523 HSELVA 528
Cdd:PRK13645 235 PFEIFS 240
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
319-526 |
5.01e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 93.27 E-value: 5.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 319 LDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSE----WAKVVSIVNQ--EPVLFSLS 392
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikqIRKKVGLVFQfpESQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 393 VAENIAYGLPNEHVSKDDIIkaakaanahdfiiSLPQGYDTLVGERGGL-------LSGGQRQRVAIARSLLKNAPILIL 465
Cdd:PRK13649 103 VLKDVAFGPQNFGVSQEEAE-------------ALAREKLALVGISESLfeknpfeLSGGQMRRVAIAGILAMEPKILVL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145334131 466 DEATSALDAVSERLVQSALNRLMKDRTTLV-IAHRLSTVQS-ANQIAVCSDGKIIELGTHSEL 526
Cdd:PRK13649 170 DEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSGKPKDI 232
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
303-528 |
7.23e-21 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 91.58 E-value: 7.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPlrpDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRmfDKSEWAKV---V 379
Cdd:COG0410 6 VENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDIT--GLPPHRIArlgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 380 SIVNQEPVLF-SLSVAENI---AYGLPNEHVSKDDIikaakaanahDFIISL-PQgydtlVGER----GGLLSGGQRQRV 450
Cdd:COG0410 81 GYVPEGRRIFpSLTVEENLllgAYARRDRAEVRADL----------ERVYELfPR-----LKERrrqrAGTLSGGEQQML 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 451 AIARSLLKNAPILILDEATSALdavSERLVQ---SALNRLMKDRTTLVI----AHRLSTVqsANQIAVCSDGKIIELGTH 523
Cdd:COG0410 146 AIGRALMSRPKLLLLDEPSLGL---APLIVEeifEIIRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEGTA 220
|
....*
gi 145334131 524 SELVA 528
Cdd:COG0410 221 AELLA 225
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
303-528 |
9.83e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 92.46 E-value: 9.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPLRPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEdvRMFDKSEW--AKVVS 380
Cdd:PRK13642 7 VENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE--LLTAENVWnlRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 381 IVNQEP--VLFSLSVAENIAYGLPNEHVSKDDIIK----AAKAANAHDFIISLPqgydtlvgergGLLSGGQRQRVAIAR 454
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENQGIPREEMIKrvdeALLAVNMLDFKTREP-----------ARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145334131 455 SLLKNAPILILDEATSALDAVSERLVQSALNRLmKDR---TTLVIAHRLSTVQSANQIAVCSDGKIIELGTHSELVA 528
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEI-KEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
300-536 |
1.01e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 92.39 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 300 DVCLDDVHFAYPLR-P-DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVgGEDVRMFDKSE--- 374
Cdd:PRK13634 2 DITFQKVEHRYQYKtPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKNkkl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 375 --WAKVVSIVNQ--EPVLFSLSVAENIAYGLPNEHVSKDDIIKAAkaanahDFIISLpQGYDTLVGERGGL-LSGGQRQR 449
Cdd:PRK13634 81 kpLRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEEDAKQKA------REMIEL-VGLPEELLARSPFeLSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 450 VAIARSLLKNAPILILDEATSALDAVSERLVQSALNRLMKDR--TTLVIAHRLSTV-QSANQIAVCSDGKIIELGTHSEL 526
Cdd:PRK13634 154 VAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSMEDAaRYADQIVVMHKGTVFLQGTPREI 233
|
250
....*....|
gi 145334131 527 VAQKGSYASL 536
Cdd:PRK13634 234 FADPDELEAI 243
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
12-232 |
1.04e-20 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 92.37 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 12 LRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDLGALNSIVNDNISrdrGF-RAFTEVFGTICILFTLSPQLAPV----LG 86
Cdd:cd18784 71 IRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLN---IFlRSLVKAIGVIVFMFKLSWQLSLVtligLP 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 87 LLMLAVSVLVAVYKRSTVPVYKShgLAQAtmSDCVSETFSAIRTVRSFSGEKRQMSIFGSQI-LAYKL---SGLKLGTFK 162
Cdd:cd18784 148 LIAIVSKVYGDYYKKLSKAVQDS--LAKA--NEVAEETISSIRTVRSFANEDGEANRYSEKLkDTYKLkikEALAYGGYV 223
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 163 SINEsITRVAVYISLLAlycLGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDLRGTFAAIDRI 232
Cdd:cd18784 224 WSNE-LTELALTVSTLY---YGGHLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
293-521 |
1.07e-20 |
|
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: 90.79 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 293 RTLTWaGDVCLDDVHFayplRPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEP---TQGRITVGGEDVrm 369
Cdd:cd03234 2 RVLPW-WDVGLKAKNW----NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 370 fDKSEWAKVVSIVNQEPVLFS-LSVAENIAYGLPNE-HVSKDDIIKAAKaanahDFIISLPQGYDTLVG-ERGGLLSGGQ 446
Cdd:cd03234 75 -KPDQFQKCVAYVRQDDILLPgLTVRETLTYTAILRlPRKSSDAIRKKR-----VEDVLLRDLALTRIGgNLVKGISGGE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145334131 447 RQRVAIARSLLKNAPILILDEATSALDAVSERLVQSALNRLMK-DRTTLVIAH--RLSTVQSANQIAVCSDGKIIELG 521
Cdd:cd03234 149 RRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARrNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
303-496 |
1.07e-20 |
|
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: 90.96 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPLRP-DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKV--- 378
Cdd:COG4181 11 LRGLTKTVGTGAgELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARLrar 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 379 -VSIVNQ-EPVLFSLSVAENIAygLPNEHVSKDDIIKaakaanahdfiislpQGYDTLvgERGGL----------LSGGQ 446
Cdd:COG4181 91 hVGFVFQsFQLLPTLTALENVM--LPLELAGRRDARA---------------RARALL--ERVGLghrldhypaqLSGGE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 145334131 447 RQRVAIARSLLKNAPILILDEATSALDAVSERLVQSALNRLMKDR-TTLVI 496
Cdd:COG4181 152 QQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgTTLVL 202
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
315-526 |
1.43e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 91.26 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 315 DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYE------PTQGRITVGGEDVRMFDKSEWAKVVSIVNQEPVL 388
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 389 FS-LSVAENIAYGLpNEHVSKDDIIKAAKAANAHDFIISLPQGYDTLvGERGGLLSGGQRQRVAIARSLLKNAPILILDE 467
Cdd:PRK14246 102 FPhLSIYDNIAYPL-KSHGIKEKREIKKIVEECLRKVGLWKEVYDRL-NSPASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 468 ATSALDAVSERLVQSALNRLMKDRTTLVIAHRLSTV-QSANQIAVCSDGKIIELGTHSEL 526
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
314-518 |
1.90e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 94.61 E-value: 1.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 314 PDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYePT---QGRITVGGEDVRM--FDKSEwAKVVSIVNQEPVL 388
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQAsnIRDTE-RAGIAIIHQELAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 389 FS-LSVAENIAYGlpNE----HVSKDDIIKAAKAANAHDfiISLPQGYDTLVGErgglLSGGQRQRVAIARSLLKNAPIL 463
Cdd:PRK13549 94 VKeLSVLENIFLG--NEitpgGIMDYDAMYLRAQKLLAQ--LKLDINPATPVGN----LGLGQQQLVEIAKALNKQARLL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 145334131 464 ILDEATSALDAvSERLVQSALNRLMKDR--TTLVIAHRLSTVQS-ANQIAVCSDGKII 518
Cdd:PRK13549 166 ILDEPTASLTE-SETAVLLDIIRDLKAHgiACIYISHKLNEVKAiSDTICVIRDGRHI 222
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
307-518 |
3.13e-20 |
|
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: 89.70 E-value: 3.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 307 HFAYPLRPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEdVRMFDKSEWAKVVSIV--NQ 384
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VPWKRRKKFLRRIGVVfgQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 385 EPVLFSLSVAENIA-----YGLPNEHVSKDDIIKAAKAANAHDFIISLPQgydtlvgergglLSGGQRQRVAIARSLLKN 459
Cdd:cd03267 104 TQLWWDLPVIDSFYllaaiYDLPPARFKKRLDELSELLDLEELLDTPVRQ------------LSLGQRMRAEIAAALLHE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145334131 460 APILILDEATSALDAVSERLVQSALNRLMKDRTTLVI--AHRLSTVQS-ANQIAVCSDGKII 518
Cdd:cd03267 172 PEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLltSHYMKDIEAlARRVLVIDKGRLL 233
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
303-527 |
3.34e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 90.14 E-value: 3.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPlrpDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVSIV 382
Cdd:COG4604 4 IKNVSKRYG---GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 383 NQEPVLFS-LSVAENIAYG-LP----------NEHVSK-------DDiikaakaaNAHDFIislpqgyDTlvgergglLS 443
Cdd:COG4604 81 RQENHINSrLTVRELVAFGrFPyskgrltaedREIIDEaiayldlED--------LADRYL-------DE--------LS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 444 GGQRQRVAIARSLLKNAPILILDEATSALD---AVSerlVQSALNRLMKD--RTTLVIAHRLSTVQS-ANQIAVCSDGKI 517
Cdd:COG4604 138 GGQRQRAFIAMVLAQDTDYVLLDEPLNNLDmkhSVQ---MMKLLRRLADElgKTVVIVLHDINFASCyADHIVAMKDGRV 214
|
250
....*....|
gi 145334131 518 IELGTHSELV 527
Cdd:COG4604 215 VAQGTPEEII 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
317-526 |
4.45e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 90.10 E-value: 4.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 317 KVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYE-----PTQGRITVGGEDV--RMFDKSEWAKVVSIVNQEPVLF 389
Cdd:PRK14258 21 KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIyeRRVNLNRLRRQVSMVHPKPNLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 390 SLSVAENIAYGLP----NEHVSKDDIIKAAkaanahdfiISLPQGYDTLVGE--RGGL-LSGGQRQRVAIARSLLKNAPI 462
Cdd:PRK14258 101 PMSVYDNVAYGVKivgwRPKLEIDDIVESA---------LKDADLWDEIKHKihKSALdLSGGQQQRLCIARALAVKPKV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 463 LILDEATSALDAVS----ERLVQSAlnRLMKDRTTLVIAHRLstvqsaNQIAVCSD------------GKIIELGTHSEL 526
Cdd:PRK14258 172 LLMDEPCFGLDPIAsmkvESLIQSL--RLRSELTMVIVSHNL------HQVSRLSDftaffkgnenriGQLVEFGLTKKI 243
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
273-521 |
7.25e-20 |
|
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: 88.36 E-value: 7.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 273 VNIRHLDKYYMSNLKSTNNLRTLTWAGDVCLddvhfayplRPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARF 352
Cdd:cd03220 1 IELENVSKSYPTYKGGSSSLKKLGILGRKGE---------VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 353 YEPTQGRITVGGedvrmfdksewaKVVSIVNQ----EPvlfSLSVAENI-----AYGLpnehvSKDDIIKAAkaanahDF 423
Cdd:cd03220 72 YPPDSGTVTVRG------------RVSSLLGLgggfNP---ELTGRENIylngrLLGL-----SRKEIDEKI------DE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 424 IIS---LPQGYDTLVGErgglLSGGQRQRVAIARSLLKNAPILILDEATSALDAVSERLVQSALNRLMKDRTTLVIA-HR 499
Cdd:cd03220 126 IIEfseLGDFIDLPVKT----YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVsHD 201
|
250 260
....*....|....*....|...
gi 145334131 500 LSTVQS-ANQIAVCSDGKIIELG 521
Cdd:cd03220 202 PSSIKRlCDRALVLEKGKIRFDG 224
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
313-527 |
7.54e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 93.19 E-value: 7.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 313 RPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLArFYEPT----QGRITVGGEDVrmfDKSEWAKVVSIVNQEPVL 388
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMPI---DAKEMRAISAYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 389 F-SLSVAENIAYglpNEHVSKDDIIKAAKAANAHDFII---SLPQGYDTLVGERGGL--LSGGQRQRVAIARSLLKNAPI 462
Cdd:TIGR00955 111 IpTLTVREHLMF---QAHLRMPRRVTKKEKRERVDEVLqalGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145334131 463 LILDEATSALDAVSERLVQSALNRL-MKDRTTLVIAHRLST--VQSANQIAVCSDGKIIELGTHSELV 527
Cdd:TIGR00955 188 LFCDEPTSGLDSFMAYSVVQVLKGLaQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAV 255
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
318-537 |
8.64e-20 |
|
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: 89.53 E-value: 8.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 318 VLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEdvrmfdksewakvVSIVNQEPVLFSLSVAENI 397
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 398 AYGlpnehVSKDDIIKAAKAAN--AHDFIISLPQGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEATSALDAV 475
Cdd:cd03291 119 IFG-----VSYDEYRYKSVVKAcqLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145334131 476 SERLV-QSALNRLMKDRTTLVIAHRLSTVQSANQIAVCSDGKIIELGTHSELVAQKGSYASLV 537
Cdd:cd03291 194 TEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKL 256
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
315-535 |
1.29e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 89.91 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 315 DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVggEDVRMFDKSEWA------------------ 376
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV--GDIYIGDKKNNHelitnpyskkiknfkelr 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 377 KVVSIVNQEP--VLFSLSVAENIAYGLPNEHVSKDDIIKAAKAanahdFIISLPQGYDTLvgERGGL-LSGGQRQRVAIA 453
Cdd:PRK13631 116 RRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSEAKKLAKF-----YLNKMGLDDSYL--ERSPFgLSGGQKRRVAIA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 454 RSLLKNAPILILDEATSALDAVSER-LVQSALNRLMKDRTTLVIAHRLSTV-QSANQIAVCSDGKIIELGTHSELVAQKG 531
Cdd:PRK13631 189 GILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEIFTDQH 268
|
....
gi 145334131 532 SYAS 535
Cdd:PRK13631 269 IINS 272
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
315-540 |
1.35e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 91.06 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 315 DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVSIVNQEPVL-FSLSV 393
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 394 AENIAYGlPNEHVSKDDIIKAAKAANAHDFI--ISLPQGYDTLVGErgglLSGGQRQRVAIARSLLKNAPILILDEATSA 471
Cdd:PRK09536 95 RQVVEMG-RTPHRSRFDTWTETDRAAVERAMerTGVAQFADRPVTS----LSGGERQRVLLARALAQATPVLLLDEPTAS 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145334131 472 LDAVSERLVQSALNRLMKDRTTLVIA-HRLS-TVQSANQIAVCSDGKIIELG------THSELVAQKGSYAsLVGTQ 540
Cdd:PRK09536 170 LDINHQVRTLELVRRLVDDGKTAVAAiHDLDlAARYCDELVLLADGRVRAAGppadvlTADTLRAAFDART-AVGTD 245
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
1-228 |
1.59e-19 |
|
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: 89.07 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 1 MTAIW----ENVMAILRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDLGALNSIVNDNISRdrGFRAFTEVFGTICILFT 76
Cdd:cd18577 67 QTACWtitgERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGL--LIQSLSTFIAGFIIAFI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 77 LSPQLA----PVLGLLMLAVSVLVAVYKRSTVPVYKSHGLAqatmSDCVSETFSAIRTVRSFSGEKRQMSIFGSQILAYK 152
Cdd:cd18577 145 YSWKLTlvllATLPLIAIVGGIMGKLLSKYTKKEQEAYAKA----GSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKAR 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 153 LSGLKLGTFKSINESITRVAVYISllalYCLG---GSK-VKTGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDL-RGTFA 227
Cdd:cd18577 221 KAGIKKGLVSGLGLGLLFFIIFAM----YALAfwyGSRlVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFaKARAA 296
|
.
