|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
20-596 |
1.29e-173 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 504.70 E-value: 1.29e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 20 PKKILPFIWQMTKGNRWLLFGAFLLALIGETVVSFLPYVYKIVVDGIQTQGTaevVSFIVFWSIVYVSAFLFFATIFRLS 99
Cdd:COG1132 5 PRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGD---LSALLLLLLLLLGLALLRALLSYLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 100 SFLgvrgISRAVESTAYpALR----DYLQKHSHRFFSGNFAGGLNAKEIQVGGGMRNLLHEAIWTVTATAIGLLVTTGLM 175
Cdd:COG1132 82 RYL----LARLAQRVVA-DLRrdlfEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 176 FSVDVRAGVTFVTLIVVIILCNLPLFKWQGGIARMHAKAIAKIRGVSIDALTNMRAVHSFAQGSQELSRLTETLEDARVI 255
Cdd:COG1132 157 FVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 256 GVKKSDVAQYILIINTIIILLAVSGILALLIISFQQGTATSGDFVLVFALISSVWRELTRIGFMINNISQIYSEAEEGLV 335
Cdd:COG1132 237 NLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 336 AISQAHEVIDVENAQDLVAKKGEIVLDGISFAH-EAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGA 414
Cdd:COG1132 317 LLDEPPEIPDPPGAVPLPPVRGEIEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 415 IKIDDQNIAEVTQDSLRRAISVVPQEPALFHRSIRENIAYARPDATDEEVRDAAQKAHALEFIDMLPEGMNTLVGERGVK 494
Cdd:COG1132 397 ILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVN 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 495 LSGGQRQRVAIARAILKDAPILILDEATSALDSESEVAVQKALKELMYGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDG 574
Cdd:COG1132 477 LSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQG 556
|
570 580
....*....|....*....|..
gi 1083564009 575 THEELLKNSGTYATLWNHQAGG 596
Cdd:COG1132 557 THEELLARGGLYARLYRLQFGE 578
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
47-601 |
7.08e-134 |
|
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: 403.82 E-value: 7.08e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 47 IGETVVSFLPYVYKIVVDGIQTQGTAEVVSFIVFwsIVYVSAFLFFATIF-RLSSFLGVRGISRAVESTAYPALRdYLQK 125
Cdd:COG5265 47 LAAALALVVPPLLKDAIDALLSGAAALLVVPVGL--LLAYGLLRLLSVLFgELRDALFARVTQRAVRRLALEVFR-HLHA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 126 HSHRFFSGNFAGGLnAKEIQVG-GGMRNLLHEAIWTVTATAIGLLVTTGLMFSV-DVR-AGVTFVTLIVVIILcNLPLFK 202
Cdd:COG5265 124 LSLRFHLERQTGGL-SRDIERGtKGIEFLLRFLLFNILPTLLEIALVAGILLVKyDWWfALITLVTVVLYIAF-TVVVTE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 203 WQGGIARMHAKAIAKIRGVSIDALTNMRAVHSFAQGSQELSRLTETLEDARVIGVK------KSDVAQyiliinTIIILL 276
Cdd:COG5265 202 WRTKFRREMNEADSEANTRAVDSLLNYETVKYFGNEAREARRYDEALARYERAAVKsqtslaLLNFGQ------ALIIAL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 277 AVSGILALLIISFQQGTATSGDFVLVFALISSVWRELTRIGFMINNISQIYSEAEEGLVAISQAHEVIDVENAQDLVAKK 356
Cdd:COG5265 276 GLTAMMLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPPEVADAPDAPPLVVGG 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 357 GEIVLDGISFAHEAV-EVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAIS 435
Cdd:COG5265 356 GEVRFENVSFGYDPErPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIG 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 436 VVPQEPALFHRSIRENIAYARPDATDEEVRDAAQKAHALEFIDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKDAPI 515
Cdd:COG5265 436 IVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPI 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 516 LILDEATSALDSESEVAVQKALKELMYGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGTHEELLKNSGTYATLWNHQAG 595
Cdd:COG5265 516 LIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQE 595
|
....*.
gi 1083564009 596 GFLQEE 601
Cdd:COG5265 596 EEEAEE 601
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
151-594 |
1.57e-115 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 359.92 E-value: 1.57e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 151 RNLLHEAIWTVTATAIGLLVTTGLMFSVDVRAGVTFVTLIVVIILCNLPLFKWQGGIARMHAKAIAKIRGVSIDALTNMR 230
Cdd:COG2274 266 REFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 231 AVHSFAQGSQELSRLTETLEDARVIGVKKSDVAQYILIINTIIILLAVSGILALLIISFQQGTATSGDFVLVFALISSVw 310
Cdd:COG2274 346 TIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRF- 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 311 reLTRIGFMINNISQIYseaeEGLVAISQAHEVIDVE-------NAQDLVAKKGEIVLDGISFAH--EAVEVFKNFNLTI 381
Cdd:COG2274 425 --LAPVAQLIGLLQRFQ----DAKIALERLDDILDLPpereegrSKLSLPRLKGDIELENVSFRYpgDSPPVLDNISLTI 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 382 KDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAISVVPQEPALFHRSIRENIAYARPDATD 461
Cdd:COG2274 499 KPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATD 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 462 EEVRDAAQKAHALEFIDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDEATSALDSESEVAVQKALKELM 541
Cdd:COG2274 579 EEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL 658
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1083564009 542 YGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGTHEELLKNSGTYATLWNHQA 594
Cdd:COG2274 659 KGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
359-590 |
4.45e-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: 334.58 E-value: 4.45e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHE--AVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAISV 436
Cdd:cd03251 1 VEFKNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 437 VPQEPALFHRSIRENIAYARPDATDEEVRDAAQKAHALEFIDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKDAPIL 516
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1083564009 517 ILDEATSALDSESEVAVQKALKELMYGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGTHEELLKNSGTYATLW 590
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
359-593 |
3.34e-108 |
|
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: 324.88 E-value: 3.34e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEA---VEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAIS 435
Cdd:cd03249 1 IEFKNVSFRYPSrpdVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 436 VVPQEPALFHRSIRENIAYARPDATDEEVRDAAQKAHALEFIDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKDAPI 515
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083564009 516 LILDEATSALDSESEVAVQKALKELMYGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGTHEELLKNSGTYATLWNHQ 593
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
23-589 |
3.14e-107 |
|
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: 334.36 E-value: 3.14e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 23 ILPFIWQMTKGNRWLLFGAFLLALIGETVVSFLPYVYKIVVD-GIQTQGTAEVVSFIVFwsIVYVSAFLFFATIFR--LS 99
Cdd:TIGR02204 5 PLAALWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMIDhGFSKDSSGLLNRYFAF--LLVVALVLALGTAARfyLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 100 SFLGVRgisraVESTAYPALRDYLQKHSHRFFSGNFAGGL------NAKEIQ--VGG----GMRNLLheaiwtvtaTAIG 167
Cdd:TIGR02204 83 TWLGER-----VVADIRRAVFAHLISLSPSFFDKNRSGEVvsrlttDTTLLQsvIGSslsmALRNAL---------MCIG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 168 LLvttGLMFSVDVRAgVTFVTLIVVIILcnLPLF---KWQGGIARMHAKAIAKIRGVSIDALTNMRAVHSFAQGSQELSR 244
Cdd:TIGR02204 149 GL---IMMFITSPKL-TSLVLLAVPLVL--LPILlfgRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 245 LTETLEDARVIGVKKSDVAQYILIINTIIILLAVSGIL---ALLIISFQQGTATSGDFVLV-------FALISSVWRELT 314
Cdd:TIGR02204 223 FGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLwvgAHDVIAGKMSAGTLGQFVFYavmvagsIGTLSEVWGELQ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 315 RIgfminnisqiySEAEEGLVAISQAHEVIDV-ENAQDLVAK-KGEIVLDGISFAHEA---VEVFKNFNLTIKDGERIGL 389
Cdd:TIGR02204 303 RA-----------AGAAERLIELLQAEPDIKApAHPKTLPVPlRGEIEFEQVNFAYPArpdQPALDGLNLTVRPGETVAL 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 390 VGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAISVVPQEPALFHRSIRENIAYARPDATDEEVRDAAQ 469
Cdd:TIGR02204 372 VGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAAR 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 470 KAHALEFIDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDEATSALDSESEVAVQKALKELMYGKTVIAI 549
Cdd:TIGR02204 452 AAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLII 531
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1083564009 550 AHRLSTLRDMSRILVLEHGTIQEDGTHEELLKNSGTYATL 589
Cdd:TIGR02204 532 AHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARL 571
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
359-593 |
3.95e-107 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 321.87 E-value: 3.95e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFA-HEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAISVV 437
Cdd:cd03253 1 IEFENVTFAyDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 438 PQEPALFHRSIRENIAYARPDATDEEVRDAAQKAHALEFIDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILI 517
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1083564009 518 LDEATSALDSESEVAVQKALKELMYGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGTHEELLKNSGTYATLWNHQ 593
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
330-584 |
1.95e-100 |
|
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: 316.31 E-value: 1.95e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 330 AEEGLVAISQAHEVIDVENAQDLVAKKG-EIVLDGISFAH-EAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLRE 407
Cdd:COG4988 307 AAEKIFALLDAPEPAAPAGTAPLPAAGPpSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGF 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 408 YDIAGGAIKIDDQNIAEVTQDSLRRAISVVPQEPALFHRSIRENIAYARPDATDEEVRDAAQKAHALEFIDMLPEGMNTL 487
Cdd:COG4988 387 LPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTP 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 488 VGERGVKLSGGQRQRVAIARAILKDAPILILDEATSALDSESEVAVQKALKELMYGKTVIAIAHRLSTLRDMSRILVLEH 567
Cdd:COG4988 467 LGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDD 546
|
250
....*....|....*..
