|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-575 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 673.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 1 MESMKWIWQYVRKYRLLMIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMC 80
Cdd:COG1132 6 RKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 81 ERIGQNSLFRIREDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTL 160
Cdd:COG1132 86 ARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 161 ALVIVTPLIAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSR 240
Cdd:COG1132 166 IVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 241 TYLPVLDSLAGMLVVITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASSFKIQDMMATDAKIP 320
Cdd:COG1132 246 LFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 321 IHAE-KPAPSLQGHVEFKNVSFHFEDDpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVD 399
Cdd:COG1132 326 DPPGaVPLPPVRGEIEFENVSFSYPGD--RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 400 ARKWHVRELRNHIATVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQ 479
Cdd:COG1132 404 IRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 480 RISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLA 559
Cdd:COG1132 484 RIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLA 563
|
570
....*....|....*.
gi 1755737710 560 EKGYYFDIYNKQLGTE 575
Cdd:COG1132 564 RGGLYARLYRLQFGEE 579
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-572 |
5.07e-170 |
|
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: 499.75 E-value: 5.07e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 3 SMKWIWQYVRKYRLLMIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCER 82
Cdd:COG2274 143 GLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLR 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 83 IGQNSLFRIREDLYKKLQSLDFDFFNNTRVGDIMARMtGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLAL 162
Cdd:COG2274 223 LGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVV 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 163 VIVTPLIAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTY 242
Cdd:COG2274 302 LLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 243 LPVLDSLAGMLVVITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPM-RMSGwLINDVQRFIASSFKIQDMMATDAKIPI 321
Cdd:COG2274 382 STLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVaQLIG-LLQRFQDAKIALERLDDILDLPPEREE 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 322 HAEK-PAPSLQGHVEFKNVSFHFEDDpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDA 400
Cdd:COG2274 461 GRSKlSLPRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDL 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 401 RKWHVRELRNHIATVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQR 480
Cdd:COG2274 540 RQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQR 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 481 ISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAE 560
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
570
....*....|..
gi 1755737710 561 KGYYFDIYNKQL 572
Cdd:COG2274 700 KGLYAELVQQQL 711
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
7-574 |
2.40e-128 |
|
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: 387.92 E-value: 2.40e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 7 IWQYVRKYRLLMIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQN 86
Cdd:TIGR02203 5 LWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLLSWVSNK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 87 SLFRIREDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVT 166
Cdd:TIGR02203 85 VVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVML 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 167 PLIAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVL 246
Cdd:TIGR02203 165 PVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPIT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 247 DSLAGMLVVITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASSFKIQDMMATdakiPIHAE-- 324
Cdd:TIGR02203 245 QLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDS----PPEKDtg 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 325 -KPAPSLQGHVEFKNVSFHFEDDpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKW 403
Cdd:TIGR02203 321 tRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 404 HVRELRNHIATVMQDIFLFSDTIEGNIAFGAP-DATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRIS 482
Cdd:TIGR02203 400 TLASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 483 LARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAEKG 562
Cdd:TIGR02203 480 IARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNG 559
|
570
....*....|..
gi 1755737710 563 YYFDIYNKQLGT 574
Cdd:TIGR02203 560 LYAQLHNMQFRE 571
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
4-564 |
2.76e-128 |
|
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: 387.90 E-value: 2.76e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 4 MKWIWQYVRKYRLLMIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTII---RTICRYtYQIMc 80
Cdd:TIGR02204 6 LAALWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMIDHGFSKDSSGLLNRYFAFLLVVALVlalGTAARF-YLVT- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 81 eRIGQNSLFRIREDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTL 160
Cdd:TIGR02204 84 -WLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 161 ALVIVTPLIAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEdfkkRNLDSADVSR 240
Cdd:TIGR02204 163 LVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVE----KAYEAARQRI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 241 TYLPVLDSLAGML----VVITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASSFKIQDMMAT- 315
Cdd:TIGR02204 239 RTRALLTAIVIVLvfgaIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAe 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 316 -DAKIPIHAEKPAPSLQGHVEFKNVSFHFEDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEIL 394
Cdd:TIGR02204 319 pDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRIL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 395 IDGVDARKWHVRELRNHIATVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLS 474
Cdd:TIGR02204 399 LDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLS 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 475 GGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTH 554
Cdd:TIGR02204 479 GGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTH 558
|
570
....*....|
gi 1755737710 555 SSLLAEKGYY 564
Cdd:TIGR02204 559 AELIAKGGLY 568
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
18-309 |
1.13e-125 |
|
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: 370.99 E-value: 1.13e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 18 MIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFRIREDLYK 97
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 98 KLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTMKMS 177
Cdd:cd18542 81 HLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 178 SKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVVIT 257
Cdd:cd18542 161 KKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1755737710 258 LIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASSFKI 309
Cdd:cd18542 241 LWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
82-571 |
4.00e-122 |
|
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: 373.00 E-value: 4.00e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 82 RIGQNSLFRIREDLYKKLQSLDFDFFNNTRVGDimarMTGD----TDAIRHFVSWVSYNILENVFLFSFAIIIMAAI-DW 156
Cdd:COG5265 104 RVTQRAVRRLALEVFRHLHALSLRFHLERQTGG----LSRDiergTKGIEFLLRFLLFNILPTLLEIALVAGILLVKyDW 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 157 KLTLALVIVTPLIAILTMKMSskaqpvfyEIRESFSRlnSMVEENISGNRV----------VKAFAREDFEMKKFHEHNE 226
Cdd:COG5265 180 WFALITLVTVVLYIAFTVVVT--------EWRTKFRR--EMNEADSEANTRavdsllnyetVKYFGNEAREARRYDEALA 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 227 DFKKrnldsADV-SRTYLPVLDS-----LAGMLVVItLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWlindVQ 300
Cdd:COG5265 250 RYER-----AAVkSQTSLALLNFgqaliIALGLTAM-MLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGF----VY 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 301 RFIASSF-KIQDM---MATDAKIpihAEKP-APSL---QGHVEFKNVSFHFedDPNTDVLKNISLKASPGQTIAILGETG 372
Cdd:COG5265 320 REIRQALaDMERMfdlLDQPPEV---ADAPdAPPLvvgGGEVRFENVSFGY--DPERPILKGVSFEVPAGKTVAIVGPSG 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 373 AGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIATVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADAD 452
Cdd:COG5265 395 AGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIH 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 453 HFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRIS 532
Cdd:COG5265 475 DFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLS 554
|
490 500 510
....*....|....*....|....*....|....*....
gi 1755737710 533 SVKEADEILILNHGEIIERGTHSSLLAEKGYYFDIYNKQ 571
Cdd:COG5265 555 TIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQ 593
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
12-564 |
1.47e-117 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 364.43 E-value: 1.47e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 12 RKYRLLMIGvFILIFIASGISIIYPLLGGKVIDDVV----YQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQns 87
Cdd:TIGR00958 158 RDWPWLISA-FVFLTLSSLGEMFIPFYTGRVIDTLGgdkgPPALASAIFFMCLLSIASSVSAGLRGGSFNYTMARINL-- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 88 lfRIREDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRhfvSWVSYNIleNVFLFSF-----AIIIMAAIDWKLTLAL 162
Cdd:TIGR00958 235 --RIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMS---RSLSLNV--NVLLRNLvmllgLLGFMLWLSPRLTMVT 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 163 VIVTPLIAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTY 242
Cdd:TIGR00958 308 LINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGY 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 243 LpVLDSLAGMLV-VITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASSFKIQDMMATDAKIPI 321
Cdd:TIGR00958 388 L-WTTSVLGMLIqVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPL 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 322 HAEKPAPSLQGHVEFKNVSFHFEDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDAR 401
Cdd:TIGR00958 467 TGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLV 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 402 KWHVRELRNHIATVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRI 481
Cdd:TIGR00958 547 QYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRI 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 482 SLARALLKNPSILILDDTTSAVDMETEVKIQgELKKiTENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAEK 561
Cdd:TIGR00958 627 AIARALVRKPRVLILDEATSALDAECEQLLQ-ESRS-RASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
...
gi 1755737710 562 GYY 564
Cdd:TIGR00958 705 GCY 707
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
334-568 |
1.04e-112 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 335.35 E-value: 1.04e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDPNTdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIA 413
Cdd:cd03251 1 VEFKNVTFRYPGDGPP-VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 414 TVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSI 493
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1755737710 494 LILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAEKGYYFDIY 568
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
21-571 |
5.27e-112 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 345.93 E-value: 5.27e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 21 VFILIFIASgISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIIST-IIRTICRYTYQIMcerigqnsLF--------RI 91
Cdd:PRK10789 1 VALLIIIAM-LQLIPPKVVGIIVDGVTEQHMTTGQILMWIGTMVLIaVVVYLLRYVWRVL--------LFgasyqlavEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 92 REDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRhFVSWVSYNILENVFLFSFAIIIMAA--IDWKLTLALVIVTPLI 169
Cdd:PRK10789 72 REDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVV-FAAGEGVLTLVDSLVMGCAVLIVMStqISWQLTLLALLPMPVM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 170 AILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSL 249
Cdd:PRK10789 151 AIMIKRYGDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 250 AGMLVVITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASSFKIQDMMAtDAKIPIHAEKPAPS 329
Cdd:PRK10789 231 IGMANLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLA-EAPVVKDGSEPVPE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 330 LQGHVEFKNVSFHFeddPNTD--VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRE 407
Cdd:PRK10789 310 GRGELDVNIRQFTY---PQTDhpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 408 LRNHIATVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARAL 487
Cdd:PRK10789 387 WRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARAL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 488 LKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAEKGYYFDI 567
Cdd:PRK10789 467 LLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDM 546
|
....
gi 1755737710 568 YNKQ 571
Cdd:PRK10789 547 YRYQ 550
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
153-564 |
1.04e-111 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 345.41 E-value: 1.04e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 153 AIDWKLTL---ALVIVTPLIAILTMKMSSKAQPvfyEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHnedfk 229
Cdd:PRK13657 153 FMNWRLSLvlvVLGIVYTLITTLVMRKTKDGQA---AVEEHYHDLFAHVSDAIGNVSVVQSYNRIEAETQALRDI----- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 230 KRNLDSADvsrtyLPVLD--SLAGML--------VVITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPM-RMSGWlIND 298
Cdd:PRK13657 225 ADNLLAAQ-----MPVLSwwALASVLnraastitMLAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLdQVVAF-INQ 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 299 VqrfIASSFKIQDMMATDAKIPIHAEKP-APSLQ---GHVEFKNVSFHFedDPNTDVLKNISLKASPGQTIAILGETGAG 374
Cdd:PRK13657 299 V---FMAAPKLEEFFEVEDAVPDVRDPPgAIDLGrvkGAVEFDDVSFSY--DNSRQGVEDVSFEAKPGQTVAIVGPTGAG 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 375 KSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIATVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHF 454
Cdd:PRK13657 374 KSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDF 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 455 IETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSV 534
Cdd:PRK13657 454 IERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTV 533
|
410 420 430
....*....|....*....|....*....|
gi 1755737710 535 KEADEILILNHGEIIERGTHSSLLAEKGYY 564
Cdd:PRK13657 534 RNADRILVFDNGRVVESGSFDELVARGGRF 563
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-562 |
7.84e-111 |
|
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: 342.51 E-value: 7.84e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 5 KWIWQYVRKYRLLMIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKT-NLLIPLLLIMIISTIIRTICRYTYQIMCERI 83
Cdd:COG4988 6 KRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAPlSALLPLLGLLLAVLLLRALLAWLRERAAFRA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 84 GQNSLFRIREDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVS-WVSYNILenVFLFSFAI-IIMAAIDWKLTLA 161
Cdd:COG4988 86 AARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFArYLPQLFL--AALVPLLIlVAVFPLDWLSGLI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 162 LVIVTPLI---AILTMKMSSKAQpvfYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRN------ 232
Cdd:COG4988 164 LLVTAPLIplfMILVGKGAAKAS---RRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTmkvlrv 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 233 --LDSAdvsrtylpVLDSLAGMLVVITLIFGGYLVIKGQMTLGdlVAFngFLWMLNG----PMR---------MSGwlin 297
Cdd:COG4988 241 afLSSA--------VLEFFASLSIALVAVYIGFRLLGGSLTLF--AAL--FVLLLAPefflPLRdlgsfyharANG---- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 298 dvqrfIASSFKIQDMMATDAKIPIHAEKPAPSLQG-HVEFKNVSFHFEDDPNtdVLKNISLKASPGQTIAILGETGAGKS 376
Cdd:COG4988 305 -----IAAAEKIFALLDAPEPAAPAGTAPLPAAGPpSIELEDVSFSYPGGRP--ALDGLSLTIPPGERVALVGPSGAGKS 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 377 TLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIATVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIE 456
Cdd:COG4988 378 TLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVA 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 457 TMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKE 536
Cdd:COG4988 458 ALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQ 537
|
570 580
....*....|....*....|....*.
gi 1755737710 537 ADEILILNHGEIIERGTHSSLLAEKG 562
Cdd:COG4988 538 ADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
67-569 |
4.02e-110 |
|
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: 340.98 E-value: 4.02e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 67 IIRTICRYtyqimCER-IGQNSLFRI----REDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHF---------VSW 132
Cdd:COG4987 66 IGRTVFRY-----LERlVSHDATLRLladlRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLylrvllpllVAL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 133 VSYnilenvflfSFAIIIMAAIDWK----LTLALVIVTPLIAILTMKMSSKAQpvfYEIRESFSRLNSMVEENISGNRVV 208
Cdd:COG4987 141 LVI---------LAAVAFLAFFSPAlalvLALGLLLAGLLLPLLAARLGRRAG---RRLAAARAALRARLTDLLQGAAEL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 209 KAFAREDFEMKKFHEHNEDFKK--RNLDSADVSRTYLPVLdsLAGMLVVITLIFGGYLVIKGQM--------TLGDLVAF 278
Cdd:COG4987 209 AAYGALDRALARLDAAEARLAAaqRRLARLSALAQALLQL--AAGLAVVAVLWLAAPLVAAGALsgpllallVLAALALF 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 279 NGFlwmlnGPMRMSGWLINDVqrfIASSFKIQDMMATDAKIPIHAEKPAPSLQGHVEFKNVSFHFEDDPnTDVLKNISLK 358
Cdd:COG4987 287 EAL-----APLPAAAQHLGRV---RAAARRLNELLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAG-RPVLDGLSLT 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 359 ASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIATVMQDIFLFSDTIEGNIAFGAPDAT 438
Cdd:COG4987 358 LPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDAT 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 439 MEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKI 518
Cdd:COG4987 438 DEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA 517
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1755737710 519 TENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAEKGYYFDIYN 569
Cdd:COG4987 518 LAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
334-571 |
1.39e-105 |
|
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: 317.56 E-value: 1.39e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIA 413
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 414 TVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSI 493
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1755737710 494 LILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAEKGYYFDIYNKQ 571
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-573 |
2.65e-104 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 326.21 E-value: 2.65e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 5 KWIWQYVRKYRL-LMIGVFILIFIASG----ISIIYPLLggkviDDVVYQNKTNLLIPLLLIMIISTIIRTICRY--TYQ 77
Cdd:PRK11176 14 RRLWPTIAPFKAgLIVAGVALILNAASdtfmLSLLKPLL-----DDGFGKADRSVLKWMPLVVIGLMILRGITSFisSYC 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 78 ImcERIGQNSLFRIREDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNIL-ENVFLFSFaIIIMAAIDW 156
Cdd:PRK11176 89 I--SWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVrEGASIIGL-FIMMFYYSW 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 157 KLTLALVIVTPLIAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSA 236
Cdd:PRK11176 166 QLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 237 DVSRTYLPVLDSLAGMLVVITLIFGGYLVIKGQMTLGDL-VAFNGFLWMlngpMRMSGWLIN---DVQRFIASS---FKI 309
Cdd:PRK11176 246 SASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTItVVFSSMIAL----MRPLKSLTNvnaQFQRGMAACqtlFAI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 310 QDMmATDAKIPIHAEKPApslQGHVEFKNVSFHFEDDpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPT 389
Cdd:PRK11176 322 LDL-EQEKDEGKRVIERA---KGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDID 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 390 SGEILIDGVDARKWHVRELRNHIATVMQDIFLFSDTIEGNIAFGAPDA-TMEDVRRMARIADADHFIETMPESYDTIVGE 468
Cdd:PRK11176 397 EGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 469 RGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEI 548
Cdd:PRK11176 477 NGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEI 556
|
570 580
....*....|....*....|....*
gi 1755737710 549 IERGTHSSLLAEKGYYFDIYNKQLG 573
Cdd:PRK11176 557 VERGTHAELLAQNGVYAQLHKMQFG 581
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
334-571 |
9.51e-103 |
|
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: 309.93 E-value: 9.51e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFedDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIA 413
Cdd:cd03253 1 IEFENVTFAY--DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 414 TVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSI 493
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1755737710 494 LILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAEKGYYFDIYNKQ 571
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
332-562 |
5.65e-102 |
|
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: 307.61 E-value: 5.65e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 332 GHVEFKNVSFHFedDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNH 411
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 412 IATVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNP 491
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1755737710 492 SILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAEKG 562
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
6-573 |
2.07e-98 |
|
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: 313.99 E-value: 2.07e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 6 WIWQYVRKYRLLMIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTI-------IRTicrYTYQI 78
Cdd:TIGR01846 129 WFIPAIIRYRKQFREVLLISLALQLFALVTPLLFQVVIDKVLVHRGLSTLSVLALAMLAVAIfepalggLRT---YLFAH 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 79 MCERIGqnslFRIREDLYKKLQSLDFDFFNNTRVGDIMARMTgDTDAIRHFVSWVSYNILENVFlfsFAIIIMAAIDW-- 156
Cdd:TIGR01846 206 LTSRID----VELGARLYRHLLGLPLGYFESRRVGDTVARVR-ELEQIRNFLTGSALTVVLDLL---FVVVFLAVMFFys 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 157 -KLTLALVIVTPLIAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDS 235
Cdd:TIGR01846 278 pTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRV 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 236 ADVSRTYLPVLDSLAGMLVVITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASSFKIQDMMAT 315
Cdd:TIGR01846 358 TNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDILNS 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 316 DAKiPIHAEKPA-PSLQGHVEFKNVSFHFEDDpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEIL 394
Cdd:TIGR01846 438 PTE-PRSAGLAAlPELRGAITFENIRFRYAPD-SPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVL 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 395 IDGVDARKWHVRELRNHIATVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLS 474
Cdd:TIGR01846 516 VDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLS 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 475 GGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTH 554
Cdd:TIGR01846 596 GGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRH 675
|
570
....*....|....*....
gi 1755737710 555 SSLLAEKGYYFDIYNKQLG 573
Cdd:TIGR01846 676 EELLALQGLYARLWQQQSG 694
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
153-565 |
4.86e-90 |
|
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: 289.10 E-value: 4.86e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 153 AIDWKLTLALV---IVTPLIAILTMKMSSKAQPVfyeIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEdfk 229
Cdd:TIGR01192 153 AMDWRLSIVLMvlgILYILIAKLVMQRTKNGQAA---VEHHYHNVFKHVSDSISNVSVVHSYNRIEAETSALKQFTN--- 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 230 krNLDSADVsrtylPVLD--SLAGML--------VVITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPM-RMSGWlind 298
Cdd:TIGR01192 227 --NLLSAQY-----PVLDwwALASGLnrmastisMMCILVIGTVLVIKGELSVGEVIAFIGFANLLIGRLdQMSGF---- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 299 VQRFIASSFKIQDMMATDAKIpIHAEKPA-----PSLQGHVEFKNVSFHFeddPNTDV-LKNISLKASPGQTIAILGETG 372
Cdd:TIGR01192 296 ITQIFEARAKLEDFFDLEDSV-FQREEPAdapelPNVKGAVEFRHITFEF---ANSSQgVFDVSFEAKAGQTVAIVGPTG 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 373 AGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIATVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADAD 452
Cdd:TIGR01192 372 AGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAH 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 453 HFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRIS 532
Cdd:TIGR01192 452 DFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLS 531
|
410 420 430
....*....|....*....|....*....|...
gi 1755737710 533 SVKEADEILILNHGEIIERGTHSSLLAEKGYYF 565
Cdd:TIGR01192 532 TVRNADLVLFLDQGRLIEKGSFQELIQKDGRFY 564
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
334-571 |
5.80e-85 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 264.35 E-value: 5.80e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIA 413
Cdd:cd03252 1 ITFEHVRFRYKPD-GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 414 TVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSI 493
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1755737710 494 LILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAEKGYYFDIYNKQ 571
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
106-564 |
1.17e-82 |
|
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: 272.97 E-value: 1.17e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 106 FFNNTRVGDIMARMTGDtDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLaLVIVTPLIAILTMKMSSKAQPVF- 184
Cdd:TIGR03796 244 FFAQRHAGDIASRVQLN-DQVAEFLSGQLATTALDAVMLVFYALLMLLYDPVLTL-IGIAFAAINVLALQLVSRRRVDAn 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 185 YEIRESFSRLNSMVEENISGNRVVKAFARED--------FEMKKFHEHNEdfkkrnLDSADVSRTYLP-VLDSLAGMLVv 255
Cdd:TIGR03796 322 RRLQQDAGKLTGVAISGLQSIETLKASGLESdffsrwagYQAKLLNAQQE------LGVLTQILGVLPtLLTSLNSALI- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 256 itLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPM-RMSGwLINDVQRFIASSFKIQDMM-------ATDAKIPIHAEKPA 327
Cdd:TIGR03796 395 --LVVGGLRVMEGQLTIGMLVAFQSLMSSFLEPVnNLVG-FGGTLQELEGDLNRLDDVLrnpvdplLEEPEGSAATSEPP 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 328 PSLQGHVEFKNVSFHFE--DDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHV 405
Cdd:TIGR03796 472 RRLSGYVELRNITFGYSplEPP---LIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPR 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 406 RELRNHIATVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLAR 485
Cdd:TIGR03796 549 EVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIAR 628
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1755737710 486 ALLKNPSILILDDTTSAVDMETEVKIQGELKKitENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAEKGYY 564
Cdd:TIGR03796 629 ALVRNPSILILDEATSALDPETEKIIDDNLRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAY 705
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
18-305 |
4.41e-82 |
|
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: 258.63 E-value: 4.41e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 18 MIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFRIREDLYK 97
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 98 KLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTMKMS 177
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 178 SKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVVIT 257
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1755737710 258 LIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIAS 305
Cdd:cd07346 241 LLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALAS 288
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
332-552 |
2.35e-78 |
|
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: 246.35 E-value: 2.35e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 332 GHVEFKNVSFHFEDDPNtDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNH 411
Cdd:cd03245 1 GRIEFRNVSFSYPNQEI-PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 412 IATVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNP 491
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1755737710 492 SILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERG 552
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
17-305 |
2.86e-78 |
|
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: 248.87 E-value: 2.86e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 17 LMIGVFILIfIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIM-IISTIIRTICRYTYQIMCERIGQNSLFRIREDL 95
Cdd:cd18541 1 YLLGILFLI-LVDLLQLLIPRIIGRAIDALTAGTLTASQLLRYALLiLLLALLIGIFRFLWRYLIFGASRRIEYDLRNDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 96 YKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTMK 175
Cdd:cd18541 80 FAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 176 MSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVV 255
Cdd:cd18541 160 LGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1755737710 256 ITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIAS 305
Cdd:cd18541 240 IVLWYGGRLVIRGTITLGDLVAFNSYLGMLIWPMMALGWVINLIQRGAAS 289
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
334-547 |
1.09e-76 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 240.36 E-value: 1.09e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDPNTdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIA 413
Cdd:cd03228 1 IEFKNVSFSYPGRPKP-VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 414 TVMQDIFLFSDTIEGNIafgapdatmedvrrmariadadhfietmpesydtivgergvgLSGGQKQRISLARALLKNPSI 493
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1755737710 494 LILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGE 547
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
107-575 |
3.31e-75 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 250.41 E-value: 3.31e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 107 FNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTMKMSSKAQPVFYE 186
Cdd:PRK10790 116 FDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAIMIFPAVLVVMVIYQRYSTPIVRR 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 187 IRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVV--ITLIFGgyL 264
Cdd:PRK10790 196 VRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFLLRPLLSLFSALILcgLLMLFG--F 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 265 VIKGQMTLGDLVAFNGFLWMLNGPmrmsgwLI------NDVQRFIASSFKIQDMMatDAKIPIHAEKPAPSLQGHVEFKN 338
Cdd:PRK10790 274 SASGTIEVGVLYAFISYLGRLNEP------LIelttqqSMLQQAVVAGERVFELM--DGPRQQYGNDDRPLQSGRIDIDN 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 339 VSFHFEDDpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIATVMQD 418
Cdd:PRK10790 346 VSFAYRDD--NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQD 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 419 IFLFSDTIEGNIAFGApDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDD 498
Cdd:PRK10790 424 PVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDE 502
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1755737710 499 TTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAEKGYYFDIYNKQLGTE 575
Cdd:PRK10790 503 ATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLAGE 579
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
11-569 |
5.72e-75 |
|
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: 252.35 E-value: 5.72e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 11 VRKYRLLMIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFR 90
Cdd:TIGR01193 151 ITRQKKLIVNIVIAAIIVTLISIAGSYYLQKIIDTYIPHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSID 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 91 IREDLYKKLQSLDFDFFNNTRVGDIMARMTgDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIA 170
Cdd:TIGR01193 231 IILSYIKHLFELPMSFFSTRRTGEIVSRFT-DASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFLLSLLSIPVYA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 171 ILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNL--DSADVSRTYLPVLDS 248
Cdd:TIGR01193 310 VIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFkyQKADQGQQAIKAVTK 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 249 LagMLVVITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASSFKIQDMMATDAK-IPIHAEKPA 327
Cdd:TIGR01193 390 L--ILNVVILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEfINKKKRTEL 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 328 PSLQGHVEFKNVSFHFedDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRE 407
Cdd:TIGR01193 468 NNLNGDIVINDVSYSY--GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHT 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 408 LRNHIATVMQDIFLFSDTIEGNIAFGA-PDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARA 486
Cdd:TIGR01193 546 LRQFINYLPQEPYIFSGSILENLLLGAkENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARA 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 487 LLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFiIAHRISSVKEADEILILNHGEIIERGTHSSLLAEKGYYFD 566
Cdd:TIGR01193 626 LLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDKTIIF-VAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYAS 704
|
...
gi 1755737710 567 IYN 569
Cdd:TIGR01193 705 LIH 707
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
149-543 |
8.52e-75 |
|
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: 247.59 E-value: 8.52e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 149 IIMAAI---DWKLTLALVIVTPLIAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHN 225
Cdd:TIGR02857 134 AILAAVfpqDWISGLILLLTAPLIPIFMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSS 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 226 EDFKKRN--------LDSAdvsrtylpVLDSLAGMLVVITLIFGGYLVIKGQMTLgdlvaFNGFLWML-----NGPMRMS 292
Cdd:TIGR02857 214 EEYRERTmrvlriafLSSA--------VLELFATLSVALVAVYIGFRLLAGDLDL-----ATGLFVLLlapefYLPLRQL 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 293 GWLINDVQRFIASSFKIQDMMATDAkIPIHAEKPAPSLQGH-VEFKNVSFHFEDDPNtdVLKNISLKASPGQTIAILGET 371
Cdd:TIGR02857 281 GAQYHARADGVAAAEALFAVLDAAP-RPLAGKAPVTAAPASsLEFSGVSVAYPGRRP--ALRPVSFTVPPGERVALVGPS 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 372 GAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIATVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADA 451
Cdd:TIGR02857 358 GAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGL 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 452 DHFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRI 531
Cdd:TIGR02857 438 DEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRL 517
|
410
....*....|..
gi 1755737710 532 SSVKEADEILIL 543
Cdd:TIGR02857 518 ALAALADRIVVL 529
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
330-548 |
1.42e-72 |
|
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: 231.59 E-value: 1.42e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 330 LQGHVEFKNVSFHFEDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELR 409
Cdd:cd03248 8 LKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 410 NHIATVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARALLK 489
Cdd:cd03248 88 SKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1755737710 490 NPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEI 548
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
18-309 |
1.02e-70 |
|
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: 229.32 E-value: 1.02e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 18 MIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMII----STIIRTICRYTYQIMCERIGQNSLFRIRE 93
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDVLIQLGPGGNTSLLLLLVLglagAYVLSALLGILRGRLLARLGERITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 94 DLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILT 173
Cdd:cd18563 81 DLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 174 MKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGML 253
Cdd:cd18563 161 YFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1755737710 254 VVITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASSFKI 309
Cdd:cd18563 241 TLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
141-548 |
3.08e-65 |
|
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: 222.70 E-value: 3.08e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 141 VFLFSFAIIIMAAIdwkLTLALVIVTPLIAILTMKMSSKAQpvfyeirESFSRLNSMVEENISGNRVVKAFAREDFEMKK 220
Cdd:COG4618 150 LFLFHPLLGLLALV---GALVLVALALLNERLTRKPLKEAN-------EAAIRANAFAEAALRNAEVIEAMGMLPALRRR 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 221 FHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVVITLIFGGYLVIKGQMTLGDLVAFNgflwMLNG----P--MRMSGW 294
Cdd:COG4618 220 WQRANARALALQARASDRAGGFSALSKFLRLLLQSAVLGLGAYLVIQGEITPGAMIAAS----ILMGralaPieQAIGGW 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 295 liNDVQRFIASSFKIQDMMATDAKIPIHAEKPAPslQGHVEFKNVSFHFeddPNTD--VLKNISLKASPGQTIAILGETG 372
Cdd:COG4618 296 --KQFVSARQAYRRLNELLAAVPAEPERMPLPRP--KGRLSVENLTVVP---PGSKrpILRGVSFSLEPGEVLGVIGPSG 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 373 AGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIATVMQDIFLFSDTIEGNIA-FGAPDAtmEDVRRMARIADA 451
Cdd:COG4618 369 SGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIArFGDADP--EKVVAAAKLAGV 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 452 DHFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVK----IQgELKKitENTTTFII 527
Cdd:COG4618 447 HEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAAlaaaIR-ALKA--RGATVVVI 523
|
410 420
....*....|....*....|.
gi 1755737710 528 AHRISSVKEADEILILNHGEI 548
Cdd:COG4618 524 THRPSLLAAVDKLLVLRDGRV 544
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
332-553 |
1.90e-63 |
|
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: 207.73 E-value: 1.90e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 332 GHVEFKNVSFHFEDDPNTdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNH 411
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPP-VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 412 IATVMQDIFLFSDTIEGNIA-FG-APDATMEDVRRMARIADadhFIETMPESYDTIVGERGVGLSGGQKQRISLARALLK 489
Cdd:cd03244 80 ISIIPQDPVLFSGTIRSNLDpFGeYSDEELWQALERVGLKE---FVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755737710 490 NPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGT 553
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
303-571 |
4.94e-63 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 217.39 E-value: 4.94e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 303 IASSFKIQDMMATDAKIPIHAEKPAPSLQGHVEFKNVSFHFEDDPNTdVLKNISLKASPGQTIAILGETGAGKSTLVNLI 382
Cdd:PRK11160 308 IASARRINEITEQKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQP-VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 383 CRFYDPTSGEILIDGVDARKWHVRELRNHIATVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETmPESY 462
Cdd:PRK11160 387 TRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLED-DKGL 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 463 DTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILI 542
Cdd:PRK11160 466 NAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICV 545
|
250 260
....*....|....*....|....*....
gi 1755737710 543 LNHGEIIERGTHSSLLAEKGYYFDIYNKQ 571
Cdd:PRK11160 546 MDNGQIIEQGTHQELLAQQGRYYQLKQRL 574
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
18-309 |
1.05e-62 |
|
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: 208.09 E-value: 1.05e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 18 MIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFRIREDLYK 97
Cdd:cd18545 2 LLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 98 KLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTMKMS 177
Cdd:cd18545 82 HLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 178 SKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVVIT 257
Cdd:cd18545 162 RRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTALV 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1755737710 258 LIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASSFKI 309
Cdd:cd18545 242 YWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
18-306 |
8.28e-62 |
|
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: 206.10 E-value: 8.28e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 18 MIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTI------IRTICRYTYQIMCERIGQNSLFRI 91
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGVDFSGLLRILLLllglylLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 92 REDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAI 171
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 172 LTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAG 251
Cdd:cd18547 161 VTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNFINN 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1755737710 252 MLVVITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASS 306
Cdd:cd18547 241 LGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGA 295
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
18-306 |
1.17e-61 |
|
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: 205.46 E-value: 1.17e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 18 MIGVFILIFIASGISIIYPLLGGKVIDDV-VYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFRIREDLY 96
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVtIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 97 KKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTMKM 176
Cdd:cd18778 81 DKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 177 SSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVVI 256
Cdd:cd18778 161 SKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1755737710 257 TLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPM-RMSGwLINDVQRFIASS 306
Cdd:cd18778 241 VLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPItSLHG-LNEMLQRALAGA 290
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
18-309 |
3.83e-61 |
|
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: 204.16 E-value: 3.83e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 18 MIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMI--ISTIIRTICRYTYQIMCERIGQNSLFRIREDL 95
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYIVPGQGDLQGLLLLALLylGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 96 YKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTMK 175
Cdd:cd18544 81 FSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 176 MSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVV 255
Cdd:cd18544 161 FRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1755737710 256 ITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASSFKI 309
Cdd:cd18544 241 LVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
67-530 |
3.34e-58 |
|
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: 203.36 E-value: 3.34e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 67 IIRTICRYtyqimCER-IGQNSLFRI----REDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENV 141
Cdd:TIGR02868 64 IGRAVFRY-----LERlVGHDAALRSlgalRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVAL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 142 FLFSFAIIIMAAIDWKLTLALVI-------VTPLIAILTMKMSSKAqpvfyeIRESFSRLNSMVEENISGNRVVKAFARE 214
Cdd:TIGR02868 139 VVGAAAVAAIAVLSVPAALILAAglllagfVAPLVSLRAARAAEQA------LARLRGELAAQLTDALDGAAELVASGAL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 215 DFEMKKFHEHNEDFKK--RNLDSADVSRTYLPVLdsLAGMLVVITLIFGGYLVIKGQMT--------LGDLVAFNGFlwm 284
Cdd:TIGR02868 213 PAALAQVEEADRELTRaeRRAAAATALGAALTLL--AAGLAVLGALWAGGPAVADGRLApvtlavlvLLPLAAFEAF--- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 285 lnGPMRMSgwlINDVQRFIASSFKIQDmmATDAKIPI-----HAEKPAPSLQGHVEFKNVSFHFEDDPntDVLKNISLKA 359
Cdd:TIGR02868 288 --AALPAA---AQQLTRVRAAAERIVE--VLDAAGPVaegsaPAAGAVGLGKPTLELRDLSAGYPGAP--PVLDGVSLDL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 360 SPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIATVMQDIFLFSDTIEGNIAFGAPDATM 439
Cdd:TIGR02868 359 PPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATD 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 440 EDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKIT 519
Cdd:TIGR02868 439 EELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAAL 518
|
490
....*....|.