gi 145334131 228 A 228
Cdd:cd18577 297 A 297
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
303-500 |
2.21e-19 |
|
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: 87.83 E-value: 2.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAyplRPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQG-RITV-----GGEDVRmfdksEWA 376
Cdd:COG1119 6 LRNVTVR---RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLfgerrGGEDVW-----ELR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 377 KVVSIVN---QEPVLFSLSVAENIAYGL-----PNEHVSKDDIIKAakaanaHDFIISLpqGYDTLVGERGGLLSGGQRQ 448
Cdd:COG1119 78 KRIGLVSpalQLRFPRDETVLDVVLSGFfdsigLYREPTDEQRERA------RELLELL--GLAHLADRPFGTLSQGEQR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 145334131 449 RVAIARSLLKNAPILILDEATSALDAVSERLVQSALNRLMKDR-TTLV-IAHRL 500
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVlVTHHV 203
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
303-518 |
2.52e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 91.71 E-value: 2.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPL-RPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVS- 380
Cdd:PRK10535 7 LKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRRe 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 381 ----IVNQEPVLFSLSVAENIAygLPNEHVSKDdiiKAAKAANAHDFIISLpqGYDTLVGERGGLLSGGQRQRVAIARSL 456
Cdd:PRK10535 87 hfgfIFQRYHLLSHLTAAQNVE--VPAVYAGLE---RKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145334131 457 LKNAPILILDEATSALDAVSERLVQSALNRLmKDR--TTLVIAHRLSTVQSANQIAVCSDGKII 518
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQL-RDRghTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
298-499 |
2.99e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 91.02 E-value: 2.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 298 AGDVCLDDVHFAyplRPDVKVL-DGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITV-GGEDVrMFdksew 375
Cdd:COG4178 360 DGALALEDLTLR---TPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV-LF----- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 376 akvvsiVNQEPVLFSLSVAENIAYGLPNEHVSKDDIIKAAKAANAHDFIISLPQGYDtlvgeRGGLLSGGQRQRVAIARS 455
Cdd:COG4178 431 ------LPQRPYLPLGTLREALLYPATAEAFSDAELREALEAVGLGHLAERLDEEAD-----WDQVLSLGEQQRLAFARL 499
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 145334131 456 LLKNAPILILDEATSALDAVSERLVQSALNRLMKDRTTLVIAHR 499
Cdd:COG4178 500 LLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
314-515 |
3.11e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 90.61 E-value: 3.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 314 PDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKV-VSIVNQE-PVLFSL 391
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQElSVIDEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 392 SVAENIAYG-LPNEH---VSKDDIIKAAKAANAHDFIISLPQGYDTLVGErgglLSGGQRQRVAIARSLLKNAPILILDE 467
Cdd:PRK09700 96 TVLENLYIGrHLTKKvcgVNIIDWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 145334131 468 ATSAL-DAVSERLVqSALNRLMKDRTTLV-IAHRLSTV-QSANQIAVCSDG 515
Cdd:PRK09700 172 PTSSLtNKEVDYLF-LIMNQLRKEGTAIVyISHKLAEIrRICDRYTVMKDG 221
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
300-526 |
3.73e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 89.32 E-value: 3.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 300 DVCLDDVHFAYPlrpDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEdvRMFDKSEWAKVV 379
Cdd:PRK11000 3 SVTLRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK--RMNDVPPAERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 380 SIVNQEPVLFS-LSVAENIAYGLPNEHVSKDDIIKAAKAANAhdfIISLpqgyDTLVGERGGLLSGGQRQRVAIARSLLK 458
Cdd:PRK11000 78 GMVFQSYALYPhLSVAENMSFGLKLAGAKKEEINQRVNQVAE---VLQL----AHLLDRKPKALSGGQRQRVAIGRTLVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145334131 459 NAPILILDEATSALDA---VSERLVQSALNRLMKdRTTLVIAH-RLSTVQSANQIAVCSDGKIIELGTHSEL 526
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAalrVQMRIEISRLHKRLG-RTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
316-529 |
3.85e-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: 90.63 E-value: 3.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 316 VKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITV--GGEDVRMFD-----KSEWAKVVSIVNQEPVL 388
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvGDEWVDMTKpgpdgRGRAKRYIGILHQEYDL 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 389 FS-LSVAEN----IAYGLPNEHVSKDDIIKAAKAANAHDFIIS-LPQGYDTlvgergglLSGGQRQRVAIARSLLKNAPI 462
Cdd:TIGR03269 377 YPhRTVLDNlteaIGLELPDELARMKAVITLKMVGFDEEKAEEiLDKYPDE--------LSEGERHRVALAQVLIKEPRI 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 463 LILDEATSALDAVSERLV-QSALN-RLMKDRTTLVIAHRLSTVQS-ANQIAVCSDGKIIELGTHSELVAQ 529
Cdd:TIGR03269 449 VILDEPTGTMDPITKVDVtHSILKaREEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
6-202 |
4.25e-19 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 87.99 E-value: 4.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 6 ENVMAILRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDLGALNSIVNDNISrdRGFRAFTEVFGTICILFTLSPQLApvl 85
Cdd:cd18574 71 ERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVS--QGLRSVTQTVGCVVSLYLISPKLT--- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 86 GLLMLAVSVLVAV-----------YKRSTVPVYKSHGLAqatmsdcvSETFSAIRTVRSFSGEKRQMSIFGSQILAYKLS 154
Cdd:cd18574 146 LLLLVIVPVVVLVgtlygsflrklSRRAQAQVAKATGVA--------DEALGNIRTVRAFAMEDRELELYEEEVEKAAKL 217
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 145334131 155 GLKLGTFKSINESITRVAVYISLLALYCLGGSKVKTGELAVGTVVSFI 202
Cdd:cd18574 218 NEKLGLGIGIFQGLSNLALNGIVLGVLYYGGSLVSRGELTAGDLMSFL 265
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
1-232 |
5.86e-19 |
|
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: 87.46 E-value: 5.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 1 MTAIWENVMAILRAQIFRRvlIQKA--EFFDKYKVGELTGLLTSDLGALNSIVNDNISRdrGFRAFTEVFGTICILFTLS 78
Cdd:cd18547 69 MARVSQRTVYDLRKDLFEK--LQRLplSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQ--LISSILTIVGTLIMMLYIS 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 79 PQLApVLGLLMLAVSVLVAVY--KRStvpvYKSHGLAQATMSDC---VSETFSAIRTVRSFSGEKRQMSIFGSQILAYKL 153
Cdd:cd18547 145 PLLT-LIVLVTVPLSLLVTKFiaKRS----QKYFRKQQKALGELngyIEEMISGQKVVKAFNREEEAIEEFDEINEELYK 219
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145334131 154 SGLKLGTFKSINESITRVAVYISLLALYCLGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDLRGTFAAIDRI 232
Cdd:cd18547 220 ASFKAQFYSGLLMPIMNFINNLGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
301-526 |
6.56e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 90.81 E-value: 6.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 301 VCLDDVHFAYPLRPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQ-LLARFYEPTQGRITVGGEdvrmfdksewakvV 379
Cdd:PLN03232 615 ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGS-------------V 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 380 SIVNQEPVLFSLSVAENIAYGlpNEHVSKDDIIKAAKAANAHDfiISLPQGYD-TLVGERGGLLSGGQRQRVAIARSLLK 458
Cdd:PLN03232 682 AYVPQVSWIFNATVRENILFG--SDFESERYWRAIDVTALQHD--LDLLPGRDlTEIGERGVNISGGQKQRVSMARAVYS 757
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145334131 459 NAPILILDEATSALDA-VSERLVQSALNRLMKDRTTLVIAHRLSTVQSANQIAVCSDGKIIELGTHSEL 526
Cdd:PLN03232 758 NSDIYIFDDPLSALDAhVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL 826
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
305-528 |
8.95e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 90.57 E-value: 8.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 305 DVHFAYPLRPDVKVLDGLSLTLNSGTVTALVGSSGAGK-STIVQLLARFYEPTQGRITVGGEdvrmfdksewakvVSIVN 383
Cdd:PLN03130 619 NGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKtSLISAMLGELPPRSDASVVIRGT-------------VAYVP 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 384 QEPVLFSLSVAENIAYGLPNEHVSKDdiIKAAKAANAHDFIIsLPQGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPIL 463
Cdd:PLN03130 686 QVSWIFNATVRDNILFGSPFDPERYE--RAIDVTALQHDLDL-LPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVY 762
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145334131 464 ILDEATSALDA-VSERLVQSALNRLMKDRTTLVIAHRLSTVQSANQIAVCSDGKIIELGTHSELVA 528
Cdd:PLN03130 763 IFDDPLSALDAhVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSN 828
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
315-521 |
9.26e-19 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 84.50 E-value: 9.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 315 DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARF--YEPTQGRITVGGEDVRMFDKSEWAKV-VSIVNQEPVLFSl 391
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLgIFLAFQYPPEIP- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 392 svaeniayGLPNEhvskddiikaakaanahDFIISLPQGydtlvgergglLSGGQRQRVAIARSLLKNAPILILDEATSA 471
Cdd:cd03217 91 --------GVKNA-----------------DFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 145334131 472 LDAVSERLVQSALNRLM-KDRTTLVIAH--RLSTVQSANQIAVCSDGKIIELG 521
Cdd:cd03217 135 LDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
314-519 |
9.32e-19 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 89.08 E-value: 9.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 314 PDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYePT---QGRITVGGEDVRMFD--KSEWAKVVsIVNQEPVL 388
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEVCRFKDirDSEALGIV-IIHQELAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 389 FS-LSVAENIAYGlpNEHVSKDdiikaakaanahdfIISLPQGY----------------DTLVGERGgllsGGQRQRVA 451
Cdd:NF040905 90 IPyLSIAENIFLG--NERAKRG--------------VIDWNETNrrarellakvgldespDTLVTDIG----VGKQQLVE 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145334131 452 IARSLLKNAPILILDEATSAL-DAVSERLvqsaLNRLMKDR----TTLVIAHRLSTV-QSANQIAVCSDGKIIE 519
Cdd:NF040905 150 IAKALSKDVKLLILDEPTAALnEEDSAAL----LDLLLELKaqgiTSIIISHKLNEIrRVADSITVLRDGRTIE 219
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
302-526 |
1.09e-18 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 85.27 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 302 CLDDVHFAYPlrpDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVrMFDKSEW--AKVV 379
Cdd:TIGR03410 2 EVSNLNVYYG---QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDI-TKLPPHEraRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 380 SIVNQEPVLFS-LSVAENIAYGLPNehvskddiiKAAKAANAHDFIISLPQGYDTLVGERGGLLSGGQRQRVAIARSLLK 458
Cdd:TIGR03410 78 AYVPQGREIFPrLTVEENLLTGLAA---------LPRRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVT 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145334131 459 NAPILILDEATSALDAVSERLVQSALNRL--MKDRTTLVIAHRLS-TVQSANQIAVCSDGKIIELGTHSEL 526
Cdd:TIGR03410 149 RPKLLLLDEPTEGIQPSIIKDIGRVIRRLraEGGMAILLVEQYLDfARELADRYYVMERGRVVASGAGDEL 219
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
6-232 |
1.10e-18 |
|
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: 86.72 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 6 ENVMAILRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDLGALNSIVNDNISRdrGFRAFTEVFGTICILFTLSPQLAPVL 85
Cdd:cd18542 68 QKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVE--LVRAVLLFIGALIIMFSINWKLTLIS 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 86 GLLMLAVSVLVAVYKRSTVPVYKSHGLAQATMSDCVSETFSAIRTVRSFSGEKRQMSIFGSQILAYKLSGLKLGTFKSIN 165
Cdd:cd18542 146 LAIIPFIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKY 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145334131 166 ESITRVAVYISLLALYCLGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDLRGTFAAIDRI 232
Cdd:cd18542 226 WPLMDFLSGLQIVLVLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
313-526 |
1.15e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 84.54 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 313 RPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRmfDKSEWAKVVSIVNQEPVLFSLS 392
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID--DPDVAEACHYLGHRNAMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 393 VAENIA-----YGLPNEHVSkddiiKAAKAANAHDfIISLPQGYdtlvgergglLSGGQRQRVAIARSLLKNAPILILDE 467
Cdd:PRK13539 90 VAENLEfwaafLGGEELDIA-----AALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDE 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 145334131 468 ATSALDAVSERLVQSalnrlmkdrttlVIAHRLSTvqsanqiavcsdGKIIELGTHSEL 526
Cdd:PRK13539 154 PTAALDAAAVALFAE------------LIRAHLAQ------------GGIVIAATHIPL 188
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
317-530 |
1.59e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 85.99 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 317 KVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWA----KVVSIVNQ--EPVLFS 390
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIrpvrKRIGMVFQfpESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 391 LSVAENIAYGLPNEHVSKDDiikaaKAANAHDFIISLpqGYDTLVGERGGL-LSGGQRQRVAIARSLLKNAPILILDEAT 469
Cdd:PRK13646 101 DTVEREIIFGPKNFKMNLDE-----VKNYAHRLLMDL--GFSRDVMSQSPFqMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145334131 470 SALDAVSERLVQSALNRLMKD--RTTLVIAHRLSTV-QSANQIAVCSDGKIIELGTHSELVAQK 530
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQTDenKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKDK 237
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
303-527 |
1.86e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 85.22 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPLRpdvKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVSIV 382
Cdd:PRK10575 14 LRNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 383 NQE-PVLFSLSVAENIAYGLPNEH-----VSKDDIIKAakaanahDFIISLpQGYDTLVGERGGLLSGGQRQRVAIARSL 456
Cdd:PRK10575 91 PQQlPAAEGMTVRELVAIGRYPWHgalgrFGAADREKV-------EEAISL-VGLKPLAHRLVDSLSGGERQRAWIAMLV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145334131 457 LKNAPILILDEATSALDAVSERLVQSALNRLMKDRTTLVIA--HRLS-TVQSANQIAVCSDGKIIELGTHSELV 527
Cdd:PRK10575 163 AQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAvlHDINmAARYCDYLVALRGGEMIAQGTPAELM 236
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
317-532 |
3.05e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 84.64 E-value: 3.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 317 KVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRM----------FDKSEWAKV---VSIVN 383
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLvrdkdgqlkvADKNQLRLLrtrLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 384 QEPVLFS-LSVAENI------AYGLpnehvSKDDIIKAAKAANAHDFIISLPQgydtlvGERGGLLSGGQRQRVAIARSL 456
Cdd:PRK10619 99 QHFNLWShMTVLENVmeapiqVLGL-----SKQEARERAVKYLAKVGIDERAQ------GKYPVHLSGGQQQRVSIARAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 457 LKNAPILILDEATSALDAvseRLVQSALnRLMKD-----RTTLVIAHRLSTVQS-ANQIAVCSDGKIIELGTHSELVAQK 530
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDP---ELVGEVL-RIMQQlaeegKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGNP 243
|
..
gi 145334131 531 GS 532
Cdd:PRK10619 244 QS 245
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
273-522 |
3.36e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 83.98 E-value: 3.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 273 VNIRHLDKYYMSNLKSTNNLRTLTWAGDvclddvhfaYPLRPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARF 352
Cdd:COG1134 5 IEVENVSKSYRLYHEPSRSLKELLLRRR---------RTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 353 YEPTQGRITVGGedvrmfdksewaKVVSIV------NQEpvlfsLSVAENI-----AYGLPNEHVSKddiikaakaanAH 421
Cdd:COG1134 76 LEPTSGRVEVNG------------RVSALLelgagfHPE-----LTGRENIylngrLLGLSRKEIDE-----------KF 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 422 DFIIS---LPQGYDTLVgergGLLSGGQRQRVAIARSLLKNAPILILDEATSALDAVSERLVQSALNRLMKDRTTLVIA- 497
Cdd:COG1134 128 DEIVEfaeLGDFIDQPV----KTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVs 203
|
250 260
....*....|....*....|....*.
gi 145334131 498 HRLSTVQS-ANQIAVCSDGKIIELGT 522
Cdd:COG1134 204 HSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
315-527 |
4.32e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 83.60 E-value: 4.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 315 DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVR--MFDKSEWAKVVSIVNQEPVLF-SL 391
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEAGMVFQQFYLFpHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 392 SVAENIAYGlPnEHV---SKDDIIKaakaanahdfiislpQGYDTL--VG--ERGG----LLSGGQRQRVAIARSLLKNA 460
Cdd:PRK09493 93 TALENVMFG-P-LRVrgaSKEEAEK---------------QARELLakVGlaERAHhypsELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145334131 461 PILILDEATSALDAvseRLVQSALnRLMKD-----RTTLVIAHRLSTVQS-ANQIAVCSDGKIIELGTHSELV 527
Cdd:PRK09493 156 KLMLFDEPTSALDP---ELRHEVL-KVMQDlaeegMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
310-538 |
4.99e-18 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 88.30 E-value: 4.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 310 YPLRPDVkVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRItvggedvrmfdkseWA-KVVSIVNQEPVL 388
Cdd:PTZ00243 668 FELEPKV-LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV--------------WAeRSIAYVPQQAWI 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 389 FSLSVAENIAYGLPNEHVSKDDIIKAAKAANAhdfIISLPQGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEA 468
Cdd:PTZ00243 733 MNATVRGNILFFDEEDAARLADAVRVSQLEAD---LAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDP 809
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145334131 469 TSALDA-VSERLVQSALNRLMKDRTTLVIAHRLSTVQSANQIAVCSDGKiIELGTHSELVAQKGSYASLVG 538
Cdd:PTZ00243 810 LSALDAhVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGR-VEFSGSSADFMRTSLYATLAA 879
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
318-533 |
5.40e-18 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 84.14 E-value: 5.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 318 VLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEpTQGRITVGGEDVRMFDKSEWAKVVSIVNQEPVLFSLSVAENI 397
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 398 AyglPNEHVSKDDIIKAAKAANAHDFIISLPQGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEATSALDAVSE 477
Cdd:cd03289 98 D---PYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITY 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 145334131 478 RLVQSALNRLMKDRTTLVIAHRLSTVQSANQIAVCSDGKIIELGTHSELVAQKGSY 533
Cdd:cd03289 175 QVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
6-232 |
5.62e-18 |
|
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: 84.36 E-value: 5.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 6 ENVMAILRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDLGALNSIVNDNISrdRGFRAFTEVFGTICILFTLSPQLAPVL 85
Cdd:cd18544 70 QRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLV--TLIGDLLLLIGILIAMFLLNWRLALIS 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 86 GLLMLAVSVLVAVYKRSTVPVYKSHGLAQATMSDCVSETFSAIRTVRSFSGEKRQMSIFGSQILAYKLSGLKL----GTF 161
Cdd:cd18544 148 LLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSiklfALF 227
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145334131 162 KSINESITRVAvyISLLALYclGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDLRGTFAAIDRI 232
Cdd:cd18544 228 RPLVELLSSLA--LALVLWY--GGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
316-529 |
5.70e-18 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 87.05 E-value: 5.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 316 VKVLDGLSLTLNSGTVTALVGSSGAGKS----TIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKV----VSIVNQEPv 387
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRIrgnrIAMIFQEP- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 388 LFSL----SVAENIAyglpnEhvskddiikaakaanahdfIISLPQGY----------DTLvgERGGL------------ 441
Cdd:COG4172 102 MTSLnplhTIGKQIA-----E-------------------VLRLHRGLsgaaararalELL--ERVGIpdperrldayph 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 442 -LSGGQRQRVAIARSLLkNAP-ILILDEATSALDAVserlVQSALNRLMKD--RTT----LVIAHRLSTVQS-ANQIAVC 512
Cdd:COG4172 156 qLSGGQRQRVMIAMALA-NEPdLLIADEPTTALDVT----VQAQILDLLKDlqRELgmalLLITHDLGVVRRfADRVAVM 230
|
250
....*....|....*..
gi 145334131 513 SDGKIIELGTHSELVAQ 529
Cdd:COG4172 231 RQGEIVEQGPTAELFAA 247
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
303-522 |
8.77e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 83.50 E-value: 8.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPlrPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDK-SEWAKVVSI 381
Cdd:PRK13644 4 LENVSYSYP--DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 382 VNQEP--VLFSLSVAENIAYGLPNEHVSKddiikaakaanahdfiISLPQGYDTLVGERG---------GLLSGGQRQRV 450
Cdd:PRK13644 82 VFQNPetQFVGRTVEEDLAFGPENLCLPP----------------IEIRKRVDRALAEIGlekyrhrspKTLSGGQGQCV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145334131 451 AIARSLLKNAPILILDEATSALDAVSERLVQSALNRLM-KDRTTLVIAHRLSTVQSANQIAVCSDGKIIELGT 522
Cdd:PRK13644 146 ALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHeKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
319-474 |
9.52e-18 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 81.76 E-value: 9.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 319 LDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEP---TQGRITVGGEDVRmfDKSEWAKVVSIVNQEPVLFS-LSVA 394
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLT--ALPAEQRRIGILFQDDLLFPhLSVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 395 ENIAYGLPNeHVSKDDIIKAAKAANAHdfiISLPQGYDTLVGErgglLSGGQRQRVAIARSLLKNAPILILDEATSALDA 474
Cdd:COG4136 95 ENLAFALPP-TIGRAQRRARVEQALEE---AGLAGFADRDPAT----LSGGQRARVALLRALLAEPRALLLDEPFSKLDA 166
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
303-474 |
1.05e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.89 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPLRPdvkVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGeDVRmfdksewakvVSIV 382
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR----------IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 383 NQEPVLFS-LSVAENIAYGLP------------NEHVSKDDIIKAAKAANAHDF--------------IIS---LPQG-Y 431
Cdd:COG0488 67 PQEPPLDDdLTVLDTVLDGDAelraleaeleelEAKLAEPDEDLERLAELQEEFealggweaearaeeILSglgFPEEdL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 145334131 432 DTLVGErgglLSGGQRQRVAIARSLLKNAPILILDEATSALDA 474
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDL 185
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
318-517 |
1.08e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 82.80 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 318 VLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGG-------EDVR-MFDKSE---WAKVVsivnqep 386
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTaplaearEDTRlMFQDARllpWKKVI------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 387 vlfslsvaENIAYGLpnehvsKDDIIkaakaanahdfiislPQGYDTL--VG--ERGG----LLSGGQRQRVAIARSLLK 458
Cdd:PRK11247 100 --------DNVGLGL------KGQWR---------------DAALQALaaVGlaDRANewpaALSGGQKQRVALARALIH 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145334131 459 NAPILILDEATSALDAVSERLVQSALNRLMKDR--TTLVIAHRLS-TVQSANQIAVCSDGKI 517
Cdd:PRK11247 151 RPGLLLLDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
306-526 |
1.08e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 84.37 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 306 VHF------AYPLRP--DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAK 377
Cdd:PRK15079 16 VHFdikdgkQWFWQPpkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 378 V---VSIVNQEPvLFSL----SVAENIAYGLPNEH--VSKDDIIKAAKAANAHdfIISLPQgydtLVGERGGLLSGGQRQ 448
Cdd:PRK15079 96 VrsdIQMIFQDP-LASLnprmTIGEIIAEPLRTYHpkLSRQEVKDRVKAMMLK--VGLLPN----LINRYPHEFSGGQCQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 449 RVAIARSLLKNAPILILDEATSALDAVSERLVQSALNRLMKD-RTTLV-IAHRLSTVQS-ANQIAVCSDGKIIELGTHSE 525
Cdd:PRK15079 169 RIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIfIAHDLAVVKHiSDRVLVMYLGHAVELGTYDE 248
|
.