gi 1083564009 568 GTIQEDGTHEELLKNSG 584
Cdd:COG4988 547 GRIVEQGTHEELLAKNG 563
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
163-601 |
1.80e-98 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 311.90 E-value: 1.80e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 163 ATAIGLLVTTGLMFSVDVR-AGVTFVTLIVVIILCNLPLFK---WQGGIARMHAKAIAKirgVSiDALTNMRAVHSFAQ- 237
Cdd:PRK13657 139 ATLVALVVLLPLALFMNWRlSLVLVVLGIVYTLITTLVMRKtkdGQAAVEEHYHDLFAH---VS-DAIGNVSVVQSYNRi 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 238 --GSQELSRLTETLEDArvigvkksdvaQY--------ILIINTIIILLAVSGILALLIISFQQGTATSGDFV--LVFA- 304
Cdd:PRK13657 215 eaETQALRDIADNLLAA-----------QMpvlswwalASVLNRAASTITMLAILVLGAALVQKGQLRVGEVVafVGFAt 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 305 -LISsvwreltRIGFMINNISQIYSEA---EEGLVAISQAHEVIDVENAQDLVAKKGEIVLDGISFAH----EAVEvfkN 376
Cdd:PRK13657 284 lLIG-------RLDQVVAFINQVFMAApklEEFFEVEDAVPDVRDPPGAIDLGRVKGAVEFDDVSFSYdnsrQGVE---D 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 377 FNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAISVVPQEPALFHRSIRENIAYAR 456
Cdd:PRK13657 354 VSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGR 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 457 PDATDEEVRDAAQKAHALEFIDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDEATSALDSESEVAVQKA 536
Cdd:PRK13657 434 PDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAA 513
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1083564009 537 LKELMYGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGTHEELLKNSGTYATLWnhQAGGFLQEE 601
Cdd:PRK13657 514 LDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALL--RAQGMLQED 576
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
53-593 |
1.81e-97 |
|
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: 308.95 E-value: 1.81e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 53 SFLPYVYKIVVDGIQTQGTAEVvsfivfwsIVYVSAFLFFATIFR-LSSFLGVRGISRAVESTAYPALRDYLQKH---SH 128
Cdd:TIGR02203 31 STLAALLKPLLDDGFGGRDRSV--------LWWVPLVVIGLAVLRgICSFVSTYLLSWVSNKVVRDIRVRMFEKLlglPV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 129 RFFSGNFAGGLNAKEIQVGGGMRNLLHEAIWTV---TATAIGLLVttgLMFSVDVRagvtfVTLIVVIILcnlPLFKWQG 205
Cdd:TIGR02203 103 SFFDRQPTGTLLSRITFDSEQVASAATDAFIVLvreTLTVIGLFI---VLLYYSWQ-----LTLIVVVML---PVLSILM 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 206 --------GIARMHAKAIAKIRGVSIDALTNMRAVHSFAQGSQELSRLTETLEDARVIGVKKSDVAQYILIINTIIILLA 277
Cdd:TIGR02203 172 rrvskrlrRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQLIASLA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 278 VSGILALLIISFQQGTATSGDFVLVFALISSVWRELTRIgfminniSQIYSEAEEGLVAISQAHEVIDVENAQD-----L 352
Cdd:TIGR02203 252 LAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSL-------TNVNAPMQRGLAAAESLFTLLDSPPEKDtgtraI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 353 VAKKGEIVLDGISFAH--EAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSL 430
Cdd:TIGR02203 325 ERARGDVEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 431 RRAISVVPQEPALFHRSIRENIAYARP-DATDEEVRDAAQKAHALEFIDMLPEGMNTLVGERGVKLSGGQRQRVAIARAI 509
Cdd:TIGR02203 405 RRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARAL 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 510 LKDAPILILDEATSALDSESEVAVQKALKELMYGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGTHEELLKNSGTYATL 589
Cdd:TIGR02203 485 LKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQL 564
|
....
gi 1083564009 590 WNHQ 593
Cdd:TIGR02203 565 HNMQ 568
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
161-592 |
3.38e-97 |
|
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: 307.85 E-value: 3.38e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 161 VTATAIGLLVTTGLMFSVDVRAGVT-FVTLIVVIILcnLPLF--KWQGGIARMHAKAIAKIRGVSIDALTNMRAVHSFAQ 237
Cdd:COG4987 136 LLVALLVILAAVAFLAFFSPALALVlALGLLLAGLL--LPLLaaRLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGA 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 238 GSQELSRLTETLEDARVIGVKKSDVAQYILIINTIIILLAVSGILALLIISFQQGTAtSGDFVLVFAL-----------I 306
Cdd:COG4987 214 LDRALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGAL-SGPLLALLVLaalalfealapL 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 307 SSVWRELTRigfminnisqiYSEAEEGLVAISQAHEVIDVENAQDLVAKKGEIVLDGISFAH--EAVEVFKNFNLTIKDG 384
Cdd:COG4987 293 PAAAQHLGR-----------VRAAARRLNELLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPG 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 385 ERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAISVVPQEPALFHRSIRENIAYARPDATDEEV 464
Cdd:COG4987 362 ERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEEL 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 465 RDAAQKAHALEFIDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDEATSALDSESEVAVQKALKELMYGK 544
Cdd:COG4987 442 WAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR 521
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1083564009 545 TVIAIAHRLSTLRDMSRILVLEHGTIQEDGTHEELLKNSGTYATLWNH 592
Cdd:COG4987 522 TVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQR 569
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
357-584 |
1.82e-93 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 286.43 E-value: 1.82e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 357 GEIVLDGISFAH-EAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAIS 435
Cdd:cd03254 1 GEIEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 436 VVPQEPALFHRSIRENIAYARPDATDEEVRDAAQKAHALEFIDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKDAPI 515
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1083564009 516 LILDEATSALDSESEVAVQKALKELMYGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGTHEELLKNSG 584
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
299-596 |
1.48e-89 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 288.46 E-value: 1.48e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 299 FVLVFALISSVWRELT----------RIGFM--INNISQIYSEAEEGLVAISQAHEVIDVENAQD---LVAK--KGEIVL 361
Cdd:PRK11176 265 FVLYAASFPSVMDTLTagtitvvfssMIALMrpLKSLTNVNAQFQRGMAACQTLFAILDLEQEKDegkRVIEraKGDIEF 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 362 DGISFAHEAVEV--FKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAISVVPQ 439
Cdd:PRK11176 345 RNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQ 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 440 EPALFHRSIRENIAYARPDA-TDEEVRDAAQKAHALEFIDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILIL 518
Cdd:PRK11176 425 NVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILIL 504
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083564009 519 DEATSALDSESEVAVQKALKELMYGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGTHEELLKNSGTYATLWNHQAGG 596
Cdd:PRK11176 505 DEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQFGQ 582
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
54-589 |
3.61e-82 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 272.37 E-value: 3.61e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 54 FLPYVYKIVVDGIQTQGTAEVVSFIVFwsivyvsaflfFATIFRLSSFL--GVR-GISRAVESTAYPALRDYLQKHSHR- 129
Cdd:TIGR00958 179 FIPFYTGRVIDTLGGDKGPPALASAIF-----------FMCLLSIASSVsaGLRgGSFNYTMARINLRIREDLFRSLLRq 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 130 ---FFSGNFAGGLNAKEIQVGGGMRNLLHEAIWTVTATAIGLLVTTGLMFSVDVRagVTFVTLIVV--IILCNLPLFKWQ 204
Cdd:TIGR00958 248 dlgFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPR--LTMVTLINLplVFLAEKVFGKRY 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 205 GGIARMHAKAIAKIRGVSIDALTNMRAVHSFAQGSQELSRLTETLEDARVIGvKKSDVAqyiliINTIIILLAVSGILAL 284
Cdd:TIGR00958 326 QLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLN-KRKALA-----YAGYLWTTSVLGMLIQ 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 285 LIISF------QQGTATSGDfvlvfaLISSVWRELtRIGFMINNISQIYSEAEEGLVAISQAHEVID----VENAQDLVA 354
Cdd:TIGR00958 400 VLVLYyggqlvLTGKVSSGN------LVSFLLYQE-QLGEAVRVLSYVYSGMMQAVGASEKVFEYLDrkpnIPLTGTLAP 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 355 K--KGEIVLDGISFA---HEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDS 429