gi 1755737710 520 ENTTTFIIAHR 530
Cdd:TIGR02868 519 SGRTVVLITHH 529
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
18-305 |
1.37e-56 |
|
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: 191.87 E-value: 1.37e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 18 MIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFRIREDLYK 97
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 98 KLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTMKMS 177
Cdd:cd18552 81 KLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 178 SKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVVIT 257
Cdd:cd18552 161 KRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1755737710 258 LIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIAS 305
Cdd:cd18552 241 LWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAA 288
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
18-306 |
2.45e-56 |
|
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: 191.16 E-value: 2.45e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 18 MIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFRIREDLYK 97
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 98 KLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYnILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTMKMS 177
Cdd:cd18543 81 HLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPF-LLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 178 SKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVVIT 257
Cdd:cd18543 160 RRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAV 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1755737710 258 LIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASS 306
Cdd:cd18543 240 LALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAA 288
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
15-302 |
2.22e-55 |
|
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: 188.81 E-value: 2.22e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 15 RLLMIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFRIRED 94
Cdd:cd18549 1 KKLFFLDLFCAVLIAALDLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 95 LYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIrhfvSWVSYNILENVFLFSF----AIIIMAAIDWKLTLALVIVTPLIA 170
Cdd:cd18549 81 LFEHLQKLSFSFFDNNKTGQLMSRITNDLFDI----SELAHHGPEDLFISIItiigSFIILLTINVPLTLIVFALLPLMI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 171 ILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLA 250
Cdd:cd18549 157 IFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAMAYFFSGMNFFT 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1755737710 251 GMLVVITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMsgwLINDVQRF 302
Cdd:cd18549 237 NLLNLVVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRR---LVNFTEQY 285
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
110-560 |
8.46e-55 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 194.49 E-value: 8.46e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 110 TRVGDIMARMTGDTDAIRHFVS-----------WVSYNILEnVFLFS--FAIIIMAAidwkltlALVIVTplIAILTMKM 176
Cdd:TIGR01842 95 RRGSGDGLQALRDLDQLRQFLTgpglfaffdapWMPIYLLV-CFLLHpwIGILALGG-------AVVLVG--LALLNNRA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 177 SSKAqpvFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSAD-------VSRTYLPVLDSL 249
Cdd:TIGR01842 165 TKKP---LKEATEASIRANNLADSALRNAEVIEAMGMMGNLTKRWGRFHSKYLSAQSAASDragmlsnLSKYFRIVLQSL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 250 agMLVVitlifGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMsgwLINDVQRFIAS--SFK-IQDMMATDAKIPIHAEKP 326
Cdd:TIGR01842 242 --VLGL-----GAYLAIDGEITPGMMIAGSILVGRALAPIDG---AIGGWKQFSGArqAYKrLNELLANYPSRDPAMPLP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 327 APslQGHVEFKNVSFhFEDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVR 406
Cdd:TIGR01842 312 EP--EGHLSVENVTI-VPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRE 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 407 ELRNHIATVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARA 486
Cdd:TIGR01842 389 TFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARA 468
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1755737710 487 LLKNPSILILDDTTSAVDMETEVKIQ---GELKKitENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAE 560
Cdd:TIGR01842 469 LYGDPKLVVLDEPNSNLDEEGEQALAnaiKALKA--RGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-564 |
1.10e-54 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 200.64 E-value: 1.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 3 SMKWIWQYVRKYRLLMIGVFILIFIASGISIIYPLLGGKVIDDV-----VYQNKTNLLIPLLLIMIISTIIRTICRYTYQ 77
Cdd:PTZ00265 812 NLRIVYREIFSYKKDVTIIALSILVAGGLYPVFALLYAKYVSTLfdfanLEANSNKYSLYILVIAIAMFISETLKNYYNN 891
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 78 IMCERIGQNSLFRIRED-LYKKLQSLDFD-----FFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIM 151
Cdd:PTZ00265 892 VIGEKVEKTMKRRLFENiLYQEISFFDQDkhapgLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYFCPIVA 971
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 152 AAidwkLTLALVIVTPLIAILTMKMSSKA-------QP----VFYEIRESFSRLNSMVEENISGNRVVKAFAREDFeMKK 220
Cdd:PTZ00265 972 AV----LTGTYFIFMRVFAIRARLTANKDvekkeinQPgtvfAYNSDDEIFKDPSFLIQEAFYNMNTVIIYGLEDY-FCN 1046
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 221 FHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLV-VITLIFGGYLVIKGQMTLGDLVAfNGFLWMLNGP-----MRMSGw 294
Cdd:PTZ00265 1047 LIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFInSFAYWFGSFLIRRGTILVDDFMK-SLFTFLFTGSyagklMSLKG- 1124
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 295 linDVQRFIASSFKIQDMMATDAKIPIHAE-----KPAPSLQGHVEFKNVSFHFEDDPNTDVLKNISLKASPGQTIAILG 369
Cdd:PTZ00265 1125 ---DSENAKLSFEKYYPLIIRKSNIDVRDNggiriKNKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVG 1201
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 370 ETGAGKSTLVNLICRFYD------------------------------------------------------PTSGEILI 395
Cdd:PTZ00265 1202 ETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILL 1281
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 396 DGVDARKWHVRELRNHIATVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSG 475
Cdd:PTZ00265 1282 DGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSG 1361
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 476 GQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRISSVKEADEILILNH----GEII 549
Cdd:PTZ00265 1362 GQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVFNNpdrtGSFV 1441
|
650
....*....|....*..
gi 1755737710 550 E-RGTHSSLL-AEKGYY 564
Cdd:PTZ00265 1442 QaHGTHEELLsVQDGVY 1458
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
22-306 |
5.83e-53 |
|
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: 182.30 E-value: 5.83e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 22 FILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFRIREDLYKKLQS 101
Cdd:cd18576 2 LILLLLSSAIGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 102 LDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTM------- 174
Cdd:cd18576 82 LPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVlfgrrir 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 175 KMSSKAQpvfyeirESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLV 254
Cdd:cd18576 162 KLSKKVQ-------DELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAI 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1755737710 255 VITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASS 306
Cdd:cd18576 235 VAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGAS 286
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
16-290 |
1.26e-52 |
|
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: 181.94 E-value: 1.26e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 16 LLMIGVFILIFIASGISIIYPLlgGKVIDDVVYQNKTNLLIPLLLIMIIS---------------TIIRTICRYTYQIMC 80
Cdd:cd18564 1 LALALLALLLETALRLLEPWPL--KVVIDDVLGDKPLPGLLGLAPLLGPDplallllaaaalvgiALLRGLASYAGTYLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 81 ERIGQNSLFRIREDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTL 160
Cdd:cd18564 79 ALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 161 ALVIVTPLIAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSR 240
Cdd:cd18564 159 IALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1755737710 241 TYLPVLDSLAGMLVVITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMR 290
Cdd:cd18564 239 LLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVR 288
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
352-569 |
7.21e-51 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 184.28 E-value: 7.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYdPTSGEILIDGVDARKWHVRELRNHIATVMQDIFLFSDTIEGNIA 431
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVL 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 432 FGAPDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKI 511
Cdd:PRK11174 445 LGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLV 524
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1755737710 512 QGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAEKGYYFDIYN 569
Cdd:PRK11174 525 MQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLA 582
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
335-548 |
2.78e-50 |
|
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: 171.25 E-value: 2.78e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 335 EFKNVSFHFEDDPNTdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIAT 414
Cdd:cd03246 2 EVENVSFRYPGAEPP-VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 415 VMQDIFLFSDTIEGNIafgapdatmedvrrmariadadhfietmpesydtivgergvgLSGGQKQRISLARALLKNPSIL 494
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1755737710 495 ILDDTTSAVDMETEVKIQ---GELKKitENTTTFIIAHRISSVKEADEILILNHGEI 548
Cdd:cd03246 119 VLDEPNSHLDVEGERALNqaiAALKA--AGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
18-289 |
2.79e-50 |
|
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: 175.36 E-value: 2.79e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 18 MIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFRIREDLYK 97
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 98 KLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTMKMS 177
Cdd:cd18550 81 HLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 178 SKAQPVFYEIRESFSRLNSMVEE--NISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVV 255
Cdd:cd18550 161 RRRRKLTREQQEKLAELNSIMQEtlSVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPA 240
|
250 260 270
....*....|....*....|....*....|....
gi 1755737710 256 ITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPM 289
Cdd:cd18550 241 LVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPL 274
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
95-565 |
3.23e-50 |
|
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: 187.46 E-value: 3.23e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 95 LYKKLQSlDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVF-LFSFAIIIMAAIdwklTLALVIVTPLIAILT 173
Cdd:TIGR00957 1045 LHNKLRS-PMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFnVIGALIVILLAT----PIAAVIIPPLGLLYF 1119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 174 MKMSSKAQPVFYEIR-ESFSR--LNSMVEENISGNRVVKAFAR-EDFEmkkfheHNEDFK----KRNLDSADVSRTYLPV 245
Cdd:TIGR00957 1120 FVQRFYVASSRQLKRlESVSRspVYSHFNETLLGVSVIRAFEEqERFI------HQSDLKvdenQKAYYPSIVANRWLAV 1193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 246 LDSLAGMLVVItliFGGYLVIKGQMTL-----GDLVAFN-GFLWMLNGPMRMSgwliNDVQRFIASSFKIQDMMATDAKI 319
Cdd:TIGR00957 1194 RLECVGNCIVL---FAALFAVISRHSLsaglvGLSVSYSlQVTFYLNWLVRMS----SEMETNIVAVERLKEYSETEKEA 1266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 320 PIHAEKPAPSL----QGHVEFKNVSFHFEDDPNTdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILI 395
Cdd:TIGR00957 1267 PWQIQETAPPSgwppRGRVEFRNYCLRYREDLDL-VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII 1345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 396 DGVDARKWHVRELRNHIATVMQDIFLFSDTIEGNI-AFGApdATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLS 474
Cdd:TIGR00957 1346 DGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdPFSQ--YSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLS 1423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 475 GGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTH 554
Cdd:TIGR00957 1424 VGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAP 1503
|
490
....*....|.
gi 1755737710 555 SSLLAEKGYYF 565
Cdd:TIGR00957 1504 SNLLQQRGIFY 1514
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
74-306 |
1.47e-48 |
|
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: 171.21 E-value: 1.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 74 YTYQIMCERIGQNSLFRIREDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAA 153
Cdd:cd18565 72 YLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFY 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 154 IDWKLTLALVIVTPLIAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNL 233
Cdd:cd18565 152 LNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANW 231
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1755737710 234 DSADVSRTYLPVLDSLAGMLVVITLIFGGYLVIKG------QMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASS 306
Cdd:cd18565 232 RAIRLRAAFFPVIRLVAGAGFVATFVVGGYWVLDGpplftgTLTVGTLVTFLFYTQRLLWPLTRLGDLIDQYQRAMASA 310
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
334-561 |
2.10e-48 |
|
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: 168.28 E-value: 2.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIA 413
Cdd:COG1122 1 IELENLSFSYPGG--TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 414 TVMQ--DIFLFSDTIEGNIAFG-----APDATMED-VRRMARIADADHFIETMPESydtivgergvgLSGGQKQRISLAR 485
Cdd:COG1122 79 LVFQnpDDQLFAPTVEEDVAFGpenlgLPREEIRErVEEALELVGLEHLADRPPHE-----------LSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1755737710 486 ALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIA-HRISSVKE-ADEILILNHGEIIERGTHSSLLAEK 561
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVAElADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
332-553 |
4.63e-47 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 163.74 E-value: 4.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 332 GHVEFKNVSFHFEDDpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNH 411
Cdd:cd03369 5 GEIEVENLSVRYAPD-LPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 412 IATVMQDIFLFSDTIEGNIAfgaPDATMEDVRRMARIAdadhfietmpesydtiVGERGVGLSGGQKQRISLARALLKNP 491
Cdd:cd03369 84 LTIIPQDPTLFSGTIRSNLD---PFDEYSDEEIYGALR----------------VSEGGLNLSQGQRQLLCLARALLKRP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1755737710 492 SILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGT 553
Cdd:cd03369 145 RVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
335-547 |
7.91e-47 |
|
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: 163.41 E-value: 7.91e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 335 EFKNVSFHFEDDpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIAT 414
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 415 VMQ--DIFLFSDTIEGNIAFGA-----PDATMED-VRRMARIADADHFIETMPESydtivgergvgLSGGQKQRISLARA 486
Cdd:cd03225 80 VFQnpDDQFFGPTVEEEVAFGLenlglPEEEIEErVEEALELVGLEGLRDRSPFT-----------LSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1755737710 487 LLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIA-HRISSVKE-ADEILILNHGE 547
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLEDGK 211
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
334-547 |
9.78e-47 |
|
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: 162.64 E-value: 9.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDPNTD--VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGvdarkwhvrelrnH 411
Cdd:cd03250 1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 412 IATVMQDIFLFSDTIEGNIAFGAPdatmEDVRRMARIADA-----DhfIETMPESYDTIVGERGVGLSGGQKQRISLARA 486
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKP----FDEERYEKVIKAcalepD--LEILPDGDLTEIGEKGINLSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1755737710 487 LLKNPSILILDDTTSAVDMETEVKI-----QGELKKiteNTTTFIIAHRISSVKEADEILILNHGE 547
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVGRHIfenciLGLLLN---NKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
352-501 |
1.92e-46 |
|
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: 160.12 E-value: 1.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIATVMQDIFLFSD-TIEGNI 430
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1755737710 431 AFGapdATMEDVRRMARIADADHFIETMPESY--DTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTS 501
Cdd:pfam00005 81 RLG---LLLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
22-309 |
5.14e-46 |
|
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: 163.50 E-value: 5.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 22 FILIFIASGISIIYPLLGGKVIDDVV---YQNKTNLLIPLLLIMIISTIIRTICRYT-YQIMCERIgqnsLFRIREDLYK 97
Cdd:cd18557 2 LLFLLISSAAQLLLPYLIGRLIDTIIkggDLDVLNELALILLAIYLLQSVFTFVRYYlFNIAGERI----VARLRRDLFS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 98 KLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTMKMS 177
Cdd:cd18557 78 SLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 178 SKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVVIT 257
Cdd:cd18557 158 RYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1755737710 258 LIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASSFKI 309
Cdd:cd18557 238 LWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
18-309 |
9.57e-46 |
|
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: 163.04 E-value: 9.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 18 MIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFRIREDLYK 97
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 98 KLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTMKMS 177
Cdd:cd18546 81 HLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 178 SKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVVIT 257
Cdd:cd18546 161 RRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1755737710 258 LIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASSFKI 309
Cdd:cd18546 241 LLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
18-289 |
1.05e-45 |
|
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: 162.43 E-value: 1.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 18 MIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIIS--TIIRTICRYTYQIMCERIGQNSLFRIREDL 95
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLllGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 96 YKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTMK 175
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 176 MSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVV 255
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....
gi 1755737710 256 ITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPM 289
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
143-579 |
1.84e-45 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 172.91 E-value: 1.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 143 LFSFAIIIMAAIDW------KLTLALVIVTPLIAILTMKMSSKAQpvfyeIRESFSRL---NSM--VEENISGNRVVKAF 211
Cdd:PTZ00265 178 IFTYASAFLGLYIWslfknaRLTLCITCVFPLIYICGVICNKKVK-----INKKTSLLynnNTMsiIEEALVGIRTVVSY 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 212 AREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVVITLIFGGYLVIKGQMTLGDLVAFNG--FLWMLNG-- 287
Cdd:PTZ00265 253 CGEKTILKKFNLSEKLYSKYILKANFMESLHIGMINGFILASYAFGFWYGTRIIISDLSNQQPNNDFHGgsVISILLGvl 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 288 -PMRMSGWLINDVQRFIASsfkiqdMMATDAKIPIHAEKPA----------PSLQgHVEFKNVSFHFEDDPNTDVLKNIS 356
Cdd:PTZ00265 333 iSMFMLTIILPNITEYMKS------LEATNSLYEIINRKPLvennddgkklKDIK-KIQFKNVRFHYDTRKDVEIYKDLN 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 357 LKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILI-DGVDARKWHVRELRNHIATVMQDIFLFSDTIEGNIAF--- 432
Cdd:PTZ00265 406 FTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYsly 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 433 ---------------GAPDATMEDVRRMAR----------------------------IADAD-----------HFIETM 458
Cdd:PTZ00265 486 slkdlealsnyynedGNDSQENKNKRNSCRakcagdlndmsnttdsneliemrknyqtIKDSEvvdvskkvlihDFVSAL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 459 PESYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELK--KITENTTTFIIAHRISSVKE 536
Cdd:PTZ00265 566 PDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRY 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 537 ADEILILNHGE-----------------------------------------------IIERGTHSSLLAEKG--YYFDI 567
Cdd:PTZ00265 646 ANTIFVLSNRErgstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinnagsyIIEQGTHDALMKNKNgiYYTMI 725
|
570
....*....|..
gi 1755737710 568 YNKQLGTEANVN 579
Cdd:PTZ00265 726 NNQKVSSKKSSN 737
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
15-305 |
1.97e-45 |
|
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: 162.26 E-value: 1.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 15 RLLMIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFRIRED 94
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 95 LYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTM 174
Cdd:cd18540 81 AFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 175 KMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLV 254
Cdd:cd18540 161 YFQKKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIAT 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1755737710 255 VITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIAS 305
Cdd:cd18540 241 ALVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQAS 291
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
334-552 |
5.47e-45 |
|
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: 158.45 E-value: 5.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRElRNhIA 413
Cdd:cd03259 1 LELKGLSKTYGSVR---ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER-RN-IG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 414 TVMQDIFLFSD-TIEGNIAFG-----APDATMED-VRRMARIADADHFIETMPESydtivgergvgLSGGQKQRISLARA 486
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGlklrgVPKAEIRArVRELLELVGLEGLLNRYPHE-----------LSGGQQQRVALARA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1755737710 487 LLKNPSILILDDTTSAVDMETEVKIQGELKKITENT--TTFIIAHRISSVKE-ADEILILNHGEIIERG 552
Cdd:cd03259 145 LAREPSLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
18-309 |
2.64e-44 |
|
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: 159.14 E-value: 2.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 18 MIGVFILIFIASGISIIYPLLGGKVIDDVVYQNK-TNLLIPLLLIMIISTIIRTICRYtyqiMCERIGQNSLFRIREDLY 96
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGGSsGGLLALLVALFLLQAVLSALSSY----LLGRTGERVVLDLRRRLW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 97 KKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTMKM 176
Cdd:cd18551 77 RRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 177 SSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLdSLAGMLVVI 256
Cdd:cd18551 157 GRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLM-GLAVQLALL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1755737710 257 T-LIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASSFKI 309
Cdd:cd18551 236 VvLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
334-559 |
5.43e-44 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 163.92 E-value: 5.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDPNTDV--LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWH---VREL 408
Cdd:COG1123 261 LEVRNLSKRYPVRGKGGVraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 409 RNHIATVMQDIF--LF-SDTIEGNIAFGApdatmeDVRRMARIADADHFIETM-------PESYDTIVGErgvgLSGGQK 478
Cdd:COG1123 341 RRRVQMVFQDPYssLNpRMTVGDIIAEPL------RLHGLLSRAERRERVAELlervglpPDLADRYPHE----LSGGQR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 479 QRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRISSVKE-ADEILILNHGEIIERGTHS 555
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTE 490
|
....
gi 1755737710 556 SLLA 559
Cdd:COG1123 491 EVFA 494
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
334-552 |
1.80e-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: 153.24 E-value: 1.80e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHvRELRNHIA 413
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 414 TVMQDIFLFSDTIEGNIafgapdatmedvrrmariadadhfietmpesydtivGERgvgLSGGQKQRISLARALLKNPSI 493
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL------------------------------------GRR---FSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1755737710 494 LILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERG 552
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
18-306 |
2.54e-43 |
|
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: 156.40 E-value: 2.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 18 MIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFRIREDLYK 97
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 98 KLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTMKMS 177
Cdd:cd18548 81 KIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 178 SKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVVIT 257
Cdd:cd18548 161 KKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1755737710 258 LIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASS 306
Cdd:cd18548 241 LWFGGHLINAGSLQVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASA 289
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
334-552 |
4.43e-43 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 153.82 E-value: 4.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDPNTD-VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVD---ARKWHVRELR 409
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDllkLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 410 NHIATVMQDIFL---FSDTIEGNIAFGAPDATMEDVRRMARIADADHFIEtMPESyDTIVGERGVGLSGGQKQRISLARA 486
Cdd:cd03257 82 KEIQMVFQDPMSslnPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVG-VGLP-EEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1755737710 487 LLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRISSVKE-ADEILILNHGEIIERG 552
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
334-560 |
7.65e-43 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 153.30 E-value: 7.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDdpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHvRELRNHIA 413
Cdd:COG1131 1 IEVRGLTKRYGD---KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP-AEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 414 TVMQDIFLFSD-TIEGNIAFGapdATMEDVRRMARIADADHFIET--MPESYDTIVGErgvgLSGGQKQRISLARALLKN 490
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRFF---ARLYGLPRKEARERIDELLELfgLTDAADRKVGT----LSGGMKQRLGLALALLHD 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1755737710 491 PSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIA-HRISSVKE-ADEILILNHGEIIERGTHSSLLAE 560
Cdd:COG1131 150 PELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
334-551 |
6.31e-42 |
|
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: 150.31 E-value: 6.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFED-DPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDarkwhVRELRNHI 412
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP-----VTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 413 ATVMQDIFLFS-DTIEGNIAFGapdATMEDVRRMARIADADHFIETmpesydtiVGERGVG------LSGGQKQRISLAR 485
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALG---LELQGVPKAEARERAEELLEL--------VGLSGFEnayphqLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755737710 486 ALLKNPSILILDDTTSAVDMETEVKIQGELKKI--TENTTTFIIAHrisSVKEA----DEILILN--HGEIIER 551
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIwrETGKTVLLVTH---DIDEAvflaDRVVVLSarPGRIVAE 215
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
334-559 |
9.28e-42 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 150.42 E-value: 9.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDPN-TDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDA---RKWHVRELR 409
Cdd:cd03258 2 IELKNVSKVFGDTGGkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 410 NHIATVMQDIFLFSD-TIEGNIAF-----GAPDATMED-VRRMARIADADHFIETMPESydtivgergvgLSGGQKQRIS 482
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALpleiaGVPKAEIEErVLELLELVGLEDKADAYPAQ-----------LSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 483 LARALLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRISSVKE-ADEILILNHGEIIERGTHSSLLA 559
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFA 230
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
335-562 |
1.10e-41 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 150.39 E-value: 1.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 335 EFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKwHVRELRNHIAT 414
Cdd:COG4555 3 EVENLSKKYGKVP---ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 415 VMQDIFLFSD-TIEGNIAFGAPDATMEDVRRMARIADADHFIEtMPESYDTIVGErgvgLSGGQKQRISLARALLKNPSI 493
Cdd:COG4555 79 LPDERGLYDRlTVRENIRYFAELYGLFDEELKKRIEELIELLG-LEEFLDRRVGE----LSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1755737710 494 LILDDTTSAVDMETEVKIQGELKKITENTTTFIIA-HRISSVKE-ADEILILNHGEIIERGTHSSLLAEKG 562
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
334-553 |
1.89e-40 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 150.25 E-value: 1.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDdpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARkwHVR-ELRNhI 412
Cdd:COG3842 6 LELENVSKRYGD---VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT--GLPpEKRN-V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 413 ATVMQDIFLFSD-TIEGNIAFG-----APDATMED-VRRMARIADADHFIETMPESydtivgergvgLSGGQKQRISLAR 485
Cdd:COG3842 80 GMVFQDYALFPHlTVAENVAFGlrmrgVPKAEIRArVAELLELVGLEGLADRYPHQ-----------LSGGQQQRVALAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755737710 486 ALLKNPSILILDDTTSAVDMETEVKIQGELKKITENT-TTFIIA-HrisSVKEA----DEILILNHGEIIERGT 553
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELgITFIYVtH---DQEEAlalaDRIAVMNDGRIEQVGT 219
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
335-547 |
1.52e-39 |
|
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: 141.61 E-value: 1.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 335 EFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIAT 414
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 415 VMQdiflfsdtiegniafgapdatmedvrrmariadadhfietmpesydtivgergvgLSGGQKQRISLARALLKNPSIL 494
Cdd:cd00267 78 VPQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1755737710 495 ILDDTTSAVDMETEVKIQGELKKITENTTTFIIA-HRISSVKEA-DEILILNHGE 547
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEEGRTVIIVtHDPELAELAaDRVIVLKDGK 157
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
313-565 |
3.54e-39 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 154.13 E-value: 3.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 313 MATDAKIPIHAEKPAPS--LQGHVEFKNVSFHFEDD--PntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDP 388
Cdd:PLN03130 1215 LPSEAPLVIENNRPPPGwpSSGSIKFEDVVLRYRPElpP---VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVEL 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 389 TSGEILIDGVDARKWHVRELRNHIATVMQDIFLFSDTIEGNI-AFGA-PDATMEDVRRMARIADAdhfIETMPESYDTIV 466
Cdd:PLN03130 1292 ERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLdPFNEhNDADLWESLERAHLKDV---IRRNSLGLDAEV 1368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 467 GERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHG 546
Cdd:PLN03130 1369 SEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAG 1448
|
250
....*....|....*....
gi 1755737710 547 EIIERGTHSSLLAEKGYYF 565
Cdd:PLN03130 1449 RVVEFDTPENLLSNEGSAF 1467
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
334-548 |
4.00e-39 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 142.63 E-value: 4.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHF-EDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVREL---- 408
Cdd:cd03255 1 IELKNLSKTYgGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 409 RNHIATVMQDIFLFSD-TIEGNIAFGAPDATMEDVRRMARIADA------DHFIETMPESydtivgergvgLSGGQKQRI 481
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELPLLLAGVPKKERRERAEELlervglGDRLNHYPSE-----------LSGGQQQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1755737710 482 SLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRISSVKEADEILILNHGEI 548
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
330-568 |
4.34e-39 |
|
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: 143.90 E-value: 4.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 330 LQGHVEFKNVSFHFEDDPNTdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELR 409
Cdd:cd03288 16 LGGEIKIHDLCVRYENNLKP-VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 410 NHIATVMQDIFLFSDTIEGNIAfgaPDATMEDVR--RMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARAL 487
Cdd:cd03288 95 SRLSIILQDPILFSGSIRFNLD---PECKCTDDRlwEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 488 LKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAEKGYYFDI 567
Cdd:cd03288 172 VRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFAS 251
|
.
gi 1755737710 568 Y 568
Cdd:cd03288 252 L 252
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
22-309 |
1.08e-38 |
|
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: 143.84 E-value: 1.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 22 FILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTIC----RYTYQImcerIGQNSLFRIREDLYK 97
Cdd:cd18572 2 FVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFsglrGGCFSY----AGTRLVRRLRRDLFR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 98 KLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTMKMS 177
Cdd:cd18572 78 SLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 178 SKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVVIT 257
Cdd:cd18572 158 RYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1755737710 258 LIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASSFKI 309
Cdd:cd18572 238 LFYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
106-565 |
1.50e-38 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 152.44 E-value: 1.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 106 FFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVF--LFSFAIIIMAAidwklTLALVIVTPLI-----AILTMKMSS 178
Cdd:PLN03232 1000 FFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWqlLSTFALIGTVS-----TISLWAIMPLLilfyaAYLYYQSTS 1074
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 179 KA---------QPVFYEIRESFSRLNSMveenisgnRVVKAFAREDFEMKKFHEHNEDFKKRNLDSadvSRTYLPVLDSL 249
Cdd:PLN03232 1075 REvrrldsvtrSPIYAQFGEALNGLSSI--------RAYKAYDRMAKINGKSMDNNIRFTLANTSS---NRWLTIRLETL 1143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 250 AGMLVVITLIFG--GYLVIKGQM----TLGDLVAFN-GFLWMLNGPMRMSGWLINDVQRFIASSFKIQdmMATDAKIPIH 322
Cdd:PLN03232 1144 GGVMIWLTATFAvlRNGNAENQAgfasTMGLLLSYTlNITTLLSGVLRQASKAENSLNSVERVGNYID--LPSEATAIIE 1221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 323 AEKPAPS--LQGHVEFKNVsfHFEDDPN-TDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVD 399
Cdd:PLN03232 1222 NNRPVSGwpSRGSIKFEDV--HLRYRPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCD 1299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 400 ARKWHVRELRNHIATVMQDIFLFSDTIEGNI-AFGA-PDATMEDVRRMARIADAdhfIETMPESYDTIVGERGVGLSGGQ 477
Cdd:PLN03232 1300 VAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIdPFSEhNDADLWEALERAHIKDV---IDRNPFGLDAEVSEGGENFSVGQ 1376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 478 KQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSL 557
Cdd:PLN03232 1377 RQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQEL 1456
|
....*...
gi 1755737710 558 LAEKGYYF 565
Cdd:PLN03232 1457 LSRDTSAF 1464
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
334-552 |
1.58e-38 |
|
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: 141.16 E-value: 1.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDpntDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYD-----PTSGEILIDGVDARKWHVR-- 406
Cdd:cd03260 1 IELRDLNVYYGDK---HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 407 ELRNHIATVMQDIFLFSDTIEGNIAFG----------APDATMEDVRRMARIADAdhfietmpesydtiVGER--GVGLS 474
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiklkeELDERVEEALRKAALWDE--------------VKDRlhALGLS 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1755737710 475 GGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKE-ADEILILNHGEIIERG 552
Cdd:cd03260 144 GGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFG 222
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
334-547 |
2.52e-38 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 139.24 E-value: 2.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFeddPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARK--WHVRELRNH 411
Cdd:cd03229 1 LELKNVSKRY---GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDleDELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 412 IATVMQDIFLFSD-TIEGNIAFgapdatmedvrrmariadadhfietmpesydtivgergvGLSGGQKQRISLARALLKN 490
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIAL---------------------------------------GLSGGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 491 PSILILDDTTSAVDMETEVKIQGELKKITEN--TTTFIIAHRISSVKE-ADEILILNHGE 547
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
333-550 |
2.65e-38 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 141.77 E-value: 2.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 333 HVEFKNVSFHFEDDPN-TDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDarkwhVRELRNH 411
Cdd:COG1116 7 ALELRGVSKRFPTGGGgVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP-----VTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 412 IATVMQDIFLFs-dTIEGNIAFGAPdatMEDVRRMARIADADHFIEtmpesydtIVGERGVG------LSGGQKQRISLA 484
Cdd:COG1116 82 RGVVFQEPALLpwlTVLDNVALGLE---LRGVPKAERRERARELLE--------LVGLAGFEdayphqLSGGMRQRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755737710 485 RALLKNPSILILDDTTSAVDMETEVKIQGELKKI--TENTTTFIIAHrisSVKEA----DEILILNH--GEIIE 550
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTH---DVDEAvflaDRVVVLSArpGRIVE 221
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
334-559 |
3.52e-38 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 140.90 E-value: 3.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDPNtdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIA 413
Cdd:cd03295 1 IEFENVTKRYGGGKK--AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 414 TVMQDIFLFSD-TIEGNIAFgAPdaTMEDVRRMARIADADHFIETM---PESYdtivGERGVG-LSGGQKQRISLARALL 488
Cdd:cd03295 79 YVIQQIGLFPHmTVEENIAL-VP--KLLKWPKEKIRERADELLALVgldPAEF----ADRYPHeLSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755737710 489 KNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRI-SSVKEADEILILNHGEIIERGTHSSLLA 559
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
334-559 |
1.66e-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: 145.43 E-value: 1.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDPNTdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPT---SGEILIDGVDARKWHVRELRN 410
Cdd:COG1123 5 LEVRDLSVRYPGGDVP-AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 411 HIATVMQDIF--LFSDTIEGNIAFG------APDATMEDVRRMARIADADHFIETMPESydtivgergvgLSGGQKQRIS 482
Cdd:COG1123 84 RIGMVFQDPMtqLNPVTVGDQIAEAlenlglSRAEARARVLELLEAVGLERRLDRYPHQ-----------LSGGQRQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 483 LARALLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRISSVKE-ADEILILNHGEIIERGTHSSLLA 559
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
334-548 |
1.92e-37 |
|
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: 136.37 E-value: 1.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFeddPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKwHVRELRNHIA 413
Cdd:cd03230 1 IEVRNLSKRY---GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 414 TVMQDIFLFSD-TIEGNIAfgapdatmedvrrmariadadhfietmpesydtivgergvgLSGGQKQRISLARALLKNPS 492
Cdd:cd03230 77 YLPEEPSLYENlTVRENLK-----------------------------------------LSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1755737710 493 ILILDDTTSAVDMETEVKIQGELKKIT-ENTTTFIIAHRISSVKE-ADEILILNHGEI 548
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKkEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
334-559 |
2.51e-37 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 138.78 E-value: 2.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHF-EDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHI 412
Cdd:COG1124 2 LEVRNLSVSYgQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 413 ATVMQDiflfsdtiegniAFGA--PDATMEDV-----------RRMARIADAdhfIET--MPESY-DTIVGErgvgLSGG 476
Cdd:COG1124 82 QMVFQD------------PYASlhPRHTVDRIlaeplrihglpDREERIAEL---LEQvgLPPSFlDRYPHQ----LSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 477 QKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRISSVKE-ADEILILNHGEIIERGT 553
Cdd:COG1124 143 QRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREerGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELT 222
|
....*.
gi 1755737710 554 HSSLLA 559
Cdd:COG1124 223 VADLLA 228
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
15-311 |
8.03e-37 |
|
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: 138.73 E-value: 8.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 15 RLLMIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFRIRED 94
Cdd:cd18570 1 KKLLILILLLSLLITLLGIAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 95 LYKKLQSLDFDFFNNTRVGDIMARMTgDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTM 174
Cdd:cd18570 81 YFKHLLKLPLSFFETRKTGEIISRFN-DANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 175 KMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLV 254
Cdd:cd18570 160 LFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGS 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1755737710 255 VITLIFGGYLVIKGQMTLGDLVAFNGflwmlngpmrMSGWLINDVQRFIASSFKIQD 311
Cdd:cd18570 240 LLILWIGSYLVIKGQLSLGQLIAFNA----------LLGYFLGPIENLINLQPKIQE 286
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
335-548 |
1.88e-36 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 134.94 E-value: 1.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 335 EFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIAT 414
Cdd:COG4619 2 ELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 415 VMQDIFLFSDTIEGNIAFGA----PDATMEDVRR-MARIAdadhfietMPESY-DTIVGErgvgLSGGQKQRISLARALL 488
Cdd:COG4619 79 VPQEPALWGGTVRDNLPFPFqlreRKFDRERALElLERLG--------LPPDIlDKPVER----LSGGERQRLALIRALL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1755737710 489 KNPSILILDDTTSAVDMETEVKIQGELKKI--TENTTTFIIAH---RISSVkeADEILILNHGEI 548
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREYlaEEGRAVLWVSHdpeQIERV--ADRVLTLEAGRL 209
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
333-553 |
2.74e-36 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 138.29 E-value: 2.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 333 HVEFKNVSFHFE-DDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVD---ARKWHVREL 408
Cdd:COG1135 1 MIELENLSKTFPtKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDltaLSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 409 RNHIATVMQDIFLF-SDTIEGNIAF-----GAPDAtmedvRRMARIAD----------ADHFietmPESydtivgergvg 472
Cdd:COG1135 81 RRKIGMIFQHFNLLsSRTVAENVALpleiaGVPKA-----EIRKRVAEllelvglsdkADAY----PSQ----------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 473 LSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRISSVKE-ADEILILNHGEII 549
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIV 220
|
....