gi 145334131 526 L 526
Cdd:PRK15079 249 V 249
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1-232 |
1.16e-17 |
|
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: 83.71 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 1 MTAIWENVMAILRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDLGALNSIVNDNISRdrGFRAFTEVFGTICILFTLSPQ 80
Cdd:cd18563 67 LARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPD--FLTNILMIIGIGVVLFSLNWK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 81 LAPVLGLLMLAVSVLVAVYKRSTVPVYKSHGLAQATMSDCVSETFSAIRTVRSFSGEKRQMSIFGSQILAYKLSGLKLGT 160
Cdd:cd18563 145 LALLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEK 224
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145334131 161 FKSINESITRVAVYISLLALYCLGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDLRGTFAAIDRI 232
Cdd:cd18563 225 LWATFFPLLTFLTSLGTLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
310-529 |
1.52e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 82.93 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 310 YPLRPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVSIVNQEP--V 387
Cdd:PRK13652 11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 388 LFSLSVAENIAYGLPN----EHVSKDDIIKAAKAANAHDFIISLPQGydtlvgergglLSGGQRQRVAIARSLLKNAPIL 463
Cdd:PRK13652 91 IFSPTVEQDIAFGPINlgldEETVAHRVSSALHMLGLEELRDRVPHH-----------LSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145334131 464 ILDEATSALDAVSERLVQSALNRLMKDRTTLVI--AHRLSTVQS-ANQIAVCSDGKIIELGTHSELVAQ 529
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIfsTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
319-498 |
1.62e-17 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 81.74 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 319 LDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDV------RMfdksewakvvsIVNQEPVLFS-L 391
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQItepgpdRM-----------VVFQNYSLLPwL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 392 SVAENIAYGLP--NEHVSKDDIIKAAKAanaHDFIISLPQGYDtlvgERGGLLSGGQRQRVAIARSLLKNAPILILDEAT 469
Cdd:TIGR01184 70 TVRENIALAVDrvLPDLSKSERRAIVEE---HIALVGLTEAAD----KRPGQLSGGMKQRVAIARALSIRPKVLLLDEPF 142
|
170 180 190
....*....|....*....|....*....|.
gi 145334131 470 SALDAVSERLVQSALNRLMKDR--TTLVIAH 498
Cdd:TIGR01184 143 GALDALTRGNLQEELMQIWEEHrvTVLMVTH 173
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
314-518 |
2.51e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 84.67 E-value: 2.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 314 PDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRmFD--KSEWAKVVSIVNQEPVLF-S 390
Cdd:PRK10762 15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT-FNgpKSSQEAGIGIIHQELNLIpQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 391 LSVAENIAYGlpNEHVSKDDIIKAAKAANAHDFI---ISLPQGYDTLVGErgglLSGGQRQRVAIARSLLKNAPILILDE 467
Cdd:PRK10762 94 LTIAENIFLG--REFVNRFGRIDWKKMYAEADKLlarLNLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 145334131 468 ATSAL-DAVSERLVqSALNRLMKDRTTLV-IAHRLSTV-QSANQIAVCSDGKII 518
Cdd:PRK10762 168 PTDALtDTETESLF-RVIRELKSQGRGIVyISHRLKEIfEICDDVTVFRDGQFI 220
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
294-528 |
2.75e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 82.07 E-value: 2.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 294 TLTWAGDVCLDDVHFAYPLRpdvkvldglsltlnsgTVTALVGSSGAGKSTIVQLLARFYEPTQG-----RITVGGEDVR 368
Cdd:PRK14271 28 TLGFAGKTVLDQVSMGFPAR----------------AVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 369 MF-DKSEWAKVVSIVNQEPVLFSLSVAENIAYGL-PNEHVSKDDIIKAAKAANAHdfiISLPQGYDTLVGERGGLLSGGQ 446
Cdd:PRK14271 92 NYrDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVrAHKLVPRKEFRGVAQARLTE---VGLWDAVKDRLSDSPFRLSGGQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 447 RQRVAIARSLLKNAPILILDEATSALDAVSERLVQSALNRLMKDRTTLVIAHRLS-TVQSANQIAVCSDGKIIELGTHSE 525
Cdd:PRK14271 169 QQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQ 248
|
...
gi 145334131 526 LVA 528
Cdd:PRK14271 249 LFS 251
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
318-527 |
3.46e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.57 E-value: 3.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 318 VLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVSIVNQEPVL-FSLSVAEN 396
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 397 IAYG-LPNEHV----SKDDIIKAAKAANAhdfiislpQGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEATSA 471
Cdd:PRK10253 102 VARGrYPHQPLftrwRKEDEEAVTKAMQA--------TGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145334131 472 LDaVSERL----VQSALNRlMKDRTTLVIAHRLS-TVQSANQIAVCSDGKIIELGTHSELV 527
Cdd:PRK10253 174 LD-ISHQIdlleLLSELNR-EKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
318-517 |
1.08e-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: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 318 VLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEpTQGRITVGGEDVRMFDKSEWAKVVSIVNQEPVLFSLSVAENI 397
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 398 AyglPNEHVSKDDIIKAAKAANAHDFIISLPQGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEATSALDAVSE 477
Cdd:TIGR01271 1313 D---PYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTL 1389
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 145334131 478 RLVQSALNRLMKDRTTLVIAHRLSTVQSANQIAVCSDGKI 517
Cdd:TIGR01271 1390 QIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSV 1429
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
318-521 |
1.12e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 79.89 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 318 VLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQ-----GRITVGGEDVRM--FDKSEWAKVVSIVNQEPVLFS 390
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYSpdVDPIEVRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 391 -LSVAENIAYGLP-NEHV-SKDDIIKAAKAANAHdfiISLPQGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDE 467
Cdd:PRK14267 99 hLTIYDNVAIGVKlNGLVkSKKELDERVEWALKK---AALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 145334131 468 ATSALDAVSERLVQSALNRLMKDRTTLVIAHrlSTVQSA---NQIAVCSDGKIIELG 521
Cdd:PRK14267 176 PTANIDPVGTAKIEELLFELKKEYTIVLVTH--SPAQAArvsDYVAFLYLGKLIEVG 230
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
319-510 |
1.16e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 80.21 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 319 LDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYE--PT---QGRITVGGEDV--RMFDKSEWAKVVSIVNQEPVLFSL 391
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 392 SVAENIAYGlPNEHVSKDDIikaakaanahDFII--SLPQG--YDTL---VGERGGLLSGGQRQRVAIARSLLKNAPILI 464
Cdd:PRK14243 106 SIYDNIAYG-ARINGYKGDM----------DELVerSLRQAalWDEVkdkLKQSGLSLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 145334131 465 LDEATSALDAVSERLVQSALNRLMKDRTTLVIAHRLstvQSANQIA 510
Cdd:PRK14243 175 MDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM---QQAARVS 217
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
315-526 |
1.29e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 80.54 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 315 DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRmfdksewakvVSIVNQ------EPVL 388
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD----------PEDRRRigylpeERGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 389 F-SLSVAENIAY-----GLPnehvSKDDIIKAAKAANAHDfiisLPQGYDTLVGErgglLSGGQRQRVAIARSLLKNAPI 462
Cdd:COG4152 83 YpKMKVGEQLVYlarlkGLS----KAEAKRRADEWLERLG----LGDRANKKVEE----LSKGNQQKVQLIAALLHDPEL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145334131 463 LILDEATSALDAVSERLVQSALNRLMKDRTTlVI--AHRLSTVQS-ANQIAVCSDGKIIELGTHSEL 526
Cdd:COG4152 151 LILDEPFSGLDPVNVELLKDVIRELAAKGTT-VIfsSHQMELVEElCDRIVIINKGRKVLSGSVDEI 216
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
303-529 |
1.29e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 80.55 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAY-PLRP-DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGgeDVRMFDKSEWAKV-- 378
Cdd:PRK13643 4 FEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG--DIVVSSTSKQKEIkp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 379 ----VSIVNQEP--VLFSLSVAENIAYGLPNEHVSKDDIIKAAKAANAhdfIISLPQGYdtlvGERGGL-LSGGQRQRVA 451
Cdd:PRK13643 82 vrkkVGVVFQFPesQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLE---MVGLADEF----WEKSPFeLSGGQMRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 452 IARSLLKNAPILILDEATSALDAVSERLVQSALNRLMKD-RTTLVIAHRLSTVQS-ANQIAVCSDGKIIELGTHSELVAQ 529
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
316-498 |
1.37e-16 |
|
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: 79.02 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 316 VKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITV--GGEDVRMFDKSEW------AKVVSIVNQ--- 384
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQASPReilalrRRTIGYVSQflr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 385 ------------EPvLFSLSVAENIAY----------GLPNE--HVSkddiikaakaanahdfiislPQGYdtlvgergg 440
Cdd:COG4778 104 viprvsaldvvaEP-LLERGVDREEARararellarlNLPERlwDLP--------------------PATF--------- 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 145334131 441 llSGGQRQRVAIARSLLKNAPILILDEATSALDAVSERLVQSALNRLMKDRTTLV-IAH 498
Cdd:COG4778 154 --SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFH 210
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
317-530 |
1.91e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 78.78 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 317 KVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWA-KVVSIVNQEPVLF-SLSVA 394
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARArRGIGYLPQEASIFrRLSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 395 ENIAYGLPNEHVSKDDIIKAAKAANAHDFIISlpqgydTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEATSALDA 474
Cdd:PRK10895 97 DNLMAVLQIRDDLSAEQREDRANELMEEFHIE------HLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145334131 475 VS--------ERLVQSALNRLMKD---RTTLVIAHRLSTVqsanqiavcSDGKIIELGTHSELVAQK 530
Cdd:PRK10895 171 ISvidikriiEHLRDSGLGVLITDhnvRETLAVCERAYIV---------SQGHLIAHGTPTEILQDE 228
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
315-518 |
2.15e-16 |
|
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: 81.79 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 315 DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYE--PTQGRITVGGEDVRMFDKSEW-AKVVSIVNQEPVLF-S 390
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVpE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 391 LSVAENIAYG----LPNEHVSKDDIIKAAKAANAHdfiISLPQGYDTL-VGERGgllsGGQRQRVAIARSLLKNAPILIL 465
Cdd:TIGR02633 93 LSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRE---LQLDADNVTRpVGDYG----GGQQQLVEIAKALNKQARLLIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 145334131 466 DEATSALDAvSERLVQSALNRLMKDR--TTLVIAHRLSTVQS-ANQIAVCSDGKII 518
Cdd:TIGR02633 166 DEPSSSLTE-KETEILLDIIRDLKAHgvACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
12-229 |
2.28e-16 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 79.69 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 12 LRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDLGALNSIV--NDNISrdrgFRAFTEVFGTICILFTLSPQLAPVLGLLM 89
Cdd:cd18590 71 LRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSValNANVL----LRSLVKTLGMLGFMLSLSWQLTLLTLIEM 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 90 LAVSVLVAVYKRSTVPVYKSHGLAQATMSDCVSETFSAIRTVRSFSGEKRQMSIFgSQILA--YKLSGLKlGTFKSINES 167
Cdd:cd18590 147 PLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRY-SEALErtYNLKDRR-DTVRAVYLL 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145334131 168 ITRV-AVYISLLALYClGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDLRGTFAAI 229
Cdd:cd18590 225 VRRVlQLGVQVLMLYC-GRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAA 286
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
318-524 |
2.99e-16 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 78.52 E-value: 2.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 318 VLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDvrmFD---------KSEWAKVVSIVNQEPVL 388
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQ---FDfsqkpsekaIRLLRQKVGMVFQQYNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 389 FS-LSVAENI------AYGLPNEHvSKDDIIKAAKAANAHDFIISLPQgydtlvgerggLLSGGQRQRVAIARSLLKNAP 461
Cdd:COG4161 94 WPhLTVMENLieapckVLGLSKEQ-AREKAMKLLARLRLTDKADRFPL-----------HLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145334131 462 ILILDEATSALDAVSERLVQSALNRLMKDRTTLVI-AHRLSTVQS-ANQIAVCSDGKIIELGTHS 524
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIvTHEVEFARKvASQVVYMEKGRIIEQGDAS 226
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
318-545 |
3.36e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 77.15 E-value: 3.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 318 VLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRmFDKSEWAK-VVSIVNQEPVLFSLSVAEN 396
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLD-FQRDSIARgLLYLGHAPGIKTTLSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 397 IAYglpnehvskddiikaakaanAHDFIiSLPQGYDTL--VGERG------GLLSGGQRQRVAIARSLLKNAPILILDEA 468
Cdd:cd03231 94 LRF--------------------WHADH-SDEQVEEALarVGLNGfedrpvAQLSAGQQRRVALARLLLSGRPLWILDEP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145334131 469 TSALDAVSERLVqsalnrlmkdrTTLVIAHrlstvqsanqiavCSDGKIIELGTHSELVAQKGSYASLvgtqRLAFE 545
Cdd:cd03231 153 TTALDKAGVARF-----------AEAMAGH-------------CARGGMVVLTTHQDLGLSEAGAREL----DLGFK 201
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
303-529 |
3.65e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 79.01 E-value: 3.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPLRPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEdvRMFDKSEWAK--VVS 380
Cdd:PRK13650 7 VKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD--LLTEENVWDIrhKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 381 IVNQEP--VLFSLSVAENIAYGLPNEHVSkddiikaakaanaHDFIISLPQGYDTLVG------ERGGLLSGGQRQRVAI 452
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENKGIP-------------HEEMKERVNEALELVGmqdfkeREPARLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 453 ARSLLKNAPILILDEATSALDAVSER-LVQSAlnRLMKDR---TTLVIAHRLSTVQSANQIAVCSDGKIIELGTHSELVA 528
Cdd:PRK13650 152 AGAVAMRPKIIILDEATSMLDPEGRLeLIKTI--KGIRDDyqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFS 229
|
.
gi 145334131 529 Q 529
Cdd:PRK13650 230 R 230
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
318-528 |
3.95e-16 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 78.25 E-value: 3.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 318 VLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGgeDVrMFDKS-----------EWAKVVSIVNQEP 386
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVG--DI-TIDTArslsqqkglirQLRQHVGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 387 VLFS-LSVAENIAYGlpnehvskddiiKAAKAANAHDFIISLPQGYDTLVGERGG------LLSGGQRQRVAIARSLLKN 459
Cdd:PRK11264 95 NLFPhRTVLENIIEG------------PVIVKGEPKEEATARARELLAKVGLAGKetsyprRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145334131 460 APILILDEATSALDA--VSErlVQSALNRLMKDRTTLVI-AHRLSTVQS-ANQIAVCSDGKIIELGTHSELVA 528
Cdd:PRK11264 163 PEVILFDEPTSALDPelVGE--VLNTIRQLAQEKRTMVIvTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
304-521 |
4.12e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 81.29 E-value: 4.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 304 DDVHFAYPLRPDVK--------VLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYePTQGRITVGGEDVRMFDKSEW 375
Cdd:PRK15134 279 EQLQVAFPIRKGILkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 376 AKV---VSIVNQEPvlFS-----LSVAENIAYGLPNEHvskddiiKAAKAANAHDFIISLPQ--GYDTLVGER-GGLLSG 444
Cdd:PRK15134 358 LPVrhrIQVVFQDP--NSslnprLNVLQIIEEGLRVHQ-------PTLSAAQREQQVIAVMEevGLDPETRHRyPAEFSG 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 445 GQRQRVAIARSLLKNAPILILDEATSALDavseRLVQSALNRLMKDRTT------LVIAHRLSTVQS-ANQIAVCSDGKI 517
Cdd:PRK15134 429 GQRQRIAIARALILKPSLIILDEPTSSLD----KTVQAQILALLKSLQQkhqlayLFISHDLHVVRAlCHQVIVLRQGEV 504
|
....
gi 145334131 518 IELG 521
Cdd:PRK15134 505 VEQG 508
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
315-504 |
4.17e-16 |
|
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: 77.32 E-value: 4.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 315 DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAkvvsIVNQEPVLF-SLSV 393
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIG----YLPEERGLYpKMKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 394 AENIAY-----GLPNEHVSKDDIIKAAKAANAHDFIISLPQgydtlvgergglLSGGQRQRVAIARSLLKNAPILILDEA 468
Cdd:cd03269 88 IDQLVYlaqlkGLKKEEARRRIDEWLERLELSEYANKRVEE------------LSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 145334131 469 TSALDAVSERLVQSALNRLMKDRTTLVI-AHRLSTVQ 504
Cdd:cd03269 156 FSGLDPVNVELLKDVIRELARAGKTVILsTHQMELVE 192
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
317-530 |
4.56e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 78.72 E-value: 4.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 317 KVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKS----EWAKVVSIVNQ--EPVLFS 390
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNknlkKLRKKVSLVFQfpEAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 391 LSVAENIAYGLPNEHVSKDDIIKAAKAANAHdfiISLPqgyDTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEATS 470
Cdd:PRK13641 101 NTVLKDVEFGPKNFGFSEDEAKEKALKWLKK---VGLS---EDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145334131 471 ALDAVS-ERLVQSALNRLMKDRTTLVIAHRLSTV-QSANQIAVCSDGKIIELGTHSELVAQK 530
Cdd:PRK13641 175 GLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
301-516 |
4.73e-16 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 75.18 E-value: 4.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 301 VCLDDVHFAYPLRPdvkVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGedvrmfdksewakvvs 380
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 381 ivnqepvlfslsvAENIAYglpnehvskddiikaakaanahdfiisLPQgydtlvgergglLSGGQRQRVAIARSLLKNA 460
Cdd:cd03221 62 -------------TVKIGY---------------------------FEQ------------LSGGEKMRLALAKLLLENP 89
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145334131 461 PILILDEATSALDAVSerlvQSALNRLMKD--RTTLVIAH-R--LSTVqsANQIAVCSDGK 516
Cdd:cd03221 90 NLLLLDEPTNHLDLES----IEALEEALKEypGTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
303-525 |
5.15e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.88 E-value: 5.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPlrpDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVgGEDVRM--FDKsewakvvs 380
Cdd:COG0488 318 LEGLSKSYG---DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKIgyFDQ-------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 381 ivNQEPVLFSLSVAENIAYGLPN---EHV---------SKDDIikaakaanahdfiislpqgyDTLVGErgglLSGGQRQ 448
Cdd:COG0488 386 --HQEELDPDKTVLDELRDGAPGgteQEVrgylgrflfSGDDA--------------------FKPVGV----LSGGEKA 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 449 RVAIARSLLKNAPILILDEATSALDAVSERLVQSALNRLmkDRTTLVIAH-R--LSTVqsANQIAVCSDGKIIE-LGTHS 524
Cdd:COG0488 440 RLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF--PGTVLLVSHdRyfLDRV--ATRILEFEDGGVREyPGGYD 515
|
.