Cdd:TIGR00958 473 LnlEGLIEFQDVSFSypnRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHY 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 430 LRRAISVVPQEPALFHRSIRENIAYARPDATDEEVRDAAQKAHALEFIDMLPEGMNTLVGERGVKLSGGQRQRVAIARAI 509
Cdd:TIGR00958 553 LHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARAL 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 510 LKDAPILILDEATSALDSESEVAVQKALKElmYGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGTHEELLKNSGTYATL 589
Cdd:TIGR00958 633 VRKPRVLILDEATSALDAECEQLLQESRSR--ASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
323-595 |
1.48e-80 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 267.76 E-value: 1.48e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 323 ISQIYSEAEEGLVAISQAHEVID--VENAQD----LVAKKGEIVLDGISF--AHEAVEVFKNFNLTIKDGERIGLVGKSG 394
Cdd:TIGR01846 414 LAQLWQDFQQTGIALERLGDILNspTEPRSAglaaLPELRGAITFENIRFryAPDSPEVLSNLNLDIKPGEFIGIVGPSG 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 395 AGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAISVVPQEPALFHRSIRENIAYARPDATDEEVRDAAQKAHAL 474
Cdd:TIGR01846 494 SGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAH 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 475 EFIDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDEATSALDSESEVAVQKALKELMYGKTVIAIAHRLS 554
Cdd:TIGR01846 574 DFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLS 653
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1083564009 555 TLRDMSRILVLEHGTIQEDGTHEELLKNSGTYATLWNHQAG 595
Cdd:TIGR01846 654 TVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQQQSG 694
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
359-593 |
2.09e-80 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 253.18 E-value: 2.09e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAH--EAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAISV 436
Cdd:cd03252 1 ITFEHVRFRYkpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 437 VPQEPALFHRSIRENIAYARPDATDEEVRDAAQKAHALEFIDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKDAPIL 516
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1083564009 517 ILDEATSALDSESEVAVQKALKELMYGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGTHEELLKNSGTYATLWNHQ 593
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
359-568 |
5.38e-79 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 246.91 E-value: 5.38e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAH--EAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAISV 436
Cdd:cd03228 1 IEFKNVSFSYpgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 437 VPQEPALFHRSIRENIayarpdatdeevrdaaqkahalefidmlpegmntlvgergvkLSGGQRQRVAIARAILKDAPIL 516
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1083564009 517 ILDEATSALDSESEVAVQKALKELMYGKTVIAIAHRLSTLRDMSRILVLEHG 568
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
357-575 |
2.08e-72 |
|
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: 231.61 E-value: 2.08e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 357 GEIVLDGISFAH--EAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAI 434
Cdd:cd03244 1 GDIEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 435 SVVPQEPALFHRSIRENIAyarPD--ATDEEVRDAAQKAHALEFIDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKD 512
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLD---PFgeYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1083564009 513 APILILDEATSALDSESEVAVQKALKELMYGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGT 575
Cdd:cd03244 158 SKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
163-601 |
2.76e-72 |
|
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: 242.87 E-value: 2.76e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 163 ATAIGLLVTTGLMFSVDVRAGVTFVTL-IVVIILCNLPLFKWQGGIARMHAKAIAKIRGVSiDALTNMRAVHSFAQGSQE 241
Cdd:TIGR01192 139 ATFVALFLLIPTAFAMDWRLSIVLMVLgILYILIAKLVMQRTKNGQAAVEHHYHNVFKHVS-DSISNVSVVHSYNRIEAE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 242 LSRLTETLEdaRVIGVKKSDVAQYILIINTIIILLAVSGILALLIISF--QQGTATSGDFVLVFALISSVWRELTRIGFM 319
Cdd:TIGR01192 218 TSALKQFTN--NLLSAQYPVLDWWALASGLNRMASTISMMCILVIGTVlvIKGELSVGEVIAFIGFANLLIGRLDQMSGF 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 320 INNISQIYSEAEEGLVAISQAHEVIDVENAQDLVAKKGEIVLDGIS--FAHEAVEVFkNFNLTIKDGERIGLVGKSGAGK 397
Cdd:TIGR01192 296 ITQIFEARAKLEDFFDLEDSVFQREEPADAPELPNVKGAVEFRHITfeFANSSQGVF-DVSFEAKAGQTVAIVGPTGAGK 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 398 STLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAISVVPQEPALFHRSIRENIAYARPDATDEEVRDAAQKAHALEFI 477
Cdd:TIGR01192 375 TTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFI 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 478 DMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDEATSALDSESEVAVQKALKELMYGKTVIAIAHRLSTLR 557
Cdd:TIGR01192 455 LKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVR 534
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1083564009 558 DMSRILVLEHGTIQEDGTHEELLKNSGTYATLWnhQAGGFLQEE 601
Cdd:TIGR01192 535 NADLVLFLDQGRLIEKGSFQELIQKDGRFYKLL--RRSGLLTNQ 576
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
330-565 |
2.53e-70 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 236.03 E-value: 2.53e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 330 AEEGLVAISQAHEVIDVENAQDLVAKKGEIVLDGISFAHE-AVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREY 408
Cdd:TIGR02857 293 AAEALFAVLDAAPRPLAGKAPVTAAPASSLEFSGVSVAYPgRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFV 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 409 DIAGGAIKIDDQNIAEVTQDSLRRAISVVPQEPALFHRSIRENIAYARPDATDEEVRDAAQKAHALEFIDMLPEGMNTLV 488
Cdd:TIGR02857 373 DPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPI 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1083564009 489 GERGVKLSGGQRQRVAIARAILKDAPILILDEATSALDSESEVAVQKALKELMYGKTVIAIAHRLSTLRDMSRILVL 565
Cdd:TIGR02857 453 GEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
357-574 |
1.12e-69 |
|
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: 224.39 E-value: 1.12e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 357 GEIVLDGISFAH--EAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAI 434
Cdd:cd03245 1 GRIEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 435 SVVPQEPALFHRSIRENIAYARPDATDEEVRDAAQKAHALEFIDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKDAP 514
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 515 ILILDEATSALDSESEVAVQKALKELMYGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDG 574
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
356-570 |
3.13e-69 |
|
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: 223.50 E-value: 3.13e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 356 KGEIVLDGISFAHE---AVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRR 432
Cdd:cd03248 9 KGIVKFQNVTFAYPtrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 433 AISVVPQEPALFHRSIRENIAYARPDATDEEVRDAAQKAHALEFIDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKD 512
Cdd:cd03248 89 KVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1083564009 513 APILILDEATSALDSESEVAVQKALKELMYGKTVIAIAHRLSTLRDMSRILVLEHGTI 570
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
331-593 |
1.47e-68 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 232.81 E-value: 1.47e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 331 EEGLVAISQAHEVIDVENAQDLVAKKGEIvldgisFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLreydi 410
Cdd:PRK11174 329 ETPLAHPQQGEKELASNDPVTIEAEDLEI------LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALL----- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 411 aG-----GAIKIDDQNIAEVTQDSLRRAISVVPQEPALFHRSIRENIAYARPDATDEEVRDAAQKAHALEFIDMLPEGMN 485
Cdd:PRK11174 398 -GflpyqGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLD 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 486 TLVGERGVKLSGGQRQRVAIARAILKDAPILILDEATSALDSESEVAVQKALKELMYGKTVIAIAHRLSTLRDMSRILVL 565
Cdd:PRK11174 477 TPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVM 556
|
250 260
....*....|....*....|....*...