gi 1755737710 550 ERGT 553
Cdd:COG1135 221 EQGP 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
334-550 |
2.85e-36 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 134.79 E-value: 2.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDPntDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVD---ARKWHVRELRN 410
Cdd:COG2884 2 IRFENVSKRYPGGR--EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrLKRREIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 411 HIATVMQDIFLFSD-TIEGNIAF-----GAPDATMEdvrrmARIADA------DHFIETMPESydtivgergvgLSGGQK 478
Cdd:COG2884 80 RIGVVFQDFRLLPDrTVYENVALplrvtGKSRKEIR-----RRVREVldlvglSDKAKALPHE-----------LSGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755737710 479 QRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIA-HRISSVKEADE-ILILNHGEIIE 550
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
351-558 |
6.26e-36 |
|
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: 134.39 E-value: 6.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHvRELRNhIATVMQDIFLFSD-TIEGN 429
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLP-PEKRD-ISYVPQNYALFPHmTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 430 IAFG-----APDATME-DVRRMARIADADHFIETMPESydtivgergvgLSGGQKQRISLARALLKNPSILILDDTTSAV 503
Cdd:cd03299 92 IAYGlkkrkVDKKEIErKVLEIAEMLGIDHLLNRKPET-----------LSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1755737710 504 DMETEVKIQGELKKI-TENTTTFI-IAHRISSVKE-ADEILILNHGEIIERGTHSSLL 558
Cdd:cd03299 161 DVRTKEKLREELKKIrKEFGVTVLhVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
335-552 |
3.62e-35 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 130.63 E-value: 3.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 335 EFKNVSFHFeddPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIAT 414
Cdd:cd03214 1 EVENLSVGY---GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 415 VMQdiflfsdtiegniafgapdaTMEDVrrmariaDADHFIEtmpESYDTivgergvgLSGGQKQRISLARALLKNPSIL 494
Cdd:cd03214 78 VPQ--------------------ALELL-------GLAHLAD---RPFNE--------LSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1755737710 495 ILDDTTSAVDMETEVKIQGELKKIT--ENTTTFIIAHRISSV-KEADEILILNHGEIIERG 552
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRLAreRGKTVVMVLHDLNLAaRYADRVILLKDGRIVAQG 180
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
334-550 |
8.49e-35 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 130.93 E-value: 8.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDPN-TDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVREL---- 408
Cdd:COG1136 5 LELRNLTKSYGTGEGeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 409 RNHIATVMQDIFLFSD-TIEGNIAF-----GAPDAtmEDVRRMARIADA---DHFIETMPESydtivgergvgLSGGQKQ 479
Cdd:COG1136 85 RRHIGFVFQFFNLLPElTALENVALplllaGVSRK--ERRERARELLERvglGDRLDHRPSQ-----------LSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1755737710 480 RISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENT-TTFIIA-HRISSVKEADEILILNHGEIIE 550
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELgTTIVMVtHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
334-553 |
1.59e-34 |
|
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: 130.70 E-value: 1.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVREL---RN 410
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 411 HIATVMQDIFLFSD-TIEGNIAFGAPDATMEDVRRMARIAdadhfIETMPEsydtiVGERGVG------LSGGQKQRISL 483
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPLREHTRLSEEEIREIV-----LEKLEA-----VGLRGAEdlypaeLSGGMKKRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755737710 484 ARALLKNPSILILDDTTSAVDMETEVKIQG---ELKKiTENTTTFIIAHRISSVKE-ADEILILNHGEIIERGT 553
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASGVIDDlirSLKK-ELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGT 220
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
334-553 |
2.68e-34 |
|
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: 130.55 E-value: 2.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFeddPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIA 413
Cdd:COG1120 2 LEAENLSVGY---GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 414 TVMQDI---FLFS--DTIE-GNI----AFGAPDATMED-VRRMARIADADHFIETmpeSYDTivgergvgLSGGQKQRIS 482
Cdd:COG1120 79 YVPQEPpapFGLTvrELVAlGRYphlgLFGRPSAEDREaVEEALERTGLEHLADR---PVDE--------LSGGERQRVL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755737710 483 LARALLKNPSILILDDTTSAVDMETEVKIQGELKKIT--ENTTTFIIAHRIS-SVKEADEILILNHGEIIERGT 553
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLAreRGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGP 221
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
335-561 |
2.95e-34 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 130.00 E-value: 2.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 335 EFKNVSFHFEDDpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRN---H 411
Cdd:cd03256 2 EVENLSKTYPNG--KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrrQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 412 IATVMQDIFLFSD-TIEGNIAFGAPdATMEDVRRMAR------IADADHFIET--MPESYDTIVGErgvgLSGGQKQRIS 482
Cdd:cd03256 80 IGMIFQQFNLIERlSVLENVLSGRL-GRRSTWRSLFGlfpkeeKQRALAALERvgLLDKAYQRADQ----LSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 483 LARALLKNPSILILDDTTSAVDMETEVKIQGELKKI--TENTTTFIIAHRISSVKE-ADEILILNHGEIIERGTHSSLLA 559
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPAELTD 234
|
..
gi 1755737710 560 EK 561
Cdd:cd03256 235 EV 236
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
334-553 |
3.67e-34 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 132.89 E-value: 3.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRElRNhIA 413
Cdd:COG3839 4 LELENVSKSYGGVE---ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-RN-IA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 414 TVMQDIFLF-SDTIEGNIAFG-----APDATMED-VRRMARIADADHFIETMPEsydtivgergvGLSGGQKQRISLARA 486
Cdd:COG3839 79 MVFQSYALYpHMTVYENIAFPlklrkVPKAEIDRrVREAAELLGLEDLLDRKPK-----------QLSGGQRQRVALGRA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1755737710 487 LLKNPSILILDDTTSAVDMETEVKIQGELKKITENT-TTFIIA-HRISsvkEA----DEILILNHGEIIERGT 553
Cdd:COG3839 148 LVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLgTTTIYVtHDQV---EAmtlaDRIAVMNDGRIQQVGT 217
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
334-553 |
3.96e-34 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 129.71 E-value: 3.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVD---ARKWHVRELRN 410
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDitgLSEKELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 411 HIATVMQDIFLFSD-TIEGNIAF------GAPDATMED-VR---RMARIADADHFietMPesydtivGErgvgLSGGQKQ 479
Cdd:COG1127 83 RIGMLFQGGALFDSlTVFENVAFplrehtDLSEAEIRElVLeklELVGLPGAADK---MP-------SE----LSGGMRK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1755737710 480 RISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRISSVKE-ADEILILNHGEIIERGT 553
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGT 225
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
334-561 |
7.85e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 129.73 E-value: 7.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDPNTdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIA 413
Cdd:PRK13632 8 IKVENVSFSYPNSENN-ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 414 TVMQ--DIFLFSDTIEGNIAFG-----APDATMED-VRRMARIADADHFIETMPESydtivgergvgLSGGQKQRISLAR 485
Cdd:PRK13632 87 IIFQnpDNQFIGATVEDDIAFGlenkkVPPKKMKDiIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 486 ALLKNPSILILDDTTSAVD---METEVKIQGELKKitENTTTFI-IAHRISSVKEADEILILNHGEIIERGTHSSLLAEK 561
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDpkgKREIKKIMVDLRK--TRKKTLIsITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
334-561 |
1.10e-33 |
|
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: 129.09 E-value: 1.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDAR-KWHVRELRNHI 412
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLdEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 413 ATVMQ--DIFLFSDTIEGNIAFG-----APDATMEdvrrmARIADA------DHFIETMPESydtivgergvgLSGGQKQ 479
Cdd:TIGR04520 80 GMVFQnpDNQFVGATVEDDVAFGlenlgVPREEMR-----KRVDEAlklvgmEDFRDREPHL-----------LSGGQKQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 480 RISLARALLKNPSILILDDTTSAVD-------METEVKIQGElkkitENTTTFIIAHRISSVKEADEILILNHGEIIERG 552
Cdd:TIGR04520 144 RVAIAGVLAMRPDIIILDEATSMLDpkgrkevLETIRKLNKE-----EGITVISITHDMEEAVLADRVIVMNKGKIVAEG 218
|
....*....
gi 1755737710 553 THSSLLAEK 561
Cdd:TIGR04520 219 TPREIFSQV 227
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
334-553 |
1.71e-33 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 127.80 E-value: 1.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDdpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDG--VDARKWHVRELRNH 411
Cdd:COG1126 2 IEIENLHKSFGD---LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGedLTDSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 412 IATVMQDIFLFSD-TIEGNIAFgAPdatmEDVRRMAR---IADADHFIET--MPESYDTIVGErgvgLSGGQKQRISLAR 485
Cdd:COG1126 79 VGMVFQQFNLFPHlTVLENVTL-AP----IKVKKMSKaeaEERAMELLERvgLADKADAYPAQ----LSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1755737710 486 ALLKNPSILILDDTTSAVD--METEV-KIQGELKKitENTTTFIIAHRISSVKE-ADEILILNHGEIIERGT 553
Cdd:COG1126 150 ALAMEPKVMLFDEPTSALDpeLVGEVlDVMRDLAK--EGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGP 219
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
334-570 |
1.96e-33 |
|
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: 127.35 E-value: 1.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARkwHVRELRNHIA 413
Cdd:cd03300 1 IELENVSKFYGGFV---ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT--NLPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 414 TVMQDIFLFSD-TIEGNIAFG------APDATMEDVRRMARIADADHFIETMPESydtivgergvgLSGGQKQRISLARA 486
Cdd:cd03300 76 TVFQNYALFPHlTVFENIAFGlrlkklPKAEIKERVAEALDLVQLEGYANRKPSQ-----------LSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 487 LLKNPSILILDDTTSAVDMETEVKIQGELKKITENT-TTFI-IAHRISsvkEA----DEILILNHGEIIERGTHSsllae 560
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELgITFVfVTHDQE---EAltmsDRIAVMNKGKIQQIGTPE----- 216
|
250
....*....|
gi 1755737710 561 kgyyfDIYNK 570
Cdd:cd03300 217 -----EIYEE 221
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
334-548 |
2.39e-33 |
|
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: 126.60 E-value: 2.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFeddPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRElRNhIA 413
Cdd:cd03301 1 VELENVTKRF---GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-RD-IA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 414 TVMQDIFLFSD-TIEGNIAFG------APDATMEDVRRMARIADADHFIETMPESydtivgergvgLSGGQKQRISLARA 486
Cdd:cd03301 76 MVFQNYALYPHmTVYDNIAFGlklrkvPKDEIDERVREVAELLQIEHLLDRKPKQ-----------LSGGQRQRVALGRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1755737710 487 LLKNPSILILDDTTSAVDMETEVKIQGELKKITEN--TTTFIIAH-RISSVKEADEILILNHGEI 548
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlgTTTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
335-546 |
5.50e-33 |
|
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: 125.72 E-value: 5.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 335 EFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKwhvreLRNHIAT 414
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK-----ERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 415 VMQdiflfsdtiEGNIAFGAPdATMEDVRRMARIADADHFIETMPESYDTI------VG-----ERGVG-LSGGQKQRIS 482
Cdd:cd03235 73 VPQ---------RRSIDRDFP-ISVRDVVLMGLYGHKGLFRRLSKADKAKVdealerVGlselaDRQIGeLSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1755737710 483 LARALLKNPSILILDDTTSAVDMETEVKIQGELKKIT-ENTTTFIIAHRISSVKE-ADEILILNHG 546
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRrEGMTILVVTHDLGLVLEyFDRVLLLNRT 208
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
334-548 |
1.30e-32 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 124.44 E-value: 1.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEddPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRE---LRN 410
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 411 HIATVMQDIFLFSD-TIEGNIAFG------APDATMEDVRRMARIADADHFIETMPEsydtivgergvGLSGGQKQRISL 483
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFAlevtgvPPREIRKRVPAALELVGLSHKHRALPA-----------ELSGGEQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1755737710 484 ARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEA--DEILILNHGEI 548
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTtrHRVIALERGKL 214
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
334-553 |
2.04e-32 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 127.61 E-value: 2.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFE-DDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVREL---R 409
Cdd:PRK11153 2 IELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 410 NHIATVMQDIFLFSD-TIEGNIAF-----GAPDATMEdvrrmARIAD-------ADHfIETMPESydtivgergvgLSGG 476
Cdd:PRK11153 82 RQIGMIFQHFNLLSSrTVFDNVALplelaGTPKAEIK-----ARVTEllelvglSDK-ADRYPAQ-----------LSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 477 QKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRISSVKE-ADEILILNHGEIIERGT 553
Cdd:PRK11153 145 QKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
334-548 |
2.44e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 124.82 E-value: 2.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDarkwhVRELRNHIA 413
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP-----PRRARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 414 TVMQDIflfsdtiegNIAFGAPdATMEDVRRMARI--------------ADADHFIET--MPESYDTIVGErgvgLSGGQ 477
Cdd:COG1121 79 YVPQRA---------EVDWDFP-ITVRDVVLMGRYgrrglfrrpsradrEAVDEALERvgLEDLADRPIGE----LSGGQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1755737710 478 KQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKIT-ENTTTFIIAHRISSVKE-ADEILILNHGEI 548
Cdd:COG1121 145 QQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRrEGKTILVVTHDLGAVREyFDRVLLLNRGLV 217
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
337-549 |
3.39e-32 |
|
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: 123.14 E-value: 3.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 337 KNVSFHFEDdpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDArkwHVRELRNHIATVM 416
Cdd:cd03226 3 ENISFSYKK--GTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 417 QDI--FLFSDTIEGNIAFGAPDATmedvrrmARIADADHFIETM---------PESydtivgergvgLSGGQKQRISLAR 485
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGLKELD-------AGNEQAETVLKDLdlyalkerhPLS-----------LSGGQKQRLAIAA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1755737710 486 ALLKNPSILILDDTTSAVD---METEVKIQGELKKitENTTTFIIAHRISSVKE-ADEILILNHGEII 549
Cdd:cd03226 140 ALLSGKDLLIFDEPTSGLDyknMERVGELIRELAA--QGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
334-553 |
1.01e-31 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 125.64 E-value: 1.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFeddPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKW-HVRElRNhI 412
Cdd:COG1118 3 IEVRNISKRF---GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNlPPRE-RR-V 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 413 ATVMQDIFLFSD-TIEGNIAFGAPDATM------EDVRRMARIADADHFIETMPESydtivgergvgLSGGQKQRISLAR 485
Cdd:COG1118 78 GFVFQHYALFPHmTVAENIAFGLRVRPPskaeirARVEELLELVQLEGLADRYPSQ-----------LSGGQRQRVALAR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1755737710 486 ALLKNPSILILDDTTSAVDmeTEVK--IQGELKKITENT--TTFIIAH------RIssvkeADEILILNHGEIIERGT 553
Cdd:COG1118 147 ALAVEPEVLLLDEPFGALD--AKVRkeLRRWLRRLHDELggTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGT 217
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
22-290 |
1.30e-31 |
|
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: 124.45 E-value: 1.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 22 FILIFIASGISIIYPLLGGKVIDDVVYQNK-------TNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFRIRED 94
Cdd:cd18554 5 IVIGLVRFGIPLLLPLILKYIVDDVIQGSSltldekvYKLFTIIGIMFFIFLILRPPVEYYRQYFAQWIANKILYDIRKD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 95 LYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTM 174
Cdd:cd18554 85 LFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 175 KMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLV 254
Cdd:cd18554 165 YFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVNTITDLAP 244
|
250 260 270
....*....|....*....|....*....|....*.
gi 1755737710 255 VITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMR 290
Cdd:cd18554 245 LLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLR 280
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
334-558 |
2.40e-31 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 121.74 E-value: 2.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDdpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDAR--KWHVRELRNH 411
Cdd:PRK09493 2 IEFKNVSKHFGP---TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 412 IATVMQDIFLFSD-TIEGNIAFGaP----DATMEDVRRMAR--------IADADHFietmPESydtivgergvgLSGGQK 478
Cdd:PRK09493 79 AGMVFQQFYLFPHlTALENVMFG-PlrvrGASKEEAEKQARellakvglAERAHHY----PSE-----------LSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 479 QRISLARALLKNPSILILDDTTSAVDMET--EV-KIQGELKkiTENTTTFIIAHRISSVKE-ADEILILNHGEIIERGTH 554
Cdd:PRK09493 143 QRVAIARALAVKPKLMLFDEPTSALDPELrhEVlKVMQDLA--EEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDP 220
|
....
gi 1755737710 555 SSLL 558
Cdd:PRK09493 221 QVLI 224
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
159-559 |
3.02e-31 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 129.86 E-value: 3.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 159 TLALVIVTPLIAILTMKMSSKAqpvfyeiRESFSRLN---SMVEENISGNRVVKAFARED-FEMKKFHEHNED---FKKR 231
Cdd:PLN03130 447 SLMLVLMFPIQTFIISKMQKLT-------KEGLQRTDkriGLMNEVLAAMDTVKCYAWENsFQSKVQTVRDDElswFRKA 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 232 NLDSADVSRtylpVLDSLAgmlVVITLI-FGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASSFKIQ 310
Cdd:PLN03130 520 QLLSAFNSF----ILNSIP---VLVTVVsFGVFTLLGGDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLE 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 311 DMMATDAKI-----PIHAEKPAPSLqghvefKNVSFHFEDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRF 385
Cdd:PLN03130 593 ELLLAEERVllpnpPLEPGLPAISI------KNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGE 666
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 386 YDPTSGEILIdgvdarkwhvreLRNHIATVMQDIFLFSDTIEGNIAFGAP-DAtmEDVRRMARIADADHFIETMPESYDT 464
Cdd:PLN03130 667 LPPRSDASVV------------IRGTVAYVPQVSWIFNATVRDNILFGSPfDP--ERYERAIDVTALQHDLDLLPGGDLT 732
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 465 IVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMET-----EVKIQGELKKITENTTTFIIaHRISSVkeaDE 539
Cdd:PLN03130 733 EIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVgrqvfDKCIKDELRGKTRVLVTNQL-HFLSQV---DR 808
|
410 420
....*....|....*....|
gi 1755737710 540 ILILNHGEIIERGTHSSLLA 559
Cdd:PLN03130 809 IILVHEGMIKEEGTYEELSN 828
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
334-548 |
4.30e-31 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 120.33 E-value: 4.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDG--VDARKWHVRELRNH 411
Cdd:cd03262 1 IEIKNLHKSFGDFH---VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkLTDDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 412 IATVMQDIFLFSD-TIEGNIAFG-----------APDATMEDVRRMARIADADHFIETmpesydtivgergvgLSGGQKQ 479
Cdd:cd03262 78 VGMVFQQFNLFPHlTVLENITLApikvkgmskaeAEERALELLEKVGLADKADAYPAQ---------------LSGGQQQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1755737710 480 RISLARALLKNPSILILDDTTSAVDMET--EV-KIQGELKKitENTTTFIIAHRISSVKE-ADEILILNHGEI 548
Cdd:cd03262 143 RVAIARALAMNPKVMLFDEPTSALDPELvgEVlDVMKDLAE--EGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
352-560 |
4.83e-31 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 121.98 E-value: 4.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWH---VRELRNH-IATVMQDIFLFSD-TI 426
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRKkISMVFQSFALLPHrTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 427 EGNIAFGapdatME--DVRRMARIADADHFIETMP-ESY-DTIVGErgvgLSGGQKQRISLARALLKNPSILILDDTTSA 502
Cdd:cd03294 120 LENVAFG-----LEvqGVPRAEREERAAEALELVGlEGWeHKYPDE----LSGGMQQRVGLARALAVDPDILLMDEAFSA 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1755737710 503 VD------METE-VKIQGELKKitenTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAE 560
Cdd:cd03294 191 LDplirreMQDElLRLQAELQK----TIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
335-559 |
4.91e-31 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 120.63 E-value: 4.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 335 EFKNVSFHFEDDPntdvlKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVD-------ARKwhvre 407
Cdd:COG3840 3 RLDDLTYRYGDFP-----LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDltalppaERP----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 408 lrnhIATVMQDIFLFSD-TIEGNIAFG-APDA--TMEDVRRMARIADA---DHFIETMPESydtivgergvgLSGGQKQR 480
Cdd:COG3840 73 ----VSMLFQENNLFPHlTVAQNIGLGlRPGLklTAEQRAQVEQALERvglAGLLDRLPGQ-----------LSGGQRQR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 481 ISLARALLKNPSILILDDTTSAVD------METEVK-IQGELkkiteNTTTFIIAHRISSVKE-ADEILILNHGEIIERG 552
Cdd:COG3840 138 VALARCLVRKRPILLLDEPFSALDpalrqeMLDLVDeLCRER-----GLTVLMVTHDPEDAARiADRVLLVADGRIAADG 212
|
....*..
gi 1755737710 553 THSSLLA 559
Cdd:COG3840 213 PTAALLD 219
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
352-560 |
6.86e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 122.08 E-value: 6.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVD--ARKWHVRELRNHIATVMQ--DIFLFSDTIE 427
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDitDKKVKLSDIRKKVGLVFQypEYQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 428 GNIAFGAPDATMEDVRRMARIADAdhfIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMET 507
Cdd:PRK13637 103 KDIAFGPINLGLSEEEIENRVKRA---MNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1755737710 508 EVKIQGELKKITE--NTTTFIIAHRISSV-KEADEILILNHGEIIERGTHSSLLAE 560
Cdd:PRK13637 180 RDEILNKIKELHKeyNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
334-553 |
1.06e-30 |
|
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: 120.14 E-value: 1.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRElRNhIA 413
Cdd:cd03296 3 IEVRNVSKRFGDFV---ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE-RN-VG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 414 TVMQDIFLFSD-TIEGNIAFG---------APDATMED-VRRMARIADADHFIETMPESydtivgergvgLSGGQKQRIS 482
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVAFGlrvkprserPPEAEIRAkVHELLKLVQLDWLADRYPAQ-----------LSGGQRQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755737710 483 LARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENT--TTFIIAHRISSVKE-ADEILILNHGEIIERGT 553
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELhvTTVFVTHDQEEALEvADRVVVMNKGRIEQVGT 220
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
162-564 |
1.43e-30 |
|
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: 127.75 E-value: 1.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 162 LVIVTPLIAILTMKMSSkaqpvfYEIRESFSRLN--SMVEENISGNRVVKAFAREDFEMKKF----HEHNEDFKKRNLDS 235
Cdd:TIGR00957 467 MVLMVPLNAVMAMKTKT------YQVAHMKSKDNriKLMNEILNGIKVLKLYAWELAFLDKVegirQEELKVLKKSAYLH 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 236 ADVSRTYL--PVLDSLAGMLVVITLIFGGylVIKGQMTLGDLVAFNgflwMLNGPMRMSGWLINDVQRFIASSFKIQDMM 313
Cdd:TIGR00957 541 AVGTFTWVctPFLVALITFAVYVTVDENN--ILDAEKAFVSLALFN----ILRFPLNILPMVISSIVQASVSLKRLRIFL 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 314 ATDAKIPIHAE-KPAPSLQGH-VEFKNVSFHF-EDDPNTdvLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTS 390
Cdd:TIGR00957 615 SHEELEPDSIErRTIKPGEGNsITVHNATFTWaRDLPPT--LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVE 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 391 GEILIDGvdarkwhvrelrnHIATVMQDIFLFSDTIEGNIAFGAP------DATMEDVrrmARIADadhfIETMPESYDT 464
Cdd:TIGR00957 693 GHVHMKG-------------SVAYVPQQAWIQNDSLRENILFGKAlnekyyQQVLEAC---ALLPD----LEILPSGDRT 752
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 465 IVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVD-------METEVKIQGELKkiteNTTTFIIAHRISSVKEA 537
Cdd:TIGR00957 753 EIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDahvgkhiFEHVIGPEGVLK----NKTRILVTHGISYLPQV 828
|
410 420
....*....|....*....|....*..
gi 1755737710 538 DEILILNHGEIIERGTHSSLLAEKGYY 564
Cdd:TIGR00957 829 DVIIVMSGGKISEMGSYQELLQRDGAF 855
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
75-557 |
2.36e-30 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 127.01 E-value: 2.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 75 TYQIMCE-RIGQNSL---FRIREDL----YKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSwvsynILENVFLFSF 146
Cdd:PLN03232 352 TFGVLCEsQYFQNVGrvgFRLRSTLvaaiFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAE-----QLHGLWSAPF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 147 AIII-MAAIDWKL-------TLALVIVTPLIAILTMKMSSKAqpvfyeiRESFSRLN---SMVEENISGNRVVKAFARE- 214
Cdd:PLN03232 427 RIIVsMVLLYQQLgvaslfgSLILFLLIPLQTLIVRKMRKLT-------KEGLQWTDkrvGIINEILASMDTVKCYAWEk 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 215 DFEMKKFHEHNED---FKKRNLDSADVSRtylpVLDSLAgmlVVITLI-FGGYLVIKGQMTLGDLVAFNGFLWMLNGPMR 290
Cdd:PLN03232 500 SFESRIQGIRNEElswFRKAQLLSAFNSF----ILNSIP---VVVTLVsFGVFVLLGGDLTPARAFTSLSLFAVLRSPLN 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 291 MSGWLINDVQRFIASSFKIQDMMATDAKI-----PIHAEKPAPSLqghvefKNVSFHFEDDPNTDVLKNISLKASPGQTI 365
Cdd:PLN03232 573 MLPNLLSQVVNANVSLQRIEELLLSEERIlaqnpPLQPGAPAISI------KNGYFSWDSKTSKPTLSDINLEIPVGSLV 646
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 366 AILGETGAGKSTLVNLICRFYDPTSGEILIdgvdarkwhvreLRNHIATVMQDIFLFSDTIEGNIAFGApDATMEDVRRM 445
Cdd:PLN03232 647 AIVGGTGEGKTSLISAMLGELSHAETSSVV------------IRGSVAYVPQVSWIFNATVRENILFGS-DFESERYWRA 713
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 446 ARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKI-QGELKKITENTTT 524
Cdd:PLN03232 714 IDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVfDSCMKDELKGKTR 793
|
490 500 510
....*....|....*....|....*....|...
gi 1755737710 525 FIIAHRISSVKEADEILILNHGEIIERGTHSSL 557
Cdd:PLN03232 794 VLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL 826
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
107-564 |
3.56e-30 |
|
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: 126.56 E-value: 3.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 107 FNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTMKMSSKAQPVFYE 186
Cdd:TIGR01271 976 LNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQL 1055
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 187 IRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHehnedfKKRNLDSADvsrtYLPVLDSLAGMLVVITLIF------ 260
Cdd:TIGR01271 1056 ESEARSPIFSHLITSLKGLWTIRAFGRQSYFETLFH------KALNLHTAN----WFLYLSTLRWFQMRIDIIFvfffia 1125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 261 ------GGYLVIKGQMTLGDLVAFN---GFLWMLNGPMRMSGWL--INDVQRFI------------ASSFKIQDMMATDA 317
Cdd:TIGR01271 1126 vtfiaiGTNQDGEGEVGIILTLAMNilsTLQWAVNSSIDVDGLMrsVSRVFKFIdlpqeeprpsggGGKYQLSTVLVIEN 1205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 318 KipiHAEKPAPSlQGHVEFKNVSFHFEDDPNTdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDpTSGEILIDG 397
Cdd:TIGR01271 1206 P---HAQKCWPS-GGQMDVQGLTAKYTEAGRA-VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDG 1279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 398 VDARKWHVRELRNHIATVMQDIFLFSDTIEGNIAfgaPDA--TMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSG 475
Cdd:TIGR01271 1280 VSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLD---PYEqwSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSN 1356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 476 GQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHS 555
Cdd:TIGR01271 1357 GHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQ 1436
|
....*....
gi 1755737710 556 SLLAEKGYY 564
Cdd:TIGR01271 1437 KLLNETSLF 1445
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
334-552 |
4.62e-30 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 117.29 E-value: 4.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFeddPNTDVLKNISLKASPGQTiAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKwHVRELRNHIA 413
Cdd:cd03264 1 LQLENLTKRY---GKKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 414 TVMQDIFLFSD-TIEGNIAFGAPDATMEDVRRMARIadaDHFIE--TMPESYDTIVGergvGLSGGQKQRISLARALLKN 490
Cdd:cd03264 76 YLPQEFGVYPNfTVREFLDYIAWLKGIPSKEVKARV---DEVLElvNLGDRAKKKIG----SLSGGMRRRVGIAQALVGD 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1755737710 491 PSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKE-ADEILILNHGEIIERG 552
Cdd:cd03264 149 PSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
22-278 |
7.80e-30 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 119.16 E-value: 7.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 22 FILIFIASGISIIYPLLGGKVIDdVVYQNKTNLLIPLLLIMIISTI------IRTICRYTYQIMCERIGQNSLFRIREDL 95
Cdd:cd18573 2 LALLLVSSAVTMSVPFAIGKLID-VASKESGDIEIFGLSLKTFALAllgvfvVGAAANFGRVYLLRIAGERIVARLRKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 96 YKKLQSLDFDFFNNTRVGDIMARMTGDTDAI-RHFVSWVSyNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTM 174
Cdd:cd18573 81 FKSILRQDAAFFDKNKTGELVSRLSSDTSVVgKSLTQNLS-DGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 175 KMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLdSLAGMLV 254
Cdd:cd18573 160 FYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGST-GFSGNLS 238
|
250 260
....*....|....*....|....*
gi 1755737710 255 VIT-LIFGGYLVIKGQMTLGDLVAF 278
Cdd:cd18573 239 LLSvLYYGGSLVASGELTVGDLTSF 263
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
332-564 |
8.10e-30 |
|
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: 118.42 E-value: 8.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 332 GHVEFKNVSFHFEDDPNTdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDpTSGEILIDGVDARKWHVRELRNH 411
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNA-VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 412 IATVMQDIFLFSDTIEGNI-AFGApdATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKN 490
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLdPYGK--WSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755737710 491 PSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAEKGYY 564
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
334-550 |
9.56e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 122.82 E-value: 9.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFeddPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNH-I 412
Cdd:COG1129 5 LEMRGISKSF---GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 413 ATVMQDIFLFSD-TIEGNIAFGAPDATMEDVRRMARIADADHFIETM--PESYDTIVGErgvgLSGGQKQRISLARALLK 489
Cdd:COG1129 82 AIIHQELNLVPNlSVAENIFLGREPRRGGLIDWRAMRRRARELLARLglDIDPDTPVGD----LSVAQQQLVEIARALSR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1755737710 490 NPSILILDDTTSAVDmETEV----KIQGELKKitENTTTFIIAHRISSVKE-ADEILILNHGEIIE 550
Cdd:COG1129 158 DARVLILDEPTASLT-EREVerlfRIIRRLKA--QGVAIIYISHRLDEVFEiADRVTVLRDGRLVG 220
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
334-553 |
2.61e-29 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 119.67 E-value: 2.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDdpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARkwHVRELRNHIA 413
Cdd:PRK09452 15 VELRGISKSFDG---KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT--HVPAENRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 414 TVMQDIFLFSD-TIEGNIAFG-----APDATME----DVRRMARIadaDHFIETMPESydtivgergvgLSGGQKQRISL 483
Cdd:PRK09452 90 TVFQSYALFPHmTVFENVAFGlrmqkTPAAEITprvmEALRMVQL---EEFAQRKPHQ-----------LSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1755737710 484 ARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENT-TTFI-IAHrisSVKEA----DEILILNHGEIIERGT 553
Cdd:PRK09452 156 ARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLgITFVfVTH---DQEEAltmsDRIVVMRDGRIEQDGT 228
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
334-552 |
4.02e-29 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 114.19 E-value: 4.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSF---HFEDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLIC--RFYDPTSGEILIDGVDARKwhvREL 408
Cdd:cd03213 4 LSFRNLTVtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLDK---RSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 409 RNHIATVMQ-DIFLFSDTIEGNIAFGApdatmeDVRrmariadadhfietmpesydtivgergvGLSGGQKQRISLARAL 487
Cdd:cd03213 81 RKIIGYVPQdDILHPTLTVRETLMFAA------KLR----------------------------GLSGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1755737710 488 LKNPSILILDDTTSAVDMETEVKIQGELKKIT-ENTTTFIIAHRISS--VKEADEILILNHGEIIERG 552
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAdTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
334-553 |
6.28e-29 |
|
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: 117.08 E-value: 6.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDPNT-DVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDP---TSGEILIDGVDARKWHVRELR 409
Cdd:COG0444 2 LEVRNLKVYFPTRRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 410 ----NHIATVMQD-----------IFLFSDTIEgnIAFGAPDAtmeDVRRMAR-------IADADHFIETMP-Esydtiv 466
Cdd:COG0444 82 kirgREIQMIFQDpmtslnpvmtvGDQIAEPLR--IHGGLSKA---EARERAIellervgLPDPERRLDRYPhE------ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 467 gergvgLSGGQKQRISLARALLKNPSILILDDTTSAVDmeteVKIQGE----LKKITE--NTTTFIIAHRISSVKE-ADE 539
Cdd:COG0444 151 ------LSGGMRQRVMIARALALEPKLLIADEPTTALD----VTIQAQilnlLKDLQRelGLAILFITHDLGVVAEiADR 220
|
250
....*....|....