gi 145334131 525 E 525
Cdd:COG0488 516 D 516
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
312-521 |
1.19e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 77.05 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 312 LRPDVKVLDGLSLTLNSGTVTALVGSSGAGKS----TIVQLLARFYEPTQGRITVGGE-----DVRmfdksewAKVVSIV 382
Cdd:PRK10418 12 LQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKpvapcALR-------GRKIATI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 383 NQEP--------VLFSLSVAENIAYGLPnehvSKDDIIKAAKAANAHDFIISLPQGYDTLvgergglLSGGQRQRVAIAR 454
Cdd:PRK10418 85 MQNPrsafnplhTMHTHARETCLALGKP----ADDATLTAALEAVGLENAARVLKLYPFE-------MSGGMLQRMMIAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 455 SLLKNAPILILDEATSALDAVSERLVQSALNRLMKDRT--TLVIAHRLSTV-QSANQIAVCSDGKIIELG 521
Cdd:PRK10418 154 ALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIVEQG 223
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
315-529 |
1.94e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 75.87 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 315 DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARF--YEPTQGRITVGGEDVRMFDKSEWAKV-VSIVNQEPVLFS- 390
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDERARAgIFLAFQYPVEIPg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 391 LSVAE--NIAYGlpnehvSKDDIIKAAKaanahDFIISLpQGYDTLVG------ERG---GLlSGGQRQRVAIARSLLKN 459
Cdd:COG0396 92 VSVSNflRTALN------ARRGEELSAR-----EFLKLL-KEKMKELGldedflDRYvneGF-SGGEKKRNEILQMLLLE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145334131 460 APILILDEATSALDAVSERLVQSALNRLM-KDRTTLVIAH--RLSTVQSANQIAVCSDGKIIELGThSELVAQ 529
Cdd:COG0396 159 PKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG-KELALE 230
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
324-521 |
2.00e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 77.61 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 324 LTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGedvRMFDKSEwAKV--------VSIVNQEPVLFS-LSVA 394
Cdd:PRK11144 19 LTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNG---RVLFDAE-KGIclppekrrIGYVFQDARLFPhYKVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 395 ENIAYGLPNEHVSKDDIikaakaanahdfIISLpQGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEATSALDA 474
Cdd:PRK11144 95 GNLRYGMAKSMVAQFDK------------IVAL-LGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 145334131 475 VSERLVQSALNRLMKDRTT--LVIAHRLSTV-QSANQIAVCSDGKIIELG 521
Cdd:PRK11144 162 PRKRELLPYLERLAREINIpiLYVSHSLDEIlRLADRVVVLEQGKVKAFG 211
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
12-232 |
2.75e-15 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 76.28 E-value: 2.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 12 LRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDLGALNSIVNdNISRdRGFRAFTEVFGTICILFTLSPQLAPVLGLLMLA 91
Cdd:cd18548 74 LRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVM-MLLR-MLVRAPIMLIGAIIMAFRINPKLALILLVAIPI 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 92 VSVLVAVYKRSTVPVYKShglAQAT---MSDCVSETFSAIRTVRSFSGEKRQMSIFGSQILAYKLSGLKLGTFKSINESI 168
Cdd:cd18548 152 LALVVFLIMKKAIPLFKK---VQKKldrLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPL 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145334131 169 TRVAVYISLLALYCLGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDLRGTFAAIDRI 232
Cdd:cd18548 229 MMLIMNLAIVAILWFGGHLINAGSLQVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASAKRI 292
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
305-528 |
3.23e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 75.81 E-value: 3.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 305 DVHFAYPlrpDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWA--KVVSIV 382
Cdd:PRK13638 6 DLWFRYQ---DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLAlrQQVATV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 383 NQEP--VLFSLSVAENIAYGLPNEHVSKDDIIKAAKAANahdfiislpqgydTLVGERG------GLLSGGQRQRVAIAR 454
Cdd:PRK13638 83 FQDPeqQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEAL-------------TLVDAQHfrhqpiQCLSHGQKKRVAIAG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145334131 455 SLLKNAPILILDEATSALDAVSERLVQSALNRLMKDRTTLVI-AHRLSTV-QSANQIAVCSDGKIIELGTHSELVA 528
Cdd:PRK13638 150 ALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIsSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
317-517 |
3.39e-15 |
|
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: 73.62 E-value: 3.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 317 KVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKV-VSIV----NQEPVLFSL 391
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVpedrKREGLVLDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 392 SVAENIAyglpnehvskddiikaakaanahdfiisLPQgydtlvgerggLLSGGQRQRVAIARSLLKNAPILILDEATSA 471
Cdd:cd03215 94 SVAENIA----------------------------LSS-----------LLSGGNQQKVVLARWLARDPRVLILDEPTRG 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 145334131 472 LDAVSERLVQSALNRLMKD-RTTLVIAHRLSTV-QSANQIAVCSDGKI 517
Cdd:cd03215 135 VDVGAKAEIYRLIRELADAgKAVLLISSELDELlGLCDRILVMYEGRI 182
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
317-528 |
3.54e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 75.07 E-value: 3.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 317 KVLDGLSLTLNSGTVTALVGSSGAGKSTIvqllarFY------EPTQGRITVGGEDV---RMFDKsewAKV-VSIVNQEP 386
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDIthlPMHKR---ARLgIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 387 VLF-SLSVAENIAYGLPNEHVSKDDIIKAAkaanahdfiislpqgyDTLVGE---------RGGLLSGGQRQRVAIARSL 456
Cdd:COG1137 88 SIFrKLTVEDNILAVLELRKLSKKEREERL----------------EELLEEfgithlrksKAYSLSGGERRRVEIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 457 LKNAPILILDEATSALD--AVSE--RLVQSALNR----LMKD---RTTLVIAHRlstvqsanqIAVCSDGKIIELGTHSE 525
Cdd:COG1137 152 ATNPKFILLDEPFAGVDpiAVADiqKIIRHLKERgigvLITDhnvRETLGICDR---------AYIISEGKVLAEGTPEE 222
|
...
gi 145334131 526 LVA 528
Cdd:COG1137 223 ILN 225
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
318-529 |
5.41e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 75.51 E-value: 5.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 318 VLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGedvrmFDKSEWAKVVSIVNQEPVLF-------- 389
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG-----LDTSDEENLWDIRNKAGMVFqnpdnqiv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 390 SLSVAENIAYGLPNEHVSKDDIIK----AAKAANAHDFIISLPQgydtlvgerggLLSGGQRQRVAIARSLLKNAPILIL 465
Cdd:PRK13633 100 ATIVEEDVAFGPENLGIPPEEIRErvdeSLKKVGMYEYRRHAPH-----------LLSGGQKQRVAIAGILAMRPECIIF 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145334131 466 DEATSALDAVSERLVQSALNRLMKDR--TTLVIAHRLSTVQSANQIAVCSDGKIIELGTHSELVAQ 529
Cdd:PRK13633 169 DEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
315-528 |
7.06e-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: 77.15 E-value: 7.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 315 DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLL--ARFYEPTQGRITVggeDVRMFDKSEWAKVVSIVNQE-PVLFSL 391
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIY---HVALCEKCGYVERPSKVGEPcPVCGGT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 392 SVAENIAYGLPNEHVSKDDIIKAAKA-----------ANAHDFIISLPQ-GY--DTLVGERGGL---------------- 441
Cdd:TIGR03269 89 LEPEEVDFWNLSDKLRRRIRKRIAIMlqrtfalygddTVLDNVLEALEEiGYegKEAVGRAVDLiemvqlshrithiard 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 442 LSGGQRQRVAIARSLLKNAPILILDEATSALDAVSERLVQSALNRLMKDR--TTLVIAHRLSTVQSANQIAV-CSDGKII 518
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEVIEDLSDKAIwLENGEIK 248
|
250
....*....|
gi 145334131 519 ELGTHSELVA 528
Cdd:TIGR03269 249 EEGTPDEVVA 258
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
318-484 |
1.05e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 72.78 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 318 VLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMfDKSEWAKVVSIVNQEPVLFS-LSVAEN 396
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE-QRDEPHENILYLGHLPGLKPeLSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 397 IayglpnehvskddiikaakaanahDFIISLPQGYD-------TLVGERG------GLLSGGQRQRVAIARSLLKNAPIL 463
Cdd:TIGR01189 94 L------------------------HFWAAIHGGAQrtiedalAAVGLTGfedlpaAQLSAGQQRRLALARLWLSRRPLW 149
|
170 180
....*....|....*....|.
gi 145334131 464 ILDEATSALDAVSERLVQSAL 484
Cdd:TIGR01189 150 ILDEPTTALDKAGVALLAGLL 170
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
1-232 |
1.09e-14 |
|
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: 74.81 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 1 MTAIWENVMAILRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDLGALNSIVND---NISRDrgfrAFTeVFGTICILFTL 77
Cdd:cd18545 64 MAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNgliNLIPD----LLT-LVGIVIIMFSL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 78 SPQLApVLGLLMLAVSVLVAVY-KRSTVPVYKSHGLAQATMSDCVSETFSAIRTVRSFSGEKRQMSIF--------GSQI 148
Cdd:cd18545 139 NVRLA-LVTLAVLPLLVLVVFLlRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFdelnrenrKANM 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 149 LAYKLSGLklgtFKSINESITRVAVYIsllaLYCLGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDLRGTFAA 228
Cdd:cd18545 218 RAVRLNAL----FWPLVELISALGTAL----VYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMAS 289
|
....
gi 145334131 229 IDRI 232
Cdd:cd18545 290 AERI 293
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
317-526 |
1.40e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 74.74 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 317 KVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKV------------------ 378
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEKvleklviqktrfkkikki 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 379 ------VSIVNQ--EPVLFSLSVAENIAYGLPNEHVSKDDIIKAAKAANAhdfIISLPQGYDtlvgERGGL-LSGGQRQR 449
Cdd:PRK13651 101 keirrrVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIE---LVGLDESYL----QRSPFeLSGGQKRR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 450 VAIARSLLKNAPILILDEATSALDAVSERLVQSALNRLMKDRTTLVIA-HRLSTV-QSANQIAVCSDGKIIELG-THSEL 526
Cdd:PRK13651 174 VALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVtHDLDNVlEWTKRTIFFKDGKIIKDGdTYDIL 253
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
318-501 |
1.72e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 72.93 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 318 VLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVS-----IVNQEPVLFSLS 392
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNqklgfIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 393 VAENIAYGLPNEHVSKDDIIKAAkaanaHDFIISLpqGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEATSAL 472
Cdd:PRK11629 104 ALENVAMPLLIGKKKPAEINSRA-----LEMLAAV--GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180 190
....*....|....*....|....*....|.
gi 145334131 473 DAVSERLVQSALNRLMKDRTT--LVIAHRLS 501
Cdd:PRK11629 177 DARNADSIFQLLGELNRLQGTafLVVTHDLQ 207
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
316-498 |
2.08e-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: 73.21 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 316 VKVLDGLSLTLNSGT-----VTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMfdKSEWAKVVSIVNQEPVLFS 390
Cdd:cd03237 7 KKTLGEFTLEVEGGSiseseVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSY--KPQYIKADYEGTVRDLLSS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 391 LSvaeNIAYGLP--NEHVSKDdiikaakaanahdfiISLPQGYDTLVGErgglLSGGQRQRVAIARSLLKNAPILILDEA 468
Cdd:cd03237 85 IT---KDFYTHPyfKTEIAKP---------------LQIEQILDREVPE----LSGGELQRVAIAACLSKDADIYLLDEP 142
|
170 180 190
....*....|....*....|....*....|...
gi 145334131 469 TSALDaVSERL-VQSALNRLM--KDRTTLVIAH 498
Cdd:cd03237 143 SAYLD-VEQRLmASKVIRRFAenNEKTAFVVEH 174
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
2-232 |
2.09e-14 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 74.06 E-value: 2.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 2 TAIWENVMAILRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDLGALNSIVNDNISRdrGFRAFTEVFGTICILFTLSPQL 81
Cdd:cd18550 64 ARIGQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTS--VVSNVVTLVATLVAMLALDWRL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 82 ApVLGLLMLAVSVLVAVYKRSTVPVYKSHGLAQ-ATMSDCVSETFSA--IRTVRSFSGEKRQMSIFGSQILAYKLSGLKL 158
Cdd:cd18550 142 A-LLSLVLLPLFVLPTRRVGRRRRKLTREQQEKlAELNSIMQETLSVsgALLVKLFGREDDEAARFARRSRELRDLGVRQ 220
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145334131 159 GTFKSINESITRVAVYISLLALYCLGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDLRGTFAAIDRI 232
Cdd:cd18550 221 ALAGRWFFAALGLFTAIGPALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
318-510 |
3.35e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 74.10 E-value: 3.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 318 VLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRmfDKSEWAKV-VSIVNQEPVL-FSLSVAE 395
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP--ARARLARArIGVVPQFDNLdLEFTVRE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 396 N-IAYGlpnEHVSKDDIIKAAKAANAHDFiISLPQGYDTLVGErgglLSGGQRQRVAIARSLLKNAPILILDEATSALDA 474
Cdd:PRK13536 134 NlLVFG---RYFGMSTREIEAVIPSLLEF-ARLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDP 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 145334131 475 VSERLVQSALNRLM-KDRTTLVIAH----------RLSTVQSANQIA 510
Cdd:PRK13536 206 HARHLIWERLRSLLaRGKTILLTTHfmeeaerlcdRLCVLEAGRKIA 252
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
303-474 |
4.13e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 73.72 E-value: 4.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPlrPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEwaKVVSIV 382
Cdd:PRK11650 6 LQAVRKSYD--GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--RDIAMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 383 NQEPVLFS-LSVAENIAYGLPNEHVSKDDIIKAAKAANAhdfIISLpqgyDTLVGERGGLLSGGQRQRVAIARSLLKNAP 461
Cdd:PRK11650 82 FQNYALYPhMSVRENMAYGLKIRGMPKAEIEERVAEAAR---ILEL----EPLLDRKPRELSGGQRQRVAMGRAIVREPA 154
|
170
....*....|...
gi 145334131 462 ILILDEATSALDA 474
Cdd:PRK11650 155 VFLFDEPLSNLDA 167
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
313-522 |
4.78e-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: 75.44 E-value: 4.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 313 RPDVkvlDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMfDKSEWAKVVSIVNQEPVLF-SL 391
Cdd:TIGR01257 943 RPAV---DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFhHL 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 392 SVAENIAYGLPNEHVSKDDIIKAAKAANAHdfiislpQGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEATSA 471
Cdd:TIGR01257 1019 TVAEHILFYAQLKGRSWEEAQLEMEAMLED-------TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSG 1091
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 145334131 472 LDAVSERLVQSALNRLMKDRTTLVIAHRLSTVQS-ANQIAVCSDGKIIELGT 522
Cdd:TIGR01257 1092 VDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGT 1143
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
318-522 |
1.15e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 71.40 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 318 VLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLA-RFYEP-------TQGRITVGGEDVRMFDKSEWAKVVSIVNQ--EPV 387
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGgaprgarVTGDVTLNGEPLAAIDAPRLARLRAVLPQaaQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 388 lFSLSVAENIAYG-LPneHVSKddiikaAKAANAHDFIISLP----QGYDTLVGERGGLLSGGQRQRVAIARSLLKNAP- 461
Cdd:PRK13547 96 -FAFSAREIVLLGrYP--HARR------AGALTHRDGEIAWQalalAGATALVGRDVTTLSGGELARVQFARVLAQLWPp 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145334131 462 --------ILILDEATSALDAVSERLVQSALNRLMKDRT--TLVIAHRLS-TVQSANQIAVCSDGKIIELGT 522
Cdd:PRK13547 167 hdaaqpprYLLLDEPTAALDLAHQHRLLDTVRRLARDWNlgVLAIVHDPNlAARHADRIAMLADGAIVAHGA 238
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
6-237 |
1.20e-13 |
|
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: 72.10 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 6 ENVMAILRAQIFRRVLIQKAEFFD--KYKVGELTGLLTSDLGALNSIVNDNISRdrGFRAFTEVFGTICILFTLSPQLAp 83
Cdd:cd18578 81 ERLTRRLRKLAFRAILRQDIAWFDdpENSTGALTSRLSTDASDVRGLVGDRLGL--ILQAIVTLVAGLIIAFVYGWKLA- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 84 vlgLLMLAVS--VLVAVYKRSTVpVYKSHGLAQATMSDC---VSETFSAIRTVRSFSGEKRQMSIFGSQILAYKLSGLKL 158
Cdd:cd18578 158 ---LVGLATVplLLLAGYLRMRL-LSGFEEKNKKAYEESskiASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRR 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 159 GTFKSINESITRVAVYISLLALYCLGGSKVKTGELAVGTVvsFIGYtFTLTFAVQGLVNTFG---DLRGTFAAIDRINSI 235
Cdd:cd18578 234 ALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQF--FIVF-MALIFGAQSAGQAFSfapDIAKAKAAAARIFRL 310
|
..