gi 1083564009 566 EHGTIQEDGTHEELLKNSGTYATLWNHQ 593
Cdd:PRK11174 557 QDGQIVQQGDYAELSQAGGLFATLLAHR 584
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
348-593 |
1.39e-67 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 230.10 E-value: 1.39e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 348 NAQDLVAKKGEIVLDGISFAHEAVE--VFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEV 425
Cdd:PRK11160 328 TTSTAAADQVSLTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADY 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 426 TQDSLRRAISVVPQEPALFHRSIRENIAYARPDATDEEVRDAAQKAhALEFIDMLPEGMNTLVGERGVKLSGGQRQRVAI 505
Cdd:PRK11160 408 SEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQV-GLEKLLEDDKGLNAWLGEGGRQLSGGEQRRLGI 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 506 ARAILKDAPILILDEATSALDSESEVAVQKALKELMYGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGTHEELLKNSGT 585
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGR 566
|
....*...
gi 1083564009 586 YATLWNHQ 593
Cdd:PRK11160 567 YYQLKQRL 574
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
291-593 |
7.04e-65 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 222.67 E-value: 7.04e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 291 QGTATSGD---FVLVFALIssVWRELTrIGFMINNI---SQIYSEAEEGLvaiSQAHEVIDveNAQDLVAKKGEIVLDGI 364
Cdd:PRK10789 248 NGSLTLGQltsFVMYLGLM--IWPMLA-LAWMFNIVergSAAYSRIRAML---AEAPVVKD--GSEPVPEGRGELDVNIR 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 365 SFAHEAVE--VFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAISVVPQEPA 442
Cdd:PRK10789 320 QFTYPQTDhpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPF 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 443 LFHRSIRENIAYARPDATDEEVRDAAQKAHALEFIDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDEAT 522
Cdd:PRK10789 400 LFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDAL 479
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1083564009 523 SALDSESEVAVQKALKELMYGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGTHEELLKNSGTYATLWNHQ 593
Cdd:PRK10789 480 SAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQ 550
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
357-589 |
1.10e-59 |
|
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: 211.34 E-value: 1.10e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 357 GEIVLDGISFAHEAVE--VFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAI 434
Cdd:TIGR03796 476 GYVELRNITFGYSPLEppLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSV 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 435 SVVPQEPALFHRSIRENIAYARPDATDEEVRDAAQKAHALEFIDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKDAP 514
Cdd:TIGR03796 556 AMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPS 635
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1083564009 515 ILILDEATSALDSESEVAVQKALKElmYGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGTHEELLKNSGTYATL 589
Cdd:TIGR03796 636 ILILDEATSALDPETEKIIDDNLRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARL 708
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
356-581 |
2.94e-57 |
|
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: 201.90 E-value: 2.94e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 356 KGEIVLDGISFAH--EAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRA 433
Cdd:COG4618 328 KGRLSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 434 ISVVPQEPALFHRSIRENIAyaR-PDATDEEVRDAAQKAHALEFIDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKD 512
Cdd:COG4618 408 IGYLPQDVELFDGTIAENIA--RfGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGD 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 513 APILILDEATSALDSESEVAVQKALKELMY-GKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGTHEELLK 581
Cdd:COG4618 486 PRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
332-553 |
4.69e-57 |
|
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: 200.66 E-value: 4.69e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 332 EGLVAISQAHEvidvenAQDLVAKKGEIVLDGISFAHE-AVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDI 410
Cdd:TIGR02868 314 AGPVAEGSAPA------AGAVGLGKPTLELRDLSAGYPgAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDP 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 411 AGGAIKIDDQNIAEVTQDSLRRAISVVPQEPALFHRSIRENIAYARPDATDEEVRDAAQKAHALEFIDMLPEGMNTLVGE 490
Cdd:TIGR02868 388 LQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGE 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1083564009 491 RGVKLSGGQRQRVAIARAILKDAPILILDEATSALDSESEVAVQKALKELMYGKTVIAIAHRL 553
Cdd:TIGR02868 468 GGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
88-589 |
1.20e-52 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 191.32 E-value: 1.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 88 AFLFFATIFRLSSFLGVRGISRAVESTAYPALRDYLQKHSHRFFSGNFAGGLNAKEIQVGGgMRNLLHEAIWTVTATAIG 167
Cdd:TIGR03797 184 AAAVGAAAFQLAQSLAVLRLETRMDASLQAAVWDRLLRLPVSFFRQYSTGDLASRAMGISQ-IRRILSGSTLTTLLSGIF 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 168 LLVTTGLMFSVDVRAGVTFVTLIVVIILCNLPLFKWQggiARMHAKAIA---KIRGVS---IDALTNMRA----VHSFAQ 237
Cdd:TIGR03797 263 ALLNLGLMFYYSWKLALVAVALALVAIAVTLVLGLLQ---VRKERRLLElsgKISGLTvqlINGISKLRVagaeNRAFAR 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 238 GSQELSRLTETLEDARVIGVkksdvaqyiLIINTIIILLAVSGILALLIISFQQGTA--TSGDFVLVFALISSVWRELTR 315
Cdd:TIGR03797 340 WAKLFSRQRKLELSAQRIEN---------LLTVFNAVLPVLTSAALFAAAISLLGGAglSLGSFLAFNTAFGSFSGAVTQ 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 316 igfMINNISQIYSEAE--EGLVAISQAHEVIDVENAQ--DLvakKGEIVLDGISFAH--EAVEVFKNFNLTIKDGERIGL 389
Cdd:TIGR03797 411 ---LSNTLISILAVIPlwERAKPILEALPEVDEAKTDpgKL---SGAIEVDRVTFRYrpDGPLILDDVSLQIEPGEFVAI 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 390 VGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAISVVPQEPALFHRSIRENIAYARPdATDEEVRDAAQ 469
Cdd:TIGR03797 485 VGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAP-LTLDEAWEAAR 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 470 KAHALEFIDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDEATSALDSESEVAVQKALKELmyGKTVIAI 549
Cdd:TIGR03797 564 MAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERL--KVTRIVI 641
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1083564009 550 AHRLSTLRDMSRILVLEHGTIQEDGTHEELLKNSGTYATL 589
Cdd:TIGR03797 642 AHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQL 681
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
357-596 |
1.12e-51 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 187.23 E-value: 1.12e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 357 GEIVLDGISFAHEAVE-VFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAIS 435
Cdd:PRK10790 339 GRIDIDNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 436 VVPQEPALFHRSIRENIAYARpDATDEEVRDAAQKAHALEFIDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKDAPI 515
Cdd:PRK10790 419 MVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQI 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 516 LILDEATSALDSESEVAVQKALKELMYGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGTHEELLKNSGTYATLWNHQAG 595
Cdd:PRK10790 498 LILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLA 577
|
.