gi 1755737710 540 ILILNHGEIIERGT 553
Cdd:COG0444 221 VAVMYAGRIVEEGP 234
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
334-549 |
1.11e-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: 111.75 E-value: 1.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFeddPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNH-I 412
Cdd:cd03216 1 LELRGITKRF---GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAgI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 413 ATVMQdiflfsdtiegniafgapdatmedvrrmariadadhfietmpesydtivgergvgLSGGQKQRISLARALLKNPS 492
Cdd:cd03216 78 AMVYQ-------------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 493 ILILDDTTSAV-DMETEvKIQGELKKITENTTTFI-IAHRISSVKE-ADEILILNHGEII 549
Cdd:cd03216 103 LLILDEPTAALtPAEVE-RLFKVIRRLRAQGVAVIfISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
352-552 |
1.28e-28 |
|
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: 113.16 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 352 LKNISLKAS---PGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGV---DARK-WHVRELRNHIATVMQDIFLFSD 424
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRKkINLPPQQRKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 425 -TIEGNIAFGAP-DATMEDVRRMARIADADHFietmpesyDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSA 502
Cdd:cd03297 90 lNVRENLAFGLKrKRNREDRISVDELLDLLGL--------DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1755737710 503 VDMETEVKIQGELKKITE--NTTTFIIAHRISSV-KEADEILILNHGEIIERG 552
Cdd:cd03297 162 LDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
72-553 |
2.18e-28 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 121.04 E-value: 2.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 72 CRYTYQIMceRIGQNSLFRireDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIM 151
Cdd:PTZ00243 1019 FFLSYEAM--RRGSRNMHR---DLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVT 1093
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 152 AAIDWKLTLALVIVTPLIAILTMKMSSKAQpvfyEIRESFSRLNS----MVEENISGNRVVKAFAREDFEMKK-FHEHNE 226
Cdd:PTZ00243 1094 SASQPFVLVALVPCGYLYYRLMQFYNSANR----EIRRIKSVAKSpvftLLEEALQGSATITAYGKAHLVMQEaLRRLDV 1169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 227 DFKKRNLDsaDVSRTYLPVLDSLAGMLVVITLIFGGylvIKGQMTLGD-----LVAFNGFLWM-----LNGPMRMSGWL- 295
Cdd:PTZ00243 1170 VYSCSYLE--NVANRWLGVRVEFLSNIVVTVIALIG---VIGTMLRATsqeigLVSLSLTMAMqttatLNWLVRQVATVe 1244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 296 --INDVQRFIASSFKI--QDMMATDAKI--------------------PIHAEKPAP-SLQ-GHVEFKNVSFHFEDD-PN 348
Cdd:PTZ00243 1245 adMNSVERLLYYTDEVphEDMPELDEEVdalerrtgmaadvtgtvviePASPTSAAPhPVQaGSLVFEGVQMRYREGlPL 1324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 349 tdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIATVMQDIFLFSDTIEG 428
Cdd:PTZ00243 1325 --VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQ 1402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 429 NIafgAP--DATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSILIL-DDTTSAVDM 505
Cdd:PTZ00243 1403 NV---DPflEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDP 1479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1755737710 506 ETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGT 553
Cdd:PTZ00243 1480 ALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGS 1527
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
82-278 |
2.95e-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: 350019 [Multi-domain] Cd Length: 289 Bit Score: 114.50 E-value: 2.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 82 RIGQNSLFRIREDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFV-SWVSYnILENVFLFSFAIIIMAAIDWKLTL 160
Cdd:cd18575 62 WLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVgSSLSI-ALRNLLLLIGGLVMLFITSPKLTL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 161 ALVIVTPLIAILTM-------KMSSKAQpvfyeirESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEdfkkrnl 233
Cdd:cd18575 141 LVLLVIPLVVLPIIlfgrrvrRLSRASQ-------DRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVE------- 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1755737710 234 DSADVSRTYLPVLDSLAGmlVVITLIF---------GGYLVIKGQMTLGDLVAF 278
Cdd:cd18575 207 AAFAAALRRIRARALLTA--LVIFLVFgaivfvlwlGAHDVLAGRMSAGELSQF 258
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
351-553 |
4.79e-28 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 112.53 E-value: 4.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNH-IATVMQDIFLFSD-TIEG 428
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIGRTFQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 429 NIAFGAPDATME------DVRRMARIAD-ADHFIETM--PESYDTIVGErgvgLSGGQKQRISLARALLKNPSILILDDT 499
Cdd:cd03219 95 NVMVAAQARTGSglllarARREEREARErAEELLERVglADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1755737710 500 TSAVDMETEVKIQGELKKITENTTTF-IIAHRISSVKE-ADEILILNHGEIIERGT 553
Cdd:cd03219 171 AAGLNPEETEELAELIRELRERGITVlLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
334-553 |
4.97e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 113.63 E-value: 4.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDG--VDARKWHVRELRNH 411
Cdd:PRK13639 2 LETRDLKYSYPDG--TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 412 IATVMQ--DIFLFSDTIEGNIAFGAPDA--TMEDVRRmaRIADA------DHFIETMPESydtivgergvgLSGGQKQRI 481
Cdd:PRK13639 80 VGIVFQnpDDQLFAPTVEEDVAFGPLNLglSKEEVEK--RVKEAlkavgmEGFENKPPHH-----------LSGGQKKRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755737710 482 SLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIA-HRISSV-KEADEILILNHGEIIERGT 553
Cdd:PRK13639 147 AIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVpVYADKVYVMSDGKIIKEGT 220
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
335-559 |
9.87e-28 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 112.24 E-value: 9.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 335 EFKNVSFHFED------DPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVREL 408
Cdd:COG4167 6 EVRNLSKTFKYrtglfrRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 409 RNHIATVMQDIflfSDTIEGNIAFG----AP---DATMEDVRRMARIadadhfIETMpesydtivgeRGVGL-------- 473
Cdd:COG4167 86 CKHIRMIFQDP---NTSLNPRLNIGqileEPlrlNTDLTAEEREERI------FATL----------RLVGLlpehanfy 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 474 ----SGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENT-TTFI-IAHRISSVKE-ADEILILNHG 546
Cdd:COG4167 147 phmlSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLgISYIyVSQHLGIVKHiSDKVLVMHQG 226
|
250
....*....|...
gi 1755737710 547 EIIERGTHSSLLA 559
Cdd:COG4167 227 EVVEYGKTAEVFA 239
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
334-548 |
1.88e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 111.75 E-value: 1.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIA 413
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 414 TVMQ--DIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETMpeSYDTIVGERgvgLSGGQKQRISLARALLKNP 491
Cdd:PRK13650 85 MVFQnpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQ--DFKEREPAR---LSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1755737710 492 SILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRISSVKEADEILILNHGEI 548
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
22-278 |
1.91e-27 |
|
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: 112.02 E-value: 1.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 22 FILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICR----YTYQIMCERIGqnslFRIREDLYK 97
Cdd:cd18784 2 FFFLLAAAVGEIFIPYYTGQVIDGIVIEKSQDKFSRAIIIMGLLAIASSVAAgirgGLFTLAMARLN----IRIRNLLFR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 98 KLQSLDFDFFNNTRVGDIMARMTGDTDAIrhfVSWVSYNIleNVFLFSF-----AIIIMAAIDWKLTLALVIVTPLIAIL 172
Cdd:cd18784 78 SIVSQEIGFFDTVKTGDITSRLTSDTTTM---SDTVSLNL--NIFLRSLvkaigVIVFMFKLSWQLSLVTLIGLPLIAIV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 173 T-------MKMSSKAQpvfyeirESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPV 245
Cdd:cd18784 153 SkvygdyyKKLSKAVQ-------DSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWS 225
|
250 260 270
....*....|....*....|....*....|...
gi 1755737710 246 LDSLAGMLVVITLIFGGYLVIKGQMTLGDLVAF 278
Cdd:cd18784 226 NELTELALTVSTLYYGGHLVITGQISGGNLISF 258
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
336-576 |
3.74e-27 |
|
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: 117.32 E-value: 3.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 336 FKNVSFHFeddpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGvdarkwhvrelrnHIATV 415
Cdd:TIGR01271 431 FSNFSLYV-----TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFS 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 416 MQDIFLFSDTIEGNIAFGApdaTMEDVRRMARI--ADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSI 493
Cdd:TIGR01271 493 PQTSWIMPGTIKDNIIFGL---SYDEYRYTSVIkaCQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADL 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 494 LILDDTTSAVDMETEVKI-QGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAEKGyyfDIYNKQL 572
Cdd:TIGR01271 570 YLLDSPFTHLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRP---DFSSLLL 646
|
....
gi 1755737710 573 GTEA 576
Cdd:TIGR01271 647 GLEA 650
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
334-553 |
4.50e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 110.88 E-value: 4.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIA 413
Cdd:PRK13635 6 IRVEHISFRYPDA-ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 414 TVMQ--DIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADH------FIETMPESydtivgergvgLSGGQKQRISLAR 485
Cdd:PRK13635 85 MVFQnpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRqvgmedFLNREPHR-----------LSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 486 ALLKNPSILILDDTTSAVDMETEVKIQGELKKITENT--TTFIIAHRISSVKEADEILILNHGEIIERGT 553
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEILEEGT 223
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
319-552 |
9.98e-27 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 112.24 E-value: 9.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 319 IPIHAEKPAPSLQGHVEFKNVSFHFEDDPNTDvlkNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGV 398
Cdd:PRK11607 5 IPRPQAKTRKALTPLLEIRNLTKSFDGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 399 DARkwHVRELRNHIATVMQDIFLFSD-TIEGNIAFG-----APDATMED-VRRMARIADADHFIETMPESydtivgergv 471
Cdd:PRK11607 82 DLS--HVPPYQRPINMMFQSYALFPHmTVEQNIAFGlkqdkLPKAEIASrVNEMLGLVHMQEFAKRKPHQ---------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 472 gLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAH-RISSVKEADEILILNHGEI 548
Cdd:PRK11607 150 -LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILErvGVTCVMVTHdQEEAMTMAGRIAIMNRGKF 228
|
....
gi 1755737710 549 IERG 552
Cdd:PRK11607 229 VQIG 232
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
327-561 |
1.11e-26 |
|
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: 109.95 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 327 APSLQGHVEFKNVSFHfeddpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGvdarkwhvr 406
Cdd:cd03291 33 HSSDDNNLFFSNLCLV-----GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG--------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 407 elrnHIATVMQDIFLFSDTIEGNIAFGApdaTMEDVRRMARI--ADADHFIETMPESYDTIVGERGVGLSGGQKQRISLA 484
Cdd:cd03291 99 ----RISFSSQFSWIMPGTIKENIIFGV---SYDEYRYKSVVkaCQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1755737710 485 RALLKNPSILILDDTTSAVDMETEVKI-QGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAEK 561
Cdd:cd03291 172 RAVYKDADLYLLDSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
334-553 |
3.36e-26 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 110.17 E-value: 3.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEddpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRElrNHIA 413
Cdd:PRK10851 3 IEIANIKKSFG---RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 414 TVMQDIFLFSD-TIEGNIAFG--------APDATM--EDVRRMARIADADHFIETMPESydtivgergvgLSGGQKQRIS 482
Cdd:PRK10851 78 FVFQHYALFRHmTVFDNIAFGltvlprreRPNAAAikAKVTQLLEMVQLAHLADRYPAQ-----------LSGGQKQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755737710 483 LARALLKNPSILILDDTTSAVDMETEVKIQGELKKITEN---TTTFIIAHRISSVKEADEILILNHGEIIERGT 553
Cdd:PRK10851 147 LARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElkfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
352-553 |
4.76e-26 |
|
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: 106.30 E-value: 4.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKwHVRELRNHIATVMQDIFLfSDTIEG--N 429
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSV-DDELTGweN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 430 IAFGAPDATMEDVRRMARIADADHFIETMpESYDTIVGErgvgLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEV 509
Cdd:cd03265 94 LYIHARLYGVPGAERRERIDELLDFVGLL-EAADRLVKT----YSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1755737710 510 KIQGELKKI--TENTTTFIIAHRISSVKE-ADEILILNHGEIIERGT 553
Cdd:cd03265 169 HVWEYIEKLkeEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGT 215
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
351-550 |
5.03e-26 |
|
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: 107.58 E-value: 5.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKW---HVRELRNHIATVMQD---IFLFSD 424
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkQRRAFRRDVQLVFQDspsAVNPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 425 TIEGNIafGAPDATMEDVRRMARIADADHFIETMpESYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVD 504
Cdd:TIGR02769 106 TVRQII--GEPLRHLTSLDESEQKARIAELLDMV-GLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1755737710 505 METEVKIQGELKKITE--NTTTFIIAHRISSVKE-ADEILILNHGEIIE 550
Cdd:TIGR02769 183 MVLQAVILELLRKLQQafGTAYLFITHDLRLVQSfCQRVAVMDKGQIVE 231
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
333-551 |
6.58e-26 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 106.87 E-value: 6.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 333 HVEFKNVSFHFE-DDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGV-----DARKwhvr 406
Cdd:COG4525 3 MLTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVpvtgpGADR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 407 elrnhiATVMQDIFLFS--DTIEgNIAFGApdaTMEDVRRMARIADADHFIEtmpesydtIVGERGVG------LSGGQK 478
Cdd:COG4525 79 ------GVVFQKDALLPwlNVLD-NVAFGL---RLRGVPKAERRARAEELLA--------LVGLADFArrriwqLSGGMR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 479 QRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKI--TENTTTFIIAHrisSVKEA----DEILIL--NHGEIIE 550
Cdd:COG4525 141 QRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVwqRTGKGVFLITH---SVEEAlflaTRLVVMspGPGRIVE 217
|
.
gi 1755737710 551 R 551
Cdd:COG4525 218 R 218
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
334-553 |
1.18e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 106.37 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDPNTdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIA 413
Cdd:PRK13648 8 IVFKNVSFQYQSDASF-TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 414 TVMQDI---FLFSdTIEGNIAFG-----APDATM--------EDVRRMARiadADHfietMPESydtivgergvgLSGGQ 477
Cdd:PRK13648 87 IVFQNPdnqFVGS-IVKYDVAFGlenhaVPYDEMhrrvsealKQVDMLER---ADY----EPNA-----------LSGGQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1755737710 478 KQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRISSVKEADEILILNHGEIIERGT 553
Cdd:PRK13648 148 KQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSehNITIISITHDLSEAMEADHVIVMNKGTVYKEGT 225
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
334-558 |
1.37e-25 |
|
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: 105.94 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDdpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSG-EILIDGVDARKWHVRELRNHI 412
Cdd:COG1119 4 LELRNVTVRRGG---KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 413 ATV---MQDIFLFSDTIE--------GNIA-FGAPDATMED-VRRMARIADADHFIETmpeSYDTivgergvgLSGGQKQ 479
Cdd:COG1119 81 GLVspaLQLRFPRDETVLdvvlsgffDSIGlYREPTDEQRErARELLELLGLAHLADR---PFGT--------LSQGEQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 480 RISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFII--AHRISSVKEA-DEILILNHGEIIERGTHSS 556
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVlvTHHVEEIPPGiTHVLLLKDGRVVAAGPKEE 229
|
..
gi 1755737710 557 LL 558
Cdd:COG1119 230 VL 231
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
352-558 |
1.63e-25 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 108.97 E-value: 1.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVREL----RNHIATVMQDIFLFSD-TI 426
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSFALMPHmTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 427 EGNIAFGAPDATMEDVRRMARIADA------DHFIETMPESydtivgergvgLSGGQKQRISLARALLKNPSILILDDTT 500
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDAlrqvglENYAHSYPDE-----------LSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1755737710 501 SAVDMETEVKIQGELKKIT---ENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLL 558
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQakhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
351-549 |
4.85e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 104.40 E-value: 4.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKW--HVRElrNHIATVMQDIFL---FSDT 425
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLpeYKRA--KYIGRVFQDPMMgtaPSMT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 426 IEGNIAFgapdATMEDVRRMARIA----DADHFIET-------MPESYDTIVGErgvgLSGGQKQRISLARALLKNPSIL 494
Cdd:COG1101 99 IEENLAL----AYRRGKRRGLRRGltkkRRELFRELlatlglgLENRLDTKVGL----LSGGQRQALSLLMATLTKPKLL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1755737710 495 ILDDTTSAVD-------METEVKIQGElkkitENTTTFIIAHrisSVKEA----DEILILNHGEII 549
Cdd:COG1101 171 LLDEHTAALDpktaalvLELTEKIVEE-----NNLTTLMVTH---NMEQAldygNRLIMMHEGRII 228
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
334-553 |
8.83e-25 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 102.58 E-value: 8.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDPNTdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKwHVRELRNHIA 413
Cdd:cd03263 1 LQIRNLTKTYKKGTKP-AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 414 TVMQDIFLFSD-TIEGNIAFGAPdatMEDVRRMARIADADHFIETM-PESY-DTIVGErgvgLSGGQKQRISLARALLKN 490
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFYAR---LKGLPKSEIKEEVELLLRVLgLTDKaNKRART----LSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1755737710 491 PSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHrisSVKEA----DEILILNHGEIIERGT 553
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTH---SMDEAealcDRIAIMSDGKLRCIGS 215
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
334-553 |
1.08e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 104.11 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDPNTdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGE---ILIDGVDARKWHVRELRN 410
Cdd:PRK13640 6 VEFKHVSFTYPDSKKP-ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 411 HIATVMQ--DIFLFSDTIEGNIAFG-----APDATMED-VRRMARIADADHFIETMPESydtivgergvgLSGGQKQRIS 482
Cdd:PRK13640 85 KVGIVFQnpDNQFVGATVGDDVAFGlenraVPRPEMIKiVRDVLADVGMLDYIDSEPAN-----------LSGGQKQRVA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1755737710 483 LARALLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRISSVKEADEILILNHGEIIERGT 553
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
324-552 |
1.09e-24 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 103.19 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 324 EKPAPSLQGHVEFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYD--P---TSGEILIDGV 398
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDKQ---ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 399 D--ARKWHVRELRNHIATVMQDIFLFSDTIEGNIAFGAP----------DATMEDVRRMARIADadhfietmpESYDTIv 466
Cdd:COG1117 79 DiyDPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGLRlhgikskselDEIVEESLRKAALWD---------EVKDRL- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 467 GERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVD-METEvKIQ---GELKKiteNTTTFIIAH------RISsvke 536
Cdd:COG1117 149 KKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpISTA-KIEeliLELKK---DYTIVIVTHnmqqaaRVS---- 220
|
250
....*....|....*.
gi 1755737710 537 aDEILILNHGEIIERG 552
Cdd:COG1117 221 -DYTAFFYLGELVEFG 235
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
342-546 |
1.53e-24 |
|
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: 102.02 E-value: 1.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 342 HFEDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGV--DARKWHVRELRNH--IATVMQ 417
Cdd:cd03290 7 YFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKneSEPSFEATRSRNRysVAYAAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 418 DIFLFSDTIEGNIAFGAPdatmEDVRRMARIADADHF---IETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSIL 494
Cdd:cd03290 87 KPWLLNATVEENITFGSP----FNKQRYKAVTDACSLqpdIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1755737710 495 ILDDTTSAVD--METEVKIQGELKKITENTTTFI-IAHRISSVKEADEILILNHG 546
Cdd:cd03290 163 FLDDPFSALDihLSDHLMQEGILKFLQDDKRTLVlVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
334-563 |
2.16e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 103.32 E-value: 2.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDP--NTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVD----ARKWHVRE 407
Cdd:PRK13646 3 IRFDNVSYTYQKGTpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITithkTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 408 LRNHIATVMQ--DIFLFSDTIEGNIAFGAPDATM--EDVRrmariADADHFIETMPESYDtIVGERGVGLSGGQKQRISL 483
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMnlDEVK-----NYAHRLLMDLGFSRD-VMSQSPFQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 484 ARALLKNPSILILDDTTSAVDMETEVKIQGELKKIT--ENTTTFIIAHRISSV-KEADEILILNHGEIIERGTHSSLLAE 560
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKD 236
|
...
gi 1755737710 561 KGY 563
Cdd:PRK13646 237 KKK 239
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
362-552 |
2.64e-24 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 101.03 E-value: 2.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 362 GQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARkwHVRELRNHIATVMQDIFLFSD-TIEGNIAFG-APD--A 437
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT--AAPPADRPVSMLFQENNLFAHlTVEQNVGLGlSPGlkL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 438 TMEDVRRMARIA---DADHFIETMPESydtivgergvgLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGE 514
Cdd:cd03298 102 TAEDRQAIEVALarvGLAGLEKRLPGE-----------LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1755737710 515 LKKITENT--TTFIIAHRISSVKE-ADEILILNHGEIIERG 552
Cdd:cd03298 171 VLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
349-560 |
2.90e-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: 100.97 E-value: 2.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 349 TDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKW--HVReLRNHIATVMQDIFLFSD-T 425
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLppHER-ARAGIGYVPEGRRIFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 426 IEGNIAFGApdatmeDVRRMARIAdadhfiETMPESYDT--IVGER----GVGLSGGQKQRISLARALLKNPSILILDDT 499
Cdd:cd03224 92 VEENLLLGA------YARRRAKRK------ARLERVYELfpRLKERrkqlAGTLSGGEQQMLAIARALMSRPKLLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1755737710 500 T-----SAVDmetevKIQGELKKI-TENTTTFIIAHRISSVKE-ADEILILNHGEIIERGTHSSLLAE 560
Cdd:cd03224 160 SeglapKIVE-----EIFEAIRELrDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLAD 222
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
334-560 |
2.93e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 102.14 E-value: 2.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDpntDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSG-----EILIDG---VDARKWHV 405
Cdd:PRK11264 4 IEVKNLVKKFHGQ---TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTarsLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 406 RELRNHIATVMQDIFLF------SDTIEGN-IAFGAPDatmEDVRRMARIADADHFIETMPESYDtivgERgvgLSGGQK 478
Cdd:PRK11264 81 RQLRQHVGFVFQNFNLFphrtvlENIIEGPvIVKGEPK---EEATARARELLAKVGLAGKETSYP----RR---LSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 479 QRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKIT-ENTTTFIIAHRISSVKE-ADEILILNHGEIIERGTHSS 556
Cdd:PRK11264 151 QRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAqEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKA 230
|
....
gi 1755737710 557 LLAE 560
Cdd:PRK11264 231 LFAD 234
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
331-549 |
3.35e-24 |
|
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: 101.19 E-value: 3.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 331 QGHVEFKNV-SFHFEDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLI-CRFYDP--TSGEILIDGVDARKWHVR 406
Cdd:cd03234 1 QRVLPWWDVgLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEGGgtTSGQILFNGQPRKPDQFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 407 ElrnHIATVMQ-DIFLFSDTIEGNIAFGAPDAT---MEDVRRMARIADadhfiETMPESYDTIVG-ERGVGLSGGQKQRI 481
Cdd:cd03234 81 K---CVAYVRQdDILLPGLTVRETLTYTAILRLprkSSDAIRKKRVED-----VLLRDLALTRIGgNLVKGISGGERRRV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1755737710 482 SLARALLKNPSILILDDTTSAVDMETEVKIQGELKKI-TENTTTFIIAH--RISSVKEADEILILNHGEII 549
Cdd:cd03234 153 SIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLaRRNRIVILTIHqpRSDLFRLFDRILLLSSGEIV 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
352-553 |
5.22e-24 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 105.92 E-value: 5.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 352 LKNISLKASPGQTIAILGETGAGKSTL----VNLIcrfydPTSGEILIDGVD---ARKWHVRELRNHIATVMQDIF---- 420
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDGQDldgLSRRALRPLRRRMQVVFQDPFgsls 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 421 --LfsdTIEGNIAFG----APDATMEDvrRMARIADAdhfietMPEsydtivgergVGL------------SGGQKQRIS 482
Cdd:COG4172 377 prM---TVGQIIAEGlrvhGPGLSAAE--RRARVAEA------LEE----------VGLdpaarhryphefSGGQRQRIA 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755737710 483 LARALLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRISSVKE-ADEILILNHGEIIERGT 553
Cdd:COG4172 436 IARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQRehGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGP 509
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
354-552 |
6.19e-24 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 102.89 E-value: 6.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 354 NISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVD---ARKWHVRELRNHIATVMQDIFLFSD---TIE 427
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDitgLSGRELRPLRRRMQMVFQDPYASLNprmTVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 428 GNIAFGApdatmeDVRRMARIADADHFIETMPESydtivgergVGL------------SGGQKQRISLARALLKNPSILI 495
Cdd:COG4608 116 DIIAEPL------RIHGLASKAERRERVAELLEL---------VGLrpehadryphefSGGQRQRIGIARALALNPKLIV 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1755737710 496 LDDTTSAVDmeteVKIQ-------GELKKitE-NTTTFIIAHRISSVKE-ADEILILNHGEIIERG 552
Cdd:COG4608 181 CDEPVSALD----VSIQaqvlnllEDLQD--ElGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIA 240
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
67-277 |
6.80e-24 |
|
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: 102.17 E-value: 6.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 67 IIRTICRYTYQIMCERIGQNSLFRIREDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSF 146
Cdd:cd18577 58 IGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 147 AIIIMAAIDWKLTLALVIVTPLIAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNE 226
Cdd:cd18577 138 GFIIAFIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALE 217
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1755737710 227 D-----FKKRNLDSAdvsrtylpvldSLAGMLVVITLIF------GGYLVIKGQMTLGDLVA 277
Cdd:cd18577 218 KarkagIKKGLVSGL-----------GLGLLFFIIFAMYalafwyGSRLVRDGEISPGDVLT 268
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
352-546 |
1.09e-23 |
|
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: 99.85 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDarkwhVRELRNHIATVMQDIFLFS-DTIEGNI 430
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQ-----ITEPGPDRMVVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 431 AFgAPDATMEDVRRMARIADADHFIET--MPESYDTIVGErgvgLSGGQKQRISLARALLKNPSILILDDTTSAVDMETE 508
Cdd:TIGR01184 76 AL-AVDRVLPDLSKSERRAIVEEHIALvgLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1755737710 509 VKIQGELKKITENT--TTFIIAHRI-SSVKEADEILILNHG 546
Cdd:TIGR01184 151 GNLQEELMQIWEEHrvTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
334-560 |
1.15e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 100.83 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDdpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKW-HVRELRNHI 412
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFsKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 413 ATVMQ--DIFLFSDTIEGNIAFGAPDATMEDVRRMARIADAdhFIETMPESYDTivgERGVGLSGGQKQRISLARALLKN 490
Cdd:PRK13644 80 GIVFQnpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRA--LAEIGLEKYRH---RSPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1755737710 491 PSILILDDTTSAVDMETEVKIQGELKKITENTTTFI-IAHRISSVKEADEILILNHGEIIERGTHSSLLAE 560
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVyITHNLEELHDADRIIVMDRGKIVLEGEPENVLSD 225
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
334-504 |
1.54e-23 |
|
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: 98.71 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKwHVRELRNHIA 413
Cdd:COG4133 3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 414 TVMQDIFLFSD-TIEGNIAFGA----PDATMEDVRRMARIADADHFIetmpesyDTIVGErgvgLSGGQKQRISLARALL 488
Cdd:COG4133 79 YLGHADGLKPElTVRENLRFWAalygLRADREAIDEALEAVGLAGLA-------DLPVRQ----LSAGQKRRVALARLLL 147
|
170
....*....|....*.
gi 1755737710 489 KNPSILILDDTTSAVD 504
Cdd:COG4133 148 SPAPLWLLDEPFTALD 163
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
356-504 |
1.97e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 99.27 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 356 SLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDarkwHVRE--LRNHIATVMQDIFLFSD-TIEGNIAF 432
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD----HTTTppSRRPVSMLFQENNLFSHlTVAQNIGL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1755737710 433 G-AP-----DATMEDVRRMARIADADHFIETMPesydtivGErgvgLSGGQKQRISLARALLKNPSILILDDTTSAVD 504
Cdd:PRK10771 95 GlNPglklnAAQREKLHAIARQMGIEDLLARLP-------GQ----LSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
337-553 |
2.13e-23 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 99.80 E-value: 2.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 337 KNVSFHFeddPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIAtVM 416
Cdd:COG4559 5 ENLSVRL---GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRA-VL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 417 -QDIFL-FSDTIE-----GNIAFGAPDATMED-VRRMARIADADHFIETmpeSYDTivgergvgLSGGQKQRISLARALL 488
Cdd:COG4559 81 pQHSSLaFPFTVEevvalGRAPHGSSAAQDRQiVREALALVGLAHLAGR---SYQT--------LSGGEQQRVQLARVLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 489 -------KNPSILILDDTTSAVD-------METevkiqgeLKKIT-ENTTTFIIAHRIS-SVKEADEILILNHGEIIERG 552
Cdd:COG4559 150 qlwepvdGGPRWLFLDEPTSALDlahqhavLRL-------ARQLArRGGGVVAVLHDLNlAAQYADRILLLHQGRLVAQG 222
|
.
gi 1755737710 553 T 553
Cdd:COG4559 223 T 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
334-549 |
2.53e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 103.57 E-value: 2.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFeddPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGvdaRKWHVRE----LR 409
Cdd:COG3845 6 LELRGITKRF---GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIRSprdaIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 410 NHIATVMQDIFLFSD-TIEGNIAFGAPDATmedvRRMARIADADHFIETMPESY------DTIVGErgvgLSGGQKQRIS 482
Cdd:COG3845 80 LGIGMVHQHFMLVPNlTVAENIVLGLEPTK----GGRLDRKAARARIRELSERYgldvdpDAKVED----LSVGEQQRVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1755737710 483 LARALLKNPSILILDDTTsAV--DMETEvKIQGELKKITENTTTFI-IAHRISSVKE-ADEILILNHGEII 549
Cdd:COG3845 152 ILKALYRGARILILDEPT-AVltPQEAD-ELFEILRRLAAEGKSIIfITHKLREVMAiADRVTVLRRGKVV 220
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
334-559 |
4.26e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 99.40 E-value: 4.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIA 413
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 414 TVMQ--DIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETMpeSYDTIVGERgvgLSGGQKQRISLARALLKNP 491
Cdd:PRK13642 85 MVFQnpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNML--DFKTREPAR---LSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 492 SILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLA 559
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVIHEIKEkyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
348-553 |
4.56e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 99.11 E-value: 4.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 348 NTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIATVMQ--DIFLFSDT 425
Cdd:PRK13652 16 SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQnpDDQIFSPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 426 IEGNIAFGAPDATMEDVRRMARIADADHFIETmpESYDTIVGERgvgLSGGQKQRISLARALLKNPSILILDDTTSAVDM 505
Cdd:PRK13652 96 VEQDIAFGPINLGLDEETVAHRVSSALHMLGL--EELRDRVPHH---LSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1755737710 506 ETEVKIQGELKKITEN--TTTFIIAHRISSVKE-ADEILILNHGEIIERGT 553
Cdd:PRK13652 171 QGVKELIDFLNDLPETygMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGT 221
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
351-559 |
5.79e-23 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 97.75 E-value: 5.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVREL-RNHIATVMQDIFLFSD-TIEG 428
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFPSlTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 429 NIAFGAPdatmedVRRmariaDADHFIETMPESYDT--IVGER----GVGLSGGQKQRISLARALLKNPSILILDDTT-- 500
Cdd:COG0410 98 NLLLGAY------ARR-----DRAEVRADLERVYELfpRLKERrrqrAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSlg 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1755737710 501 ---SAVDmetevKIQGELKKITENTTTFII----AHRISSVkeADEILILNHGEIIERGTHSSLLA 559
Cdd:COG0410 167 lapLIVE-----EIFEIIRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAAELLA 225
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
334-561 |
1.13e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 97.88 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIA 413
Cdd:PRK13647 5 IEVEDLHFRYKDG--TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 414 TVMQDI--FLFSDTIEGNIAFG------APDATMEDVRRMARIADADHFIETMPESydtivgergvgLSGGQKQRISLAR 485
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGpvnmglDKDEVERRVEEALKAVRMWDFRDKPPYH-----------LSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1755737710 486 ALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIA-HRISSVKE-ADEILILNHGEIIERGTHSSLLAEK 561
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDED 229
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
22-309 |
1.34e-22 |
|
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: 98.09 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 22 FILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMII-------------STIIRTicrYTYQIMCERIgqnsL 88
Cdd:cd18780 2 TIALLVSSGTNLALPYFFGQVIDAVTNHSGSGGEEALRALNQAvlillgvvligsiATFLRS---WLFTLAGERV----V 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 89 FRIREDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRhfvSWVSYNI---LENVFLFSFAIIIMAAIDWKLTLALVIV 165
Cdd:cd18780 75 ARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQ---NAVTVNLsmlLRYLVQIIGGLVFMFTTSWKLTLVMLSV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 166 TPLIAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPV 245
Cdd:cd18780 152 VPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGF 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1755737710 246 LDSLAGMLVVITLIFGGYLVIKGQMTLGDLVAFNgfLWMLNGPMRMSGW--LINDVQRFIASSFKI 309
Cdd:cd18780 232 MGAAAQLAIVLVLWYGGRLVIDGELTTGLLTSFL--LYTLTVAMSFAFLssLYGDFMQAVGASVRV 295
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
351-553 |
1.60e-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: 97.03 E-value: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNH-IATVMQDIFLFSD-TIEG 428
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLgIARTFQNPRLFPElTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 429 NIAFGA-------PDATMEDVRRMAR-----IADADHFIET--MPESYDTIVGErgvgLSGGQKQRISLARALLKNPSIL 494
Cdd:COG0411 99 NVLVAAharlgrgLLAALLRLPRARReereaRERAEELLERvgLADRADEPAGN----LSYGQQRRLEIARALATEPKLL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1755737710 495 ILDDTTSAVDM-ETEvKIQGELKKITE--NTTTFIIAHRISSVKE-ADEILILNHGEIIERGT 553
Cdd:COG0411 175 LLDEPAAGLNPeETE-ELAELIRRLRDerGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGT 236
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
351-550 |
1.65e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 97.45 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDA---RKWHVRELRNHIATVMQDiflfsdtie 427
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklNRAQRKAFRRDIQMVFQD--------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 428 gniAFGAPDA----------------TMEDVRRMARIADADHFIETMPESYDTIVGErgvgLSGGQKQRISLARALLKNP 491
Cdd:PRK10419 98 ---SISAVNPrktvreiireplrhllSLDKAERLARASEMLRAVDLDDSVLDKRPPQ----LSGGQLQRVCLARALAVEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1755737710 492 SILILDDTTSAVDMETEVKIQGELKKITENTTT--FIIAHRISSVKE-ADEILILNHGEIIE 550
Cdd:PRK10419 171 KLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
351-553 |
1.79e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 97.15 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIATVMQDIFL-FSDTIEGN 429
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 430 IAFGA------PDATMEDVRRMARIADADHFIEtmpESYDTivgergvgLSGGQKQRISLARALL------KNPSILILD 497
Cdd:PRK13548 97 VAMGRaphglsRAEDDALVAAALAQVDLAHLAG---RDYPQ--------LSGGEQQRVQLARVLAqlwepdGPPRWLLLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 498 DTTSAVDM---ETEVKIQGELKKiTENTTTFIIAHRIS-SVKEADEILILNHGEIIERGT 553
Cdd:PRK13548 166 EPTSALDLahqHHVLRLARQLAH-ERGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGT 224
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
15-293 |
2.47e-22 |
|
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: 97.28 E-value: 2.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 15 RLLMIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLL----IMIISTIIRTICRYTYQIMCERIGQNSLFR 90
Cdd:cd18782 1 RRALIEVLALSFVVQLLGLANPLLFQVIIDKVLVQQDLATLYVIGVvmlvAALLEAVLTALRTYLFTDTANRIDLELGGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 91 IredlYKKLQSLDFDFFNNTRVGDIMARmTGDTDAIRHF-VSWVSYNILENVFLFsFAIIIMAAIDWKLTLALVIVTPLI 169
Cdd:cd18782 81 I----IDHLLRLPLGFFDKRPVGELSTR-ISELDTIRGFlTGTALTTLLDVLFSV-IYIAVLFSYSPLLTLVVLATVPLQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 170 AILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEH-----NEDFKKRNLDSAdvSRTYLP 244
Cdd:cd18782 155 LLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRyarslGEGFKLTVLGTT--SGSLSQ 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1755737710 245 VLDSLAGMLVvitLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPM-RMSG 293
Cdd:cd18782 233 FLNKLSSLLV---LWVGAYLVLRGELTLGQLIAFRILSGYVTGPIlRLST 279
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
95-301 |
3.07e-22 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 97.18 E-value: 3.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 95 LYKKLQSLDFDFFNNTRVGDIMARMtGDTDAIRHFVSWVSYN-ILENVFLFSFaIIIMAAIDWKLTLALVIVTPLIAILt 173
Cdd:cd18588 81 LFRHLLRLPLSYFESRQVGDTVARV-RELESIRQFLTGSALTlVLDLVFSVVF-LAVMFYYSPTLTLIVLASLPLYALL- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 174 mkmSSKAQPVF-YEIRESF---SRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSL 249
Cdd:cd18588 158 ---SLLVTPILrRRLEEKFqrgAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLI 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1755737710 250 AGMLVVITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGP-MRMSGwLINDVQR 301
Cdd:cd18588 235 QKLTTLAILWFGAYLVMDGELTIGQLIAFNMLAGQVSQPvLRLVQ-LWQDFQQ 286
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
351-552 |
3.70e-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: 3.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHvrELRNHIATVmqdiflfsdtIEGNI 430
Cdd:cd03268 15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI--EALRRIGAL----------IEAPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 431 AFGAPDAtMEDVRRMARIADADHfiETMPESYDtIVGERGVG------LSGGQKQRISLARALLKNPSILILDDTTSAVD 504
Cdd:cd03268 83 FYPNLTA-RENLRLLARLLGIRK--KRIDEVLD-VVGLKDSAkkkvkgFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1755737710 505 METEVKIQGELKKITENTTTFIIA-HRISSV-KEADEILILNHGEIIERG 552
Cdd:cd03268 159 PDGIKELRELILSLRDQGITVLISsHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
338-551 |
3.95e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 95.92 E-value: 3.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 338 NVSFHFEDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVdarkwHVRELRNHIATVMQ 417
Cdd:PRK11248 3 QISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK-----PVEGPGAERGVVFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 418 DIFLFS-DTIEGNIAFGAPDATMEdvrRMARIADADHFIEtmpesydtIVGERGVG------LSGGQKQRISLARALLKN 490
Cdd:PRK11248 78 NEGLLPwRNVQDNVAFGLQLAGVE---KMQRLEIAHQMLK--------KVGLEGAEkryiwqLSGGQRQRVGIARALAAN 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1755737710 491 PSILILDDTTSAVDMETEVKIQGELKKITENT--TTFIIAHRI-SSVKEADEILIL--NHGEIIER 551
Cdd:PRK11248 147 PQLLLLDEPFGALDAFTREQMQTLLLKLWQETgkQVLLITHDIeEAVFMATELVLLspGPGRVVER 212
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
21-278 |
5.00e-22 |
|
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: 96.46 E-value: 5.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 21 VFILIFIASGISIIYPLLGGKVIDdVVYQNKTNLLIPLLLIMIISTI-------IRTICRYTYQIMCERIGQNSLFRIRE 93
Cdd:cd18574 1 AVLSALAAALVNIQIPLLLGDLVN-VISRSLKETNGDFIEDLKKPALkllglylLQSLLTFAYISLLSVVGERVAARLRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 94 DLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRH-FVSWVSYNiLENVFLFSFAIIIMAAIDWKLTLALVIVTP-LIAI 171
Cdd:cd18574 80 DLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSsFKQCVSQG-LRSVTQTVGCVVSLYLISPKLTLLLLVIVPvVVLV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 172 LTM------KMSSKAQpvfyeirESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNldsadvsrTYLPV 245
Cdd:cd18574 159 GTLygsflrKLSRRAQ-------AQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLN--------EKLGL 223
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1755737710 246 -------LDSLA-GMLVVITLIFGGYLVIKGQMTLGDLVAF 278
Cdd:cd18574 224 gigifqgLSNLAlNGIVLGVLYYGGSLVSRGELTAGDLMSF 264
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
316-548 |
5.97e-22 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 101.01 E-value: 5.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 316 DAKIPIHAEKPAPSLQGHVEFKNVSFHFEDDPNTdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEIli 395
Cdd:PTZ00243 641 GGTGGGHEATPTSERSAKTPKMKTDDFFELEPKV-LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-- 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 396 dgvdarkWHVRElrnhIATVMQDIFLFSDTIEGNIAFGAPD--ATMEDVRRMARIaDADhfIETMPESYDTIVGERGVGL 473
Cdd:PTZ00243 718 -------WAERS----IAYVPQQAWIMNATVRGNILFFDEEdaARLADAVRVSQL-EAD--LAQLGGGLETEIGEKGVNL 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 474 SGGQKQRISLARALLKNPSILILDDTTSAVDMET-----EVKIQGELKKITENTTTfiiaHRISSVKEADEILILNHGEI 548
Cdd:PTZ00243 784 SGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgervvEECFLGALAGKTRVLAT----HQVHVVPRADYVVALGDGRV 859
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
335-504 |
1.10e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 94.01 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 335 EFKNVSFHFEDdpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIAT 414
Cdd:PRK10247 9 QLQNVGYLAGD---AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 415 VMQDIFLFSDTIEGNIAF------GAPDATmedvrrmARIADADHFieTMPEsydTIVGERGVGLSGGQKQRISLARALL 488
Cdd:PRK10247 86 CAQTPTLFGDTVYDNLIFpwqirnQQPDPA-------IFLDDLERF--ALPD---TILTKNIAELSGGEKQRISLIRNLQ 153
|
170
....*....|....*.