gi 145334131 236 LN 237
Cdd:cd18578 311 LD 312
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
318-528 |
1.20e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 71.76 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 318 VLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRmfDKSEWAKV-VSIV----NQEPvlfSLS 392
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP--SRARHARQrVGVVpqfdNLDP---DFT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 393 VAENIA-----YGLPNEHVSKddiikaaKAANAHDFIiSLPQGYDTLVGErgglLSGGQRQRVAIARSLLKNAPILILDE 467
Cdd:PRK13537 97 VRENLLvfgryFGLSAAAARA-------LVPPLLEFA-KLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145334131 468 ATSALDAVSERLVQSALNRLM-KDRTTLVIAHRLSTVQS-ANQIAVCSDGKIIELGTHSELVA 528
Cdd:PRK13537 165 PTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
318-529 |
1.45e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.20 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 318 VLDGLSLTLNSGTVTALVGSSGAGKS----TIVQLLarfyePT------QGRITVGGEDVRMFDKSEWAKV----VSIVN 383
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvtalSILRLL-----PSppvvypSGDIRFHGESLLHASEQTLRGVrgnkIAMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 384 QEPVLfSLSVAENIAYGLPNehvskddiikaakaanahdfIISLPQGYDTLVG--------ERGGL-------------L 442
Cdd:PRK15134 99 QEPMV-SLNPLHTLEKQLYE--------------------VLSLHRGMRREAArgeilnclDRVGIrqaakrltdyphqL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 443 SGGQRQRVAIARSLLKNAPILILDEATSALDAVSERLVQSALNRLMK--DRTTLVIAHRLSTV-QSANQIAVCSDGKIIE 519
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVrKLADRVAVMQNGRCVE 237
|
250
....*....|
gi 145334131 520 LGTHSELVAQ 529
Cdd:PRK15134 238 QNRAATLFSA 247
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
316-498 |
2.08e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 72.92 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 316 VKVLDGLSLTLNSGT-----VTALVGSSGAGKSTIVQLLARFYEPTQGRITvggEDVRMFDKSEWAKVVSIVNQEPVLFS 390
Cdd:PRK13409 347 TKKLGDFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD---PELKISYKPQYIKPDYDGTVEDLLRS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 391 LSVAENIAYglpnehvskddiikaakaaNAHDFI--ISLPQGYDTLVGErgglLSGGQRQRVAIARSLLKNAPILILDEA 468
Cdd:PRK13409 424 ITDDLGSSY-------------------YKSEIIkpLQLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEP 480
|
170 180 190
....*....|....*....|....*....|...
gi 145334131 469 TSALDaVSERL-VQSALNRLM--KDRTTLVIAH 498
Cdd:PRK13409 481 SAHLD-VEQRLaVAKAIRRIAeeREATALVVDH 512
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
12-232 |
2.66e-13 |
|
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: 70.58 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 12 LRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDLGALNSIVNDNISRDRGFraFTEVFGTICILFTLSPQLAPV----LGL 87
Cdd:cd18589 71 LQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWY--LARGLFLFIFMLWLSPKLALLtalgLPL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 88 LMLAVSVLVAVYKRSTVPVYKShgLAQAtmSDCVSETFSAIRTVRSFSGEKRQMSIFGSqilayklsglKLGTFKSINE- 166
Cdd:cd18589 149 LLLVPKFVGKFQQSLAVQVQKS--LARA--NQVAVETFSAMKTVRSFANEEGEAQRYRQ----------RLQKTYRLNKk 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145334131 167 -----SITRVAVYISLLA-----LYcLGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDLRGTFAAIDRI 232
Cdd:cd18589 215 eaaayAVSMWTSSFSGLAlkvgiLY-YGGQLVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
316-521 |
3.47e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 69.14 E-value: 3.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 316 VKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAK-VVSIVNQEPVLFS-LSV 393
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMReAVAIVPEGRRVFSrMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 394 AENIAYGlpneHVSKDDIIKAAKAANAHDFiisLPQGYDTLVgERGGLLSGGQRQRVAIARSLLKNAPILILDEATSALD 473
Cdd:PRK11614 98 EENLAMG----GFFAERDQFQERIKWVYEL---FPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 145334131 474 AVSERLVQSALNRLMKDRTTLVIAHrlstvQSANQIAVCSD-GKIIELG 521
Cdd:PRK11614 170 PIIIQQIFDTIEQLREQGMTIFLVE-----QNANQALKLADrGYVLENG 213
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
317-524 |
3.65e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 69.27 E-value: 3.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 317 KVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDvrmFDKSEWAKV---------VSIVNQEPV 387
Cdd:PRK11124 16 QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNH---FDFSKTPSDkairelrrnVGMVFQQYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 388 LFS-LSVAENI------AYGLpNEHVSKDDIIKAAKAANAHDFIISLPQGydtlvgergglLSGGQRQRVAIARSLLKNA 460
Cdd:PRK11124 93 LWPhLTVQQNLieapcrVLGL-SKDQALARAEKLLERLRLKPYADRFPLH-----------LSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145334131 461 PILILDEATSALDAVSERLVQSALNRLMKDRTTLVI-AHRLSTVQS-ANQIAVCSDGKIIELGTHS 524
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIvTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
314-518 |
4.01e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 71.68 E-value: 4.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 314 PDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRmFDKSEWA--KVVSIVNQE-PVLFS 390
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEID-FKSSKEAleNGISMVHQElNLVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 391 LSVAENIAYG-LPNEHVSKDDIIKAAKAANAHDFIislpqGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEAT 469
Cdd:PRK10982 88 RSVMDNMWLGrYPTKGMFVDQDKMYRDTKAIFDEL-----DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 145334131 470 SALdavSERLVQSALN--RLMKDR--TTLVIAHRLSTV-QSANQIAVCSDGKII 518
Cdd:PRK10982 163 SSL---TEKEVNHLFTiiRKLKERgcGIVYISHKMEEIfQLCDEITILRDGQWI 213
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
319-525 |
4.90e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 69.10 E-value: 4.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 319 LDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYePTQGRITVGGEDVRMFDKSEWAKVVS-IVNQEPVLFSLSVAENI 397
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAyLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 398 AYGLPNEHVSkdDIIKAAKAANAHDFiislpqGYDTLVGERGGLLSGGQRQRVAIARSLLK-------NAPILILDEATS 470
Cdd:COG4138 91 ALHQPAGASS--EAVEQLLAQLAEAL------GLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145334131 471 ALDAVSerlvQSALNRLMKD-----RTTLVIAHRLS-TVQSANQIAVCSDGKIIELGTHSE 525
Cdd:COG4138 163 SLDVAQ----QAALDRLLRElcqqgITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAE 219
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
317-525 |
4.94e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 68.36 E-value: 4.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 317 KVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWA----KVVSIVNQEPVLFSLS 392
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPflrrQIGMIFQDHHLLMDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 393 VAENIAYGLPNEHVSKDDIIKAAKAANAHDFIISLPQGYDTlvgerggLLSGGQRQRVAIARSLLKNAPILILDEATSAL 472
Cdd:PRK10908 96 VYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPI-------QLSGGEQQRVGIARAVVNKPAVLLADEPTGNL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 145334131 473 D-AVSERLVQ--SALNRLmkDRTTLVIAHRLSTVQSAN-QIAVCSDGKIIElGTHSE 525
Cdd:PRK10908 169 DdALSEGILRlfEEFNRV--GVTVLMATHDIGLISRRSyRMLTLSDGHLHG-GVGGE 222
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1-232 |
7.41e-13 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 69.46 E-value: 7.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 1 MTAIWENVMAILRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDLGALNSIVNDNISRdrGFRAFTEVFGTICILFTLSPQ 80
Cdd:cd18564 78 TALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLP--LLTNLLTLVGMLGVMFWLDWQ 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 81 LApvlgLLMLAVS----VLVAVYKRSTVPVYKSHGLAQATMSDCVSETFSAIRTVRSFSGEKRQMSIFGSQILAYKLSGL 156
Cdd:cd18564 156 LA----LIALAVAplllLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGL 231
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145334131 157 KLGTFKSINESITRVAVYISLLALYCLGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDLRGTFAAIDRI 232
Cdd:cd18564 232 RAARLQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
318-528 |
1.23e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 70.29 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 318 VLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLArfyeptqGRI-------TVGGEDVRMfdKSEWAKVVSIVNQEPVLFS 390
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALA-------GRIqgnnftgTILANNRKP--TKQILKRTGFVTQDDILYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 391 -LSVAENIAY----GLPNEhVSKDDIIKAAkaanahDFIIS---LPQGYDTLVGE---RGglLSGGQRQRVAIARSLLKN 459
Cdd:PLN03211 154 hLTVRETLVFcsllRLPKS-LTKQEKILVA------ESVISelgLTKCENTIIGNsfiRG--ISGGERKRVSIAHEMLIN 224
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145334131 460 APILILDEATSALDAVSE-RLVQSALNRLMKDRTTLVIAHRLST--VQSANQIAVCSDGKIIELGTHSELVA 528
Cdd:PLN03211 225 PSLLILDEPTSGLDATAAyRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
6-232 |
1.71e-12 |
|
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: 68.28 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 6 ENVMAILRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDLGALNSIVNDNIsrDRGFRAFTEVFGTICILFTLSPQLAPVL 85
Cdd:cd18546 68 ERLLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGL--VQLVVSLLTLVGIAVVLLVLDPRLALVA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 86 GLLMLAVSVLVAVYKRSTVPVYKSHGLAQATMSDCVSETFSAIRTVRSFSGEKRQMSIFGSQILAYKLSGLKlgtfksin 165
Cdd:cd18546 146 LAALPPLALATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLR-------- 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145334131 166 eSITRVAVY---------ISLLALYCLGGSKVKTGELAVGTVVSFIGYTfTLTFA-VQGLVNTFGDLRGTFAAIDRI 232
Cdd:cd18546 218 -AQRLVAIYfpgvellgnLATAAVLLVGAWRVAAGTLTVGVLVAFLLYL-RRFFApIQQLSQVFDSYQQARAALEKI 292
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
27-232 |
1.90e-12 |
|
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: 67.86 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 27 FFDKYKVGELTglltsdlgalnSIVNDnISRDRgfRAFTEVFGTI-----------CILFTLSPQLAPVLGLLMLAVSVL 95
Cdd:cd18570 92 FFETRKTGEII-----------SRFND-ANKIR--EAISSTTISLfldllmviisgIILFFYNWKLFLITLLIIPLYILI 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 96 VAVYKRSTVPVYKSHGLAQATMSDCVSETFSAIRTVRSFSGEKRQMSIFGSQILAYKLSGLKLGTFKSINESITRVAVYI 175
Cdd:cd18570 158 ILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLI 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 145334131 176 SLLALYCLGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDLRGTFAAIDRI 232
Cdd:cd18570 238 GSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
310-521 |
2.40e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.50 E-value: 2.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 310 YPLRP--------DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKV--- 378
Cdd:PRK10261 323 FPLRSgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALrrd 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 379 VSIVNQEPVLfSLSVAENIAYGLpnehvskddiikaAKAANAHdfiiSLPQGYD-----TLVGERGGLL----------- 442
Cdd:PRK10261 403 IQFIFQDPYA-SLDPRQTVGDSI-------------MEPLRVH----GLLPGKAaaarvAWLLERVGLLpehawryphef 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 443 SGGQRQRVAIARSLLKNAPILILDEATSALDAVSERLVQSALNRLMKDR--TTLVIAHRLSTVQS-ANQIAVCSDGKIIE 519
Cdd:PRK10261 465 SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFgiAYLFISHDMAVVERiSHRVAVMYLGQIVE 544
|
..
gi 145334131 520 LG 521
Cdd:PRK10261 545 IG 546
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
12-232 |
2.52e-12 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 67.51 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 12 LRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDLGALnsivndnisrdRGFRAF--------TEVFGTICILFTLSPQLAP 83
Cdd:cd18543 74 LRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLV-----------QRFLAFgpfllgnlLTLVVGLVVMLVLSPPLAL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 84 VLGLLMLAVSVLVAVYKRSTVPVYKSHGLAQATMSDCVSETFSAIRTVRSFSGEKRQM--------SIFGSQILAYKLsg 155
Cdd:cd18543 143 VALASLPPLVLVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELdrfeaaarRLRATRLRAARL-- 220
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145334131 156 lkLGTFKSINESITRVAVYISLLalycLGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDLRGTFAAIDRI 232
Cdd:cd18543 221 --RARFWPLLEALPELGLAAVLA----LGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
316-498 |
3.19e-12 |
|
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: 69.04 E-value: 3.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 316 VKVLDGLSLTLNSGT-----VTALVGSSGAGKSTIVQLLARFYEPTQGRITvggEDVRMFDKSEWakvVSIVNQEPVLFS 390
Cdd:COG1245 348 TKSYGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD---EDLKISYKPQY---ISPDYDGTVEEF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 391 LSVAENIAYG---LPNEHVSKddiikaakaanahdfiISLPQGYDTLVGErgglLSGGQRQRVAIARSLLKNAPILILDE 467
Cdd:COG1245 422 LRSANTDDFGssyYKTEIIKP----------------LGLEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDE 481
|
170 180 190
....*....|....*....|....*....|....
gi 145334131 468 ATSALDaVSERL-VQSALNRLM--KDRTTLVIAH 498
Cdd:COG1245 482 PSAHLD-VEQRLaVAKAIRRFAenRGKTAMVVDH 514
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
313-526 |
3.45e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 66.71 E-value: 3.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 313 RPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKS---EWAKVVSIVNQEPVLF 389
Cdd:PRK11831 17 RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSrlyTVRKRMSMLFQSGALF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 390 S-LSVAENIAYGLpNEHVSKDDIIKAAKAanahdfIISLPQgydtlVGERGGL------LSGGQRQRVAIARSLLKNAPI 462
Cdd:PRK11831 97 TdMNVFDNVAYPL-REHTQLPAPLLHSTV------MMKLEA-----VGLRGAAklmpseLSGGMARRAALARAIALEPDL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145334131 463 LILDEATSALDAVSER-LVQ--SALNRLMkDRTTLVIAHRLSTVQS-ANQIAVCSDGKIIELGTHSEL 526
Cdd:PRK11831 165 IMFDEPFVGQDPITMGvLVKliSELNSAL-GVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
12-232 |
4.27e-12 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 67.21 E-value: 4.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 12 LRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDLGALNSIVNDNISRdrGFRAFTEVFGTICILFTLSPQLAPVLGLLMLA 91
Cdd:cd18565 89 LRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANS--IIRVVVTVLGIGAILFYLNWQLALVALLPVPL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 92 VSVLVAVYKRSTVPVYKSHGLAQATMSDCVSETFSAIRTVRSFSGEKRQMSIFGSQILAYKLSGLKLGTFKSINESITRV 171
Cdd:cd18565 167 IIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAAFFPVIRL 246
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145334131 172 AVYISLLALYCLGGSKV------KTGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDLRGTFAAIDRI 232
Cdd:cd18565 247 VAGAGFVATFVVGGYWVldgpplFTGTLTVGTLVTFLFYTQRLLWPLTRLGDLIDQYQRAMASAKRV 313
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
301-499 |
4.59e-12 |
|
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: 64.48 E-value: 4.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 301 VCLDDVHFAYPlrPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITV-GGEDVrMFdksewakvv 379
Cdd:cd03223 1 IELENLSLATP--DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpEGEDL-LF--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 380 siVNQEPVLFSLSVAENIAYglPNEHVskddiikaakaanahdfiislpqgydtlvgergglLSGGQRQRVAIARSLLKN 459
Cdd:cd03223 69 --LPQRPYLPLGTLREQLIY--PWDDV-----------------------------------LSGGEQQRLAFARLLLHK 109
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 145334131 460 APILILDEATSALDAVSERLVQSALNRLMkdrTTLV-IAHR 499
Cdd:cd03223 110 PKFVFLDEATSALDEESEDRLYQLLKELG---ITVIsVGHR 147
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
316-533 |
5.74e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 67.03 E-value: 5.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 316 VKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGED-VRmfDKSEWAKVVSIV----NQepVLFS 390
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVpFK--RRKEFARRIGVVfgqrSQ--LWWD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 391 LSVAENIA-----YGLPNEhvskddiikaakaanahDFIISLpqgyDTLVG--ERGGL-------LSGGQRQRVAIARSL 456
Cdd:COG4586 111 LPAIDSFRllkaiYRIPDA-----------------EYKKRL----DELVEllDLGELldtpvrqLSLGQRMRCELAAAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 457 LKNAPILILDEATSALDAVSERLVQSALNRLMKDRTTLVI--AHRLSTVQS-ANQIAVCSDGKIIELGTHSELVAQKGSY 533
Cdd:COG4586 170 LHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILltSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFGPY 249
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
317-496 |
6.56e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 65.80 E-value: 6.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 317 KVLDGLSLTLNSGTVTALVGSSGAGKSTI-----------------VQLLARFYEpTQGRItvgGEDVRmfdKSEwAKVV 379
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLlrhlsglitgdksagshIELLGRTVQ-REGRL---ARDIR---KSR-ANTG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 380 SIVNQEPVLFSLSVAENIAYG-LPNEHVSKDDIIKAAKAANAHDFIISLPQGYDTLVGERGGLLSGGQRQRVAIARSLLK 458
Cdd:PRK09984 90 YIFQQFNLVNRLSVLENVLIGaLGSTPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQ 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 145334131 459 NAPILILDEATSALDAVSERLVQSALNRL-MKDRTTLVI 496
Cdd:PRK09984 170 QAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVV 208
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
275-499 |
1.00e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.59 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 275 IRHLDKYYMSNLKSTNNLRTLTWAGDVCLDDVHFayplrpdvKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYE 354
Cdd:COG2401 10 LMRVTKVYSSVLDLSERVAIVLEAFGVELRVVER--------YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 355 --PTQGRITVggedvrmfDKSEWAKVVSIVNQEPVLFSLSVAENI--AYGLpnehvskddiikaakaanahdfiiSLPQG 430
Cdd:COG2401 82 gtPVAGCVDV--------PDNQFGREASLIDAIGRKGDFKDAVELlnAVGL------------------------SDAVL 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145334131 431 YDTLVGErgglLSGGQRQRVAIARSLLKNAPILILDEATSALDAVSERLVQSALNRLMKDR-TTLVIA-HR 499
Cdd:COG2401 130 WLRRFKE----LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAgITLVVAtHH 196
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
6-232 |
2.14e-11 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 64.81 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 6 ENVMAILRAQIFRRvlIQKAEF--FDKYKVGELTGLLTSDLGALNSIVNDNISrDrGFRAFTEVFGTICILFTLSPQLAp 83
Cdd:cd18540 71 MGVSYDLRKKAFEH--LQTLSFsyFDKTPVGWIMARVTSDTQRLGEIISWGLV-D-LVWGITYMIGILIVMLILNWKLA- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 84 VLGLLMLAVSVLVAVY--KRstvpVYKSHGLAQATMSDCVS---ETFSAIRTVRSFSGEKRQMSIFGSQILAYKLSGLKL 158
Cdd:cd18540 146 LIVLAVVPVLAVVSIYfqKK----ILKAYRKVRKINSRITGafnEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRA 221
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145334131 159 GTFKSINESITRVAVYISL-LALYcLGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDLRGTFAAIDRI 232
Cdd:cd18540 222 ARLSALFLPIVLFLGSIATaLVLW-YGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
316-529 |
3.87e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 64.54 E-value: 3.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 316 VKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEP----TQGRITVGGEDVRMFDKSEWAKVV----SIVNQEPV 387
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERRKIIgreiAMIFQEPS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 388 LF---SLSVAENIAYGLPNEHVS-----------------------KDdiikaakaanaHDFII-SLPqgYDtlvgergg 440
Cdd:COG4170 100 SCldpSAKIGDQLIEAIPSWTFKgkwwqrfkwrkkraiellhrvgiKD-----------HKDIMnSYP--HE-------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 441 lLSGGQRQRVAIARSLLKNAPILILDEATSALDAVSE----RLVqSALNRLmKDRTTLVIAHRLSTV-QSANQIAVCSDG 515
Cdd:COG4170 159 -LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQaqifRLL-ARLNQL-QGTSILLISHDLESIsQWADTITVLYCG 235
|
250
....*....|....