gi 1083564009 596 G 596
Cdd:PRK10790 578 G 578
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
357-592 |
2.68e-51 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 188.02 E-value: 2.68e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 357 GEIVLDGISFAHE-AVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAIS 435
Cdd:TIGR01193 472 GDIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFIN 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 436 VVPQEPALFHRSIREN-IAYARPDATDEEVRDAAQKAHALEFIDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKDAP 514
Cdd:TIGR01193 552 YLPQEPYIFSGSILENlLLGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSK 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 515 ILILDEATSALDSESEvavQKALKELMY--GKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGTHEELLKNSGTYATLWNH 592
Cdd:TIGR01193 632 VLILDESTSNLDTITE---KKIVNNLLNlqDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
357-575 |
3.21e-49 |
|
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: 169.90 E-value: 3.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 357 GEIVLDGIS--FAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAI 434
Cdd:cd03369 5 GEIEVENLSvrYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 435 SVVPQEPALFHRSIRENI-AYARpdATDEEVRDAAQkahalefidmlpegmntlVGERGVKLSGGQRQRVAIARAILKDA 513
Cdd:cd03369 85 TIIPQDPTLFSGTIRSNLdPFDE--YSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKRP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1083564009 514 PILILDEATSALDSESEVAVQKALKELMYGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGT 575
Cdd:cd03369 145 RVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
365-574 |
1.92e-47 |
|
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: 164.02 E-value: 1.92e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 365 SFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVtQDSLRRAISVVPQEPALF 444
Cdd:cd03247 9 SYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLISVLNQRPYLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 445 HRSIRENIayarpdatdeevrdaaqkahalefidmlpegmntlvgerGVKLSGGQRQRVAIARAILKDAPILILDEATSA 524
Cdd:cd03247 88 DTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVG 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1083564009 525 LDSESEVAVQKALKELMYGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDG 574
Cdd:cd03247 129 LDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
299-586 |
2.52e-47 |
|
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: 178.99 E-value: 2.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 299 FVLVFALIS-----------SVWRELtRIGFMINNISQIYSEAEEGLVAISQAHEVIDVENAQDLVAK----------KG 357
Cdd:TIGR00957 1205 FAALFAVISrhslsaglvglSVSYSL-QVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQetappsgwppRG 1283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 358 EIVLDGISFAH-EAVE-VFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAIS 435
Cdd:TIGR00957 1284 RVEFRNYCLRYrEDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKIT 1363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 436 VVPQEPALFHRSIRENI----AYarpdaTDEEVRDAAQKAHALEFIDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILK 511
Cdd:TIGR00957 1364 IIPQDPVLFSGSLRMNLdpfsQY-----SDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLR 1438
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1083564009 512 DAPILILDEATSALDSESEVAVQKALKELMYGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGTHEELLKNSGTY 586
Cdd:TIGR00957 1439 KTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIF 1513
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
356-581 |
6.83e-47 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 172.92 E-value: 6.83e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 356 KGEIVLDGISFAH--EAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRA 433
Cdd:TIGR01842 314 EGHLSVENVTIVPpgGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKH 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 434 ISVVPQEPALFHRSIRENIAYARPDATDEEVRDAAQKAHALEFIDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKDA 513
Cdd:TIGR01842 394 IGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDP 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1083564009 514 PILILDEATSALDSESEVAVQKALKEL-MYGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGTHEELLK 581
Cdd:TIGR01842 474 KLVVLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLA 542
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
359-569 |
1.94e-46 |
|
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: 162.25 E-value: 1.94e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVE-----VFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIkiddqniaevtqdSLRRA 433
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-------------SVPGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 434 ISVVPQEPALFHRSIRENIAYARPdaTDEEVRDAAQKAHALEF-IDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKD 512
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKP--FDEERYEKVIKACALEPdLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSD 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1083564009 513 APILILDEATSALDSESEVAV-QKAL-KELMYGKTVIAIAHRLSTLRDMSRILVLEHGT 569
Cdd:cd03250 146 ADIYLLDDPLSAVDAHVGRHIfENCIlGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
344-586 |
1.59e-45 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 173.68 E-value: 1.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 344 IDVENAQDLvakKGEIVLDGISFAHEA---VEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIA--------- 411
Cdd:PTZ00265 1154 IRIKNKNDI---KGKIEIMDVNFRYISrpnVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKndhhivfkn 1230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 412 ---------------------------------------------GGAIKIDDQNIAEVTQDSLRRAISVVPQEPALFHR 446
Cdd:PTZ00265 1231 ehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNM 1310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 447 SIRENIAYARPDATDEEVRDAAQKAHALEFIDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDEATSALD 526
Cdd:PTZ00265 1311 SIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083564009 527 SESEVAVQKALKEL--MYGKTVIAIAHRLSTLRDMSRILVLEH----GT-IQEDGTHEELLK-NSGTY 586
Cdd:PTZ00265 1391 SNSEKLIEKTIVDIkdKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSfVQAHGTHEELLSvQDGVY 1458
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
369-582 |
2.35e-45 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 168.16 E-value: 2.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 369 EAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDS---LRRAISVVPQEP--AL 443
Cdd:COG1123 276 GGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlreLRRRVQMVFQDPysSL 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 444 FHR-SIRENIAYA---RPDATDEEVRDAAqkAHALEFIDMLPEGMNTLVGErgvkLSGGQRQRVAIARAILKDAPILILD 519
Cdd:COG1123 356 NPRmTVGDIIAEPlrlHGLLSRAERRERV--AELLERVGLPPDLADRYPHE----LSGGQRQRVAIARALALEPKLLILD 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 520 EATSALDseseVAVQKALKELM------YGKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEELLKN 582
Cdd:COG1123 430 EPTSALD----VSVQAQILNLLrdlqreLGLTYLFISHDLAVVRYIAdRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
359-570 |
2.68e-45 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 159.21 E-value: 2.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAISVVP 438
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 439 QEPALFHRSIRENIAYarPDATDEEVRDAAQKAHALEFIDMLPEGMNTLVGErgvkLSGGQRQRVAIARAILKDAPILIL 518
Cdd:COG4619 81 QEPALWGGTVRDNLPF--PFQLRERKFDRERALELLERLGLPPDILDKPVER----LSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 519 DEATSALDSESEVAVQKALKELMY--GKTVIAIAH------RLSTlrdmsRILVLEHGTI 570
Cdd:COG4619 155 DEPTSALDPENTRRVEELLREYLAeeGRAVLWVSHdpeqieRVAD-----RVLTLEAGRL 209
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
371-574 |
1.20e-44 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 158.44 E-value: 1.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 371 VEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSL---RRAISVVPQEP--AL-F 444
Cdd:cd03257 18 VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirRKEIQMVFQDPmsSLnP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 445 HRSIRENIAYARPDATDEEVRDAAQKAHALEFIDM-LPEG-MNTLVGErgvkLSGGQRQRVAIARAILKDAPILILDEAT 522
Cdd:cd03257 98 RMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVgLPEEvLNRYPHE----LSGGQRQRVAIARALALNPKLLIADEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1083564009 523 SALDSESEVAVQKALKEL--MYGKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDG 574
Cdd:cd03257 174 SALDVSVQAQILDLLKKLqeELGLTLLFITHDLGVVAKIAdRVAVMYAGKIVEEG 228
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
359-580 |
7.07e-43 |
|
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: 154.43 E-value: 7.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAISVVP 438
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 439 QEPAL-FHRSIRENIAYAR---------PDATDEE-VRDAAQKAHALEFIDmlpegmnTLVGErgvkLSGGQRQRVAIAR 507
Cdd:COG1120 82 QEPPApFGLTVRELVALGRyphlglfgrPSAEDREaVEEALERTGLEHLAD-------RPVDE----LSGGERQRVLIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1083564009 508 AILKDAPILILDEATSALDSESEVAVQKALKEL--MYGKTVIAIAHRLS-TLRDMSRILVLEHGTIQEDGTHEELL 580
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
359-582 |
1.52e-42 |
|
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: 152.49 E-value: 1.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFA-HEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSL---LLREYdiaGGAIKIDDQNIAEVTQDSLRRAI 434
Cdd:COG1122 1 IELENLSFSyPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLlngLLKPT---SGEVLVDGKDITKKNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 435 SVVPQEPA--LFHRSIRENIAYA------RPDATDEEVRDAAQKAHALEFIDMLPEgmntlvgergvKLSGGQRQRVAIA 506
Cdd:COG1122 78 GLVFQNPDdqLFAPTVEEDVAFGpenlglPREEIRERVEEALELVGLEHLADRPPH-----------ELSGGQKQRVAIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083564009 507 RAILKDAPILILDEATSALDSESEVAVQKALKEL-MYGKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEELLKN 582
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVAELAdRVIVLDDGRIVADGTPREVFSD 224
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
359-584 |
2.29e-42 |
|
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: 152.70 E-value: 2.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTqDSLRRAISVVP 438
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 439 QEPALF-HRSIRENIAYArpdATDEEVRDAAQKAHALEFIDM--LPEGMNTLVGErgvkLSGGQRQRVAIARAILKDAPI 515
Cdd:COG4555 81 DERGLYdRLTVRENIRYF---AELYGLFDEELKKRIEELIELlgLEEFLDRRVGE----LSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1083564009 516 LILDEATSALDSESEVAVQKALKELM-YGKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEELLKNSG 584
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEALCdRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
374-523 |
3.26e-42 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 148.95 E-value: 3.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 374 FKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAISVVPQEPALF-HRSIRENI 452
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1083564009 453 AYARPDATDEEVRDAAQKAHALEFIDmLPEGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDEATS 523
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLG-LGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
359-581 |
3.51e-42 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 152.26 E-value: 3.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGIS----FAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAI 434
Cdd:COG1124 2 LEVRNLSvsygQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 435 SVVPQEPAL-FH------RSIRENIAYARPDATDEEVRDAAQKAH-ALEFIDMLPEgmntlvgergvKLSGGQRQRVAIA 506
Cdd:COG1124 82 QMVFQDPYAsLHprhtvdRILAEPLRIHGLPDREERIAELLEQVGlPPSFLDRYPH-----------QLSGGQRQRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 507 RAILKDAPILILDEATSALDseseVAVQKA----LKELM--YGKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEEL 579
Cdd:COG1124 151 RALILEPELLLLDEPTSALD----VSVQAEilnlLKDLReeRGLTYLFVSHDLAVVAHLCdRVAVMQNGRIVEELTVADL 226
|
..