gi 1755737710 489 KNPSILILDDTTSAVD 504
Cdd:PRK10247 154 FMPKVLLLDEITSALD 169
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
336-507 |
1.76e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.83 E-value: 1.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 336 FKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGvDARkwhvrelrnhIATV 415
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR----------IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 416 MQDIFLFSD-TIEGNIAFG----------------APDATMEDVRRMARIA---------DADHFIETM-------PESY 462
Cdd:COG0488 67 PQEPPLDDDlTVLDTVLDGdaelraleaeleeleaKLAEPDEDLERLAELQeefealggwEAEARAEEIlsglgfpEEDL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1755737710 463 DTIVGErgvgLSGGQKQRISLARALLKNPSILILDDTTSAVDMET 507
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
350-559 |
3.28e-21 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 93.70 E-value: 3.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 350 DVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDG--VDARKWHVRELRnhIATVMQDiflfsdtie 427
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhpLHFGDYSYRSQR--IRMIFQD--------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 428 gniafgaPDATMEDVRRMARIADADHFIETMPES-------YDTIvgeRGVGL------------SGGQKQRISLARALL 488
Cdd:PRK15112 96 -------PSTSLNPRQRISQILDFPLRLNTDLEPeqrekqiIETL---RQVGLlpdhasyyphmlAPGQKQRLGLARALI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1755737710 489 KNPSILILDDTTSAVDMETEVKIQG---ELKKITENTTTFIIAHrISSVKE-ADEILILNHGEIIERGTHSSLLA 559
Cdd:PRK15112 166 LRPKVIIADEALASLDMSMRSQLINlmlELQEKQGISYIYVTQH-LGMMKHiSDQVLVMHQGEVVERGSTADVLA 239
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
254-543 |
4.95e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 96.80 E-value: 4.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 254 VVITLIFGGYLVIKGQMTLGDLV----AFNgflwMLNGPMRmsgWLIN---DVQRFIAS-----SFkiQDMMATDAKIPI 321
Cdd:COG4178 280 VIFPILVAAPRYFAGEITLGGLMqaasAFG----QVQGALS---WFVDnyqSLAEWRATvdrlaGF--EEALEAADALPE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 322 HAEKPAPSLQGHVEFKNVSFHfedDPNTDVL-KNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILidgvda 400
Cdd:COG4178 351 AASRIETSEDGALALEDLTLR---TPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA------ 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 401 rkwhvrelRNHIATVM---QDIFLFSDTIEGNIAFGAPDATMEDvrrmARIADA------DHFIETMPESYDtivgeRGV 471
Cdd:COG4178 422 --------RPAGARVLflpQRPYLPLGTLREALLYPATAEAFSD----AELREAleavglGHLAERLDEEAD-----WDQ 484
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1755737710 472 GLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILIL 543
Cdd:COG4178 485 VLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLEL 556
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
334-553 |
5.65e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 93.23 E-value: 5.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDPNTD---VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKW-HVRELR 409
Cdd:PRK13633 5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 410 NHIATVMQ--DIFLFSDTIEGNIAFG------APDATMEDVRRMARIADADHFIETMPESydtivgergvgLSGGQKQRI 481
Cdd:PRK13633 85 NKAGMVFQnpDNQIVATIVEEDVAFGpenlgiPPEEIRERVDESLKKVGMYEYRRHAPHL-----------LSGGQKQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755737710 482 SLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITEN--TTTFIIAHRISSVKEADEILILNHGEIIERGT 553
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKygITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
334-553 |
6.60e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 93.76 E-value: 6.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDPNTD--VLKNISLKASPGQTIAILGETGAGKSTLVN-----LICRFYDPTSGEILI----DGVDARK 402
Cdd:PRK13631 22 LRVKNLYCVFDEKQENElvALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglIKSKYGTIQVGDIYIgdkkNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 403 WHV-------RELRNHIATVMQ--DIFLFSDTIEGNIAFG--APDATMEDVRRMARiadadHFIETMPESYDTIvgERG- 470
Cdd:PRK13631 102 NPYskkiknfKELRRRVSMVFQfpEYQLFKDTIEKDIMFGpvALGVKKSEAKKLAK-----FYLNKMGLDDSYL--ERSp 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 471 VGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETE---VKIQGELKKitENTTTFIIAHRISSVKE-ADEILILNHG 546
Cdd:PRK13631 175 FGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEhemMQLILDAKA--NNKTVFVITHTMEHVLEvADEVIVMDKG 252
|
....*..
gi 1755737710 547 EIIERGT 553
Cdd:PRK13631 253 KILKTGT 259
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
335-563 |
7.01e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 92.05 E-value: 7.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 335 EFKNVSFHFEDdpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRF--YDPTSGEILIDGVD---------ARKw 403
Cdd:COG0396 2 EIKNLHVSVEG---KEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDilelspderARA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 404 hvrelrnhiatvmqDIFL---------------FSDTIEGNIAFGAPDAT--MEDVRRMARIADadhfietMPESYdtiv 466
Cdd:COG0396 78 --------------GIFLafqypveipgvsvsnFLRTALNARRGEELSARefLKLLKEKMKELG-------LDEDF---- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 467 GERGV--GLSGGQKQRISLARALLKNPSILILDDTTSAVDMETeVKIQGE-LKKI-TENTTTFIIAH--RISSVKEADEI 540
Cdd:COG0396 133 LDRYVneGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDA-LRIVAEgVNKLrSPDRGILIITHyqRILDYIKPDFV 211
|
250 260
....*....|....*....|....*
gi 1755737710 541 LILNHGEIIERGTHS--SLLAEKGY 563
Cdd:COG0396 212 HVLVDGRIVKSGGKElaLELEEEGY 236
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
334-557 |
8.97e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 94.02 E-value: 8.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDdpNTdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKwhvRELRNH-I 412
Cdd:PRK11432 7 VVLKNITKRFGS--NT-VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH---RSIQQRdI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 413 ATVMQDIFLFSD-TIEGNIAFGAPDATMEDVRRMARIADADHFI--ETMPESY-DTIvgergvglSGGQKQRISLARALL 488
Cdd:PRK11432 81 CMVFQSYALFPHmSLGENVGYGLKMLGVPKEERKQRVKEALELVdlAGFEDRYvDQI--------SGGQQQRVALARALI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1755737710 489 KNPSILILDDTTSAVDMETEVKIQgelKKITE-----NTTTFIIAHRISsvkEA----DEILILNHGEIIERGTHSSL 557
Cdd:PRK11432 153 LKPKVLLFDEPLSNLDANLRRSMR---EKIRElqqqfNITSLYVTHDQS---EAfavsDTVIVMNKGKIMQIGSPQEL 224
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
334-561 |
9.32e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 92.60 E-value: 9.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDdpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDG--VDARKWHVRELRNH 411
Cdd:PRK13636 6 LKVEELNYNYSD--GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 412 IATVMQ--DIFLFSDTIEGNIAFGAPDATM--EDVRRMARIADADHFIETMPESYDTivgergvGLSGGQKQRISLARAL 487
Cdd:PRK13636 84 VGMVFQdpDNQLFSASVYQDVSFGAVNLKLpeDEVRKRVDNALKRTGIEHLKDKPTH-------CLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 488 LKNPSILILDDTTSAVD-------METEVKIQGELkkiteNTTTFIIAHRISSVK-EADEILILNHGEIIERGTHSSLLA 559
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDpmgvseiMKLLVEMQKEL-----GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFA 231
|
..
gi 1755737710 560 EK 561
Cdd:PRK13636 232 EK 233
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
352-553 |
1.06e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 95.88 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICrFYDPT----SGEILIDG--VDARKWHVRElrnhiATVMQ-DIFLFSD 424
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGmpIDAKEMRAIS-----AYVQQdDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 425 TIEGNIAFGAP---DATMEDVRRMARIadaDHFIETMP--ESYDTIVGERGV--GLSGGQKQRISLARALLKNPSILILD 497
Cdd:TIGR00955 115 TVREHLMFQAHlrmPRRVTKKEKRERV---DEVLQALGlrKCANTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1755737710 498 DTTSAVD--METEVkIQgELKKITENTTTFIIA-HRISS--VKEADEILILNHGEIIERGT 553
Cdd:TIGR00955 192 EPTSGLDsfMAYSV-VQ-VLKGLAQKGKTIICTiHQPSSelFELFDKIILMAEGRVAYLGS 250
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
352-553 |
1.67e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 92.72 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVD---ARKWHVRELRNHIATVMQDIF-------- 420
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDllkADPEAQKLLRQKIQIVFQNPYgslnprkk 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 421 ---LFSDTIEGNIAFGAPDatmedvrRMARIADADHFIETMPESYDtivgeRGVGL-SGGQKQRISLARALLKNPSILIL 496
Cdd:PRK11308 111 vgqILEEPLLINTSLSAAE-------RREKALAMMAKVGLRPEHYD-----RYPHMfSGGQRQRIAIARALMLDPDVVVA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1755737710 497 DDTTSAVDMETEVKI-------QGELkkiteNTTTFIIAHRISSVKE-ADEILILNHGEIIERGT 553
Cdd:PRK11308 179 DEPVSALDVSVQAQVlnlmmdlQQEL-----GLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGT 238
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
352-561 |
1.88e-20 |
|
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: 93.25 E-value: 1.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 352 LKNISLKAS---PGQTI-AILGETGAGKSTLVNLICRFYDPTSGEILIDGV---DARKW-----HVRElrnhIATVMQDI 419
Cdd:TIGR02142 9 LGDFSLDADftlPGQGVtAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfDSRKGiflppEKRR----IGYVFQEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 420 FLFSD-TIEGNIAFGAPDATMEDVR-RMARIADA---DHFIEtmpesydtivgeRGVG-LSGGQKQRISLARALLKNPSI 493
Cdd:TIGR02142 85 RLFPHlSVRGNLRYGMKRARPSERRiSFERVIELlgiGHLLG------------RLPGrLSGGEKQRVAIGRALLSSPRL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1755737710 494 LILDDTTSAVDMETEVKIQGELKKITENTTTFI--IAHRISSVKE-ADEILILNHGEIIERGTHSSLLAEK 561
Cdd:TIGR02142 153 LLMDEPLAALDDPRKYEILPYLERLHAEFGIPIlyVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
333-552 |
3.15e-20 |
|
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: 89.35 E-value: 3.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 333 HVEFKNVSFHFEddpntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKwHVRELRNHI 412
Cdd:cd03266 8 TKRFRDVKKTVQ------AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 413 ATVMQDIFLFSD-TIEGNIAFGA------PDATMEDVRRMARIADADHFIEtmpesydtivgERGVGLSGGQKQRISLAR 485
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYFAglyglkGDELTARLEELADRLGMEELLD-----------RRVGGFSTGMRQKVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1755737710 486 ALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIA-HRISSVKE-ADEILILNHGEIIERG 552
Cdd:cd03266 150 ALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
350-559 |
3.84e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 90.41 E-value: 3.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 350 DVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDAR-------------KWHVRELRNHIATVM 416
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 417 QDIFLFSD-TIEGNIaFGAP---------DATMEDVRRMARIADADHFIETMPesydtivgergVGLSGGQKQRISLARA 486
Cdd:PRK10619 99 QHFNLWSHmTVLENV-MEAPiqvlglskqEARERAVKYLAKVGIDERAQGKYP-----------VHLSGGQQQRVSIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1755737710 487 LLKNPSILILDDTTSAVDMEtevkIQGELKKIT-----ENTTTFIIAHRISSVKE-ADEILILNHGEIIERGTHSSLLA 559
Cdd:PRK10619 167 LAMEPEVLLFDEPTSALDPE----LVGEVLRIMqqlaeEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
334-561 |
4.77e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 90.92 E-value: 4.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDPNTD--VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWH------- 404
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTElkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 405 -----------------VRELRNHIATVMQ--DIFLFSDTIEGNIAFGAPDATMEDVRRMARIADadhFIET--MPESYd 463
Cdd:PRK13651 83 vleklviqktrfkkikkIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAK---YIELvgLDESY- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 464 tiVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIA-HRISSVKE-ADEIL 541
Cdd:PRK13651 159 --LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVtHDLDNVLEwTKRTI 236
|
250 260
....*....|....*....|.
gi 1755737710 542 ILNHGEIIERG-THSSLLAEK 561
Cdd:PRK13651 237 FFKDGKIIKDGdTYDILSDNK 257
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
334-556 |
6.37e-20 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 89.30 E-value: 6.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEddpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDG--------VDARKwhV 405
Cdd:PRK11124 3 IQLNGINCFYG---AHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsktPSDKA--I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 406 RELRNHIATVMQDIFLFSD-TIEGNIAfgapDATMEdVRRMAR---IADADHFIETMpeSYDTIVGERGVGLSGGQKQRI 481
Cdd:PRK11124 78 RELRRNVGMVFQQYNLWPHlTVQQNLI----EAPCR-VLGLSKdqaLARAEKLLERL--RLKPYADRFPLHLSGGQQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1755737710 482 SLARALLKNPSILILDDTTSAVDMETE---VKIQGELKKIteNTTTFIIAHRIS-SVKEADEILILNHGEIIERGTHSS 556
Cdd:PRK11124 151 AIARALMMEPQVLLFDEPTAALDPEITaqiVSIIRELAET--GITQVIVTHEVEvARKTASRVVYMENGHIVEQGDASC 227
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
21-288 |
8.43e-20 |
|
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: 89.93 E-value: 8.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 21 VFILIFIASGI----SIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFRIREDLY 96
Cdd:cd18568 3 LLAEILLASLLlqllGLALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 97 KKLQSLDFDFFNNTRVGDIMARMtGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTMKM 176
Cdd:cd18568 83 KHLLSLPLSFFASRKVGDIITRF-QENQKIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 177 SSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDfemkKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVVI 256
Cdd:cd18568 162 SPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAER----PIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHL 237
|
250 260 270
....*....|....*....|....*....|....*.
gi 1755737710 257 TLI----FGGYLVIKGQMTLGDLVAFNGFLWMLNGP 288
Cdd:cd18568 238 GTIavlwYGAYLVISGQLTIGQLVAFNMLFGSVINP 273
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
334-559 |
9.00e-20 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 92.56 E-value: 9.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDdpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLI--CRFYDPTSGEIL----------------- 394
Cdd:TIGR03269 1 IEVKNLTKKFDG---KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIyhvalcekcgyverpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 395 ----------------IDGVDARKWHVRELRNHIATVMQDIFLF--SDTIEGNIAFGAPDATMEDVRRMARIADadhFIE 456
Cdd:TIGR03269 78 vgepcpvcggtlepeeVDFWNLSDKLRRRIRKRIAIMLQRTFALygDDTVLDNVLEALEEIGYEGKEAVGRAVD---LIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 457 TMPESYDTIVGERGvgLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKK-ITENTTTFIIAHRISSVK 535
Cdd:TIGR03269 155 MVQLSHRITHIARD--LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEaVKASGISMVLTSHWPEVI 232
|
250 260
....*....|....*....|....*.
gi 1755737710 536 E--ADEILILNHGEIIERGTHSSLLA 559
Cdd:TIGR03269 233 EdlSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
351-552 |
9.89e-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: 87.97 E-value: 9.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGvdarkwhvrelrnhiatvmqdiflfsdTIEGNI 430
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG---------------------------RVSSLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 431 AFGA---PDAT-MEDVRRMARIADADhfIETMPESYDTIVGERGVG---------LSGGQKQRISLARALLKNPSILILD 497
Cdd:cd03220 90 GLGGgfnPELTgRENIYLNGRLLGLS--RKEIDEKIDEIIEFSELGdfidlpvktYSSGMKARLAFAIATALEPDILLID 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1755737710 498 DTTSAVDMETEVKIQGELKKITENTTTFIIA-HRISSVKE-ADEILILNHGEIIERG 552
Cdd:cd03220 168 EVLAVGDAAFQEKCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
351-559 |
1.30e-19 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 87.98 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHV-RELRNHIATVMQDIFLFSD-TIEG 428
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYLPQEASIFRKlTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 429 NIafgapDATME--DVRRMARIADADHFIETMpeSYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDME 506
Cdd:cd03218 95 NI-----LAVLEirGLSKKEREEKLEELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1755737710 507 TEVKIQGELKKITE-NTTTFIIAHrisSVKE----ADEILILNHGEIIERGTHSSLLA 559
Cdd:cd03218 168 AVQDIQKIIKILKDrGIGVLITDH---NVREtlsiTDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
341-559 |
1.45e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 88.91 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 341 FHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDG--VDARKWHVRELRNHIATVMQD 418
Cdd:PRK13638 9 FRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 419 ----IFlFSDtIEGNIAF-----GAPDAtmEDVRRMAR---IADADHFIETMPESydtivgergvgLSGGQKQRISLARA 486
Cdd:PRK13638 86 peqqIF-YTD-IDSDIAFslrnlGVPEA--EITRRVDEaltLVDAQHFRHQPIQC-----------LSHGQKKRVAIAGA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1755737710 487 LLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFII-AHRISSVKE-ADEILILNHGEIIERGTHSSLLA 559
Cdd:PRK13638 151 LVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIsSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFA 225
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
354-559 |
1.61e-19 |
|
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: 90.16 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 354 NISLKASPGQTIAILGETGAGKSTLVNLI---CRfydPTSGEILIDG---VDARKWHVR--ELRnHIATVMQDIFLFSD- 424
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIaglER---PDSGRIRLGGevlQDSARGIFLppHRR-RIGYVFQEARLFPHl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 425 TIEGNIAFGApdatmedvRRMARIADADHFietmpesyDTIVG--------ERGVG-LSGGQKQRISLARALLKNPSILI 495
Cdd:COG4148 93 SVRGNLLYGR--------KRAPRAERRISF--------DEVVEllgighllDRRPAtLSGGERQRVAIGRALLSSPRLLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 496 LDDTTSAVDMETEVKIQGELKKITENTTTFII--AHrisSVKE----ADEILILNHGEIIERGTHSSLLA 559
Cdd:COG4148 157 MDEPLAALDLARKAEILPYLERLRDELDIPILyvSH---SLDEvarlADHVVLLEQGRVVASGPLAEVLS 223
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
351-552 |
1.68e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 92.08 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 351 VLKNISLKASPGQTIAILGETGAGKST----LVNLIcrfydPTSGEILIDGVDARKWHVREL---RNHIATVMQDIFLFS 423
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 424 D---TIEGNIAFG--APDATMEDVRRMARIADADHFIETMPESYDTIVGErgvgLSGGQKQRISLARALLKNPSILILDD 498
Cdd:PRK15134 376 NprlNVLQIIEEGlrVHQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAE----FSGGQRQRIAIARALILKPSLIILDE 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1755737710 499 TTSAVDMETEVKIQGELKKITEN--TTTFIIAHRISSVKE-ADEILILNHGEIIERG 552
Cdd:PRK15134 452 PTSSLDKTVQAQILALLKSLQQKhqLAYLFISHDLHVVRAlCHQVIVLRQGEVVEQG 508
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
8-319 |
1.77e-19 |
|
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: 89.43 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 8 WQYVRKYRLLMIgvfiLIFIASGIS-IIYPLLG---GKVIDdvVYQNkTNLLIPLLLIMIIST------IIRTICRYTYQ 77
Cdd:cd18578 1 LKLNKPEWPLLL----LGLIGAIIAgAVFPVFAilfSKLIS--VFSL-PDDDELRSEANFWALmflvlaIVAGIAYFLQG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 78 IMCERIGQNSLFRIREDLYKKLQSLDFDFF---NNTrVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAI 154
Cdd:cd18578 74 YLFGIAGERLTRRLRKLAFRAILRQDIAWFddpENS-TGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 155 DWKLTLALVIVTPLIAILT---MKMSSKAQpvfYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKR 231
Cdd:cd18578 153 GWKLALVGLATVPLLLLAGylrMRLLSGFE---EKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 232 NLDSADVSRTYLPVLDSLagMLVVITLIF--GGYLVIKGQMTLGD-LVAFNGFLWMLNGPMRMSGwLINDVQRFIASSFK 308
Cdd:cd18578 230 GLRRALISGLGFGLSQSL--TFFAYALAFwyGGRLVANGEYTFEQfFIVFMALIFGAQSAGQAFS-FAPDIAKAKAAAAR 306
|
330
....*....|.
gi 1755737710 309 IQDMMATDAKI 319
Cdd:cd18578 307 IFRLLDRKPEI 317
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
331-552 |
3.05e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 87.28 E-value: 3.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 331 QGHVEFKNVSFHFEDdpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYD-----PTSGEILIDGVDARKWHV 405
Cdd:PRK14247 1 MNKIEIRDLKVSFGQ---VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 406 RELRNHIATVMQ------DIFLFSdtiegNIAFGAPDATMEDVRR--MARIADADHFIETMPESYDTIVGERGvGLSGGQ 477
Cdd:PRK14247 78 IELRRRVQMVFQipnpipNLSIFE-----NVALGLKLNRLVKSKKelQERVRWALEKAQLWDEVKDRLDAPAG-KLSGGQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1755737710 478 KQRISLARALLKNPSILILDDTTSAVDMETEVKIQG---ELKKitENTTTFIIAHRISSVKEADEILILNHGEIIERG 552
Cdd:PRK14247 152 QQRLCIARALAFQPEVLLADEPTANLDPENTAKIESlflELKK--DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWG 227
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
351-553 |
3.08e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 87.06 E-value: 3.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGvdarkwhvR-----ELR---NHIATVMQDIFLF 422
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG--------RvsallELGagfHPELTGRENIYLN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 423 sdtieGNIaFGAPDATMEdvRRMARIAD-AD--HFIEtMP-ESYdtivgergvglSGGQKQRISLARALLKNPSILILDD 498
Cdd:COG1134 113 -----GRL-LGLSRKEID--EKFDEIVEfAElgDFID-QPvKTY-----------SSGMRARLAFAVATAVDPDILLVDE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1755737710 499 TTSAVDMETEVKIQGELKKITENTTTFIIA-HRISSVKE-ADEILILNHGEIIERGT 553
Cdd:COG1134 173 VLAVGDAAFQKKCLARIRELRESGRTVIFVsHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
334-559 |
3.17e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 87.24 E-value: 3.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEddpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHV-RELRNHI 412
Cdd:PRK11614 6 LSFDKVSAHYG---KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTaKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 413 ATVMQDIFLFSD-TIEGNIAFGAPDATMEDVR-RMARIADadhfieTMPESYDTIVgERGVGLSGGQKQRISLARALLKN 490
Cdd:PRK11614 83 AIVPEGRRVFSRmTVEENLAMGGFFAERDQFQeRIKWVYE------LFPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1755737710 491 PSILILDDTTSAVDMETEVKIQGELKKI-TENTTTFIIAHRIS-SVKEADEILILNHGEIIERGTHSSLLA 559
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQLrEQGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLA 226
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
351-548 |
3.65e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 87.43 E-value: 3.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILidgvdARKWHVRELRNHIATVMQDIFLFS-DTIEGN 429
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-----AGTAPLAEAREDTRLMFQDARLLPwKKVIDN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 430 IAFGAPDATMEDVRR-MARIADADHfietmpesydtiVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETE 508
Cdd:PRK11247 102 VGLGLKGQWRDAALQaLAAVGLADR------------ANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1755737710 509 VKIQGELKKI--TENTTTFIIAHRIS-SVKEADEILILNHGEI 548
Cdd:PRK11247 170 IEMQDLIESLwqQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
334-558 |
5.32e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 89.52 E-value: 5.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDdpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIA 413
Cdd:PRK09536 4 IDVSDLSVEFGD---TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 414 TVMQDIflfsdtiegNIAFgapDATMEDVRRMARIADADHFiETMPESYDTIVGE------------RGV-GLSGGQKQR 480
Cdd:PRK09536 81 SVPQDT---------SLSF---EFDVRQVVEMGRTPHRSRF-DTWTETDRAAVERamertgvaqfadRPVtSLSGGERQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 481 ISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIA-HRIS-SVKEADEILILNHGEIIERGTHSSLL 558
Cdd:PRK09536 148 VLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAiHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
329-553 |
6.65e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 87.37 E-value: 6.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 329 SLQGHVEFKNVSFHFEDDPNTD--VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILID------GVDA 400
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKTPFEfkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyaipaNLKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 401 RKwHVRELRNHIATVMQ--DIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIEtMPESYdtiVGERGVGLSGGQK 478
Cdd:PRK13645 82 IK-EVKRLRKEIGLVFQfpEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQ-LPEDY---VKRSPFELSGGQK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1755737710 479 QRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFII--AHRISSV-KEADEILILNHGEIIERGT 553
Cdd:PRK13645 157 RRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIImvTHNMDQVlRIADEVIVMHEGKVISIGS 234
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
335-549 |
9.79e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 89.78 E-value: 9.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 335 EFKNVSFHFED-DPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVREL----R 409
Cdd:PRK10535 6 ELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 410 NHIATVMQDIFLFSD-TIEGNIAFGAPDATMEDVRRMARiadADHFIETMpeSYDTIVGERGVGLSGGQKQRISLARALL 488
Cdd:PRK10535 86 EHFGFIFQRYHLLSHlTAAQNVEVPAVYAGLERKQRLLR---AQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1755737710 489 KNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFII-AHRISSVKEADEILILNHGEII 549
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIvTHDPQVAAQAERVIEIRDGEIV 222
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
331-557 |
1.01e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 89.20 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 331 QGHVEFKNVSFHFeddPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRN 410
Cdd:PRK11288 2 SPYLSFDGIGKTF---PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 411 H-IATVMQDIFLFSD-TIEGNIAFGAPDATMEDVRRMARIADADHFIETMPESYD--TIVGErgvgLSGGQKQRISLARA 486
Cdd:PRK11288 79 AgVAIIYQELHLVPEmTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDpdTPLKY----LSIGQRQMVEIAKA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1755737710 487 LLKNPSILILDDTTSAVDM-ETEV--KIQGELKKitENTTTFIIAHRISSVKE-ADEILILNHGEIIErgTHSSL 557
Cdd:PRK11288 155 LARNARVIAFDEPTSSLSArEIEQlfRVIRELRA--EGRVILYVSHRMEEIFAlCDAITVFKDGRYVA--TFDDM 225
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
334-560 |
1.13e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 86.71 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEddPNTD----VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGV----DARKWHV 405
Cdd:PRK13643 2 IKFEKVNYTYQ--PNSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIvvssTSKQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 406 RELRNHIATVMQ--DIFLFSDTIEGNIAFGAPD--ATMEDVRRMAriADADHFIETMPESYDTIVGErgvgLSGGQKQRI 481
Cdd:PRK13643 80 KPVRKKVGVVFQfpESQLFEETVLKDVAFGPQNfgIPKEKAEKIA--AEKLEMVGLADEFWEKSPFE----LSGGQMRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 482 SLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITEN-TTTFIIAHRISSVKE-ADEILILNHGEIIERGTHSSLLA 559
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQ 233
|
.
gi 1755737710 560 E 560
Cdd:PRK13643 234 E 234
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
334-552 |
1.19e-18 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 84.64 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDdpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDG--VDArkwhvrELRNH 411
Cdd:cd03269 1 LEVENVTKRFGR---VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpLDI------AARNR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 412 IATVMQDIFLFSDT--IEGNIAFgapdATMEDVRRMARIADADHFIETMP-ESYDTIVGERgvgLSGGQKQRISLARALL 488
Cdd:cd03269 72 IGYLPEERGLYPKMkvIDQLVYL----AQLKGLKKEEARRRIDEWLERLElSEYANKRVEE---LSKGNQQKVQFIAAVI 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1755737710 489 KNPSILILDDTTSAVD-METEVkIQGELKKITENTTTFII-AHRISSVKE-ADEILILNHGEIIERG 552
Cdd:cd03269 145 HDPELLILDEPFSGLDpVNVEL-LKDVIRELARAGKTVILsTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
334-553 |
1.47e-18 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 85.52 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIA 413
Cdd:COG4604 2 IEIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 414 TVMQDIFLFSD-TIEGNIAFG-------APdaTMEDVRrmaRIADADHFIETMP--ESY-DTivgergvgLSGGQKQRIS 482
Cdd:COG4604 79 ILRQENHINSRlTVRELVAFGrfpyskgRL--TAEDRE---IIDEAIAYLDLEDlaDRYlDE--------LSGGQRQRAF 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1755737710 483 LARALLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRI---SSVkeADEILILNHGEIIERGT 553
Cdd:COG4604 146 IAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADelGKTVVIVLHDInfaSCY--ADHIVAMKDGRVVAQGT 219
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
352-552 |
1.67e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 85.21 E-value: 1.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYD-----PTSGEILIDGVD--ARKWHVRELRNHIATVMQDIFLFSD 424
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNiySPRTDTVDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 425 TIEGNIAFG----------APDATMEDVRRMARIADadhfiETMPESYDTivgerGVGLSGGQKQRISLARALLKNPSIL 494
Cdd:PRK14239 101 SIYENVVYGlrlkgikdkqVLDEAVEKSLKGASIWD-----EVKDRLHDS-----ALGLSGGQQQRVCIARVLATSPKII 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1755737710 495 ILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHrisSVKEADEI-----LILNhGEIIERG 552
Cdd:PRK14239 171 LLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTR---SMQQASRIsdrtgFFLD-GDLIEYN 229
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
90-278 |
1.85e-18 |
|
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: 85.85 E-value: 1.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 90 RIREDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHfvsWVSYNIleNVFLFSFA-----IIIMAAIDWKLTLALVI 164
Cdd:cd18590 70 RLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSR---SVALNA--NVLLRSLVktlgmLGFMLSLSWQLTLLTLI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 165 VTPLIAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDfKKRNLDSADVSRTYLP 244
Cdd:cd18590 145 EMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALER-TYNLKDRRDTVRAVYL 223
|
170 180 190
....*....|....*....|....*....|....*
gi 1755737710 245 VLDSLAGMLV-VITLIFGGYLVIKGQMTLGDLVAF 278
Cdd:cd18590 224 LVRRVLQLGVqVLMLYCGRQLIQSGHLTTGSLVSF 258
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
334-561 |
1.90e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 86.04 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEddPNTDV----LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDG----VDARKWHV 405
Cdd:PRK13641 3 IKFENVDYIYS--PGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitPETGNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 406 RELRNHIATVMQ--DIFLFSDTIEGNIAFGA-------PDATMEDVRRMARIADADHFIETMPesydtivgergVGLSGG 476
Cdd:PRK13641 81 KKLRKKVSLVFQfpEAQLFENTVLKDVEFGPknfgfseDEAKEKALKWLKKVGLSEDLISKSP-----------FELSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 477 QKQRISLARALLKNPSILILDDTTSAVDMETevkiQGELKKITENT-----TTFIIAHRISSVKE-ADEILILNHGEIIE 550
Cdd:PRK13641 150 QMRRVAIAGVMAYEPEILCLDEPAAGLDPEG----RKEMMQLFKDYqkaghTVILVTHNMDDVAEyADDVLVLEHGKLIK 225
|
250
....*....|.