gi 145334131 516 KIIELGTHSELVAQ 529
Cdd:COG4170 236 QTVESGPTEQILKS 249
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
322-525 |
4.48e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 63.03 E-value: 4.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 322 LSLTLNSGTVTALVGSSGAGKSTivqLLARF--YEPTQGRITVGGEDVRMFDKSEWAKVVS-IVNQEPVLFSLSVAENIA 398
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMagLLPGSGSIQFAGQPLEAWSAAELARHRAyLSQQQTPPFAMPVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 399 YGLPnehvskdDIIKAAKAANAHDFIISLPQGYDTLvGERGGLLSGGQRQRVAIARSLLK-------NAPILILDEATSA 471
Cdd:PRK03695 92 LHQP-------DKTRTEAVASALNEVAEALGLDDKL-GRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNS 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 472 LDaVSErlvQSALNRLMKD-----RTTLVIAHRLS-TVQSANQIAVCSDGKIIELGTHSE 525
Cdd:PRK03695 164 LD-VAQ---QAALDRLLSElcqqgIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
315-522 |
4.59e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 63.12 E-value: 4.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 315 DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARF--YEPTQGRITVGGEDVRMFDKSEWAKV---------VSI-- 381
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPEERAHLgiflafqypIEIpg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 382 VNQEPVLFSLSVAENIAYGLPNehvsKDDIIKAAKAANAHDfIISLPQGYDTLVGERGglLSGGQRQRVAIARSLLKNAP 461
Cdd:CHL00131 99 VSNADFLRLAYNSKRKFQGLPE----LDPLEFLEIINEKLK-LVGMDPSFLSRNVNEG--FSGGEKKRNEILQMALLDSE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145334131 462 ILILDEATSALDAVSERLVQSALNRLM-KDRTTLVIAH--RLSTVQSANQIAVCSDGKIIELGT 522
Cdd:CHL00131 172 LAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
313-474 |
5.84e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 62.13 E-value: 5.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 313 RPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVSIVNQEPVLFSLS 392
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQPGIKTELT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 393 VAENIAYGLPNEHVSKDDIIKAAKAAnahdfiISLpQGY-DTLVGErgglLSGGQRQRVAIARSLLKNAPILILDEATSA 471
Cdd:PRK13538 91 ALENLRFYQRLHGPGDDEALWEALAQ------VGL-AGFeDVPVRQ----LSAGQQRRVALARLWLTRAPLWILDEPFTA 159
|
...
gi 145334131 472 LDA 474
Cdd:PRK13538 160 IDK 162
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
313-473 |
8.56e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 61.79 E-value: 8.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 313 RPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRmfdKSEWAKVVSIVNQEPVLFS-L 391
Cdd:PRK13543 21 RNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT---RGDRSRFMAYLGHLPGLKAdL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 392 SVAENIAY--GLPNEHVSKDDIIKAAkaanahdfIISLPQGYDTLVGErgglLSGGQRQRVAIARSLLKNAPILILDEAT 469
Cdd:PRK13543 98 STLENLHFlcGLHGRRAKQMPGSALA--------IVGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLWLLDEPY 165
|
....
gi 145334131 470 SALD 473
Cdd:PRK13543 166 ANLD 169
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
5-217 |
1.11e-10 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 62.85 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 5 WENVMAI-----LRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDLGALNSIVNdnisrdRG----FRAFTEVFGTICILF 75
Cdd:cd18549 65 WGHVMGArietdMRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISELAH------HGpedlFISIITIIGSFIILL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 76 TLSPQLAPVLgLLMLAVSVLVAVYKRstVPVYKSHGLAQATMSD---CVSETFSAIRTVRSFSGEKRQMSIFGSQILAYK 152
Cdd:cd18549 139 TINVPLTLIV-FALLPLMIIFTIYFN--KKMKKAFRRVREKIGEinaQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFL 215
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145334131 153 LSGLK----LGTFKSINESITRVAVYISLLAlyclGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGLVN 217
Cdd:cd18549 216 ESKKKaykaMAYFFSGMNFFTNLLNLVVLVA----GGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVN 280
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
303-529 |
1.48e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 63.84 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPLRP-DVKVLDglsLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVSI 381
Cdd:PRK10522 325 LRNVTFAYQDNGfSVGPIN---LTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 382 VNQEPVLFSlsvaeniaYGLPNEHVSKDDIIKAA--------KAANAHDFIISLPQgydtlvgergglLSGGQRQRVAIA 453
Cdd:PRK10522 402 VFTDFHLFD--------QLLGPEGKPANPALVEKwlerlkmaHKLELEDGRISNLK------------LSKGQKKRLALL 461
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145334131 454 RSLLKNAPILILDEATSALDAVSERLVQSALNRLMKD--RTTLVIAHRLSTVQSANQIAVCSDGKIIEL-GTHSELVAQ 529
Cdd:PRK10522 462 LALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEmgKTIFAISHDDHYFIHADRLLEMRNGQLSELtGEERDAASR 540
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
320-526 |
1.49e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 61.93 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 320 DGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGED--------------VRMFDKsewakvVSIVNQE 385
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHieglpghqiarmgvVRTFQH------VRLFREM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 386 PVLFSLSVAE------NIAYGL---PNEHVSKDDIIKAAKAANahDFIislpqGYDTLVGERGGLLSGGQRQRVAIARSL 456
Cdd:PRK11300 96 TVIENLLVAQhqqlktGLFSGLlktPAFRRAESEALDRAATWL--ERV-----GLLEHANRQAGNLAYGQQRRLEIARCM 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145334131 457 LKNAPILILDEATSALDAVSERLVQSALNRLMKDR--TTLVIAHRLSTVQS-ANQIAVCSDGKIIELGTHSEL 526
Cdd:PRK11300 169 VTQPEILMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
315-491 |
2.14e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 60.35 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 315 DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMfDKSEWAKVVSIVNQEP-VLFSLSV 393
Cdd:PRK13540 13 DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHRSgINPYLTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 394 AENIAYGLpneHVSKDDIIKAAKAAnahdfIISLPQGYDTLVgergGLLSGGQRQRVAIARSLLKNAPILILDEATSALD 473
Cdd:PRK13540 92 RENCLYDI---HFSPGAVGITELCR-----LFSLEHLIDYPC----GLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
170
....*....|....*...
gi 145334131 474 avsERLVQSALNRLMKDR 491
Cdd:PRK13540 160 ---ELSLLTIITKIQEHR 174
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
316-496 |
2.17e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 60.95 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 316 VKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKV----VSIVNQEPVLF-S 390
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLrakhVGFVFQSFMLIpT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 391 LSVAENIAygLP------NEHVSKDDIIKAAKAANAHDFIISLPqgydtlvgergGLLSGGQRQRVAIARSLLKNAPILI 464
Cdd:PRK10584 103 LNALENVE--LPallrgeSSRQSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLF 169
|
170 180 190
....*....|....*....|....*....|..
gi 145334131 465 LDEATSALDAVSERLVQSALNRLMKDRTTLVI 496
Cdd:PRK10584 170 ADEPTGNLDRQTGDKIADLLFSLNREHGTTLI 201
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
325-500 |
2.53e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.90 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 325 TLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITvggedvrmfDKSEWAKVV-------------SIVNQEpvlfsL 391
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYE---------EEPSWDEVLkrfrgtelqnyfkKLYNGE-----I 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 392 SVAENIAY---------GLPNEHVSKDDIIKAAkaanahDFIISLpQGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPI 462
Cdd:PRK13409 161 KVVHKPQYvdlipkvfkGKVRELLKKVDERGKL------DEVVER-LGLENILDRDISELSGGELQRVAIAAALLRDADF 233
|
170 180 190
....*....|....*....|....*....|....*....
gi 145334131 463 LILDEATSALDaVSERL-VQSALNRLMKDRTTLVIAHRL 500
Cdd:PRK13409 234 YFFDEPTSYLD-IRQRLnVARLIRELAEGKYVLVVEHDL 271
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
313-522 |
4.84e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 62.18 E-value: 4.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 313 RPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGE----------DVRMFDKSEWAKV---- 378
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELSEQSAAQMRHVrgad 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 379 VSIVNQEPvLFSL----SVAENIAYGLP-NEHVSKDDIIKAAKAANAHdfiISLPQGyDTLVGERGGLLSGGQRQRVAIA 453
Cdd:PRK10261 106 MAMIFQEP-MTSLnpvfTVGEQIAESIRlHQGASREEAMVEAKRMLDQ---VRIPEA-QTILSRYPHQLSGGMRQRVMIA 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145334131 454 RSLLKNAPILILDEATSALDAVSERLVQSALNRLMKDRTTLV--IAHRLSTVQS-ANQIAVCSDGKIIELGT 522
Cdd:PRK10261 181 MALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVifITHDMGVVAEiADRVLVMYQGEAVETGS 252
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
12-219 |
5.28e-10 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 60.75 E-value: 5.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 12 LRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDLGALNSIVNDNISRDrgFRAFTEVFGTICILFTLSPQLApvlgLLMLA 91
Cdd:cd18558 94 IRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVI--FQNIATFGTGFIIGFIRGWKLT----LVILA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 92 VSVLVAVYKRSTVPVYKSHGL----AQATMSDCVSETFSAIRTVRSFSGEKRQMSIFGSQILAYKLSGLKLGTFKSINES 167
Cdd:cd18558 168 ISPVLGLSAVVWAKILSGFTDkekkAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKAITFNISMG 247
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 145334131 168 ITRVAVYISLLALYCLGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGLVNTF 219
Cdd:cd18558 248 AAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSI 299
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
308-518 |
7.82e-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: 58.81 E-value: 7.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 308 FAYPLRPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLA---RFYEPTQGRITVGGEDVRMFDKSEWAKVVsIVNQ 384
Cdd:cd03233 12 TTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAnrtEGNVSVEGDIHYNGIPYKEFAEKYPGEII-YVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 385 EPVLFS-LSVAENIayglpnehvskddiikaakaanahDFIISLpQGYDTLvgeRGglLSGGQRQRVAIARSLLKNAPIL 463
Cdd:cd03233 91 EDVHFPtLTVRETL------------------------DFALRC-KGNEFV---RG--ISGGERKRVSIAEALVSRASVL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145334131 464 ILDEATSALDAVserlvqSALNRLMKDRTtlvIAH--RLSTVQSANQ-----------IAVCSDGKII 518
Cdd:cd03233 141 CWDNSTRGLDSS------TALEILKCIRT---MADvlKTTTFVSLYQasdeiydlfdkVLVLYEGRQI 199
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
7-232 |
1.13e-09 |
|
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: 59.74 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 7 NVMAILRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDLGALNSIVN---DNISRDrgfraFTEVFGTICILFTLSPQLAp 83
Cdd:cd18554 76 KILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITtglMNIWLD-----MITIIIAICIMLVLNPKLT- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 84 VLGLLMLAVSVLVAVY-----KRSTvpvyKSHGLAQATMSDCVSETFSAIRTVRSFSGEKRQMSIFGSQ-----ILAYKL 153
Cdd:cd18554 150 FVSLVIFPFYILAVKYffgrlRKLT----KERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRnghflTRALKH 225
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145334131 154 SGLKLGTFKSINeSITRVAvyiSLLALYClGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDLRGTFAAIDRI 232
Cdd:cd18554 226 TRWNAKTFSAVN-TITDLA---PLLVIGF-AAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
305-474 |
1.32e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 61.28 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 305 DVHFAYPLRPDVKV-LDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARfyEPTQGRITVGGEDV--RMFDKSeWAKVVSI 381
Cdd:TIGR00956 764 NLTYEVKIKKEKRViLNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVITGGDRLVngRPLDSS-FQRSIGY 840
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 382 VNQEPV-LFSLSVAENIAYG----LPNeHVSKDDIIKAAkaanahDFIISL---PQGYDTLVGERGGLLSGGQRQRVAIA 453
Cdd:TIGR00956 841 VQQQDLhLPTSTVRESLRFSaylrQPK-SVSKSEKMEYV------EEVIKLlemESYADAVVGVPGEGLNVEQRKRLTIG 913
|
170 180
....*....|....*....|..
gi 145334131 454 RSLLKNAPILI-LDEATSALDA 474
Cdd:TIGR00956 914 VELVAKPKLLLfLDEPTSGLDS 935
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
316-501 |
1.81e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 60.63 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 316 VKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLArfyeptqGRITvGGE---DVRM--FDKSE--WAKVVSIVNQEPVL 388
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLA-------GRKT-GGYiegDIRIsgFPKKQetFARISGYCEQNDIH 964
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 389 F-SLSVAENIAYG----LPNEhVSKDDIIKAAKAANAhdfIISLPQGYDTLVGERGGL-LSGGQRQRVAIARSLLKNAPI 462
Cdd:PLN03140 965 SpQVTVRESLIYSaflrLPKE-VSKEEKMMFVDEVME---LVELDNLKDAIVGLPGVTgLSTEQRKRLTIAVELVANPSI 1040
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 145334131 463 LILDEATSALDAVSERLVQSAL-NRLMKDRTTLVIAHRLS 501
Cdd:PLN03140 1041 IFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPS 1080
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
328-518 |
2.13e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 56.23 E-value: 2.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 328 SGTVTALVGSSGAGKSTIVQLLARFYEPTQGR-ITVGGEDVRMFDKSEWAKVvsivnqepvlfslsvaeniayglpnehv 406
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLLI---------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 407 skddiikaakaanahdfiislpqgydtLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEATSALDAVSERLVQSAL-- 484
Cdd:smart00382 53 ---------------------------IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEel 105
|
170 180 190
....*....|....*....|....*....|....*....
gi 145334131 485 -----NRLMKDRTTLVIAHRLSTVQSANqIAVCSDGKII 518
Cdd:smart00382 106 rllllLKSEKNLTVILTTNDEKDLGPAL-LRRRFDRRIV 143
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
328-502 |
2.43e-09 |
|
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: 59.80 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 328 SGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITvggedvrmfDKSEWAKVV-------------SIVNQEpvlfsLSVA 394
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYD---------EEPSWDEVLkrfrgtelqdyfkKLANGE-----IKVA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 395 ENIAY---------GLPNEHVSKDDIIKAAkaanahDFIISLpQGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILIL 465
Cdd:COG1245 164 HKPQYvdlipkvfkGTVRELLEKVDERGKL------DELAEK-LGLENILDRDISELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190
....*....|....*....|....*....|....*....
gi 145334131 466 DEATSALDaVSERL-VQSALNRLMK-DRTTLVIAHRLST 502
Cdd:COG1245 237 DEPSSYLD-IYQRLnVARLIRELAEeGKYVLVVEHDLAI 274
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
313-528 |
2.45e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 58.26 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 313 RPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKVVSIVNQEPvlfslS 392
Cdd:PRK15112 23 RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDP-----S 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 393 VAENiayglPNEHVSKddiikaakaanahdfIISLP--------------QGYDTL--VGERGG-------LLSGGQRQR 449
Cdd:PRK15112 98 TSLN-----PRQRISQ---------------ILDFPlrlntdlepeqrekQIIETLrqVGLLPDhasyyphMLAPGQKQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 450 VAIARSLLKNAPILILDEATSALDaVSERlvqSALNRLMKD-------RTTLVIAHRLSTVQSANQIAVCSDGKIIELGT 522
Cdd:PRK15112 158 LGLARALILRPKVIIADEALASLD-MSMR---SQLINLMLElqekqgiSYIYVTQHLGMMKHISDQVLVMHQGEVVERGS 233
|
....*.
gi 145334131 523 HSELVA 528
Cdd:PRK15112 234 TADVLA 239
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
323-521 |
3.00e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 57.97 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 323 SLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRmfdKSEWAKVVSIVNQ-EPVLFSLSV-AENIA-- 398
Cdd:PRK15056 27 SFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR---QALQKNLVAYVPQsEEVDWSFPVlVEDVVmm 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 399 --YG------LPNEHvskdDIIKAAKAANAHDFIislpQGYDTLVGErgglLSGGQRQRVAIARSLLKNAPILILDEATS 470
Cdd:PRK15056 104 grYGhmgwlrRAKKR----DRQIVTAALARVDMV----EFRHRQIGE----LSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 145334131 471 ALDAVSERLVQSALNRLMKD-RTTLVIAHRLSTVQSANQIAVCSDGKIIELG 521
Cdd:PRK15056 172 GVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
317-487 |
4.03e-09 |
|
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: 56.48 E-value: 4.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 317 KVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEP--TQGRITVGGEDVrmfdKSEWAKVVSIVNQEPVLF-SLSV 393
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPL----DKNFQRSTGYVEQQDVHSpNLTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 394 AENIAYGLPNehvskddiikaakaanahdfiislpqgydtlvgeRGglLSGGQRQRVAIARSLLKNAPILILDEATSALD 473
Cdd:cd03232 97 REALRFSALL----------------------------------RG--LSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
170
....*....|....
gi 145334131 474 AVSERLVQSALNRL 487
Cdd:cd03232 141 SQAAYNIVRFLKKL 154
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
319-521 |
5.15e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 57.24 E-value: 5.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 319 LDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFD-------------KSEWAkvvsIVNQE 385
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDlyalseaerrrllRTEWG----FVHQH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 386 P---VLFSLSVAENIA----------YG---------LpnEHVSKDDiikaakaanahDFIISLPQGYdtlvgerggllS 443
Cdd:PRK11701 98 PrdgLRMQVSAGGNIGerlmavgarhYGdiratagdwL--ERVEIDA-----------ARIDDLPTTF-----------S 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 444 GGQRQRVAIARSLLKNAPILILDEATSALDaVSerlVQSALNRLMKDRTT------LVIAHRLSTVQS-ANQIAVCSDGK 516
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLD-VS---VQARLLDLLRGLVRelglavVIVTHDLAVARLlAHRLLVMKQGR 229
|
....*
gi 145334131 517 IIELG 521
Cdd:PRK11701 230 VVESG 234
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
317-469 |
5.37e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 58.49 E-value: 5.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 317 KVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEwakvvSIVN----------QEP 386
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRD-----AIRAgiayvpedrkGEG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 387 VLFSLSVAENIAygLPN-EHVSK----DDIIKAAKAAnahDFIISL---PQGYDTLVGErgglLSGGQRQRVAIARSLLK 458
Cdd:COG1129 341 LVLDLSIRENIT--LASlDRLSRggllDRRRERALAE---EYIKRLrikTPSPEQPVGN----LSGGNQQKVVLAKWLAT 411
|
170
....*....|.