gi 1083564009 580 LK 581
Cdd:COG1124 227 LA 228
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
359-570 |
3.92e-42 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 149.67 E-value: 3.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVE--VFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAISV 436
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 437 VPQEPALFHRSIRENIayarpdatdeevrdaaqkahalefidmlpegmntlvgergvkLSGGQRQRVAIARAILKDAPIL 516
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1083564009 517 ILDEATSALDSESEVAVQKALKEL-MYGKTVIAIAHRLSTLRDMSRILVLEHGTI 570
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
318-593 |
1.23e-41 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 162.12 E-value: 1.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 318 FMINNISQIYSEAEEGLVAISQAHEVID----VENAQDLVAKKG--EIVLDGISFAHEA---VEVFKNFNLTIKDGERIG 388
Cdd:PTZ00265 336 FMLTIILPNITEYMKSLEATNSLYEIINrkplVENNDDGKKLKDikKIQFKNVRFHYDTrkdVEIYKDLNFTLTEGKTYA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 389 LVGKSGAGKSTLVSLLLREYDIAGGAIKIDD-QNIAEVTQDSLRRAISVVPQEPALFHRSIRENIAYA------------ 455
Cdd:PTZ00265 416 FVGESGCGKSTILKLIERLYDPTEGDIIINDsHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsn 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 456 --------------------------------RPDAT-------------DEEVRDAAQKAHALEFIDMLPEGMNTLVGE 490
Cdd:PTZ00265 496 yynedgndsqenknkrnscrakcagdlndmsnTTDSNeliemrknyqtikDSEVVDVSKKVLIHDFVSALPDKYETLVGS 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 491 RGVKLSGGQRQRVAIARAILKDAPILILDEATSALDSESEVAVQKALKELM--YGKTVIAIAHRLSTLRDMSRILVL--- 565
Cdd:PTZ00265 576 NASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLsnr 655
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1083564009 566 EHGT--------------------------------------------IQEDGTHEELLKN-SGTYATLWNHQ 593
Cdd:PTZ00265 656 ERGStvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinnagsyIIEQGTHDALMKNkNGIYYTMINNQ 728
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
360-585 |
1.58e-41 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 161.68 E-value: 1.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 360 VLDGISFAheavevfknfnltIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAISVVPQ 439
Cdd:PLN03232 1251 VLHGLSFF-------------VSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQ 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 440 EPALFHRSIRENIAyARPDATDEEVRDAAQKAHALEFIDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILD 519
Cdd:PLN03232 1318 SPVLFSGTVRFNID-PFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLD 1396
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1083564009 520 EATSALDSESEVAVQKALKELMYGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGTHEELLKNSGT 585
Cdd:PLN03232 1397 EATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTS 1462
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
359-581 |
3.04e-41 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 149.44 E-value: 3.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDsLRRAISVVP 438
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 439 QEPALF-HRSIRENIAYARP--DATDEEVRDAAQKAhaLEFIDmLPEGMNTLVGergvKLSGGQRQRVAIARAILKDAPI 515
Cdd:COG1131 80 QEPALYpDLTVRENLRFFARlyGLPRKEARERIDEL--LELFG-LTDAADRKVG----TLSGGMKQRLGLALALLHDPEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083564009 516 LILDEATSALDSESEVAVQKALKELM-YGKTVIAIAHRLSTLRDM-SRILVLEHGTIQEDGTHEELLK 581
Cdd:COG1131 153 LILDEPTSGLDPEARRELWELLRELAaEGKTVLLSTHYLEEAERLcDRVAIIDKGRIVADGTPDELKA 220
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
359-573 |
4.63e-41 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 148.65 E-value: 4.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAH----EAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLL--LREYDiaGGAIKIDDQNIAEVTQDSL-- 430
Cdd:COG1136 5 LELRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILggLDRPT--SGEVLIDGQDISSLSERELar 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 431 --RRAISVVPQEPALF-HRSIRENIA----YARpdatdeeVRDAAQKAHALEFIDMLpeGMNTLVGERGVKLSGGQRQRV 503
Cdd:COG1136 83 lrRRHIGFVFQFFNLLpELTALENVAlpllLAG-------VSRKERRERARELLERV--GLGDRLDHRPSQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1083564009 504 AIARAILKDAPILILDEATSALDSESEVAVQKALKEL--MYGKTVIAIAHRLSTLRDMSRILVLEHGTIQED 573
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
359-574 |
1.18e-40 |
|
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: 146.90 E-value: 1.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDslRRAISVVP 438
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 439 QEPALF-HRSIRENIAYA-RPDATDEEVRdaAQKAHALEFIDMLPEGMNTLVGErgvkLSGGQRQRVAIARAILKDAPIL 516
Cdd:cd03259 79 QDYALFpHLTVAENIAFGlKLRGVPKAEI--RARVRELLELVGLEGLLNRYPHE----LSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1083564009 517 ILDEATSALDSESEVAVQKALKELM--YGKTVIAIAHRLS---TLRDmsRILVLEHGTIQEDG 574
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKELQreLGITTIYVTHDQEealALAD--RIAVMNEGRIVQVG 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
359-569 |
1.29e-40 |
|
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: 145.41 E-value: 1.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDS--LRRAISV 436
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 437 VPQEPALF-HRSIRENIAYArpdatdeevrdaaqkahalefidmlpegmntlvgergvkLSGGQRQRVAIARAILKDAPI 515
Cdd:cd03229 81 VFQDFALFpHLTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1083564009 516 LILDEATSALDSESEVAVQKALKEL--MYGKTVIAIAHRLSTLRDMS-RILVLEHGT 569
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDEAARLAdRVVVLRDGK 178
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
359-578 |
1.60e-40 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 146.74 E-value: 1.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEA-VEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDS---LRRAI 434
Cdd:COG2884 2 IRFENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 435 SVVPQE-PALFHRSIRENIAYA------RPDATDEEVRDAAQKAHALEFIDMLPEgmntlvgergvKLSGGQRQRVAIAR 507
Cdd:COG2884 82 GVVFQDfRLLPDRTVYENVALPlrvtgkSRKEIRRRVREVLDLVGLSDKAKALPH-----------ELSGGEQQRVAIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1083564009 508 AILKDAPILILDEATSALDSESEVAVQKALKEL-MYGKTVIaIA-HRLSTLRDM-SRILVLEHGTIQEDGTHEE 578
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPETSWEIMELLEEInRRGTTVL-IAtHDLELVDRMpKRVLELEDGRLVRDEARGV 223
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
360-585 |
6.76e-40 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 156.82 E-value: 6.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 360 VLDGISFaheavevfknfnlTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAISVVPQ 439
Cdd:PLN03130 1254 VLHGLSF-------------EISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQ 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 440 EPALFHRSIRENIayaRP--DATDEEVRDAAQKAHALEFIDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILI 517
Cdd:PLN03130 1321 APVLFSGTVRFNL---DPfnEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILV 1397
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083564009 518 LDEATSALDSESEVAVQKALKELMYGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGTHEELLKNSGT 585
Cdd:PLN03130 1398 LDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGS 1465
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
359-570 |
9.30e-40 |
|
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: 144.55 E-value: 9.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFA----HEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLL--LREYDiaGGAIKIDDQNIA---EVTQDS 429
Cdd:cd03255 1 IELKNLSKTygggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILggLDRPT--SGEVRVDGTDISklsEKELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 430 LRRA-ISVVPQEPALF-HRSIRENIAYARPDATDEEVRDAAQKAHALEFIDmLPEGMNTLVGErgvkLSGGQRQRVAIAR 507
Cdd:cd03255 79 FRRRhIGFVFQSFNLLpDLTALENVELPLLLAGVPKKERRERAEELLERVG-LGDRLNHYPSE----LSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1083564009 508 AILKDAPILILDEATSALDSESEVAVQKALKEL--MYGKTVIAIAHRLSTLRDMSRILVLEHGTI 570
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
360-569 |
1.22e-39 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 144.15 E-value: 1.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 360 VLDGISFAHE--AVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLL---LREYDiagGAIKIDDQNIAEVTQDSLRRAI 434
Cdd:cd03225 1 ELKNLSFSYPdgARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLnglLGPTS---GEVLVDGKDLTKLSLKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 435 SVVPQEPA--LFHRSIRENIAYA------RPDATDEEVRDAAQKAHALEFIDMLPEgmntlvgergvKLSGGQRQRVAIA 506
Cdd:cd03225 78 GLVFQNPDdqFFGPTVEEEVAFGlenlglPEEEIEERVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1083564009 507 RAILKDAPILILDEATSALDSESEVAVQKALKELM-YGKTVIAIAHRLSTLRDMS-RILVLEHGT 569
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKaEGKTIIIVTHDLDLLLELAdRVIVLEDGK 211
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
359-579 |
3.97e-39 |
|
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: 143.09 E-value: 3.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDI-----AGGAIKIDDQNIAEVTQD--SLR 431
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDvlELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 432 RAISVVPQEPALFHRSIRENIAYA-------RPDATDEEVRDAAQKAHalefidmLPEGMNTLVGERGvkLSGGQRQRVA 504
Cdd:cd03260 81 RRVGMVFQKPNPFPGSIYDNVAYGlrlhgikLKEELDERVEEALRKAA-------LWDEVKDRLHALG--LSGGQQQRLC 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 505 IARAILKDAPILILDEATSALDSESEVAVQKALKELMYGKTVIAIAH------RLSTlrdmsRILVLEHGTIQEDGTHEE 578
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHnmqqaaRVAD-----RTAFLLNGRLVEFGPTEQ 226
|
.