gi 1755737710 551 RGTHSSLLAEK 561
Cdd:PRK13641 226 HASPKEIFSDK 236
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
348-561 |
1.95e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 85.07 E-value: 1.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 348 NTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIATVMQdIFLfsdTIE 427
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQ-HHL---TPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 428 GN-----IAFG-APDATMedvrrMARIADADHFIET--MPESYDTIVGERGV-GLSGGQKQRISLARALLKNPSILILDD 498
Cdd:PRK11231 90 GItvrelVAYGrSPWLSL-----WGRLSAEDNARVNqaMEQTRINHLADRRLtDLSGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1755737710 499 TTSAVDMETEVKIQGELKKITENTTTFI-IAHRIS-SVKEADEILILNHGEIIERGTHSSLLAEK 561
Cdd:PRK11231 165 PTTYLDINHQVELMRLMRELNTQGKTVVtVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
352-549 |
2.05e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 88.45 E-value: 2.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYdPT---SGEILIDGVDARKWHVREL-RNHIATVMQDIFLFSD-TI 426
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRDTeRAGIAIIHQELALVKElSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 427 EGNIAFGA---PDATMEDVRRMARiadADHFIE--TMPESYDTIVGErgvgLSGGQKQRISLARALLKNPSILILDDTTS 501
Cdd:PRK13549 100 LENIFLGNeitPGGIMDYDAMYLR---AQKLLAqlKLDINPATPVGN----LGLGQQQLVEIAKALNKQARLLILDEPTA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1755737710 502 AV-DMETEV--KIQGELKKitENTTTFIIAHRISSVKE-ADEILILNHGEII 549
Cdd:PRK13549 173 SLtESETAVllDIIRDLKA--HGIACIYISHKLNEVKAiSDTICVIRDGRHI 222
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
351-558 |
2.25e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 85.10 E-value: 2.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRF---YDP---TSGEILIDGVDARKWHVRELRNHIATVMQDIFLFSD 424
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSkikVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 425 -TIEGNIAFGAPDATMEDVRRMARIADAD-HFIETMPESYDTIvGERGVGLSGGQKQRISLARALLKNPSILILDDTTSA 502
Cdd:PRK14246 105 lSIYDNIAYPLKSHGIKEKREIKKIVEEClRKVGLWKEVYDRL-NSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1755737710 503 VDMETEVKIQGELKKITENTTTFIIAHRISSV-KEADEILILNHGEIIERGTHSSLL 558
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIF 240
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
349-529 |
3.01e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 84.10 E-value: 3.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 349 TDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVR---ELRNH-IATVMQDIFLFSD 424
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaELRNQkLGFIYQFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 425 -TIEGNIAF------GAPDATMEDVRRMARIADADHFIETMPESydtivgergvgLSGGQKQRISLARALLKNPSILILD 497
Cdd:PRK11629 102 fTALENVAMplligkKKPAEINSRALEMLAAVGLEHRANHRPSE-----------LSGGERQRVAIARALVNNPRLVLAD 170
|
170 180 190
....*....|....*....|....*....|....*
gi 1755737710 498 DTTSAVDMETEVKI---QGELkKITENTTTFIIAH 529
Cdd:PRK11629 171 EPTGNLDARNADSIfqlLGEL-NRLQGTAFLVVTH 204
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
352-580 |
6.02e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 84.06 E-value: 6.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYD--PT---SGEILIDGVDARKWHVR--ELRNHIATVMQDIFLFSD 424
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLYAPDVDpvEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 425 TIEGNIAFGAP--------DATMEDVRRMARIADadhfietmpESYDTIvGERGVGLSGGQKQRISLARALLKNPSILIL 496
Cdd:PRK14243 106 SIYDNIAYGARingykgdmDELVERSLRQAALWD---------EVKDKL-KQSGLSLSGGQQQRLCIARAIAVQPEVILM 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 497 DDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAEKGYYFDIYN--KQLGT 574
Cdd:PRK14243 176 DEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGGRYGYLVEFDRTEKIFNspQQQAT 255
|
....*.
gi 1755737710 575 EANVNG 580
Cdd:PRK14243 256 RDYVSG 261
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
338-553 |
6.91e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 87.22 E-value: 6.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 338 NVSFHfEDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARK--WHVRELRNHIATV 415
Cdd:PRK10261 19 NIAFM-QEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRrsRQVIELSEQSAAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 416 MQDI------FLFSDTIEG-NIAFGAPDATMEDVR------RMARIADADHFIET--MPESyDTIVGERGVGLSGGQKQR 480
Cdd:PRK10261 98 MRHVrgadmaMIFQEPMTSlNPVFTVGEQIAESIRlhqgasREEAMVEAKRMLDQvrIPEA-QTILSRYPHQLSGGMRQR 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1755737710 481 ISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTT--TFIIAHRISSVKE-ADEILILNHGEIIERGT 553
Cdd:PRK10261 177 VMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETGS 252
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
351-563 |
7.52e-18 |
|
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: 82.19 E-value: 7.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRF--YDPTSGEILIDGVD---------ARKwhvrelrnhiatvmqDI 419
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDitdlppeerARL---------------GI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 420 FLfsdtiegniAFGAPdATMEDVRRMariadadHFIETMpesydtivgerGVGLSGGQKQRISLARALLKNPSILILDDT 499
Cdd:cd03217 80 FL---------AFQYP-PEIPGVKNA-------DFLRYV-----------NEGFSGGEKKRNEILQLLLLEPDLAILDEP 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1755737710 500 TSAVDMETEVKIQGELKKI-TENTTTFIIAH--RISSVKEADEILILNHGEIIERGTHS--SLLAEKGY 563
Cdd:cd03217 132 DSGLDIDALRLVAEVINKLrEEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKElaLEIEKKGY 200
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
334-552 |
8.21e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 85.47 E-value: 8.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDdpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDgvDARKWHVRELRNHIA 413
Cdd:PRK11000 4 VTLRNVTKAYGD---VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIG--EKRMNDVPPAERGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 414 TVMQDIFLFSD-TIEGNIAFGAPDATMED------VRRMARIADADHFIETMPESydtivgergvgLSGGQKQRISLARA 486
Cdd:PRK11000 79 MVFQSYALYPHlSVAENMSFGLKLAGAKKeeinqrVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRT 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1755737710 487 LLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAH-RISSVKEADEILILNHGEIIERG 552
Cdd:PRK11000 148 LVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
334-562 |
1.22e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 83.53 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEddPNT----DVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILI------DGVDARKw 403
Cdd:PRK13634 3 ITFQKVEHRYQ--YKTpferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 404 hVRELRNHIATVMQdiF----LFSDTIEGNIAFGAPD--ATMEDVRRMARiadadHFIET--MPESydtIVGERGVGLSG 475
Cdd:PRK13634 80 -LKPLRKKVGIVFQ--FpehqLFEETVEKDICFGPMNfgVSEEDAKQKAR-----EMIELvgLPEE---LLARSPFELSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 476 GQKQRISLARALLKNPSILILDDTTSAVD-------METEVKIQGElkkitENTTTFIIAHRISSV-KEADEILILNHGE 547
Cdd:PRK13634 149 GQMRRVAIAGVLAMEPEVLVLDEPTAGLDpkgrkemMEMFYKLHKE-----KGLTTVLVTHSMEDAaRYADQIVVMHKGT 223
|
250 260
....*....|....*....|.
gi 1755737710 548 IIERGT------HSSLLAEKG 562
Cdd:PRK13634 224 VFLQGTpreifaDPDELEAIG 244
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
334-545 |
1.44e-17 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 80.28 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHfeDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEIlidgvdarkwhVRELRNHIA 413
Cdd:cd03223 1 IELENLSLA--TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 414 TVMQDIFLfsdtiegniafgaPDATMEDVrrmarIAdadhfietmpesY--DTIvgergvgLSGGQKQRISLARALLKNP 491
Cdd:cd03223 68 FLPQRPYL-------------PLGTLREQ-----LI------------YpwDDV-------LSGGEQQRLAFARLLLHKP 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1755737710 492 SILILDDTTSAVDMETEVKIqgeLKKITENTTTFI-IAHRISSVKEADEILILNH 545
Cdd:cd03223 111 KFVFLDEATSALDEESEDRL---YQLLKELGITVIsVGHRPSLWKFHDRVLDLDG 162
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
334-553 |
1.53e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 82.78 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEddpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDpTSGEILIDG--------VDARKWHV 405
Cdd:PRK14258 8 IKVNNLSFYYD---TQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGrveffnqnIYERRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 406 RELRNHIATVMQDIFLFSDTIEGNIAFGA------PDATMEDVRRMArIADADHFIETMPESYDTivgerGVGLSGGQKQ 479
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFPMSVYDNVAYGVkivgwrPKLEIDDIVESA-LKDADLWDEIKHKIHKS-----ALDLSGGQQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 480 RISLARALLKNPSILILDDTTSAVDMETEVKIQGELK--KITENTTTFIIAHRISSVKEADEILILNHG------EIIER 551
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenrigQLVEF 237
|
..
gi 1755737710 552 GT 553
Cdd:PRK14258 238 GL 239
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
316-507 |
1.55e-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: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 316 DAKIPIHAEKPAPSlqGH--VEFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEI 393
Cdd:COG0488 298 DKTVEIRFPPPERL--GKkvLELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 394 lidgvdarKWHVReLRnhIATV--MQDIFLFSDTIEGNIAFGAPDATMEDVRrmariadadHFIETM---PESYDTIVGE 468
Cdd:COG0488 373 --------KLGET-VK--IGYFdqHQEELDPDKTVLDELRDGAPGGTEQEVR---------GYLGRFlfsGDDAFKPVGV 432
|
170 180 190
....*....|....*....|....*....|....*....
gi 1755737710 469 rgvgLSGGQKQRISLARALLKNPSILILDDTTSAVDMET 507
Cdd:COG0488 433 ----LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIET 467
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
334-573 |
1.84e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 82.87 E-value: 1.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDPNTD--VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGV----DARKWHVRE 407
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEgrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTlitsTSKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 408 LRNHIATVMQ--DIFLFSDTIEGNIAFGAPD--ATMEDVRRMAR-----IADADHFIETMPesydtivgergVGLSGGQK 478
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALAReklalVGISESLFEKNP-----------FELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 479 QRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFI-IAHRISSVKE-ADEILILNHGEIIERGTHSS 556
Cdd:PRK13649 152 RRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSGKPKD 231
|
250
....*....|....*..
gi 1755737710 557 LLAEKGYyfdIYNKQLG 573
Cdd:PRK13649 232 IFQDVDF---LEEKQLG 245
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
350-548 |
2.00e-17 |
|
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: 80.17 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 350 DVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNH-IATVMQD-----IFLfS 423
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPEDrkregLVL-D 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 424 DTIEGNIAFGapdatmedvrrmariadadhfietmpesydtivgergVGLSGGQKQRISLARALLKNPSILILDDTTSAV 503
Cdd:cd03215 93 LSVAENIALS-------------------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1755737710 504 DMETEVKIQGELKKITENTTTFIIahrISS-----VKEADEILILNHGEI 548
Cdd:cd03215 136 DVGAKAEIYRLIRELADAGKAVLL---ISSeldelLGLCDRILVMYEGRI 182
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
65-278 |
2.08e-17 |
|
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: 82.90 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 65 STIIRTICRYTYQIMCERIGQnslfRIREDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLF 144
Cdd:cd18589 49 SAVSEFVCDLIYNITMSRIHS----RLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 145 SFAIIIMAAIDWKLTLALVIVTPLIAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEH 224
Cdd:cd18589 125 LFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQR 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1755737710 225 NEDFKKRNLDSAdVSRTYLPVLDSLAGM-LVVITLIFGGYLVIKGQMTLGDLVAF 278
Cdd:cd18589 205 LQKTYRLNKKEA-AAYAVSMWTSSFSGLaLKVGILYYGGQLVTAGTVSSGDLVTF 258
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
334-553 |
2.43e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 82.85 E-value: 2.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDdpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHvrelRNHIA 413
Cdd:COG4152 2 LELKGLTKRFGD---KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 414 ------------TVM-QDIFLfsdtiegniafgapdATMEDVRRMARIADADHFIET--MPESYDTIVGErgvgLSGGQK 478
Cdd:COG4152 75 ylpeerglypkmKVGeQLVYL---------------ARLKGLSKAEAKRRADEWLERlgLGDRANKKVEE----LSKGNQ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 479 QRISLARALLKNPSILILDDTTS-----AVDMetevkIQGELKKITENTTTfII--AHRISSVKE-ADEILILNHGEIIE 550
Cdd:COG4152 136 QKVQLIAALLHDPELLILDEPFSgldpvNVEL-----LKDVIRELAAKGTT-VIfsSHQMELVEElCDRIVIINKGRKVL 209
|
...
gi 1755737710 551 RGT 553
Cdd:COG4152 210 SGS 212
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
334-545 |
3.73e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 81.31 E-value: 3.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEddpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILidgvdarkwHVRELRnhIA 413
Cdd:PRK09544 5 VSLENVSVSFG---QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKLR--IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 414 TVMQDIFLfsdtiegniafgapDATME-DVRRMARI------AD---------ADHFIETMPESydtivgergvgLSGGQ 477
Cdd:PRK09544 71 YVPQKLYL--------------DTTLPlTVNRFLRLrpgtkkEDilpalkrvqAGHLIDAPMQK-----------LSGGE 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1755737710 478 KQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRISSV-KEADEILILNH 545
Cdd:PRK09544 126 TQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVmAKTDEVLCLNH 196
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
335-557 |
3.81e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 82.83 E-value: 3.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 335 EFKNVSFHFE--DD-------PNT-DVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARK-- 402
Cdd:PRK15079 10 EVADLKVHFDikDGkqwfwqpPKTlKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGmk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 403 ---WhvRELRNHIATVMQDIfLFS--------DTIEGNIAFGAPDATMEDVRR-----MARIADADHFIETMPESYdtiv 466
Cdd:PRK15079 90 ddeW--RAVRSDIQMIFQDP-LASlnprmtigEIIAEPLRTYHPKLSRQEVKDrvkamMLKVGLLPNLINRYPHEF---- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 467 gergvglSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKIT-ENTTTFI-IAHRISSVKE-ADEILIL 543
Cdd:PRK15079 163 -------SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQrEMGLSLIfIAHDLAVVKHiSDRVLVM 235
|
250
....*....|....
gi 1755737710 544 NHGEIIERGTHSSL 557
Cdd:PRK15079 236 YLGHAVELGTYDEV 249
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
352-504 |
4.04e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 80.69 E-value: 4.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRE---LRNHIATVMQDIFLFSD-TIE 427
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHLLMDrTVY 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1755737710 428 GNIAFG--APDATMEDVRRmaRIADADHFIETMPESYDTivgerGVGLSGGQKQRISLARALLKNPSILILDDTTSAVD 504
Cdd:PRK10908 98 DNVAIPliIAGASGDDIRR--RVSAALDKVGLLDKAKNF-----PIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
361-505 |
4.48e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 83.00 E-value: 4.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 361 PGQTI-AILGETGAGKSTLVNLICRFYDPTSGEILIDG---VDARK--WHVRELRnHIATVMQDIFLFSD-TIEGNIAFG 433
Cdd:PRK11144 22 PAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKgiCLPPEKR-RIGYVFQDARLFPHyKVRGNLRYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 434 apdatmedvrrMARiadadhfieTMPESYDTIVGERGVG---------LSGGQKQRISLARALLKNPSILILDDTTSAVD 504
Cdd:PRK11144 101 -----------MAK---------SMVAQFDKIVALLGIEplldrypgsLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
.
gi 1755737710 505 M 505
Cdd:PRK11144 161 L 161
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
350-550 |
6.38e-17 |
|
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: 80.17 E-value: 6.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 350 DVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVD---------ARkwhVRelRNHIATVMQDIF 420
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDlfaldedarAR---LR--ARHVGFVFQSFQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 421 LF-SDTIEGNIAFGAPDATMEDVRRMARIA--------DADHFietmPesydtivgergVGLSGGQKQRISLARALLKNP 491
Cdd:COG4181 101 LLpTLTALENVMLPLELAGRRDARARARALlervglghRLDHY----P-----------AQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1755737710 492 SILILDDTTSAVDMETEVKIQG---ELKKiTENTTTFIIAHRISSVKEADEILILNHGEIIE 550
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDllfELNR-ERGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
352-564 |
7.27e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 81.67 E-value: 7.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKwHVRELRNHIATVM----QdifLFSD--T 425
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFK-RRKEFARRIGVVFgqrsQ---LWWDlpA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 426 IEgniafgapdaTMEDVRRMARIADADhFIETMpesyDTIVGERGVG---------LSGGQKQRISLARALLKNPSILIL 496
Cdd:COG4586 114 ID----------SFRLLKAIYRIPDAE-YKKRL----DELVELLDLGelldtpvrqLSLGQRMRCELAAALLHRPKILFL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1755737710 497 DDTTSAVDMETEVKIQGELKKI--TENTTTFIIAHRISSVKE-ADEILILNHGEIIERGTHSSLLAEKGYY 564
Cdd:COG4586 179 DEPTIGLDVVSKEAIREFLKEYnrERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFGPY 249
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
22-294 |
1.02e-16 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 81.01 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 22 FILIFIASGISIIYPLLGGKVIDDVvyqnkTNLLIPLLLIMIISTIIRTICRYTYQIMCE-------RIGQNSLFRIRED 94
Cdd:cd18582 2 LLLLVLAKLLNVAVPFLLKYAVDAL-----SAPASALLAVPLLLLLAYGLARILSSLFNElrdalfaRVSQRAVRRLALR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 95 LYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAI-DWKLTLALVIVTPLIAILT 173
Cdd:cd18582 77 VFRHLHSLSLRFHLSRKTGALSRAIERGTRGIEFLLRFLLFNILPTILELLLVCGILWYLyGWSYALITLVTVALYVAFT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 174 MKMSskaqpvfyEIRESFSRLNSMVEENISGNRV--------VKAFAREDFEMKKFHEHNEDFKKRNLDSAdVSRTYLPV 245
Cdd:cd18582 157 IKVT--------EWRTKFRREMNEADNEANAKAVdsllnyetVKYFNNEEYEAERYDKALAKYEKAAVKSQ-TSLALLNI 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1755737710 246 LDSL---AGMLVVitLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGW 294
Cdd:cd18582 228 GQALiisLGLTAI--MLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFLGF 277
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
338-559 |
1.16e-16 |
|
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: 83.20 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 338 NVSFHfEDDPNTDVLKNISLKASPGQTIAILGETGAGKS----TLVNLICRFYDPTSGEILIDGVDARKWHVRELR---- 409
Cdd:COG4172 13 SVAFG-QGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRrirg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 410 NHIAtvMqdIF---------LFsdTIEGNIAfgapdATMEDVRRMARIADADHFIETMPEsydtiVG----ERGVG---- 472
Cdd:COG4172 92 NRIA--M--IFqepmtslnpLH--TIGKQIA-----EVLRLHRGLSGAAARARALELLER-----VGipdpERRLDayph 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 473 -LSGGQKQRISLARALLKNPSILILDDTTSAVDmeteVKIQG-------ELKKiTENTTTFIIAHRISSVKE-ADEILIL 543
Cdd:COG4172 156 qLSGGQRQRVMIAMALANEPDLLIADEPTTALD----VTVQAqildllkDLQR-ELGMALLLITHDLGVVRRfADRVAVM 230
|
250
....*....|....*.
gi 1755737710 544 NHGEIIERGTHSSLLA 559
Cdd:COG4172 231 RQGEIVEQGPTAELFA 246
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
15-303 |
1.85e-16 |
|
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: 80.25 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 15 RLLMIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIgQNSL-FRIRE 93
Cdd:cd18555 1 KKLLISILLLSLLLQLLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKL-QTKLdKSLMS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 94 DLYKKLQSLDFDFFNNTRVGDIMARMtGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILT 173
Cdd:cd18555 80 DFFEHLLKLPYSFFENRSSGDLLFRA-NSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 174 MKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGML 253
Cdd:cd18555 159 LLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1755737710 254 VVITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMrMSgwLINDVQRFI 303
Cdd:cd18555 239 PLLILWIGAYLVINGELTLGELIAFSSLAGSFLTPI-VS--LINSYNQFI 285
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
334-547 |
4.04e-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: 75.56 E-value: 4.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGvdarkwhvrelRNHIA 413
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 414 TVMQdiflfsdtiegniafgapdatmedvrrmariadadhfietmpesydtivgergvgLSGGQKQRISLARALLKNPSI 493
Cdd:cd03221 67 YFEQ-------------------------------------------------------LSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1755737710 494 LILDDTTSAVDMETEVKIQGELKKitENTTTFIIAH-R--ISSVkeADEILILNHGE 547
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALKE--YPGTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
350-549 |
4.42e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 81.22 E-value: 4.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 350 DVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRE-LRNHIATVMQD-----IFLfS 423
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYVPEDrkgegLVL-D 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 424 DTIEGNIAFgapdATMEDVRRMARI------ADADHFIETM---PESYDTIVGErgvgLSGGQKQRISLARALLKNPSIL 494
Cdd:COG1129 345 LSIRENITL----ASLDRLSRGGLLdrrrerALAEEYIKRLrikTPSPEQPVGN----LSGGNQQKVVLAKWLATDPKVL 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1755737710 495 ILDDTTSAVDMETEVKIQGELKKITENTTTFIIahrISSvkEADE-------ILILNHGEII 549
Cdd:COG1129 417 ILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIV---ISS--ELPEllglsdrILVMREGRIV 473
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
337-558 |
1.07e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.52 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 337 KNVSFHFeddPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIATVM 416
Cdd:PRK10575 15 RNVSFRV---PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 417 QDIflfsdtiegniafgaPDATMEDVRR------------MARIADADHfiETMPESYdTIVG-----ERGV-GLSGGQK 478
Cdd:PRK10575 92 QQL---------------PAAEGMTVRElvaigrypwhgaLGRFGAADR--EKVEEAI-SLVGlkplaHRLVdSLSGGER 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 479 QRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIA--HRIS-SVKEADEILILNHGEIIERGTHS 555
Cdd:PRK10575 154 QRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAvlHDINmAARYCDYLVALRGGEMIAQGTPA 233
|
...
gi 1755737710 556 SLL 558
Cdd:PRK10575 234 ELM 236
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
351-552 |
1.54e-15 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 76.22 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNhIATVM-QDIFLFSDTiegn 429
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRR-IGVVFgQKTQLWWDL---- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 430 iafgAPDATMEDVRRMARIaDADHFIETMPESYDTIVGERGV-----GLSGGQKQRISLARALLKNPSILILDDTTSAVD 504
Cdd:cd03267 111 ----PVIDSFYLLAAIYDL-PPARFKKRLDELSELLDLEELLdtpvrQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1755737710 505 METEVKIQGELKKITENTTTFII--AHRISSV-KEADEILILNHGEIIERG 552
Cdd:cd03267 186 VVAQENIRNFLKEYNRERGTTVLltSHYMKDIeALARRVLVIDKGRLLYDG 236
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
334-549 |
2.02e-15 |
|
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: 79.10 E-value: 2.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDdpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFY--DPTSGEILIDGVDARKWHVREL-RN 410
Cdd:TIGR02633 2 LEMKGIVKTFGG---VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTeRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 411 HIATVMQDIFLFSD-TIEGNIAFG----APDATMEDVRRMARiadADHFIETMpeSYDTIVGERGVG-LSGGQKQRISLA 484
Cdd:TIGR02633 79 GIVIIHQELTLVPElSVAENIFLGneitLPGGRMAYNAMYLR---AKNLLREL--QLDADNVTRPVGdYGGGQQQLVEIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 485 RALLKNPSILILDDTTSAVdmeTEVKIQGELKKITE----NTTTFIIAHRISSVKE-ADEILILNHGEII 549
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSL---TEKETEILLDIIRDlkahGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
351-504 |
2.46e-15 |
|
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: 75.55 E-value: 2.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEIL-------IDGVDARKWHVRELRNH-IATVMQdiFLf 422
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILvrhdggwVDLAQASPREILALRRRtIGYVSQ--FL- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 423 sDTI----------EGNIAFGAPDATMED-VRRM-ARIAdadhfietmpesydtiVGERGVGL-----SGGQKQRISLAR 485
Cdd:COG4778 103 -RVIprvsaldvvaEPLLERGVDREEARArARELlARLN----------------LPERLWDLppatfSGGEQQRVNIAR 165
|
170
....*....|....*....
gi 1755737710 486 ALLKNPSILILDDTTSAVD 504
Cdd:COG4778 166 GFIADPPLLLLDEPTASLD 184
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
351-559 |
2.74e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 76.29 E-value: 2.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSG-----EILIDGVDARKWH-VRELRNHIATVMQDIFLFSD 424
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRdVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 425 TIEGNIAFGAPDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVD 504
Cdd:PRK14271 116 SIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALD 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1755737710 505 METEVKIQGELKKITENTTTFIIAHRIS-SVKEADEILILNHGEIIERGTHSSLLA 559
Cdd:PRK14271 196 PTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
305-561 |
6.86e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 76.02 E-value: 6.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 305 SSFKIQDMMATDAKIPIHAEKPAPSlqghVEFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICR 384
Cdd:PRK13536 17 SPIERKHQGISEAKASIPGSMSTVA----IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 385 FYDPTSGEILIDGVDARKwHVRELRNHIATVMQ-DIFLFSDTIEGNIA-----FGAPDATMEDV-------RRMARIADA 451
Cdd:PRK13536 90 MTSPDAGKITVLGVPVPA-RARLARARIGVVPQfDNLDLEFTVRENLLvfgryFGMSTREIEAVipsllefARLESKADA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 452 dhfietmpesydtivgeRGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRI 531
Cdd:PRK13536 169 -----------------RVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHF 231
|
250 260 270
....*....|....*....|....*....|..
gi 1755737710 532 SSVKE--ADEILILNHGEIIERGTHSSLLAEK 561
Cdd:PRK13536 232 MEEAErlCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
351-504 |
8.87e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 73.37 E-value: 8.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIATvmQDIFLFSDTIEGNI 430
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGH--RNAMKPALTVAENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 431 AF---------GAPDATMEDVrRMARIADadhfietMPESYdtivgergvgLSGGQKQRISLARALLKNPSILILDDTTS 501
Cdd:PRK13539 95 EFwaaflggeeLDIAAALEAV-GLAPLAH-------LPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
...
gi 1755737710 502 AVD 504
Cdd:PRK13539 157 ALD 159
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
334-550 |
1.14e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 76.93 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDdpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDG--VDARKWHvrELRNH 411
Cdd:PRK10522 323 LELRNVTFAYQD--NGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGkpVTAEQPE--DYRKL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 412 IATVMQDIFLFSDTIEgniafgaPDATMEDVrrmariADADHFIETMP-ESYDTIVGER--GVGLSGGQKQRISLARALL 488
Cdd:PRK10522 399 FSAVFTDFHLFDQLLG-------PEGKPANP------ALVEKWLERLKmAHKLELEDGRisNLKLSKGQKKRLALLLALA 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755737710 489 KNPSILILDDTtsAVDME------------TEVKIQGElkkitentTTFIIAHRISSVKEADEILILNHGEIIE 550
Cdd:PRK10522 466 EERDILLLDEW--AADQDphfrrefyqvllPLLQEMGK--------TIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
351-566 |
1.67e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 76.46 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLIC-RFYDPT-SGEILIDGvdaRKwHVRELRNHIATVMQDIFLFSD-TIE 427
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANN---RK-PTKQILKRTGFVTQDDILYPHlTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 428 GNIAFGAPDATMEDVRRMARIADADHFIETM--PESYDTIVGERGV-GLSGGQKQRISLARALLKNPSILILDDTTSAVD 504
Cdd:PLN03211 159 ETLVFCSLLRLPKSLTKQEKILVAESVISELglTKCENTIIGNSFIrGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1755737710 505 METEVKIQGELKKITENTTTFIIA-HRISS--VKEADEILILNHGEIIERGTHSSLLAekgyYFD 566
Cdd:PLN03211 239 ATAAYRLVLTLGSLAQKGKTIVTSmHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA----YFE 299
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
351-559 |
1.89e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 76.28 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYdPT------SGEILIDG---VDARKWHVRELR-NHIATVMQDIF 420
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHGeslLHASEQTLRGVRgNKIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 421 LFSD---TIEGNIAfgapdatmeDV----RRMARIADADHFIETMPEsydtiVGERGVG---------LSGGQKQRISLA 484
Cdd:PRK15134 103 VSLNplhTLEKQLY---------EVlslhRGMRREAARGEILNCLDR-----VGIRQAAkrltdyphqLSGGERQRVMIA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1755737710 485 RALLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRISSVKE-ADEILILNHGEIIERGTHSSLLA 559
Cdd:PRK15134 169 MALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFS 246
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
351-552 |
2.81e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 73.10 E-value: 2.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIATVMQDIFLFSD-TIEGN 429
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDiTVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 430 IAFGA-PDATM------EDVRRMARIADADHFIETMPESYDTivgergvgLSGGQKQRISLARALLKNPSILILDDTTSA 502
Cdd:PRK10253 102 VARGRyPHQPLftrwrkEDEEAVTKAMQATGITHLADQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1755737710 503 VDMETEVKIQGELKKI--TENTTTFIIAHRIS-SVKEADEILILNHGEIIERG 552
Cdd:PRK10253 174 LDISHQIDLLELLSELnrEKGYTLAAVLHDLNqACRYASHLIALREGKIVAQG 226
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
351-548 |
4.02e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.09 E-value: 4.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGvdARKWHVRELRNH---IATVMQDIFLFSD-TI 426
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGG--NPCARLTPAKAHqlgIYLVPQEPLLFPNlSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 427 EGNIAFGAPdATMEDVRRMARIADA--DHFIETMPESydtivgergvGLSGGQKQRISLARALLKNPSILILDDTTSAVD 504
Cdd:PRK15439 104 KENILFGLP-KRQASMQKMKQLLAAlgCQLDLDSSAG----------SLEVADRQIVEILRGLMRDSRILILDEPTASLT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1755737710 505 -METE---VKIQGELKKiteNTTTFIIAHRISSVKE-ADEILILNHGEI 548
Cdd:PRK15439 173 pAETErlfSRIRELLAQ---GVGIVFISHKLPEIRQlADRISVMRDGTI 218
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
334-546 |
4.45e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.82 E-value: 4.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFeddPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKW-HVRELRNHI 412
Cdd:PRK09700 6 ISMAGIGKSF---GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLdHKLAAQLGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 413 ATVMQDIFLFSD-TIEGNI---------AFGAPdatMEDVRRMARIADADHFIETMPESYDTIVGErgvgLSGGQKQRIS 482
Cdd:PRK09700 83 GIIYQELSVIDElTVLENLyigrhltkkVCGVN---IIDWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1755737710 483 LARALLKNPSILILDD-TTSAVDMETE--VKIQGELKKitENTTTFIIAHRISSVKE-ADEILILNHG 546
Cdd:PRK09700 156 IAKTLMLDAKVIIMDEpTSSLTNKEVDylFLIMNQLRK--EGTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
90-294 |
6.13e-14 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 72.62 E-value: 6.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 90 RIREDLYKKLQSLDFDFFNNTRVGDIMARMTgDTDAIRHFVSWVSYN-ILENVFLFSFaIIIMAAIDWKLTLALVIVTPL 168
Cdd:cd18566 76 RLSNAAFEHLLSLPLSFFEREPSGAHLERLN-SLEQIREFLTGQALLaLLDLPFVLIF-LGLIWYLGGKLVLVPLVLLGL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 169 IAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDS 248
Cdd:cd18566 154 FVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQL 233
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1755737710 249 LAGMLVVITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMR--MSGW 294
Cdd:cd18566 234 FSQVSMVAVVAFGALLVINGDLTVGALIACTMLSGRVLQPLQraFGLW 281
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
334-553 |
1.05e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 72.57 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFedDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDarkwhVREL----R 409
Cdd:PRK11650 4 LKLQAVRKSY--DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRV-----VNELepadR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 410 NhIATVMQDIFLFSD-TIEGNIAFGAPDATMEDVRRMARIADA------DHFIETMPESydtivgergvgLSGGQKQRIS 482
Cdd:PRK11650 77 D-IAMVFQNYALYPHmSVRENMAYGLKIRGMPKAEIEERVAEAarilelEPLLDRKPRE-----------LSGGQRQRVA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755737710 483 LARALLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAH-RISSVKEADEILILNHGEIIERGT 553
Cdd:PRK11650 145 MGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRrlKTTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGT 218
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
334-557 |
1.14e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 71.33 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDA---RKWHVRELRN 410
Cdd:PRK11831 8 VDMRGVSFTRGNRC---IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamSRSRLYTVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 411 HIATVMQDIFLFSD-TIEGNIAFgapdatmeDVRRMARIADAdhFIETMPESYDTIVGERGVG------LSGGQKQRISL 483
Cdd:PRK11831 85 RMSMLFQSGALFTDmNVFDNVAY--------PLREHTQLPAP--LLHSTVMMKLEAVGLRGAAklmpseLSGGMARRAAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1755737710 484 ARALLKNPSILILDDTTSAVD---METEVKIQGELKKiTENTTTFIIAHRISSVKE-ADEILILNHGEIIERGTHSSL 557
Cdd:PRK11831 155 ARAIALEPDLIMFDEPFVGQDpitMGVLVKLISELNS-ALGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
354-553 |
1.54e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 70.79 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 354 NISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVD---------ARK------WHVRELRNHIAT---- 414
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHieglpghqiARMgvvrtfQHVRLFREMTVIenll 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 415 VMQDIFLFSDTIEGniAFGAPdatmeDVRRMAR--IADADHFIETMPEsydTIVGERGVG-LSGGQKQRISLARALLKNP 491
Cdd:PRK11300 103 VAQHQQLKTGLFSG--LLKTP-----AFRRAESeaLDRAATWLERVGL---LEHANRQAGnLAYGQQRRLEIARCMVTQP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 492 SILILDDTTSAVD-METEvkiqgELKK-ITE-----NTTTFIIAHRISSVKE-ADEILILNHGEIIERGT 553
Cdd:PRK11300 173 EILMLDEPAAGLNpKETK-----ELDElIAElrnehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGT 237
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
351-559 |
1.62e-13 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 70.44 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKW--HVRElRNHIATVMQD--IF--Lfsd 424
Cdd:COG1137 18 VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLpmHKRA-RLGIGYLPQEasIFrkL--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 425 TIEGNIAfgapdATME--DVRRMARIADADHFIEtmpE-SYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTS 501
Cdd:COG1137 94 TVEDNIL-----AVLElrKLSKKEREERLEELLE---EfGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1755737710 502 AVDMETEVKIQG---ELKK------ITEntttfiiaHrisSVKEADEIL----ILNHGEIIERGTHSSLLA 559
Cdd:COG1137 166 GVDPIAVADIQKiirHLKErgigvlITD--------H---NVRETLGICdrayIISEGKVLAEGTPEEILN 225
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
336-549 |
1.87e-13 |
|
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: 69.21 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 336 FKNVSFHF-EDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLIC---RFYDPTSGEILIDGVDARKWHVRELRNH 411
Cdd:cd03233 6 WRNISFTTgKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAnrtEGNVSVEGDIHYNGIPYKEFAEKYPGEI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 412 IATVMQDIFLFSDTIEgniafgapdATMEDVRRMariaDADHFIetmpesydtivgeRGVglSGGQKQRISLARALLKNP 491
Cdd:cd03233 86 IYVSEEDVHFPTLTVR---------ETLDFALRC----KGNEFV-------------RGI--SGGERKRVSIAEALVSRA 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1755737710 492 SILILDDTTSAVDMETEVKIQGELKKIT--ENTTTFIIAHRISS--VKEADEILILNHGEII 549
Cdd:cd03233 138 SVLCWDNSTRGLDSSTALEILKCIRTMAdvLKTTTFVSLYQASDeiYDLFDKVLVLYEGRQI 199
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
348-563 |
1.90e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 70.44 E-value: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 348 NTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRF--YDPTSGEILIDGVDARKWHVrELRNHIAtvmqdIFL-FSD 424
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEP-EERAHLG-----IFLaFQY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 425 TIEgniafgAPDATMEDVRRMARIA----------DADHFIETMPESYDtIVG------ERGV--GLSGGQKQRISLARA 486
Cdd:CHL00131 93 PIE------IPGVSNADFLRLAYNSkrkfqglpelDPLEFLEIINEKLK-LVGmdpsflSRNVneGFSGGEKKRNEILQM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 487 LLKNPSILILDDTTSAVDMETEVKIQGELKKI-TENTTTFIIAH--RISSVKEADEILILNHGEIIERGTHS--SLLAEK 561
Cdd:CHL00131 166 ALLDSELAILDETDSGLDIDALKIIAEGINKLmTSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGDAElaKELEKK 245
|
..