gi 145334131 459 NAPILILDEAT 469
Cdd:COG1129 412 DPKVLILDEPT 422
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
7-232 |
5.98e-09 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 57.55 E-value: 5.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 7 NVMAILRAQIFRRVLIQKAEFFDKYKVGELTGLLTSDLGALNSIVNDNIsrDRGFRAFTEVFGTICILFTLSPQLAPVLG 86
Cdd:cd18778 70 KVVADLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGI--PQGITNVLTLVGVAIILFSINPKLALLTL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 87 LLMLAVSVLVAVYKRSTVPVYKSHGLAQATMSDCVSETFSAIRTVRSFSGEKRQMSIFGSQILAYK---LSGLKL-GTFK 162
Cdd:cd18778 148 IPIPFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRkaqLRAMKLwAIFH 227
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 163 SINESITRvavyISLLALYCLGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDLRGTFAAIDRI 232
Cdd:cd18778 228 PLMEFLTS----LGTVLVLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
315-529 |
7.04e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 56.72 E-value: 7.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 315 DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLA--RFYEPTQGRITVGGEDVRMFDKSEWA-KVVSIVNQEPV---- 387
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPEDRAgEGIFMAFQYPVeipg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 388 ---LFSLSVAENiayglpneHVSKDDIIKAAKAANAHDFI------ISLPQgyDTLVGERGGLLSGGQRQRVAIARSLLK 458
Cdd:PRK09580 93 vsnQFFLQTALN--------AVRSYRGQEPLDRFDFQDLMeekialLKMPE--DLLTRSVNVGFSGGEKKRNDILQMAVL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145334131 459 NAPILILDEATSALDAVSERLVQSALNRLMK-DRTTLVIAH--RLSTVQSANQIAVCSDGKIIELGTHSeLVAQ 529
Cdd:PRK09580 163 EPELCILDESDSGLDIDALKIVADGVNSLRDgKRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFT-LVKQ 235
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
303-473 |
7.16e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.42 E-value: 7.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPlrpDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGE-DVRMFDKSEwakvvSI 381
Cdd:PRK11147 322 MENVNYQID---GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlEVAYFDQHR-----AE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 382 VNQEPvlfslSVAENIAYG----LPN---EHVskddiikaakAANAHDFIISlPQGYDTLVGErgglLSGGQRQRVAIAR 454
Cdd:PRK11147 394 LDPEK-----TVMDNLAEGkqevMVNgrpRHV----------LGYLQDFLFH-PKRAMTPVKA----LSGGERNRLLLAR 453
|
170
....*....|....*....
gi 145334131 455 SLLKNAPILILDEATSALD 473
Cdd:PRK11147 454 LFLKPSNLLILDEPTNDLD 472
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
315-522 |
1.09e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 57.04 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 315 DVKVLDGLSLTLNSGTVTALVGSSGAGKS----TIVQLLARfyeptQGRIT----VGGEDVRMFDKSEWAKV----VSIV 382
Cdd:PRK09473 28 DVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-----NGRIGgsatFNGREILNLPEKELNKLraeqISMI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 383 NQEPvLFSLS----VAENIAYGLP-NEHVSKDDIIKAAKAANAhdfIISLPQGYdtlvgERGGL----LSGGQRQRVAIA 453
Cdd:PRK09473 103 FQDP-MTSLNpymrVGEQLMEVLMlHKGMSKAEAFEESVRMLD---AVKMPEAR-----KRMKMypheFSGGMRQRVMIA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145334131 454 RSLLKNAPILILDEATSALDAVSERLVQSALNRLMKDRTT--LVIAHRLSTVQ-SANQIAVCSDGKIIELGT 522
Cdd:PRK09473 174 MALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaiIMITHDLGVVAgICDKVLVMYAGRTMEYGN 245
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
317-543 |
3.02e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 54.73 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 317 KVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRItvggedvRMFDKSEWAKVVSIVNQEPVLfSLSVAEn 396
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-------KRNGKLRIGYVPQKLYLDTTL-PLTVNR- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 397 iaYGLPNEHVSKDDIIKAAKAANAHDFIISLPQGydtlvgergglLSGGQRQRVAIARSLLKNAPILILDEATSALDAVS 476
Cdd:PRK09544 89 --FLRLRPGTKKEDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145334131 477 ERLVQSALNRLMK--DRTTLVIAHRLSTVQSANQIAVCSDGKIIELGT------HSELVAQKGSYaslvGTQRLA 543
Cdd:PRK09544 156 QVALYDLIDQLRRelDCAVLMVSHDLHLVMAKTDEVLCLNHHICCSGTpevvslHPEFISMFGPR----GAEQLG 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
299-518 |
4.20e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.80 E-value: 4.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 299 GDVCL--DDVHfaypLRPD--VKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSE 374
Cdd:COG3845 254 GEVVLevENLS----VRDDrgVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 375 WAKV-VSIVNQEP-----VLfSLSVAENIA---YGLP-------------NEHVSKddiikaakaanahdfIIS----LP 428
Cdd:COG3845 330 RRRLgVAYIPEDRlgrglVP-DMSVAENLIlgrYRRPpfsrggfldrkaiRAFAEE---------------LIEefdvRT 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 429 QGYDTLVgergGLLSGGQRQRVAIARSLLKNAPILILDEATSALDAVSERLVQSALnRLMKDR--TTLVIAHRLSTVQS- 505
Cdd:COG3845 394 PGPDTPA----RSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRL-LELRDAgaAVLLISEDLDEILAl 468
|
250
....*....|...
gi 145334131 506 ANQIAVCSDGKII 518
Cdd:COG3845 469 SDRIAVMYEGRIV 481
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
328-501 |
4.26e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 54.29 E-value: 4.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 328 SGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITvggedvrmfDKSEWAKVVSivnqepvLFSLSVAENIAYGLPNEHVS 407
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFD---------DPPDWDEILD-------EFRGSELQNYFTKLLEGDVK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 408 kddiikaakAANAHDFIISLPQGYDTLVG-------ERGGL-------------------LSGGQRQRVAIARSLLKNAP 461
Cdd:cd03236 89 ---------VIVKPQYVDLIPKAVKGKVGellkkkdERGKLdelvdqlelrhvldrnidqLSGGELQRVAIAAALARDAD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 145334131 462 ILILDEATSALDaVSERLVQSALNR-LMKD-RTTLVIAHRLS 501
Cdd:cd03236 160 FYFFDEPSSYLD-IKQRLNAARLIReLAEDdNYVLVVEHDLA 200
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
17-232 |
5.27e-08 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 54.49 E-value: 5.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 17 FRRVLIQKAEFFDKYKVGELTG----------LLTSdlGALNSIVNdnisrdrgfrAFTeVFGTICILFTLSPQLApVLG 86
Cdd:cd18568 82 YKHLLSLPLSFFASRKVGDIITrfqenqkirrFLTR--SALTTILD----------LLM-VFIYLGLMFYYNLQLT-LIV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 87 LLMLAVSVLVAVY-----KRSTVPVYKSHGLAQATMSdcvsETFSAIRTVRSFSGE----KRQMSIFGSQILAYkLSGLK 157
Cdd:cd18568 148 LAFIPLYVLLTLLsspklKRNSREIFQANAEQQSFLV----EALTGIATIKALAAErpirWRWENKFAKALNTR-FRGQK 222
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145334131 158 LgtfkSIN-ESITRVAVYISLLALYCLGGSKVKTGELAVGTVVSFIGYTFTLTFAVQGLVNTFGDLRGTFAAIDRI 232
Cdd:cd18568 223 L----SIVlQLISSLINHLGTIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
316-521 |
6.59e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.50 E-value: 6.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 316 VKVLDGLsltLNSGTVTALVGSSGAGKSTIVQLLA----RFYEPTQGRITVGGEDVRMFDKSEWAKVVSIVNQEPVLFSL 391
Cdd:TIGR00956 77 LKPMDGL---IKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFPHL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 392 SVAENIAY-------GLPNEHVSKDDIIKAAKAANAHdfIISLPQGYDTLVGE---RGglLSGGQRQRVAIARSLLKNAP 461
Cdd:TIGR00956 154 TVGETLDFaarcktpQNRPDGVSREEYAKHIADVYMA--TYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGGAK 229
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145334131 462 ILILDEATSALDAVSE----RLVQSALNRLmkDRTTLVIAHRLStvQSA----NQIAVCSDGKIIELG 521
Cdd:TIGR00956 230 IQCWDNATRGLDSATAlefiRALKTSANIL--DTTPLVAIYQCS--QDAyelfDKVIVLYEGYQIYFG 293
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
299-473 |
2.25e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.47 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 299 GDVCLDDVHFAYPlrpdvkVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRMFDKSEW--A 376
Cdd:PRK10762 254 GEVRLKVDNLSGP------GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGlaN 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 377 KVVSIVNQ---EPVLFSLSVAENIAygLPN-EHVSKDDIIK--AAKAANAHDFI----ISLPqGYDTLVGerggLLSGGQ 446
Cdd:PRK10762 328 GIVYISEDrkrDGLVLGMSVKENMS--LTAlRYFSRAGGSLkhADEQQAVSDFIrlfnIKTP-SMEQAIG----LLSGGN 400
|
170 180
....*....|....*....|....*..
gi 145334131 447 RQRVAIARSLLKNAPILILDEATSALD 473
Cdd:PRK10762 401 QQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
317-484 |
2.71e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 53.40 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 317 KVL-DGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGgEDVRmfdksewakvVSIVNQ--EPVLFSLSV 393
Cdd:TIGR03719 335 KLLiDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG-ETVK----------LAYVDQsrDALDPNKTV 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 394 AENIAYGLPNEHVSKDDIIKaakaanahdfiislpQGYDTLVGERG-------GLLSGGQRQRVAIARSLLKNAPILILD 466
Cdd:TIGR03719 404 WEEISGGLDIIKLGKREIPS---------------RAYVGRFNFKGsdqqkkvGQLSGGERNRVHLAKTLKSGGNVLLLD 468
|
170
....*....|....*...
gi 145334131 467 EATSALDAVSERLVQSAL 484
Cdd:TIGR03719 469 EPTNDLDVETLRALEEAL 486
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
316-528 |
4.16e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 52.11 E-value: 4.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 316 VKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARF----YEPTQGRITVGGEDVRMFDKSEWAKV----VSIVNQEP- 386
Cdd:PRK15093 20 VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRLSPRERRKLvghnVSMIFQEPq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 387 --VLFSLSVAENIAYGLPN-------------EHVSKDDIIKAAKAANAHDFIISLPqgYDtlvgergglLSGGQRQRVA 451
Cdd:PRK15093 100 scLDPSERVGRQLMQNIPGwtykgrwwqrfgwRKRRAIELLHRVGIKDHKDAMRSFP--YE---------LTEGECQKVM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 452 IARSLLKNAPILILDEATSALDAVSERLVQSALNRLMKDRTT--LVIAHRLSTV-QSANQIAVCSDGKIIELGTHSELVA 528
Cdd:PRK15093 169 IAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTtiLLISHDLQMLsQWADKINVLYCGQTVETAPSKELVT 248
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
309-476 |
4.93e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 52.24 E-value: 4.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 309 AYPlrPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGR------ITVGgedvrmfdksewakvvsIV 382
Cdd:TIGR03719 13 VVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEarpqpgIKVG-----------------YL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 383 NQEPVL-FSLSVAENI-------------------AYGLPNEHVSK-----DDIIKAAKAANAHDF---------IISLP 428
Cdd:TIGR03719 74 PQEPQLdPTKTVRENVeegvaeikdaldrfneisaKYAEPDADFDKlaaeqAELQEIIDAADAWDLdsqleiamdALRCP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 145334131 429 QGyDTLVGErgglLSGGQRQRVAIARSLLKNAPILILDEATSALDAVS 476
Cdd:TIGR03719 154 PW-DADVTK----LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
306-526 |
6.48e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 51.28 E-value: 6.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 306 VHFAYPLRPdVKVLDGLSLTLNSGTVTALVGSSGAGKS----TIVQLLARFYEPTQGRITVGGEDVRMFDKSEWAKV--- 378
Cdd:PRK11022 11 VHFGDESAP-FRAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLvga 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 379 -VSIVNQEPvLFSLsvaeNIAYGLPNEHVSKDDIIKAAKAANAHDFIISLPqgydTLVG-----ERGGL----LSGGQRQ 448
Cdd:PRK11022 90 eVAMIFQDP-MTSL----NPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLL----NQVGipdpaSRLDVyphqLSGGMSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 449 RVAIARSLLKNAPILILDEATSALD-AVSERLVQSALNRLMKDRTTLV-IAHRLSTV-QSANQIAVCSDGKIIELGTHSE 525
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDvTIQAQIIELLLELQQKENMALVlITHDLALVaEAAHKIIVMYAGQVVETGKAHD 240
|
.
gi 145334131 526 L 526
Cdd:PRK11022 241 I 241
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
329-500 |
7.47e-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: 49.49 E-value: 7.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 329 GTVTALVGSSGAGKSTIVQLLARFYEPTQgritvggedvrmfDKSEWAKVvsivnqepvlfslsvaeNIAYGlpnehvsk 408
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNG-------------DNDEWDGI-----------------TPVYK-------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 409 ddiikaakaanahdfiislPQGYDtlvgergglLSGGQRQRVAIARSLLKNAPILILDEATSALDaVSERL-VQSALNRL 487
Cdd:cd03222 67 -------------------PQYID---------LSGGELQRVAIAAALLRNATFYLFDEPSAYLD-IEQRLnAARAIRRL 117
|
170
....*....|....*
gi 145334131 488 MK--DRTTLVIAHRL 500
Cdd:cd03222 118 SEegKKTALVVEHDL 132
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
67-232 |
1.03e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 50.59 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 67 VFGTICILFTLSPQLAPVLGLLMLAVSVLVAVYKRSTVPVYKSHGLAQATMSDCVSETFSAIRTVRSFSGE----KRQMS 142
Cdd:cd18555 129 LVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEkniyKKWEN 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 143 IFGSQILAYKLSGLKLGTFKSINESITrvavYISLLALYCLGGSKVKTGELAVGTVVSFigYTFTLTFA--VQGLVNTFG 220
Cdd:cd18555 209 LFKKQLKAFKKKERLSNILNSISSSIQ----FIAPLLILWIGAYLVINGELTLGELIAF--SSLAGSFLtpIVSLINSYN 282
|
170
....*....|..
gi 145334131 221 DLRGTFAAIDRI 232
Cdd:cd18555 283 QFILLKSYLERL 294
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
319-531 |
2.87e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 50.40 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 319 LDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVrMFDKSEWAKVVSIVNQEPVLFSLSVAENIA 398
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISDVHQNMGYCPQFDAIDDLLTGREHL 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 399 Y------GLPNEHVSKddiikaakaaNAHDFIISLpqGYDTLVGERGGLLSGGQRQRVAIARSLLKNAPILILDEATSAL 472
Cdd:TIGR01257 2034 YlyarlrGVPAEEIEK----------VANWSIQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGM 2101
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145334131 473 DAVSERLVQSALNRLMKD-RTTLVIAHRLSTVQS-ANQIAVCSDGKIIELGTHSELVAQKG 531
Cdd:TIGR01257 2102 DPQARRMLWNTIVSIIREgRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSKFG 2162
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
319-510 |
2.94e-06 |
|
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: 47.35 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 319 LDGLSLTLNSGTVTALVGSSGAGKSTIvqllarfyeptqgritvggedvrmfdksewakvvsivnqepvLFSLSVAENIA 398
Cdd:cd03227 11 FVPNDVTFGEGSLTIITGPNGSGKSTI------------------------------------------LDAIGLALGGA 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 399 YglPNEHVSKDDIIKAAKAANAHDFIISLPQgydtlvgergglLSGGQRQRVAIARSL----LKNAPILILDEATSALDA 474
Cdd:cd03227 49 Q--SATRRRSGVKAGCIVAAVSAELIFTRLQ------------LSGGEKELSALALILalasLKPRPLYILDEIDRGLDP 114
|
170 180 190
....*....|....*....|....*....|....*..
gi 145334131 475 VS-ERLVQSALNRLMKDRTTLVIAHRLSTVQSANQIA 510
Cdd:cd03227 115 RDgQALAEAILEHLVKGAQVIVITHLPELAELADKLI 151
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
441-509 |
5.25e-06 |
|
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: 49.67 E-value: 5.25e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145334131 441 LLSGGQRQRVAIArsLL------KNAPILILDEATSALD-AVSERLVQsaLNRLMKDRTT-LVIAHRLSTVQSANQI 509
Cdd:TIGR02168 1089 LLSGGEKALTALA--LLfaifkvKPAPFCILDEVDAPLDdANVERFAN--LLKEFSKNTQfIVITHNKGTMEVADQL 1161
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
309-476 |
6.11e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.96 E-value: 6.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 309 AYPlrPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGR------ITVGgedvrmfdksewakvvsIV 382
Cdd:PRK11819 15 VVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEarpapgIKVG-----------------YL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 383 NQEPVL-FSLSVAENIAYGLP------------NEHVSKDDIikaakaanahDFiislpqgyDTLVGERGGL-------- 441
Cdd:PRK11819 76 PQEPQLdPEKTVRENVEEGVAevkaaldrfneiYAAYAEPDA----------DF--------DALAAEQGELqeiidaad 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145334131 442 --------------------------LSGGQRQRVAIARSLLKNAPILILDEATSALDAVS 476
Cdd:PRK11819 138 awdldsqleiamdalrcppwdakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
315-522 |
1.47e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.42 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 315 DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVqLLARFYEPTQGRitvggedvRMFDKSEW-----AKVVSIVNQEPVLF 389
Cdd:NF000106 25 EVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGR--------RPWRF*TWcanrrALRRTIG*HRPVR* 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 390 ----SLSVAENIAYGLPNEHVSKDDIIKAAKAANAHdfiISLPQGydtlVGERGGLLSGGQRQRVAIARSLLKNAPILIL 465
Cdd:NF000106 96 grreSFSGRENLYMIGR*LDLSRKDARARADELLER---FSLTEA----AGRAAAKYSGGMRRRLDLAASMIGRPAVLYL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145334131 466 DEATSALDAVSERLVQSALNRLMKDRTTLV-----------IAHRLSTVQSANQIAvcsDGKIIELGT 522
Cdd:NF000106 169 DEPTTGLDPRTRNEVWDEVRSMVRDGATVLlttqymeeaeqLAHELTVIDRGRVIA---DGKVDELKT 233
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
12-201 |
1.75e-05 |
|
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: 350056 [Multi-domain] Cd Length: 294 Bit Score: 46.74 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 12 LRAQIFRRVLIQKAEFFDKYKVGELTGLLTSdlgalnsivndnISRDRGF---RAFTEVFGTIC------ILFTLSPQLA 82
Cdd:cd18783 77 LALRTFDRLLSLPIDFFERTPAGVLTKHMQQ------------IERIRQFltgQLFGTLLDATSllvflpVLFFYSPTLA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 83 PVL----GLLMLAVSVLVAVYKRSTVPVYKSHGLAQATMSdcvsETFSAIRTVRSFSGEKRQMSIFGSQILAYKLSGLKL 158
Cdd:cd18783 145 LVVlafsALIALIILAFLPPFRRRLQALYRAEGERQAFLV----ETVHGIRTVKSLALEPRQRREWDERVARAIRARFAV 220
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 145334131 159 GTFKSINESITRVAVYISLLALYCLGGSKVKTGELAVGTVVSF 201
Cdd:cd18783 221 GRLSNWPQTLTGPLEKLMTVGVIWVGAYLVFAGSLTVGALIAF 263
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
319-509 |
1.88e-05 |
|
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: 45.39 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 319 LDGLSLTLNSGTVTALVGSSGAGKSTIVQllARFYEPTQGRItvggedvrmfdksewAKVVSIVNQEPVLF--SLSvaen 396
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYASGKARL---------------ISFLPKFSRNKLIFidQLQ---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 397 iayglpnehvskddiikaakaanahdFIISLPQGYDTLvGERGGLLSGGQRQRVAIARSLLKNAP--ILILDEATSALDA 474
Cdd:cd03238 70 --------------------------FLIDVGLGYLTL-GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQ 122
|
170 180 190
....*....|....*....|....*....|....*.