gi 1083564009 579 L 579
Cdd:cd03260 227 I 227
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
357-579 |
8.53e-39 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 145.99 E-value: 8.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 357 GEIVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLvsllLR-----EyDIAGGAIKIDDQNIAEVtqDSLR 431
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTL----LRmiaglE-DPTSGEILIGGRDVTDL--PPKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 432 RAISVVPQEPALF-HRSIRENIAYA------RPDATDEEVRDAAQKAHALEFIDMLPEGmntlvgergvkLSGGQRQRVA 504
Cdd:COG3839 75 RNIAMVFQSYALYpHMTVYENIAFPlklrkvPKAEIDRRVREAAELLGLEDLLDRKPKQ-----------LSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 505 IARAILKDAPILILDEATSALDSESEVAVQKALKEL--MYGKTVIAIAHRLS---TLRDmsRILVLEHGTIQEDGTHEEL 579
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLhrRLGTTTIYVTHDQVeamTLAD--RIAVMNDGRIQQVGTPEEL 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
359-593 |
1.05e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 142.54 E-value: 1.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVtqdslRRAISVVP 438
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 439 QEPAL---FHRSIRENIA---------YARPDATDeevRDAAqkAHALEFIDMlpEGM-NTLVGErgvkLSGGQRQRVAI 505
Cdd:COG1121 82 QRAEVdwdFPITVRDVVLmgrygrrglFRRPSRAD---REAV--DEALERVGL--EDLaDRPIGE----LSGGQQQRVLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 506 ARAILKDAPILILDEATSALDSESEVAVQKALKEL-MYGKTVIAIAHRLSTLRDM-SRILVLE-----HGTIQEDGTHEE 578
Cdd:COG1121 151 ARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREYfDRVLLLNrglvaHGPPEEVLTPEN 230
|
250
....*....|....*
gi 1083564009 579 LLKNSGTYATLWNHQ 593
Cdd:COG1121 231 LSRAYGGPVALLAHG 245
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
364-582 |
1.59e-38 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 148.90 E-value: 1.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 364 ISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAG---GAIKIDDQNIAEVTQDSLRRAISVVPQE 440
Cdd:COG1123 12 VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGRRIGMVFQD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 441 P--ALFHRSIRENIAYA--RPDATDEEVRDAAQKAhaLEFIdmlpeGMNTLVGERGVKLSGGQRQRVAIARAILKDAPIL 516
Cdd:COG1123 92 PmtQLNPVTVGDQIAEAleNLGLSRAEARARVLEL--LEAV-----GLERRLDRYPHQLSGGQRQRVAIAMALALDPDLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1083564009 517 ILDEATSALDSESEVAVQKALKELM--YGKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEELLKN 582
Cdd:COG1123 165 IADEPTTALDVTTQAEILDLLRELQreRGTTVLLITHDLGVVAEIAdRVVVMDDGRIVEDGPPEEILAA 233
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
359-581 |
2.00e-38 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 141.66 E-value: 2.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQD---SLRRAIS 435
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyELRRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 436 VVPQEPALF-HRSIRENIAYA---RPDATDEEVRDAAqkAHALEfidmlpegmntLVGERGVK------LSGGQRQRVAI 505
Cdd:COG1127 86 MLFQGGALFdSLTVFENVAFPlreHTDLSEAEIRELV--LEKLE-----------LVGLPGAAdkmpseLSGGMRKRVAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1083564009 506 ARAILKDAPILILDEATSALDSESEVAVQKALKEL--MYGKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEELLK 581
Cdd:COG1127 153 ARALALDPEILLYDEPTAGLDPITSAVIDELIRELrdELGLTSVVVTHDLDSAFAIAdRVAVLADGKIIAEGTPEELLA 231
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
352-589 |
2.62e-38 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 141.97 E-value: 2.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 352 LVAKKGEIVLDGISFAHEAV--EVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDS 429
Cdd:cd03288 13 LVGLGGEIKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 430 LRRAISVVPQEPALFHRSIRENIAYARpDATDEEVRDAAQKAHALEFIDMLPEGMNTLVGERGVKLSGGQRQRVAIARAI 509
Cdd:cd03288 93 LRSRLSIILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 510 LKDAPILILDEATSALDSESEVAVQKALKELMYGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGTHEELL-KNSGTYAT 588
Cdd:cd03288 172 VRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFAS 251
|
.
gi 1083564009 589 L 589
Cdd:cd03288 252 L 252
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
359-580 |
5.28e-38 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 140.28 E-value: 5.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVEvfKNFNLTIKDGERIGLVGKSGAGKSTLVSLllreydIAG------GAIKIDDQNIAEVTQDslRR 432
Cdd:COG3840 2 LRLDDLTYRYGDFP--LRFDLTIAAGERVAILGPSGAGKSTLLNL------IAGflppdsGRILWNGQDLTALPPA--ER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 433 AISVVPQEPALF-HRSIRENIAYA-----RPDATD-EEVRDAAQKAHALEFIDMLPEgmntlvgergvKLSGGQRQRVAI 505
Cdd:COG3840 72 PVSMLFQENNLFpHLTVAQNIGLGlrpglKLTAEQrAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 506 ARAILKDAPILILDEATSALDSesevavqkALKELM----------YGKTVIAIAHrlsTLRDMSRI----LVLEHGTIQ 571
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDP--------ALRQEMldlvdelcreRGLTVLMVTH---DPEDAARIadrvLLVADGRIA 209
|
....*....
gi 1083564009 572 EDGTHEELL 580
Cdd:COG3840 210 ADGPTAALL 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
359-573 |
4.59e-37 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 138.68 E-value: 4.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFA----HEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLllreydIAG------GAIKIDDQNIAEVTQD 428
Cdd:COG1116 8 LELRGVSKRfptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRL------IAGlekptsGEVLVDGKPVTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 429 slrraISVVPQEPALF-HRSIRENIAYARPDATdeeVRDAAQKAHALEFIDMlpegmntlVGERGVK------LSGGQRQ 501
Cdd:COG1116 82 -----RGVVFQEPALLpWLTVLDNVALGLELRG---VPKAERRERARELLEL--------VGLAGFEdayphqLSGGMRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 502 RVAIARAILKDAPILILDEATSALDSESEVAVQKALKELM--YGKTVIAIAH------RLSTlrdmsRILVLEH--GTIQ 571
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWqeTGKTVLFVTHdvdeavFLAD-----RVVVLSArpGRIV 220
|
..