gi 1755737710 562 GY 563
Cdd:CHL00131 246 GY 247
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
354-560 |
2.46e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 72.53 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 354 NISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILI----DGVDARKWHVRE---LRNHIATVMQDIFLFSD-T 425
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDGrgrAKRYIGILHQEYDLYPHrT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 426 IEGN----IAFGAPD--ATMEDVRRMARIA-DADHFIETMPESYDTivgergvgLSGGQKQRISLARALLKNPSILILDD 498
Cdd:TIGR03269 382 VLDNlteaIGLELPDelARMKAVITLKMVGfDEEKAEEILDKYPDE--------LSEGERHRVALAQVLIKEPRIVILDE 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1755737710 499 TTSAVDMETEVKIQGELKKITE--NTTTFIIAHRISSVKE-ADEILILNHGEIIERGTHSSLLAE 560
Cdd:TIGR03269 454 PTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
22-282 |
2.63e-13 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 70.72 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 22 FILIFIASGISIIYPLLGGKVIDDVVY--QNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFRIREDLYKKL 99
Cdd:cd18560 2 LLLLILGKACNVLAPLFLGRAVNALTLakVKDLESAVTLILLYALLRFSSKLLKELRSLLYRRVQQNAYRELSLKTFAHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 100 QSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAI-DWKLTLALVIVTPLIAILTMKMSs 178
Cdd:cd18560 82 HSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVPTLLELIVVSVVFAFHfGAWLALIVFLSVLLYGVFTIKVT- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 179 kaqpvfyEIRESFSRLnSMVEENISGNRV---------VKAFAREDFEMKKFHEHNEDFKKRNLdSADVSRTYLPVLDSL 249
Cdd:cd18560 161 -------EWRTKFRRA-ANKKDNEAHDIAvdsllnfetVKYFTNEKYEVDRYGEAVKEYQKSSV-KVQASLSLLNVGQQL 231
|
250 260 270
....*....|....*....|....*....|....
gi 1755737710 250 A-GMLVVITLIFGGYLVIKGQMTLGDLVAFNGFL 282
Cdd:cd18560 232 IiQLGLTLGLLLAGYRVVDGGLSVGDFVAVNTYI 265
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
352-552 |
5.82e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.81 E-value: 5.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEIL-----IDGVDARKwhVRELRNHIATVMQDIFLfsdTI 426
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIfngqrIDTLSPGK--LQALRRDIQFIFQDPYA---SL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 427 EGNIAFGapDATMEDVR---------RMARIADADHFIETMPESYDTIVGErgvgLSGGQKQRISLARALLKNPSILILD 497
Cdd:PRK10261 415 DPRQTVG--DSIMEPLRvhgllpgkaAAARVAWLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIAD 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1755737710 498 DTTSAVDMETEVKIQGELKKITEN--TTTFIIAHRISSVKE-ADEILILNHGEIIERG 552
Cdd:PRK10261 489 EAVSALDVSIRGQIINLLLDLQRDfgIAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
352-560 |
7.88e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.14 E-value: 7.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKwhvrELR-NHIATVMQdiflfSDTIEGNI 430
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ----ALQkNLVAYVPQ-----SEEVDWSF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 431 AfgapdATMEDVRRMAR--------IADA-DHFIET-------MPESYDTIVGErgvgLSGGQKQRISLARALLKNPSIL 494
Cdd:PRK15056 94 P-----VLVEDVVMMGRyghmgwlrRAKKrDRQIVTaalarvdMVEFRHRQIGE----LSGGQKKRVFLARAIAQQGQVI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1755737710 495 ILDDTTSAVDMETEVKIQGELKKI-TENTTTFIIAHRISSVKEADEILILNHGEIIERG-THSSLLAE 560
Cdd:PRK15056 165 LLDEPFTGVDVKTEARIISLLRELrDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGpTETTFTAE 232
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
347-561 |
8.80e-13 |
|
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: 70.73 E-value: 8.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 347 PNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILI-DGV-----------DARKwHVRElrnhiaT 414
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGIkvgylpqepqlDPTK-TVRE------N 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 415 VMQDIFLFSDTI----EGNIAFGAPDATMEDV-RRMARI------ADA---DHFIETMPES-----YDTIVGErgvgLSG 475
Cdd:TIGR03719 89 VEEGVAEIKDALdrfnEISAKYAEPDADFDKLaAEQAELqeiidaADAwdlDSQLEIAMDAlrcppWDADVTK----LSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 476 GQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITenTTTFIIAH-RISSVKEADEILILNHGEIIE-RGT 553
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYP--GTVVAVTHdRYFLDNVAGWILELDRGRGIPwEGN 242
|
....*...
gi 1755737710 554 HSSLLAEK 561
Cdd:TIGR03719 243 YSSWLEQK 250
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
328-559 |
9.88e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 69.06 E-value: 9.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 328 PSLQGHVEFKNVSFHFEDdpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGvDARKWHVRE 407
Cdd:PRK13537 2 PMSVAPIDFRNVEKRYGD---KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG-EPVPSRARH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 408 LRNHIATVMQDIFLFSD-TIEGNIA-----FGAPDATMEdvrrmARIADADHFIEtMPESYDTIVGErgvgLSGGQKQRI 481
Cdd:PRK13537 78 ARQRVGVVPQFDNLDPDfTVRENLLvfgryFGLSAAAAR-----ALVPPLLEFAK-LENKADAKVGE----LSGGMKRRL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 482 SLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKE--ADEILILNHGEIIERGTHSSLLA 559
Cdd:PRK13537 148 TLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAErlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
352-561 |
2.26e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 67.17 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYdPTSGEILIDGVDARKWHVRELRNHIATVMQ--------DIFLFs 423
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLSQqqsppfamPVFQY- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 424 dtiegnIAFGAPDATMEDV--RRMARIADADHFIETMPesydtivgeRGVG-LSGGQKQRISLARALLK-----NPS--I 493
Cdd:COG4138 90 ------LALHQPAGASSEAveQLLAQLAEALGLEDKLS---------RPLTqLSGGEWQRVRLAAVLLQvwptiNPEgqL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 494 LILDDTTSAVDMETEVKIQGELKKITENTTTFII-AHRIS-SVKEADEILILNHGEIIERGTHSSLLAEK 561
Cdd:COG4138 155 LLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMsSHDLNhTLRHADRVWLLKQGKLVASGETAEVMTPE 224
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
15-300 |
2.30e-12 |
|
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: 67.93 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 15 RLLMIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFRIRED 94
Cdd:cd18783 1 KRLFRDVAIASLILHVLALAPPIFFQIVIDKVLVHQSYSTLYVLTIGVVIALLFEGILGYLRRYLLLVATTRIDARLALR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 95 LYKKLQSLDFDFFNNTRVGDIMARMtGDTDAIRHFVSwvsyNILENVFLFSFAII----IMAAIDWKLT---LALVIVTP 167
Cdd:cd18783 81 TFDRLLSLPIDFFERTPAGVLTKHM-QQIERIRQFLT----GQLFGTLLDATSLLvflpVLFFYSPTLAlvvLAFSALIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 168 LIAILTMKMSSKAQPVFYeiRESFSRlNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLD 247
Cdd:cd18783 156 LIILAFLPPFRRRLQALY--RAEGER-QAFLVETVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGRLSNWPQTLTG 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1755737710 248 SLAGMLVVITLIFGGYLVIKGQMTLGDLVAFNgflwMLNGpmRMSGWLINDVQ 300
Cdd:cd18783 233 PLEKLMTVGVIWVGAYLVFAGSLTVGALIAFN----MLAG--RVAGPLVQLAG 279
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
351-561 |
3.74e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 66.46 E-value: 3.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDAR--KWHVRELRNhIATVMQDIFLFSD-TIE 427
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllPLHARARRG-IGYLPQEASIFRRlSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 428 GNIAfgAPDATMEDVRRMARIADADHFIETMPESYdtIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMET 507
Cdd:PRK10895 97 DNLM--AVLQIRDDLSAEQREDRANELMEEFHIEH--LRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPIS 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 508 EVKIqgelKKITENTT-----TFIIAHRI-SSVKEADEILILNHGEIIERGTHSSLLAEK 561
Cdd:PRK10895 173 VIDI----KRIIEHLRdsglgVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDE 228
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
351-550 |
4.17e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 65.96 E-value: 4.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVR---ELR-NHIATVMQDiFLFSDTI 426
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRaKHVGFVFQS-FMLIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 427 EgniafgapdaTMEDVRRMARIADadhfiETMPESYD---TIVGERGVG---------LSGGQKQRISLARALLKNPSIL 494
Cdd:PRK10584 104 N----------ALENVELPALLRG-----ESSRQSRNgakALLEQLGLGkrldhlpaqLSGGEQQRVALARAFNGRPDVL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1755737710 495 ILDDTTSAVDMETEVKIQGELKKITEN--TTTFIIAHRISSVKEADEILILNHGEIIE 550
Cdd:PRK10584 169 FADEPTGNLDRQTGDKIADLLFSLNREhgTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
347-549 |
5.95e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.11 E-value: 5.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 347 PNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNH-IATVMQDIFLFSD- 424
Cdd:PRK10762 15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgIGIIHQELNLIPQl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 425 TIEGNIAFGapdatMEDVRRMARI------ADADHFIETM--PESYDTIVGErgvgLSGGQKQRISLARALLKNPSILIL 496
Cdd:PRK10762 95 TIAENIFLG-----REFVNRFGRIdwkkmyAEADKLLARLnlRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIM 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1755737710 497 DDTTSAV-DMETE--VKIQGELKkiTENTTTFIIAHRISSVKE-ADEILILNHGEII 549
Cdd:PRK10762 166 DEPTDALtDTETEslFRVIRELK--SQGRGIVYISHRLKEIFEiCDDVTVFRDGQFI 220
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
348-552 |
6.92e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 66.02 E-value: 6.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 348 NTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYD-----PTSGEILIDGVDARKWHVR--ELRNHIATVMQDIF 420
Cdd:PRK14267 16 SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDpiEVRREVGMVFQYPN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 421 LFSD-TIEGNIAFGAPDATMEDVRRmariaDADHFIE------TMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSI 493
Cdd:PRK14267 96 PFPHlTIYDNVAIGVKLNGLVKSKK-----ELDERVEwalkkaALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKI 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 494 LILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHR-ISSVKEADEILILNHGEIIERG 552
Cdd:PRK14267 171 LLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
312-495 |
1.49e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 66.97 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 312 MMATDAKIPIHAEKPAPslqGHV--EFKNVSFHfeDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPT 389
Cdd:COG3845 237 MVGREVLLRVEKAPAEP---GEVvlEVENLSVR--DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPA 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 390 SGEILIDGVDARKWHVRELRNH-IATVMQD---IFLFSD-TIEGNIAFGAPDAT------MEDVRRMAriADADHFIETM 458
Cdd:COG3845 312 SGSIRLDGEDITGLSPRERRRLgVAYIPEDrlgRGLVPDmSVAENLILGRYRRPpfsrggFLDRKAIR--AFAEELIEEF 389
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1755737710 459 ---PESYDTIVGergvGLSGGQKQRISLARALLKNPSILI 495
Cdd:COG3845 390 dvrTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLI 425
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
341-552 |
1.80e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 67.44 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 341 FHFEDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLIC----RFYDPTSGEILIDGVDAR--KWHVR-------E 407
Cdd:TIGR00956 66 KKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEeiKKHYRgdvvynaE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 408 LRNHIA--TVmqdiflfSDTIEGNIAFGAPDATMEDVRRMARIADADHFIET---MPESYDTIVGERGV-GLSGGQKQRI 481
Cdd:TIGR00956 146 TDVHFPhlTV-------GETLDFAARCKTPQNRPDGVSREEYAKHIADVYMAtygLSHTRNTKVGNDFVrGVSGGERKRV 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1755737710 482 SLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRISsvKEA----DEILILNHGEIIERG 552
Cdd:TIGR00956 219 SIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANilDTTPLVAIYQCS--QDAyelfDKVIVLYEGYQIYFG 293
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
21-278 |
2.86e-11 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 64.40 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 21 VFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFRIREDLYKKLQ 100
Cdd:cd18567 7 ILLLSLALELFALASPLYLQLVIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 101 SLDFDFFNNTRVGDIMARMtGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAIL------TM 174
Cdd:cd18567 87 RLPLSYFEKRHLGDIVSRF-GSLDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALIVLAAVALYALLrlalypPL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 175 KMSSKAQpvfyeIRESfSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLV 254
Cdd:cd18567 166 RRATEEQ-----IVAS-AKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAANGLLFGLEN 239
|
250 260
....*....|....*....|....
gi 1755737710 255 VITLIFGGYLVIKGQMTLGDLVAF 278
Cdd:cd18567 240 ILVIYLGALLVLDGEFTVGMLFAF 263
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
336-546 |
2.94e-11 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 62.65 E-value: 2.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 336 FKNVSFHFeDDPNTD--VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDP--TSGEILIDGVDARKwhvrELRNH 411
Cdd:cd03232 6 WKNLNYTV-PVKGGKrqLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPLDK----NFQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 412 IATVMQ-DIFLFSDTIEGNIAFGApdatmeDVRrmariadadhfietmpesydtivgergvGLSGGQKQRISLARALLKN 490
Cdd:cd03232 81 TGYVEQqDVHSPNLTVREALRFSA------LLR----------------------------GLSVEQRKRLTIGVELAAK 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1755737710 491 PSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIA-HRISSV--KEADEILILNHG 546
Cdd:cd03232 127 PSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTiHQPSASifEKFDRLLLLKRG 185
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
344-550 |
4.88e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 62.67 E-value: 4.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 344 EDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIAtvmqdiflfs 423
Cdd:COG2401 38 LRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASLIDAIG---------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 424 dtiegniAFGAPDATMEdVRRMARIADADHFIETMPEsydtivgergvgLSGGQKQRISLARALLKNPSILILDDTTSAV 503
Cdd:COG2401 108 -------RKGDFKDAVE-LLNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1755737710 504 DMETEVKIQGELKKIT-ENTTTFIIAHRISSVKEA---DEILILNHGEIIE 550
Cdd:COG2401 168 DRQTAKRVARNLQKLArRAGITLVVATHHYDVIDDlqpDLLIFVGYGGVPE 218
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
351-515 |
7.99e-11 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 61.74 E-value: 7.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGvdarkwhvrelrnhiatvmQDIFLFSDTIEGNI 430
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG-------------------GPLDFQRDSIARGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 431 AFGAPDATME---DVRRMARIADADHFIETMPESYDTiVGERGVG------LSGGQKQRISLARALLKNPSILILDDTTS 501
Cdd:cd03231 76 LYLGHAPGIKttlSVLENLRFWHADHSDEQVEEALAR-VGLNGFEdrpvaqLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170
....*....|....
gi 1755737710 502 AVDMETEVKIQGEL 515
Cdd:cd03231 155 ALDKAGVARFAEAM 168
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
334-563 |
9.46e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 62.50 E-value: 9.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLIC--RFYDPTSGEILIDGVDARKWHVRELRNh 411
Cdd:PRK09580 2 LSIKDLHVSVEDKA---ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPEDRAG- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 412 iatvmQDIFL-FSDTIE----GNIAFgaPDATMEDVRRMARIADADHF-----IE------TMPEsyDTIVGERGVGLSG 475
Cdd:PRK09580 78 -----EGIFMaFQYPVEipgvSNQFF--LQTALNAVRSYRGQEPLDRFdfqdlMEekiallKMPE--DLLTRSVNVGFSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 476 GQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIA---HRISSVKEADEILILNHGEIIERG 552
Cdd:PRK09580 149 GEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVthyQRILDYIKPDYVHVLYQGRIVKSG 228
|
250
....*....|...
gi 1755737710 553 THSSL--LAEKGY 563
Cdd:PRK09580 229 DFTLVkqLEEQGY 241
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
351-568 |
1.01e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 64.74 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDP---TSGEILIDGVDARKWHVRElrnhIATVMQ-DIFLFSDTI 426
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLDSSFQRS----IGYVQQqDLHLPTSTV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 427 EGNIAFGAPdatmedVRRMARIADA------DHFIETMP-ESY-DTIVGERGVGLSGGQKQRISLARALLKNPSILI-LD 497
Cdd:TIGR00956 854 RESLRFSAY------LRQPKSVSKSekmeyvEEVIKLLEmESYaDAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLD 927
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1755737710 498 DTTSAVDMETEVKIQGELKKITENTTTFIIA-HRISSV--KEADEILILNHG-EII---ERGTHSSLLAEkgyYFDIY 568
Cdd:TIGR00956 928 EPTSGLDSQTAWSICKLMRKLADHGQAILCTiHQPSAIlfEEFDRLLLLQKGgQTVyfgDLGENSHTIIN---YFEKH 1002
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
352-553 |
1.05e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 62.34 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFY--DPTSG---EILIDGVD-----ARKwhVRELRNHIATVMQDIFL 421
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGshiELLGRTVQregrlARD--IRKSRANTGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 422 FSD-TIEGNIAFGA---------------PDATMEDVRRMARIADAdHFIEtmpesydtivgERGVGLSGGQKQRISLAR 485
Cdd:PRK09984 98 VNRlSVLENVLIGAlgstpfwrtcfswftREQKQRALQALTRVGMV-HFAH-----------QRVSTLSGGQQQRVAIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1755737710 486 ALLKNPSILILDDTTSAVDMETEVKIQGELKKITEN--TTTFIIAHRIS-SVKEADEILILNHGEIIERGT 553
Cdd:PRK09984 166 ALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDyALRYCERIVALRQGHVFYDGS 236
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
351-504 |
1.24e-10 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 61.22 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRN-----HIATVMQDIflfsdT 425
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENilylgHLPGLKPEL-----S 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1755737710 426 IEGNIAFGAPDATMEDVRRMARIADADhfietMPESYDTIVGErgvgLSGGQKQRISLARALLKNPSILILDDTTSAVD 504
Cdd:TIGR01189 90 ALENLHFWAAIHGGAQRTIEDALAAVG-----LTGFEDLPAAQ----LSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
351-558 |
1.40e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.15 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 351 VLKNISLKASPGQTIAILGETGAGKSTLVNL----ICRFYDP----TSGEILIDG-----VDARKwhVRELRNHIATVMQ 417
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKAlagdLTGGGAPrgarVTGDVTLNGeplaaIDAPR--LARLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 418 DIFLFS-DTIEGNIAFGAPDATMEDVRRMARIADAdhfiETMPESYDTIVGERGVGLSGGQKQRISLARALLK------- 489
Cdd:PRK13547 94 PAFAFSaREIVLLGRYPHARRAGALTHRDGEIAWQ----ALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphda 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755737710 490 --NPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRIS-SVKEADEILILNHGEIIERGTHSSLL 558
Cdd:PRK13547 170 aqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNlAARHADRIAMLADGAIVAHGAPADVL 243
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
361-553 |
1.45e-10 |
|
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: 59.69 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 361 PGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIdgvdarkwhvrelrnhiatvmqdiflfsdtiegniafgapdatme 440
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--------------------------------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 441 dvrrmarIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQ-------G 513
Cdd:smart00382 36 -------IDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelrlL 108
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1755737710 514 ELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGT 553
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLLIL 148
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
77-300 |
1.73e-10 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 62.16 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 77 QIMCERIGQNSLFRIREDLYKKLQSLDFDFFNNTRVGDIMARMTGDTdAIRHFVSWVSYNILENVFLFSFAIIIMA-AID 155
Cdd:cd18583 58 SWLWIPVEQYSYRALSTAAFNHVMNLSMDFHDSKKSGEVLKAIEQGS-SINDLLEQILFQIVPMIIDLVIAIVYLYyLFD 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 156 WKLTLALVIVTPLIAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDS 235
Cdd:cd18583 137 PYMGLIVAVVMVLYVWSTIKLTSWRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKERYREAVKNYQKAERKY 216
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1755737710 236 advsRTYLPVLDSLAGMLVVITLIFG----GYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQ 300
Cdd:cd18583 217 ----LFSLNLLNAVQSLILTLGLLAGcflaAYQVSQGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQ 281
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
346-507 |
1.96e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.60 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 346 DPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGE-ILIDGV-----------DARKwHVRElrnHIA 413
Cdd:PRK11819 17 PPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEaRPAPGIkvgylpqepqlDPEK-TVRE---NVE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 414 TVMQDIF-LFSDTIEGNIAFGAPDATMEDV-RRMARI------ADA---DHFIE-TM-----PESyDTIVGErgvgLSGG 476
Cdd:PRK11819 93 EGVAEVKaALDRFNEIYAAYAEPDADFDALaAEQGELqeiidaADAwdlDSQLEiAMdalrcPPW-DAKVTK----LSGG 167
|
170 180 190
....*....|....*....|....*....|.
gi 1755737710 477 QKQRISLARALLKNPSILILDDTTSAVDMET 507
Cdd:PRK11819 168 ERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
337-549 |
2.87e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.82 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 337 KNVSFHFeddPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRE-LRNHIATV 415
Cdd:PRK10982 2 SNISKSF---PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 416 MQDIFLFSD-TIEGNIAFGA-PDATM-EDVRRMARIADA---DHFIETMPEsydtivgERGVGLSGGQKQRISLARALLK 489
Cdd:PRK10982 79 HQELNLVLQrSVMDNMWLGRyPTKGMfVDQDKMYRDTKAifdELDIDIDPR-------AKVATLSVSQMQMIEIAKAFSY 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1755737710 490 NPSILILDDTTSAVDmETEV----KIQGELKKitENTTTFIIAHRISSVKE-ADEILILNHGEII 549
Cdd:PRK10982 152 NAKIVIMDEPTSSLT-EKEVnhlfTIIRKLKE--RGCGIVYISHKMEEIFQlCDEITILRDGQWI 213
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
324-553 |
2.91e-10 |
|
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: 63.49 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 324 EKPAPSLQGHVEFKNVSFHFE--DDPNTDVLkNISLKASpgQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDAR 401
Cdd:TIGR01257 919 ERELPGLVPGVCVKNLVKIFEpsGRPAVDRL-NITFYEN--QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE 995
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 402 KwHVRELRNHIATVMQDIFLFSD-TIEGNIAFGAPdatmedvRRMARIADADHFIETMPEsyDTIV----GERGVGLSGG 476
Cdd:TIGR01257 996 T-NLDAVRQSLGMCPQHNILFHHlTVAEHILFYAQ-------LKGRSWEEAQLEMEAMLE--DTGLhhkrNEEAQDLSGG 1065
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1755737710 477 QKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVK-EADEILILNHGEIIERGT 553
Cdd:TIGR01257 1066 MQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGT 1143
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
352-550 |
3.44e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 62.50 E-value: 3.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYdPT---SGEILIDGVDARKWHVRELRNH-IATVMQDIFLFSD-TI 426
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEVCRFKDIRDSEALgIVIIHQELALIPYlSI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 427 EGNIAFGAPDATMEDVRRMARIADADHFIET--MPESYDTIVGERGVGlsggQKQRISLARALLKNPSILILDDTTSAV- 503
Cdd:NF040905 96 AENIFLGNERAKRGVIDWNETNRRARELLAKvgLDESPDTLVTDIGVG----KQQLVEIAKALSKDVKLLILDEPTAALn 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1755737710 504 --DMETEVKIQGELKKitENTTTFIIAHRISSVKE-ADEILILNHGEIIE 550
Cdd:NF040905 172 eeDSAALLDLLLELKA--QGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
356-531 |
4.03e-10 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 60.50 E-value: 4.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 356 SLKASPG-----QTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDarkwhvrelrnhIATVMQDIflfsdtiegni 430
Cdd:cd03237 14 TLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT------------VSYKPQYI----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 431 afgAPDATMEdVRRMARIADADHFI------ETM-PESYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAV 503
Cdd:cd03237 71 ---KADYEGT-VRDLLSSITKDFYThpyfktEIAkPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYL 146
|
170 180 190
....*....|....*....|....*....|
gi 1755737710 504 DMETEVKIQGELKKITENT--TTFIIAHRI 531
Cdd:cd03237 147 DVEQRLMASKVIRRFAENNekTAFVVEHDI 176
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
353-552 |
6.74e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 60.10 E-value: 6.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 353 KNISLKASPGQTIAILGETGAGKS----TLVNLICRFYDPTSGEILIDGVDArkwHVRELRN-HIATVMQDiflfsdtie 427
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPV---APCALRGrKIATIMQN--------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 428 gniafgaPDATMEDVRRMAriadaDHFIETM-----PESYDTIVGE-RGVGL--------------SGGQKQRISLARAL 487
Cdd:PRK10418 88 -------PRSAFNPLHTMH-----THARETClalgkPADDATLTAAlEAVGLenaarvlklypfemSGGMLQRMMIALAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1755737710 488 LKNPSILILDDTTSAVDMETEVKIQGELKKI--TENTTTFIIAHRISSV-KEADEILILNHGEIIERG 552
Cdd:PRK10418 156 LCEAPFIIADEPTTDLDVVAQARILDLLESIvqKRALGMLLVTHDMGVVaRLADDVAVMSHGRIVEQG 223
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
354-504 |
8.92e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 58.66 E-value: 8.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 354 NISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKwhVRE--LRN-----HIATVMQDIflfsdTI 426
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR--QRDeyHQDllylgHQPGIKTEL-----TA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 427 EGNIAFGAPDATMEDVRRMARIADAdhfietmpesydtiVGERGV------GLSGGQKQRISLARALLKNPSILILDDTT 500
Cdd:PRK13538 92 LENLRFYQRLHGPGDDEALWEALAQ--------------VGLAGFedvpvrQLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
....
gi 1755737710 501 SAVD 504
Cdd:PRK13538 158 TAID 161
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
352-570 |
1.36e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 60.67 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIaTVMQDIFLfsdtiEGNIA 431
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQL-TGIENIEL-----KGLMM 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 432 FGAPDATMEDVRRMARIADADHFIETMPESYdtivgergvglSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKI 511
Cdd:PRK13545 114 GLTKEKIKEIIPEIIEFADIGKFIYQPVKTY-----------SSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKC 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1755737710 512 QGELKKITEN-TTTFIIAHRISSVKE-ADEILILNHGEIIERGTHSSLLAEKGYYFDIYNK 570
Cdd:PRK13545 183 LDKMNEFKEQgKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDHYDEFLKKYNQ 243
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
337-553 |
1.42e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 59.76 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 337 KNVSFHFEDD--PNTDVlKNISLKASPGQTIAILGETGAGKS----TLVNLIcRFYDPTSGEIL-IDGVDARKWHVRELR 409
Cdd:PRK11022 7 DKLSVHFGDEsaPFRAV-DRISYSVKQGEVVGIVGESGSGKSvsslAIMGLI-DYPGRVMAEKLeFNGQDLQRISEKERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 410 NHIATVMQDIFlfSDTIEG-NIAFGAPDATMEDVR------RMARIADADHFIETM----PESYDTIVGERgvgLSGGQK 478
Cdd:PRK11022 85 NLVGAEVAMIF--QDPMTSlNPCYTVGFQIMEAIKvhqggnKKTRRQRAIDLLNQVgipdPASRLDVYPHQ---LSGGMS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 479 QRISLARALLKNPSILILDDTTSAVDmeteVKIQG-------ELKKiTENTTTFIIAHRISSVKE-ADEILILNHGEIIE 550
Cdd:PRK11022 160 QRVMIAMAIACRPKLLIADEPTTALD----VTIQAqiielllELQQ-KENMALVLITHDLALVAEaAHKIIVMYAGQVVE 234
|
...
gi 1755737710 551 RGT 553
Cdd:PRK11022 235 TGK 237
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
102-312 |
2.55e-09 |
|
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they 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: 350013 [Multi-domain] Cd Length: 294 Bit Score: 58.64 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 102 LDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILeNVFLFSFAIIIMAAIDWKLTLALVIVTpLIAILTMKMSSKAQ 181
Cdd:cd18569 88 LPVEFFSQRYAGDIASRVQSNDRVANLLSGQLATTVL-NLVMAVFYALLMLQYDVPLTLIGIAIA-LLNLLVLRLVSRKR 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 182 pvfyeiRESFSRLnsMVEEN------ISGNRV---VKAFAREDFemkkFHEHNEDFKKRNLDS---ADVSRTYL----PV 245
Cdd:cd18569 166 ------VDLNRRL--LQDSGkltgttMSGLQMietLKASGAESD----FFSRWAGYQAKVLNAqqeLGRTNQLLgalpTL 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1755737710 246 LDSLAGMLVvitLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPmrmsgwlindVQRFIASSFKIQDM 312
Cdd:cd18569 234 LSALTNAAI---LGLGGLLVMDGALTIGMLVAFQSLMASFLAP----------VNSLVGLGGTLQEM 287
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
338-553 |
2.84e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 58.97 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 338 NVSFHFEDDPNTDVLK-NISLKAspGQTIAILGETGAGKS----TLVNLICRfYDPTSGEILIDG---VDARKWHVRELR 409
Cdd:PRK09473 19 RVTFSTPDGDVTAVNDlNFSLRA--GETLGIVGESGSGKSqtafALMGLLAA-NGRIGGSATFNGreiLNLPEKELNKLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 410 -NHIATVMQDiflfsDTIEGNIAFGAPDATMEDVRRMARIADADHFIET--------MPESYDTIvGERGVGLSGGQKQR 480
Cdd:PRK09473 96 aEQISMIFQD-----PMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESvrmldavkMPEARKRM-KMYPHEFSGGMRQR 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1755737710 481 ISLARALLKNPSILILDDTTSAVDMETEVKIQ---GELKKiTENTTTFIIAHRISSVKE-ADEILILNHGEIIERGT 553
Cdd:PRK09473 170 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMtllNELKR-EFNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGN 245
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
90-276 |
2.88e-09 |
|
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: 58.83 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 90 RIREDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLI 169
Cdd:cd18558 93 KIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGWKLTLVILAISPVL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 170 AI---LTMKMSSKAQPvfyEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVL 246
Cdd:cd18558 173 GLsavVWAKILSGFTD---KEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKAITFNISMGAA 249
|
170 180 190
....*....|....*....|....*....|
gi 1755737710 247 DSLAGMLVVITLIFGGYLVIKGQMTLGDLV 276
Cdd:cd18558 250 FLLIYASYALAFWYGTYLVTQQEYSIGEVL 279
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
67-271 |
3.04e-09 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350029 [Multi-domain] Cd Length: 290 Bit Score: 58.26 E-value: 3.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 67 IIRTICRYTyqimcER-IGQNSLFRIREDL----YKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENV 141
Cdd:cd18585 46 ITRTAGRYG-----ERlVSHDATFRLLSNLrvwfYRKLEPLAPARLQKYRSGDLLNRIVADIDTLDNLYLRVLSPPVVAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 142 FLFSFAIIIMAAIDWKLTLALV-------IVTPLIAILTMKMSSKaqpvfyEIRESFSRLNSMVEENISGNRVVKAFARE 214
Cdd:cd18585 121 LVILATILFLAFFSPALALILLaglllagVVIPLLFYRLGKKIGQ------QLVQLRAELRTELVDGLQGMAELLIFGAL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1755737710 215 DFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVVITLIFGGYLVIKGQMT 271
Cdd:cd18585 195 ERQRQQLEQLSDALIKEQRRLARLSGLSQALMILLSGLTVWLVLWLGAPLVQNGALD 251
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
334-563 |
3.43e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.52 E-value: 3.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEIlidgvdarKWhvRELRN--- 410
Cdd:PRK15064 320 LEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--------KW--SENANigy 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 411 ----HIATVMQDIFLF---------SD------TIEGNIAFGApdatmEDVRRMARIadadhfietmpesydtivgergv 471
Cdd:PRK15064 387 yaqdHAYDFENDLTLFdwmsqwrqeGDdeqavrGTLGRLLFSQ-----DDIKKSVKV----------------------- 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 472 gLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKItENTTTFIIAHR--ISSVkeADEILILNHGEII 549
Cdd:PRK15064 439 -LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKY-EGTLIFVSHDRefVSSL--ATRIIEITPDGVV 514
|
250
....*....|....*
gi 1755737710 550 E-RGTHSSLLAEKGY 563
Cdd:PRK15064 515 DfSGTYEEYLRSQGI 529
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
335-507 |
3.88e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.58 E-value: 3.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 335 EFKNVSFHFEDDpntDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEI--------------------- 393
Cdd:PRK11147 321 EMENVNYQIDGK---QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhcgtklevayfdqhraeldpe 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 394 ------LIDG-----VDARKwhvrelrNHIATVMQDiFLFSdtiegniafgaPDATMEDVRrmariadadhfietmpesy 462
Cdd:PRK11147 398 ktvmdnLAEGkqevmVNGRP-------RHVLGYLQD-FLFH-----------PKRAMTPVK------------------- 439
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1755737710 463 dtivgergvGLSGGQKQRISLARALLKNPSILILDDTTSAVDMET 507
Cdd:PRK11147 440 ---------ALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET 475
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
347-535 |
1.54e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 57.45 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 347 PNTDVLKN-ISLKASPGQTIAILGETGAGKSTLVNLICRFYdPTSGEILIDGVDARKWHV--------RELRNHIatvmq 417
Cdd:TIGR00954 462 PNGDVLIEsLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGRLTKPAKGKLFYVpqrpymtlGTLRDQI----- 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 418 difLFSDTIEGNIAFGAPDAtmeDVRRMARIADADHFIEtmpesydtivgeRGVG----------LSGGQKQRISLARAL 487
Cdd:TIGR00954 536 ---IYPDSSEDMKRRGLSDK---DLEQILDNVQLTHILE------------REGGwsavqdwmdvLSGGEKQRIAMARLF 597
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1755737710 488 LKNPSILILDDTTSAVDMETEVKIQGELKKIteNTTTFIIAHRISSVK 535
Cdd:TIGR00954 598 YHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKSLWK 643
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
353-548 |
1.88e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.98 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 353 KNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRE-LRNHIATVMQD-----IFL----- 421
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPEDrqssgLYLdapla 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 422 --FSDTIEGNIAF----GAPDATMEDVRRMARI--ADADHFIETmpesydtivgergvgLSGGQKQRISLARALLKNPSI 493
Cdd:PRK15439 360 wnVCALTHNRRGFwikpARENAVLERYRRALNIkfNHAEQAART---------------LSGGNQQKVLIAKCLEASPQL 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 494 LILDDTTSAVDMETEVKIQGELKKITENTTTFIIahrISS-----VKEADEILILNHGEI 548
Cdd:PRK15439 425 LIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLF---ISSdleeiEQMADRVLVMHQGEI 481
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
335-504 |
3.49e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.09 E-value: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 335 EFKNVSFHFEDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYD-PTSGEILIDGVDARKWHVRE-LRNHI 412
Cdd:PRK13549 261 EVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQaIAQGI 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 413 ATVMQD-----IFLFSDTIEgNIAFgapdATMEDVRRMARIADA------DHFIETMpeSYDTIVGERGVG-LSGGQKQR 480
Cdd:PRK13549 341 AMVPEDrkrdgIVPVMGVGK-NITL----AALDRFTGGSRIDDAaelktiLESIQRL--KVKTASPELAIArLSGGNQQK 413
|
170 180
....*....|....*....|....