gi 145334131 475 VSERLVQSALNRLM-KDRTTLVIAHRLSTVQSANQI 509
Cdd:cd03238 123 QDINQLLEVIKGLIdLGNTVILIEHNLDVLSSADWI 158
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
317-473 |
2.02e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.42 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 317 KVL-DGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGgEDVRMfdksewakvvSIVNQ-----EPvlfS 390
Cdd:PRK11819 337 RLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG-ETVKL----------AYVDQsrdalDP---N 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 391 LSVAENIAYGLpnehvskddiikaakaanahDFIislpqgydtLVGER--------------G-------GLLSGGQRQR 449
Cdd:PRK11819 403 KTVWEEISGGL--------------------DII---------KVGNReipsrayvgrfnfkGgdqqkkvGVLSGGERNR 453
|
170 180
....*....|....*....|....
gi 145334131 450 VAIARSLLKNAPILILDEATSALD 473
Cdd:PRK11819 454 LHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
442-503 |
2.83e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.55 E-value: 2.83e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145334131 442 LSGGQRQRVAIARSLLKNAPILILDEATSALDAVSERLVQSALNRLMKD-RTTLV------------IAHRLSTV 503
Cdd:PRK10938 402 LSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEgETQLLfvshhaedapacITHRLEFV 476
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
8-234 |
2.86e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 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 type 3 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. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). 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. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 45.96 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 8 VMAILRA------QIFRRVLIQKAEFFDKYKVGELTGLLTSDLGALNSIVNDNISRdrGFRAFTEVFGTICILFTLSPQL 81
Cdd:cd18580 64 VLAGLRAsrrlhdKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLD--FLQSLFSVLGSLIVIAIVSPYF 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 82 APVLGLLMLAVSVLVAVYKRSTV-----------PVYkSHglaqatmsdcVSETFSAIRTVRSFSGEKRQMSIF-----G 145
Cdd:cd18580 142 LIVLPPLLVVYYLLQRYYLRTSRqlrrlesesrsPLY-SH----------FSETLSGLSTIRAFGWQERFIEENlrlldA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 146 SQILAYklsglklgTFKSIN-------ESItrVAVYISLLALYCLGGSKVKTGELaVGTVVSfigYTFTLTFAVQGLVNT 218
Cdd:cd18580 211 SQRAFY--------LLLAVQrwlglrlDLL--GALLALVVALLAVLLRSSISAGL-VGLALT---YALSLTGSLQWLVRQ 276
|
250
....*....|....*.
gi 145334131 219 FGDLRGTFAAIDRINS 234
Cdd:cd18580 277 WTELETSMVSVERILE 292
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
301-517 |
3.06e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 301 VCLDDVHFAYPLRPdvKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEdVRMfdksewakvvs 380
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAK-VRM----------- 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 381 ivnqepVLFSlsvaeniayglpNEHVSKDDIIKAAKAANAHDFIISLPQGYDTLVGE---RGGL-------LSGGQRQRV 450
Cdd:PLN03073 575 ------AVFS------------QHHVDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGSfgvTGNLalqpmytLSGGQKSRV 636
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 451 AIARSLLKNAPILILDEATSA--LDAVsERLVQSAlnrLMKDRTTLVIAHRLSTVQ-SANQIAVCSDGKI 517
Cdd:PLN03073 637 AFAKITFKKPHILLLDEPSNHldLDAV-EALIQGL---VLFQGGVLMVSHDEHLISgSVDELWVVSEGKV 702
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
317-501 |
3.47e-05 |
|
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: 46.67 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 317 KVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGgEDVRMFdksewakvvsIVNQEPVLFSLSVAEN 396
Cdd:TIGR00954 466 VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP-AKGKLF----------YVPQRPYMTLGTLRDQ 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 397 IAYglPNehvSKDDIIKAAKAANAHDFIISLPQGYDTLvgERGG----------LLSGGQRQRVAIARSLLKNAPILILD 466
Cdd:TIGR00954 535 IIY--PD---SSEDMKRRGLSDKDLEQILDNVQLTHIL--EREGgwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILD 607
|
170 180 190
....*....|....*....|....*....|....*..
gi 145334131 467 EATSALdAVSerlVQSALNRLMKDR--TTLVIAHRLS 501
Cdd:TIGR00954 608 ECTSAV-SVD---VEGYMYRLCREFgiTLFSVSHRKS 640
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
299-517 |
3.66e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 46.36 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 299 GDVCLDDVHFA--YPLRPDVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPT-QGRITVGGE--DVRMFDKS 373
Cdd:TIGR02633 254 GDVILEARNLTcwDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKpvDIRNPAQA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 374 EWAKVVSIV---NQEPVLFSLSVAENIAYGLPNEHVSKDDIIKAAKAANAHDFI--ISLPQGYDTLVGERgglLSGGQRQ 448
Cdd:TIGR02633 334 IRAGIAMVPedrKRHGIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIqrLKVKTASPFLPIGR---LSGGNQQ 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145334131 449 RVAIARSLLKNAPILILDEATSALDAVSERLVQSALNRLMKDRTTL-VIAHRLSTVQS-ANQIAVCSDGKI 517
Cdd:TIGR02633 411 KAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIiVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
441-509 |
3.89e-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: 44.76 E-value: 3.89e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145334131 441 LLSGGQRQRVAIArsLL------KNAPILILDEATSALDAV-SERLVQsALNRLMKDRTTLVIAHRLSTVQSANQI 509
Cdd:cd03278 113 LLSGGEKALTALA--LLfaifrvRPSPFCVLDEVDAALDDAnVERFAR-LLKEFSKETQFIVITHRKGTMEAADRL 185
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
319-521 |
4.62e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.19 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 319 LDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEdvrmfdksewakvVSIVNQEPVLF-SLSVAENI 397
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-------------VSVIAISAGLSgQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 398 AY-----GLPNEHVsKDDIIKAAKAANAHDFIISLPQGYdtlvgerggllSGGQRQRVAIARSLLKNAPILILDEATSAL 472
Cdd:PRK13546 107 EFkmlcmGFKRKEI-KAMTPKIIEFSELGEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSVG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 145334131 473 DavsERLVQSALNRLMK----DRTTLVIAHRLSTVQS-ANQIAVCSDGKIIELG 521
Cdd:PRK13546 175 D---QTFAQKCLDKIYEfkeqNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYG 225
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
331-509 |
4.80e-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: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 331 VTALVGSSGAGKSTIVQ--LLARFYE-PTQGRITVGGEDVrMFDKSEWAKV---VSIVNQEP--VLFSLSVAENIAYglp 402
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEalKYALTGElPPNSKGGAHDPKL-IREGEVRAQVklaFENANGKKytITRSLAILENVIF--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 403 nehvskddiikaakaanahdfiisLPQG-YDTLVGERGGLLSGGQRQ------RVAIARSLLKNAPILILDEATSALDav 475
Cdd:cd03240 100 ------------------------CHQGeSNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLD-- 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 145334131 476 SERlVQSALNRLMKDRTTL------VIAHRLSTVQSANQI 509
Cdd:cd03240 154 EEN-IEESLAEIIEERKSQknfqliVITHDEELVDAADHI 192
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
430-521 |
5.76e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 44.91 E-value: 5.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 430 GYDTLvGERGGLLSGGQRQRVAIARSLLKNAP---ILILDEATSALDAVSERLVQSALNRLM-KDRTTLVIAHRLSTVQS 505
Cdd:cd03271 159 GYIKL-GQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVdKGNTVVVIEHNLDVIKC 237
|
90
....*....|....*.
gi 145334131 506 ANQiavcsdgkIIELG 521
Cdd:cd03271 238 ADW--------IIDLG 245
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
430-521 |
1.02e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.39 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 430 GYDTLvGERGGLLSGGQRQRVAIARSLLKNA---PILILDEATSALDAVSERLVQSALNRLM-KDRTTLVIAHRLSTVQS 505
Cdd:TIGR00630 819 GYIRL-GQPATTLSGGEAQRIKLAKELSKRStgrTLYILDEPTTGLHFDDIKKLLEVLQRLVdKGNTVVVIEHNLDVIKT 897
|
90
....*....|....*.
gi 145334131 506 ANQiavcsdgkIIELG 521
Cdd:TIGR00630 898 ADY--------IIDLG 905
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
315-544 |
1.14e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 44.62 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 315 DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLA------------RFYEPTqgRITVggEDVRMFDKSEWAKvvsiv 382
Cdd:PRK10938 15 DTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAgelpllsgerqsQFSHIT--RLSF--EQLQKLVSDEWQR----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 383 NQEPVL------FSLSVAENIayglpNEHVSKDDIIKAAKAANahdfiislpqGYDTLVGERGGLLSGGQRQRVAIARSL 456
Cdd:PRK10938 86 NNTDMLspgeddTGRTTAEII-----QDEVKDPARCEQLAQQF----------GITALLDRRFKYLSTGETRKTLLCQAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 457 LKNAPILILDEATSALDAVSERLVQSALNRLMKDRTTLV-IAHRLSTVQS-ANQIAVCSDGKIIELGTHSELVAQkgsya 534
Cdd:PRK10938 151 MSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVlVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ----- 225
|
250
....*....|
gi 145334131 535 SLVgtQRLAF 544
Cdd:PRK10938 226 ALV--AQLAH 233
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
280-533 |
1.27e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.88 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 280 KYYMSNlKSTNNLRTLTW-AGDvclDDVHFAyplrpdvkvLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQG 358
Cdd:PRK13545 13 KYKMYN-KPFDKLKDLFFrSKD---GEYHYA---------LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 359 RITVGGEdvrmfdksewAKVVSI---VNQEpvlfsLSVAENIA-----YGLPNEHVsKDDIIKAAKAANAHDFIISLPQG 430
Cdd:PRK13545 80 TVDIKGS----------AALIAIssgLNGQ-----LTGIENIElkglmMGLTKEKI-KEIIPEIIEFADIGKFIYQPVKT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 431 YdtlvgerggllSGGQRQRVAIARSLLKNAPILILDEATSALDAVSERLVQSALNRLM-KDRTTLVIAHRLSTVQSANQI 509
Cdd:PRK13545 144 Y-----------SSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKeQGKTIFFISHSLSQVKSFCTK 212
|
250 260
....*....|....*....|....*
gi 145334131 510 AV-CSDGKIIELGTHSELVAQKGSY 533
Cdd:PRK13545 213 ALwLHYGQVKEYGDIKEVVDHYDEF 237
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
12-201 |
1.75e-04 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 43.74 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 12 LRAQIFRRVLIQKAEFFDKYKVGELTGLLtSDLGALNSIVNDN---ISRDRGFrafteVFGTICILFTLSPQLA------ 82
Cdd:cd18782 77 LGGTIIDHLLRLPLGFFDKRPVGELSTRI-SELDTIRGFLTGTaltTLLDVLF-----SVIYIAVLFSYSPLLTlvvlat 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 83 -PVLGLLMLAVSvlvAVYKRSTVPVYKSHGLAQATMsdcvSETFSAIRTVRSFSGEKRQMSIFGSQILAYKLSGLKLGTF 161
Cdd:cd18782 151 vPLQLLLTFLFG---PILRRQIRRRAEASAKTQSYL----VESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVL 223
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 145334131 162 KSINESITRVAVYISLLALYCLGGSKVKTGELAVGTVVSF 201
Cdd:cd18782 224 GTTSGSLSQFLNKLSSLLVLWVGAYLVLRGELTLGQLIAF 263
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
315-532 |
2.05e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 44.35 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 315 DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRITVGGEDVRmfDKSEWAKVVSIV---------NQE 385
Cdd:NF033858 13 KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA--DARHRRAVCPRIaympqglgkNLY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 386 PvlfSLSVAENIayglpnehvskddiikaakaanahDFiislpqgYDTLVG----ERG----------GL---------- 441
Cdd:NF033858 91 P---TLSVFENL------------------------DF-------FGRLFGqdaaERRrridellratGLapfadrpagk 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 442 LSGGQRQRVAIARSLLKNAPILILDEATSALDAVSER----LVqsalNRLMKDRTTL-VIahrlstVQSA--------NQ 508
Cdd:NF033858 137 LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRqfweLI----DRIRAERPGMsVL------VATAymeeaerfDW 206
|
250 260
....*....|....*....|....
gi 145334131 509 IAVCSDGKIIELGTHSELVAQKGS 532
Cdd:NF033858 207 LVAMDAGRVLATGTPAELLARTGA 230
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
303-531 |
2.65e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.73 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 303 LDDVHFAYPLRPdvkVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRI------TVG----------GED 366
Cdd:PRK15064 322 VENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwsenaNIGyyaqdhaydfEND 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 367 VRMFD-KSEWAK-------VVSIVNQepVLFslsvaeniayglpnehvSKDDiikaakaanahdfiislpqgydtlVGER 438
Cdd:PRK15064 399 LTLFDwMSQWRQegddeqaVRGTLGR--LLF-----------------SQDD------------------------IKKS 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 439 GGLLSGGQRQRVAIARSLLKNAPILILDEATSALDAVSERLVQSALNrlMKDRTTLVIAHRLSTVQS-ANQIAVCSDGKI 517
Cdd:PRK15064 436 VKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALE--KYEGTLIFVSHDREFVSSlATRIIEITPDGV 513
|
250
....*....|....*
gi 145334131 518 IE-LGTHSELVAQKG 531
Cdd:PRK15064 514 VDfSGTYEEYLRSQG 528
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
441-509 |
6.93e-04 |
|
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: 42.65 E-value: 6.93e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145334131 441 LLSGGQRQRVAIArsLL------KNAPILILDEATSALDAVSERLVQSALNRLMKDRTTLVIAHRLSTVQSANQI 509
Cdd:pfam02463 1077 LLSGGEKTLVALA--LIfaiqkyKPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKL 1149
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
315-360 |
9.08e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.08 E-value: 9.08e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 145334131 315 DVKVLDGLSLTLNSGTVTALVGSSGAGKSTIVQLLARFYEPTQGRI 360
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI 369
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
442-473 |
9.86e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 41.84 E-value: 9.86e-04
10 20 30
....*....|....*....|....*....|..
gi 145334131 442 LSGGQRQRVAIARSLLKNAPILILDEATSALD 473
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| ABC_6TM_NdvA_beta-glucan_exporter_like |
cd18562 |
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar ... |
75-205 |
1.22e-03 |
|
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar proteins; This group represents the six-transmembrane domain of NdvA, an ATP-dependent exporter of cyclic beta glucans, and similar proteins. NdvA is required for nodulation of legume roots and is involved in beta-(1,2)-glucan export to the periplasm. NdvA mutants in Brucella abortus and Sinorhizobium meliloti have been shown to exhibit decreased virulence in mice and inhibit intracellular multiplication in HeLa cells. These results suggest that cyclic beta-(1,2)-glucan is required to transport into the periplasmatic space to function as a virulence factor. 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: 350006 [Multi-domain] Cd Length: 289 Bit Score: 41.07 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 75 FTLSPQLAPVLGLLMLAVSVLVAVYKRSTvpvykSHGLAQA-----TMSDCVSETFSAIRTVRSFS---GEKRQMSIFGS 146
Cdd:cd18562 132 LWMNWRLALLLVVLAAVYAALNRLVMRRT-----KAGQAAVeehhsALSGRVGDVIGNVTVVQSYTrlaAETSALRGITR 206
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 145334131 147 QILAYKLSGLklgTFKSINESITRVAVYISLLALYCLGGSKVKTGELAVGTVVSFIGYT 205
Cdd:cd18562 207 RLLAAQYPVL---NWWALASVLTRAASTLTMVAIFALGAWLVQRGELTVGEIVSFVGFA 262
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
442-533 |
1.23e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.60 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 442 LSGGQRQRVAIARSLLKNA---PILILDEATSAL--DAVSeRLVQsALNRLM-KDRTTLVIAHRLSTVQSANQIAvcsD- 514
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLhfEDIR-KLLE-VLHRLVdKGNTVVVIEHNLDVIKTADWII---Dl 905
|
90 100
....*....|....*....|....*..
gi 145334131 515 --------GKIIELGTHSELVAQKGSY 533
Cdd:PRK00349 906 gpeggdggGEIVATGTPEEVAKVEASY 932
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
443-545 |
6.06e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.46 E-value: 6.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 443 SGGQRQRVAIARSLLKNAPILILDEATSALDAVSERLVQSALNRLMKdrTTLVIAHRLSTVQSanqiaVCSDgkIIELgT 522
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK--TFIVVSHAREFLNT-----VVTD--ILHL-H 415
|
90 100 110
....*....|....*....|....*....|
gi 145334131 523 HSELVAQKGSYASL-------VGTQRLAFE 545
Cdd:PLN03073 416 GQKLVTYKGDYDTFertreeqLKNQQKAFE 445
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
442-533 |
6.69e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.24 E-value: 6.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334131 442 LSGGQRQRVAIARSLLKNAP---ILILDEATSAL--DAVsERLVQsALNRLMkDR--TTLVIAHRLSTVQSAnqiavcsD 514
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTgktLYILDEPTTGLhfHDI-RKLLE-VLHRLV-DKgnTVVVIEHNLDVIKTA-------D 896
|
90 100 110
....*....|....*....|....*....|..
gi 145334131 515 -------------GKIIELGTHSELVAQKGSY 533
Cdd:COG0178 897 wiidlgpeggdggGEIVAEGTPEEVAKVKASY 928
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
440-473 |
7.13e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 38.94 E-value: 7.13e-03
10 20 30
....*....|....*....|....*....|....
gi 145334131 440 GLLSGGQRQRVAIARSLLKNAPILILDEATSALD 473
Cdd:PRK10982 390 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID 423
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
426-473 |
7.52e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.11 E-value: 7.52e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 145334131 426 SLPQGYDTLvgerggllSGGQRQ------RVAIARSLLKNAPILILDEATSALD 473
Cdd:PRK01156 794 GMVEGIDSL--------SGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLD 839
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
442-473 |
8.78e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 38.78 E-value: 8.78e-03
10 20 30
....*....|....*....|....*....|..
gi 145334131 442 LSGGQRQRVAIARSLLKNAPILILDEATSALD 473
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| |