gi 1755737710 481 ISLARALLKNPSILILDDTTSAVD 504
Cdd:PRK13549 414 AVLAKCLLLNPKILILDEPTRGID 437
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
354-552 |
6.24e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 54.16 E-value: 6.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 354 NISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVREL----RNHIAT-----VMQ---DIFL 421
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaeRRRLLRtewgfVHQhprDGLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 422 FSDTIEGNIA----------FGAPDATMED-VRRM----ARIADAdhfietmPESYdtivgergvglSGGQKQRISLARA 486
Cdd:PRK11701 104 MQVSAGGNIGerlmavgarhYGDIRATAGDwLERVeidaARIDDL-------PTTF-----------SGGMQQRLQIARN 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1755737710 487 LLKNPSILILDDTTSAVDmeteVKIQGELKKITENTTT------FIIAHRISSVK-EADEILILNHGEIIERG 552
Cdd:PRK11701 166 LVTHPRLVFMDEPTGGLD----VSVQARLLDLLRGLVRelglavVIVTHDLAVARlLAHRLLVMKQGRVVESG 234
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
326-507 |
6.90e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 55.33 E-value: 6.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 326 PAPSLQGHV-EFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILI-DGVdarkw 403
Cdd:TIGR03719 314 PGPRLGDKViEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETV----- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 404 hvrelrnHIATVMQdiflFSDTIEGN------IAFGAPDATMEDVRRMARiadadhfietmpeSYDTIVGERG------V 471
Cdd:TIGR03719 386 -------KLAYVDQ----SRDALDPNktvweeISGGLDIIKLGKREIPSR-------------AYVGRFNFKGsdqqkkV 441
|
170 180 190
....*....|....*....|....*....|....*..
gi 1755737710 472 G-LSGGQKQRISLARALLKNPSILILDDTTSAVDMET 507
Cdd:TIGR03719 442 GqLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVET 478
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
338-538 |
9.30e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 52.64 E-value: 9.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 338 NVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKwhvrelrnHIATVMQ 417
Cdd:PRK13540 6 ELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK--------DLCTYQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 418 DIFLFSD--------TIEGNIAFGA-PDATMEDVRRMARIADADHFIetmpesyDTIVGErgvgLSGGQKQRISLARALL 488
Cdd:PRK13540 75 QLCFVGHrsginpylTLRENCLYDIhFSPGAVGITELCRLFSLEHLI-------DYPCGL----LSSGQKRQVALLRLWM 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1755737710 489 KNPSILILDDTTSAVDmetEVKIQGELKKITENT----TTFIIAHRISSVKEAD 538
Cdd:PRK13540 144 SKAKLWLLDEPLVALD---ELSLLTIITKIQEHRakggAVLLTSHQDLPLNKAD 194
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
368-504 |
1.50e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 54.36 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 368 LGETGAGKST----LVNLIcrfyDPTSGEILIDG--VDARKWHVR--------------ELrnhiaTVMQDIFLFsdtie 427
Cdd:NF033858 298 LGSNGCGKSTtmkmLTGLL----PASEGEAWLFGqpVDAGDIATRrrvgymsqafslygEL-----TVRQNLELH----- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 428 gniA--FGAPDATMED-VRRMARIADADHFIETMPESydtivgergvgLSGGQKQRISLARALLKNPSILILDDTTSAVD 504
Cdd:NF033858 364 ---ArlFHLPAAEIAArVAEMLERFDLADVADALPDS-----------LPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
352-504 |
1.52e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 54.24 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRE-LRNHIATVMQDI----FLFSDTI 426
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANGIVYISEDRkrdgLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 427 EGNIAFGAPDA---TMEDVRRMARIADADHFIETM----PeSYDTIVGErgvgLSGGQKQRISLARALLKNPSILILDDT 499
Cdd:PRK10762 348 KENMSLTALRYfsrAGGSLKHADEQQAVSDFIRLFniktP-SMEQAIGL----LSGGNQQKVAIARGLMTRPKVLILDEP 422
|
....*
gi 1755737710 500 TSAVD 504
Cdd:PRK10762 423 TRGVD 427
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
355-560 |
1.58e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 52.63 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 355 ISLKASPGQTIAILGETGAGKSTLVNLICRFYdPTSGEILIDGVDARKWHVRELRNHIATVMQ--------DIFLFSDTI 426
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQqqtppfamPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 427 EG-NIAFGAPDATMEDVRRMARIADADHfietmpesydtivgeRGVG-LSGGQKQRISLARALLK-----NPS--ILILD 497
Cdd:PRK03695 94 QPdKTRTEAVASALNEVAEALGLDDKLG---------------RSVNqLSGGEWQRVRLAAVVLQvwpdiNPAgqLLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1755737710 498 DTTSAVDMETEVKIQGELKKITENTTTFIIA-HRIS-SVKEADEILILNHGEIIERGTHSSLLAE 560
Cdd:PRK03695 159 EPMNSLDVAQQAALDRLLSELCQQGIAVVMSsHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTP 223
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
320-506 |
1.67e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.16 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 320 PIHAEKPApsLQGHvefkNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVD 399
Cdd:PRK13543 4 PLHTAPPL--LAAH----ALAFSRNEEP---VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 400 A----RKWHVRELrNHIATVMQDIflfsdtiegniafgapdATMEDVrrmariadadHFI--------ETMPESYDTIVG 467
Cdd:PRK13543 75 AtrgdRSRFMAYL-GHLPGLKADL-----------------STLENL----------HFLcglhgrraKQMPGSALAIVG 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1755737710 468 ERGVG------LSGGQKQRISLARALLKNPSILILDDTTSAVDME 506
Cdd:PRK13543 127 LAGYEdtlvrqLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
335-548 |
1.68e-07 |
|
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: 54.06 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 335 EFKNVSFHFEDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPT-SGEILIDG--VDARKwHVRELRNH 411
Cdd:TIGR02633 259 EARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpVDIRN-PAQAIRAG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 412 IATVMQDIF---LFSDTIEG-NIAFGAPDA-----TMEDVRRMARIADADHFIETMPESYDTIVGergvGLSGGQKQRIS 482
Cdd:TIGR02633 338 IAMVPEDRKrhgIVPILGVGkNITLSVLKSfcfkmRIDAAAELQIIGSAIQRLKVKTASPFLPIG----RLSGGNQQKAV 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1755737710 483 LARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIahrISS-----VKEADEILILNHGEI 548
Cdd:TIGR02633 414 LAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIV---VSSelaevLGLSDRVLVIGEGKL 481
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
334-504 |
2.76e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.59 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 334 VEFKNVSFHFEDdpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVD-ARKWHVRELRNHI 412
Cdd:NF033858 2 ARLEGVSHRYGK---TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDmADARHRRAVCPRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 413 ATVMQDI--FLFSD-TIEGNIAF-----GAPDAtmEDVRRMARIADA---DHFietmpesydtivGERGVG-LSGGQKQR 480
Cdd:NF033858 79 AYMPQGLgkNLYPTlSVFENLDFfgrlfGQDAA--ERRRRIDELLRAtglAPF------------ADRPAGkLSGGMKQK 144
|
170 180
....*....|....*....|....
gi 1755737710 481 ISLARALLKNPSILILDDTTSAVD 504
Cdd:NF033858 145 LGLCCALIHDPDLLILDEPTTGVD 168
|
|
| ABC_6TM_NdvA_beta-glucan_exporter_like |
cd18562 |
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar ... |
143-285 |
3.77e-07 |
|
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: 51.86 E-value: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 143 LFSFAIIIMAA--IDWKLTL---ALVIVTPLIAILTMKMSSKAQPvfyEIRESFSRLNSMVEENISGNRVVKAFAREDFE 217
Cdd:cd18562 121 LVSLIVLLPVAlwMNWRLALllvVLAAVYAALNRLVMRRTKAGQA---AVEEHHSALSGRVGDVIGNVTVVQSYTRLAAE 197
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1755737710 218 MKKFHehneDFKKRNLDSAdvsrtyLPVLDSLAGMLVV--------ITLIF--GGYLVIKGQMTLGDLVAFNGFLWML 285
Cdd:cd18562 198 TSALR----GITRRLLAAQ------YPVLNWWALASVLtraastltMVAIFalGAWLVQRGELTVGEIVSFVGFATLL 265
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
16-299 |
4.82e-07 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain 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.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 51.83 E-value: 4.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 16 LLMIGVFILIFIASGISIIYPLLGgkVIDDVvyQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFRIREDL 95
Cdd:cd18559 2 FLLIKLVLCNHVFSGPSNLWLLLW--FDDPV--NGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 96 YKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSynileNVFLFSFAIIIMAAIDW-KLTLALVIVTPLIAIL-- 172
Cdd:cd18559 78 YHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVI-----KMWMGPLQNVIGLYLLIlLAGPMAAVGIPLGLLYvp 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 173 ---TMKMSSKAqpvfYEIRESFSRLN--SMVEENISGNRVVKAFAREdfemkkfhehnEDFKKRNLDSADVSRTYLPVLD 247
Cdd:cd18559 153 vnrVYAASSRQ----LKRLESVSKDPryKLFNETLLGISVIKAFEWE-----------EAFIRQVDAKRDNELAYLPSIV 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1755737710 248 SL---------AGMLVVITLIFGGYLVIKGQMTLGDLVAFNGF--LWMLNGPMRMSGWLINDV 299
Cdd:cd18559 218 YLralavrlwcVGPCIVLFASFFAYVSRHSLAGLVALKVFYSLalTTYLNWPLNMSPEVITNI 280
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
354-529 |
5.80e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.20 E-value: 5.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 354 NISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGvdarkwHVRelrnhIATVMQDIFLFS-----DTI-- 426
Cdd:PRK15064 19 NISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDP------NER-----LGKLRQDQFAFEeftvlDTVim 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 427 ----------EGNIAFGAPDATMEDVRRMA----RIADADHFietMPESYdtiVGE--RGVGL------------SGGQK 478
Cdd:PRK15064 88 ghtelwevkqERDRIYALPEMSEEDGMKVAdlevKFAEMDGY---TAEAR---AGEllLGVGIpeeqhyglmsevAPGWK 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1755737710 479 QRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKitENTTTFIIAH 529
Cdd:PRK15064 162 LRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNE--RNSTMIIISH 210
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
351-506 |
6.78e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.09 E-value: 6.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEI-LIDGVDARKWHVRELRnhiatvmqdiFLFSDTiegn 429
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQLE----------FLRADE---- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 430 iafgAPdatmedVRRMARIADAdhfiETMPESYDTI---------VGERGVGLSGGQKQRISLARALLKNPSILILDDTT 500
Cdd:PRK10636 393 ----SP------LQHLARLAPQ----ELEQKLRDYLggfgfqgdkVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPT 458
|
....*.
gi 1755737710 501 SAVDME 506
Cdd:PRK10636 459 NHLDLD 464
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
352-553 |
7.30e-07 |
|
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: 50.69 E-value: 7.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 352 LKNISLKASPGQTIAILGETGAGKSTLVN------LICRFY----DPTSGEIlIDGVDARKWHV--------RELRNHIA 413
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdtlypaLARRLHlkkeQPGNHDR-IEGLEHIDKVIvidqspigRTPRSNPA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 414 T---VMQDIF-LFSDTIEG---------------NIAfgapdatmeDVRRMArIADADHFIETMPESYDTI--------- 465
Cdd:cd03271 90 TytgVFDEIReLFCEVCKGkrynretlevrykgkSIA---------DVLDMT-VEEALEFFENIPKIARKLqtlcdvglg 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 466 ---VGERGVGLSGGQKQRISLARALLK---NPSILILDDTTSAVDMETEVKIQGELKKITEN-TTTFIIAHRISSVKEAD 538
Cdd:cd03271 160 yikLGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKgNTVVVIEHNLDVIKCAD 239
|
250 260
....*....|....*....|.
gi 1755737710 539 EILIL------NHGEIIERGT 553
Cdd:cd03271 240 WIIDLgpeggdGGGQVVASGT 260
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
355-559 |
8.78e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 50.96 E-value: 8.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 355 ISLKASPGQTIAILGETGAGKSTLVNLICRF----YDPTSGEILIDGVDARKWHVRELRNHIATVMQDIFLF-------S 423
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRLSPRERRKLVGHNVSMIFQEpqscldpS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 424 DTIEGNIAFGAPDATMED---------VRR----MARIADADHfietmpesyDTIVGERGVGLSGGQKQRISLARALLKN 490
Cdd:PRK15093 106 ERVGRQLMQNIPGWTYKGrwwqrfgwrKRRaielLHRVGIKDH---------KDAMRSFPYELTEGECQKVMIAIALANQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1755737710 491 PSILILDDTTSAVDMETEVKIQGELKKITEN--TTTFIIAHRISSV-KEADEILILNHGEIIERGTHSSLLA 559
Cdd:PRK15093 177 PRLLIADEPTNAMEPTTQAQIFRLLTRLNQNnnTTILLISHDLQMLsQWADKINVLYCGQTVETAPSKELVT 248
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
314-498 |
1.03e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.55 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 314 ATDAKIPIHAEKPA----PSLQGHVEFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLIC----RF 385
Cdd:PRK10938 237 LEGVQLPEPDEPSArhalPANEPRIVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpQG 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 386 Y--DPT-------SGEILidgvdarkWhvrELRNHIATVMQDIFL---------------FSDTIegNIAFGAPDA---- 437
Cdd:PRK10938 314 YsnDLTlfgrrrgSGETI--------W---DIKKHIGYVSSSLHLdyrvstsvrnvilsgFFDSI--GIYQAVSDRqqkl 380
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1755737710 438 TMEDVRRM---ARIADAD-HfietmpesydtivgergvGLSGGQkQRISL-ARALLKNPSILILDD 498
Cdd:PRK10938 381 AQQWLDILgidKRTADAPfH------------------SLSWGQ-QRLALiVRALVKHPTLLILDE 427
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
335-504 |
1.24e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 51.33 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 335 EFKNVSFHFEDDPNTDVLKNISLKASPGQTIAILGETGAGKSTL-VNLICRFYDP-TSGEILIDGVDARKWHVRE-LRNH 411
Cdd:NF040905 259 EVKNWTVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYGRnISGTVFKDGKEVDVSTVSDaIDAG 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 412 IATVMQDI----FLFSDTIEGNIafgapdaTMEDVRRMARIADADHFIET-MPESYDT---I----VGERGVGLSGGQKQ 479
Cdd:NF040905 339 LAYVTEDRkgygLNLIDDIKRNI-------TLANLGKVSRRGVIDENEEIkVAEEYRKkmnIktpsVFQKVGNLSGGNQQ 411
|
170 180
....*....|....*....|....*
gi 1755737710 480 RISLARALLKNPSILILDDTTSAVD 504
Cdd:NF040905 412 KVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
352-531 |
1.55e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.96 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 352 LKNISLKASPGQ-----TIAILGETGAGKSTLVNLICRFYDPTSGEILIDgvdarkwhVRelrnhIATVMQDIFlfsdti 426
Cdd:PRK13409 350 LGDFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE--------LK-----ISYKPQYIK------ 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 427 egniafGAPDATMEDVRRMARIADADHFIET-------MPESYDTIVGErgvgLSGGQKQRISLARALLKNPSILILDDT 499
Cdd:PRK13409 411 ------PDYDGTVEDLLRSITDDLGSSYYKSeiikplqLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEP 480
|
170 180 190
....*....|....*....|....*....|....
gi 1755737710 500 TSAVDMETEVKIQGELKKITENT--TTFIIAHRI 531
Cdd:PRK13409 481 SAHLDVEQRLAVAKAIRRIAEEReaTALVVDHDI 514
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
473-546 |
1.73e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.47 E-value: 1.73e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1755737710 473 LSGGQKQRISLARALLKNP--SILILDDTTSAVDMETEVKIQGELKK-ITENTTTFIIAHRISSVKEADEILILNHG 546
Cdd:cd03238 88 LSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKGlIDLGNTVILIEHNLDVLSSADWIIDFGPG 164
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
67-276 |
1.75e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 49.97 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 67 IIRTICRYTYQIMCERIGQNSLFRIREDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVsyniLENVFL-FS 145
Cdd:cd18561 47 VLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRY----LPQLLVaLL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 146 FAIII---MAAIDWKLTLALVIVTPLIAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFH 222
Cdd:cd18561 123 GPLLIliyLFFLDPLVALILLVFALLIPLSPALWDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELA 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1755737710 223 EHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVVITLIFGGYLVIKGQMTLGDLV 276
Cdd:cd18561 203 ARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALGVGALRVLGGQLTLSSLL 256
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
441-562 |
1.77e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.50 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 441 DVRRMARIADADHFIETMpeSYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITE 520
Cdd:NF000106 115 DLSRKDARARADELLERF--SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVR 192
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1755737710 521 NTTTFIIAHRISSVKE--ADEILILNHGEIIERGTHSSLLAEKG 562
Cdd:NF000106 193 DGATVLLTTQYMEEAEqlAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| ABC_6TM_ABCB6 |
cd18581 |
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, ... |
82-293 |
2.14e-06 |
|
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, mitochondrial; This group represents the ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, ABCB6 (ABC transporter subfamily B, member 6) is closely related to yeast ATM1 and human ABCB7, which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350025 [Multi-domain] Cd Length: 300 Bit Score: 49.55 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 82 RIGQNSLFRIREDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAidwkltlA 161
Cdd:cd18581 72 PVQQFTTREISVKLFAHLHSLSLRWHLSRKTGEVLRVMDRGTSSINSLLSYVLFNIGPTIADIIIAIIYFAI-------A 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 162 LVIVTPLIAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRV--------VKAFAREDFEMKKFHEHNEDFKKrnl 233
Cdd:cd18581 145 FNPWFGLIVFVTMALYLILTIIITEWRTKFRREMNKLDNEKRAKAVdsllnfetVKYYNAERFEVERYRRAIDDYQV--- 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1755737710 234 dsAD-VSRTYLPVLDSLAGMLVVITLIFG----GYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSG 293
Cdd:cd18581 222 --AEwKSNASLNLLNTAQNLIITIGLLAGsllcAYFVVEGKLTVGDFVLFLTYIIQLYAPLNFFG 284
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
319-507 |
2.24e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.50 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 319 IPihaekPAPSLQGHV-EFKNVSFHFEDDpntdVL-KNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILI- 395
Cdd:PRK11819 314 IP-----PGPRLGDKViEAENLSKSFGDR----LLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIg 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 396 DGVdarkwhvrelrnHIATVMQdiflFSDTIEgniafgaPDATMEDVrrmarIADADHFIE----TMP-ESYDTIVGERG 470
Cdd:PRK11819 385 ETV------------KLAYVDQ----SRDALD-------PNKTVWEE-----ISGGLDIIKvgnrEIPsRAYVGRFNFKG 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1755737710 471 ------VG-LSGGQKQRISLARALLKNPSILILDDTTSAVDMET 507
Cdd:PRK11819 437 gdqqkkVGvLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVET 480
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
320-513 |
2.57e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.63 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 320 PIHAEKPAPSLqghVEFKNVSFHFEDDPNtdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILidgvd 399
Cdd:PLN03073 498 PTPDDRPGPPI---ISFSDASFGYPGGPL--LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF----- 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 400 aRKWHVRelrnhiatvmqdIFLFSDT-IEGniafgaPDATMEDVRRMARIadadhFIETMPESYDTIVGERGVG------ 472
Cdd:PLN03073 568 -RSAKVR------------MAVFSQHhVDG------LDLSSNPLLYMMRC-----FPGVPEQKLRAHLGSFGVTgnlalq 623
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1755737710 473 ----LSGGQKQRISLARALLKNPSILILDDTTSAVDME-TEVKIQG 513
Cdd:PLN03073 624 pmytLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDaVEALIQG 669
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
338-507 |
7.81e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.79 E-value: 7.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 338 NVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLIcrfydptSGEILIDgvDARKWHVRELRnhIATVMQ 417
Cdd:PRK11147 8 GAWLSFSDAP---LLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLD--DGRIIYEQDLI--VARLQQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 418 DIflfSDTIEGN----IAFG------------------APDATMEDVRRMARI-ADADH------------FIETMPESY 462
Cdd:PRK11147 74 DP---PRNVEGTvydfVAEGieeqaeylkryhdishlvETDPSEKNLNELAKLqEQLDHhnlwqlenrineVLAQLGLDP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1755737710 463 DTIVGErgvgLSGGQKQRISLARALLKNPSILILDDTTSAVDMET 507
Cdd:PRK11147 151 DAALSS----LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
106-301 |
9.06e-06 |
|
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: 47.88 E-value: 9.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 106 FFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTMkmsskaqpvFY 185
Cdd:cd18580 89 FFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQR---------YY 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 186 -----EIR----ESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHnedfkkrnLDSAdvSRTYLP----------VL 246
Cdd:cd18580 160 lrtsrQLRrlesESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRL--------LDAS--QRAFYLllavqrwlglRL 229
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1755737710 247 DSLAGMLVVITLIFGgyLVIKGQMTLGDL-VAFN---GFLWMLNGPMRMSGWLIND---VQR 301
Cdd:cd18580 230 DLLGALLALVVALLA--VLLRSSISAGLVgLALTyalSLTGSLQWLVRQWTELETSmvsVER 289
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
351-504 |
9.24e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 48.69 E-value: 9.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLIC--RFYDPTSGEILIDGVDARKWHVRELRNHIAtvMQDIFLFSDTIEG 428
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAgrKTGGYIEGDIRISGFPKKQETFARISGYCE--QNDIHSPQVTVRE 972
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1755737710 429 NIAFGAPDATMEDVRRMARIADADHFIE--TMPESYDTIVGERGV-GLSGGQKQRISLARALLKNPSILILDDTTSAVD 504
Cdd:PLN03140 973 SLIYSAFLRLPKEVSKEEKMMFVDEVMElvELDNLKDAIVGLPGVtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
90-294 |
1.30e-05 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). 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. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 47.21 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 90 RIREDLYKKLQSLDFdffnNTRVGDIMARMTGDTDAIRHFVSWVSyniLENVFLFSFAIIIMAAI----DWKLTLALVIV 165
Cdd:cd18586 76 ELGRRVFRAVLELPL----ESRPSGYWQQLLRDLDTLRNFLTGPS---LFAFFDLPWAPLFLAVIflihPPLGWVALVGA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 166 TPLIAILTMKMSSKAQPVFYEIRESFSRlNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPV 245
Cdd:cd18586 149 PVLVGLAWLNHRATRKPLGEANEAQAAR-DALAAETLRNAETIKALGMLGNLRRRWEARHAETLELQIRASDLAGAISAI 227
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1755737710 246 LDSLAGMLVVITLIFGGYLVIKGQMTLGDLVAFNgflwMLNG----PMR--MSGW 294
Cdd:cd18586 228 GKTLRMALQSLILGVGAYLVIDGELTIGALIAAS----ILSGralaPIDqlVGAW 278
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
471-547 |
2.17e-05 |
|
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: 45.26 E-value: 2.17e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1755737710 471 VGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENT--TTFIIAHRISSVKEADEILILNHGE 547
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGkkTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
351-559 |
2.25e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.53 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPT---SGEILIDGVDARKWHVRELRNHIAtvMQDIFLFSDTIE 427
Cdd:PLN03140 180 ILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFVPRKTSAYIS--QNDVHVGVMTVK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 428 GNIAFGAP--------DATMEDVRRM--ARI---ADADHFIE---------TMPESY-----------DTIVGERGV-GL 473
Cdd:PLN03140 258 ETLDFSARcqgvgtryDLLSELARREkdAGIfpeAEVDLFMKatamegvksSLITDYtlkilgldickDTIVGDEMIrGI 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 474 SGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEA----DEILILNHGEII 549
Cdd:PLN03140 338 SGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQPAPETfdlfDDIILLSEGQIV 417
|
250
....*....|
gi 1755737710 550 ERGTHSSLLA 559
Cdd:PLN03140 418 YQGPRDHILE 427
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
352-531 |
2.44e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 47.09 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 352 LKNISLKASPGQ-----TIAILGETGAGKSTLVNLICRFYDPTSGEI------------LIDGVDARkwhVRE-LRNHIA 413
Cdd:COG1245 351 YGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEVdedlkisykpqyISPDYDGT---VEEfLRSANT 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 414 TVMQDIFLFSdtiegniafgapdatmEDVRRMAriadadhfIETMpesYDTIVGErgvgLSGGQKQRISLARALLKNPSI 493
Cdd:COG1245 428 DDFGSSYYKT----------------EIIKPLG--------LEKL---LDKNVKD----LSGGELQRVAIAACLSRDADL 476
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1755737710 494 LILDDTTSAVDMETEVKIQGELKKITENT--TTFIIAHRI 531
Cdd:COG1245 477 YLLDEPSAHLDVEQRLAVAKAIRRFAENRgkTAMVVDHDI 516
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
352-536 |
4.71e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.19 E-value: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGvDARKWHVRELRNHIATVMQdiflfsdtiegNIA 431
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-EVSVIAISAGLSGQLTGIE-----------NIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 432 FG------APDATMEDVRRMARIADADHFIETMPESYdtivgergvglSGGQKQRISLARALLKNPSILILDDTTSAVDm 505
Cdd:PRK13546 108 FKmlcmgfKRKEIKAMTPKIIEFSELGEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSVGD- 175
|
170 180 190
....*....|....*....|....*....|....*
gi 1755737710 506 etEVKIQGELKKITE----NTTTFIIAHRISSVKE 536
Cdd:PRK13546 176 --QTFAQKCLDKIYEfkeqNKTIFFVSHNLGQVRQ 208
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
361-529 |
5.67e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.96 E-value: 5.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 361 PGQTIAILGETGAGKSTLVNLI--------CRFYDPTSGEILIDgvdarkwHVRelrnhiATVMQDifLFSDTIEGNIaf 432
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILsgelipnlGDYEEEPSWDEVLK-------RFR------GTELQN--YFKKLYNGEI-- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 433 gapdatmedvrrmaRIADADHFIETMPESYDTIVG-------ERGV-------------------GLSGGQKQRISLARA 486
Cdd:PRK13409 161 --------------KVVHKPQYVDLIPKVFKGKVRellkkvdERGKldevverlglenildrdisELSGGELQRVAIAAA 226
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1755737710 487 LLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAH 529
Cdd:PRK13409 227 LLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEH 269
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
473-553 |
6.89e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.77 E-value: 6.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 473 LSGGQKQRISLARALLK---NPSILILDDTTSAVDMETEVKIQGELKKITEN-TTTFIIAHRISSVKEADEILIL----- 543
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKgNTVVVIEHNLDVIKTADYIIDLgpegg 909
|
90
....*....|.
gi 1755737710 544 -NHGEIIERGT 553
Cdd:TIGR00630 910 dGGGTVVASGT 920
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
360-380 |
1.61e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 44.15 E-value: 1.61e-04
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
352-548 |
7.63e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.41 E-value: 7.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEIlidgvdarKWHVRELRNHIA-TVMQDIFLF------SD 424
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTI--------TLHGKKINNHNAnEAINHGFALvteerrST 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 425 TIEGN--IAFGAPDATME---------DVRRMAriADADHFIETM---PESYDTIVGErgvgLSGGQKQRISLARALLKN 490
Cdd:PRK10982 336 GIYAYldIGFNSLISNIRnyknkvgllDNSRMK--SDTQWVIDSMrvkTPGHRTQIGS----LSGGNQQKVIIGRWLLTQ 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1755737710 491 PSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIahrISS-----VKEADEILILNHGEI 548
Cdd:PRK10982 410 PEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIII---ISSempelLGITDRILVMSNGLV 469
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
471-543 |
2.83e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 38.88 E-value: 2.83e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1755737710 471 VGLSGGQKQRISLARAL----LKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIA-HRISSVKEADEILIL 543
Cdd:cd03227 76 LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVItHLPELAELADKLIHI 153
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
99-281 |
3.26e-03 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of 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: 350052 [Multi-domain] Cd Length: 294 Bit Score: 39.84 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 99 LQSLDFDFFNNTRVGDIMARMTGDTdAIR-----HFVSWVsyniLENVFLFSFAIIIMAAiDWKLTLaLVIVTPLIAILT 173
Cdd:cd18779 85 LLRLPYRFFQQRSTGDLLMRLSSNA-TIRelltsQTLSAL----LDGTLVLGYLALLFAQ-SPLLGL-VVLGLAALQVAL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 174 MKMSSKAQPVFYEiRE--SFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEH-----NEDFKKRNLDSadvsrtylpVL 246
Cdd:cd18779 158 LLATRRRVRELMA-RElaAQAEAQSYLVEALSGIETLKASGAEDRALDRWSNLfvdqlNASLRRGRLDA---------LV 227
|
170 180 190
....*....|....*....|....*....|....*....
gi 1755737710 247 DSLAGMLVVIT----LIFGGYLVIKGQMTLGDLVAFNGF 281
Cdd:cd18779 228 DALLATLRLAAplvlLWVGAWQVLDGQLSLGTMLALNAL 266
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
344-383 |
3.68e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 38.92 E-value: 3.68e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1755737710 344 EDDPNTDVLKNIsLKaspGQTIAILGETGAGKSTLVNLIC 383
Cdd:cd01854 71 KTGEGLDELREL-LK---GKTSVLVGQSGVGKSTLLNALL 106
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
473-543 |
3.75e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 3.75e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1755737710 473 LSGGQKQRISLARALL---KNPSILILDDTTSAVDM-ETEVKIQGELKKITENTTTFIIAHRISSVKEADEILIL 543
Cdd:PRK00635 810 LSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHThDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLEL 884
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
141-287 |
4.54e-03 |
|
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.
Pssm-ID: 350031 Cd Length: 293 Bit Score: 39.34 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 141 VFLFsfaIIIMAAIDWKLTLALVIVTPLIAILT------MKMSSKAQpvfyeIRESFSRlNSMVEENISGNRVVKAFARE 214
Cdd:cd18587 128 VLLF---LAVIALIGGPLALVPLVAIPLVLLYGlllqkpLRRLVEES-----MRESAQK-NALLVESLSGLETIKALGAE 198
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1755737710 215 DfemkKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLV----VITLIFGGYLVIKGQMTLGDLVAFNgflwMLNG 287
Cdd:cd18587 199 G----RMQRRWEEAVAALARSSLKSRLLSSSATNFAQFVQqlvtVAIVIVGVYLISDGELTMGGLIACV----ILSG 267
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| ABC_6TM_AarD_CydDC_like |
cd18781 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine ... |
7-230 |
7.92e-03 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; This subgroup belongs to the ABC_6TM_AarD_CydDC_like subgroup of the ABC_6TM exporter family. The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs). 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: 350054 [Multi-domain] Cd Length: 290 Bit Score: 38.67 E-value: 7.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 7 IWQYVRkyrlLMIGVFILIFIASGISIIYPllggkviddvvYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQN 86
Cdd:cd18781 3 LLQWIS----LLANIAFVFSIANLLQKLLE-----------GKLTTASLLIVLGILAIAIIVRFICTRLASRASYRASAD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755737710 87 SLFRIREDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAI----RHFVSWVSYNILENVFLFsfaiIIMAAIDWKLTLAL 162
Cdd:cd18781 68 VKKTLREKIYDKLLRLGPSYQEKVSTAEVVQLSVEGVEQLeiyfGRYLPQFFYSMLAPLTLF----VVLAPINWKAALVL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1755737710 163 VIVTPLIAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKK 230
Cdd:cd18781 144 LICVPLIPISIIAVQKIAKKLLSKYWGSYTDLGDSFLENLQGLTTLKIYQADERRHEEMNEEAEDFRK 211
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| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
474-505 |
8.10e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.07 E-value: 8.10e-03
10 20 30
....*....|....*....|....*....|..
gi 1755737710 474 SGGQKQRISLARALLKNPSILILDDTTSAVDM 505
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
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|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
364-384 |
8.55e-03 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 38.59 E-value: 8.55e-03
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