gi 1083564009 572 ED 573
Cdd:COG1116 221 EE 222
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
361-569 |
5.30e-37 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 135.06 E-value: 5.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 361 LDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAISVVPQe 440
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 441 palfhrsireniayarpdatdeevrdaaqkahalefidmlpegmntlvgergvkLSGGQRQRVAIARAILKDAPILILDE 520
Cdd:cd00267 81 ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1083564009 521 ATSALDSESEVAVQKALKELMY-GKTVIAIAHRLSTLRDMS-RILVLEHGT 569
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAELAAdRVIVLKDGK 157
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
368-584 |
8.20e-37 |
|
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: 136.94 E-value: 8.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 368 HEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSL--LLREYDiaGGAIKIDDQNIAEVTQDSL---RRAISVVPQEPA 442
Cdd:cd03258 15 GGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCinGLERPT--SGSVLVDGTDLTLLSGKELrkaRRRIGMIFQHFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 443 LF-HRSIRENIAYARPDAtdeEVRDAAQKAHALEFIDMLpeGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDEA 521
Cdd:cd03258 93 LLsSRTVFENVALPLEIA---GVPKAEIEERVLELLELV--GLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1083564009 522 TSALDSESEVAVQKALKEL--MYGKTVIAIAHRLSTLRDM-SRILVLEHGTIQEDGTHEELLKNSG 584
Cdd:cd03258 168 TSALDPETTQSILALLRDInrELGLTIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
359-582 |
1.16e-36 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 137.05 E-value: 1.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVE-VFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAISVV 437
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 438 PQEPALF-HRSIRENIAYArpdATDEEVRDAAQKAHALEFIDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKDAPIL 516
Cdd:cd03295 81 IQQIGLFpHMTVEENIALV---PKLLKWPKEKIRERADELLALVGLDPAEFADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1083564009 517 ILDEATSALDSESEVAVQKALKEL--MYGKTVIAIAHRL-STLRDMSRILVLEHGTIQEDGTHEELLKN 582
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLqqELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
359-579 |
1.61e-36 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 139.85 E-value: 1.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLllreydIAG------GAIKIDDQNIAEVTQDslRR 432
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRM------IAGfetpdsGRILLDGRDVTGLPPE--KR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 433 AISVVPQEPALF-HRSIRENIAY---ARpdatdeEVRDAAQKAHALEFIDMLpeGMNTLvGERGVK-LSGGQRQRVAIAR 507
Cdd:COG3842 78 NVGMVFQDYALFpHLTVAENVAFglrMR------GVPKAEIRARVAELLELV--GLEGL-ADRYPHqLSGGQQQRVALAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 508 AILKDAPILILDEATSALDSESEVAVQKALKELM--YGKTVIAIAHrlstlrD------MS-RILVLEHGTIQEDGTHEE 578
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALDAKLREEMREELRRLQreLGITFIYVTH------DqeealaLAdRIAVMNDGRIEQVGTPEE 222
|
.
gi 1083564009 579 L 579
Cdd:COG3842 223 I 223
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
359-573 |
1.78e-36 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 135.68 E-value: 1.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISF----AHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVtqdslRRAI 434
Cdd:cd03293 1 LEVRNVSKtyggGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP-----GPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 435 SVVPQEPALF-HRSIRENIAYArPDATDeeVRDAAQKAHALEFIDMlpegmntlVGERGVK------LSGGQRQRVAIAR 507
Cdd:cd03293 76 GYVFQQDALLpWLTVLDNVALG-LELQG--VPKAEARERAEELLEL--------VGLSGFEnayphqLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1083564009 508 AILKDAPILILDEATSALDSESEVAVQKALKELM--YGKTVIAIAHRLS---TLRDmsRILVLE--HGTIQED 573
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWreTGKTVLLVTHDIDeavFLAD--RVVVLSarPGRIVAE 215
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
359-574 |
4.47e-36 |
|
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: 134.30 E-value: 4.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVtqDSLRRAISVVP 438
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDL--PPKDRDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 439 QEPALF-HRSIRENIAY------ARPDATDEEVRDAAQKAHALEFIDMLPEgmntlvgergvKLSGGQRQRVAIARAILK 511
Cdd:cd03301 79 QNYALYpHMTVYDNIAFglklrkVPKDEIDERVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRAIVR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083564009 512 DAPILILDEATSALDSESEVAVQKALKELM--YGKTVIAIAH---RLSTLRDmsRILVLEHGTIQEDG 574
Cdd:cd03301 148 EPKVFLMDEPLSNLDAKLRVQMRAELKRLQqrLGTTTIYVTHdqvEAMTMAD--RIAVMNDGQIQQIG 213
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
355-582 |
4.71e-36 |
|
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: 137.49 E-value: 4.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 355 KKGEI-VLDGISFaheavevfknfnlTIKDGERIGLVGKSGAGKSTLVSLLLR---EYDIAGGAIKIDDQNIAEVTQDSL 430
Cdd:COG0444 14 RRGVVkAVDGVSF-------------DVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 431 R----RAISVVPQEP--AL--FHR---SIRENIAYARpDATDEEVRDAAqkahalefIDMLpegmnTLVG----ERGVK- 494
Cdd:COG0444 81 RkirgREIQMIFQDPmtSLnpVMTvgdQIAEPLRIHG-GLSKAEARERA--------IELL-----ERVGlpdpERRLDr 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 495 ----LSGGQRQRVAIARAILKDAPILILDEATSALDseseVAVQKA----LKELM--YGKTVIAIAHRLSTLRDMS-RIL 563
Cdd:COG0444 147 ypheLSGGMRQRVMIARALALEPKLLIADEPTTALD----VTIQAQilnlLKDLQreLGLAILFITHDLGVVAEIAdRVA 222
|
250
....*....|....*....
gi 1083564009 564 VLEHGTIQEDGTHEELLKN 582
Cdd:COG0444 223 VMYAGRIVEEGPVEELFEN 241
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
359-582 |
6.31e-36 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 137.52 E-value: 6.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGIS--FAH--EAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSL--LLREYDiaGGAIKIDDQNIAEVTQDSLRR 432
Cdd:COG1135 2 IELENLSktFPTkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCinLLERPT--SGSVLVDGVDLTALSERELRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 433 A---ISVVPQEPALFH-RSIRENIAY----ARpdatdeeVRDAAQKAHALEFIDmlpegmntLVG--ERG----VKLSGG 498
Cdd:COG1135 80 ArrkIGMIFQHFNLLSsRTVAENVALpleiAG-------VPKAEIRKRVAELLE--------LVGlsDKAdaypSQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 499 QRQRVAIARAILKDAPILILDEATSALDSESEVAVQKALKEL--MYGKTVIAIAHRLSTLRDM-SRILVLEHGTIQEDGT 575
Cdd:COG1135 145 QKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDInrELGLTIVLITHEMDVVRRIcDRVAVLENGRIVEQGP 224
|
....*..
gi 1083564009 576 HEELLKN 582
Cdd:COG1135 225 VLDVFAN 231
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
361-574 |
1.91e-35 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 131.40 E-value: 1.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 361 LDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAISVVPQe 440
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 441 palfhrsireniayarpdatdeevrdaaqkahALEFIDMLPegmntlVGERGVK-LSGGQRQRVAIARAILKDAPILILD 519
Cdd:cd03214 81 --------------------------------ALELLGLAH------LADRPFNeLSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1083564009 520 EATSALDSESEVAVQKALKEL--MYGKTVIAIAHRLS-TLRDMSRILVLEHGTIQEDG 574
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLarERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
359-581 |
5.88e-35 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 131.86 E-value: 5.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQD---SLRRAIS 435
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 436 VVPQEPALF-HRSIRENIA---YARPDATDEEVRDAaqkahALEFIDM--LPEGMNTLVGErgvkLSGGQRQRVAIARAI 509
Cdd:cd03261 81 MLFQSGALFdSLTVFENVAfplREHTRLSEEEIREI-----VLEKLEAvgLRGAEDLYPAE----LSGGMKKRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1083564009 510 LKDAPILILDEATSALDSESEVAVQKALKEL--MYGKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEELLK 581
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDLDTAFAIAdRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
359-570 |
1.91e-34 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 128.28 E-value: 1.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEvTQDSLRRAISVVP 438
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 439 QEPALFHR-SIRENIayarpdatdeevrdaaqkahalefidmlpegmntlvgergvKLSGGQRQRVAIARAILKDAPILI 517
Cdd:cd03230 80 EEPSLYENlTVRENL-----------------------------------------KLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1083564009 518 LDEATSALDSESEVAVQKALKELM-YGKTVIAIAHRLSTLRDMS-RILVLEHGTI 570
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKkEGKTILLSSHILEEAERLCdRVAILNNGRI 173
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
370-582 |
2.73e-34 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 130.11 E-value: 2.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 370 AVEVFKNFNLTIKDGERIGLVGKSGAGKSTLvsllLR-----EyDIAGGAIKIDDQNIA--EVTQDSLRRAISVVPQEPA 442
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTL----LRcinllE-EPDSGTITVDGEDLTdsKKDINKLRRKVGMVFQQFN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 443 LF-HRSIRENIAYA------RPDAtdeevrDAAQKAHAL-------EFIDMLPEgmntlvgergvKLSGGQRQRVAIARA 508
Cdd:COG1126 88 LFpHLTVLENVTLApikvkkMSKA------EAEERAMELlervglaDKADAYPA-----------QLSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083564009 509 ILKDAPILILDEATSALDSE--SEV-AVQKALKELmyGKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEELLKN 582
Cdd:COG1126 151 LAMEPKVMLFDEPTSALDPElvGEVlDVMRDLAKE--GMTMVVVTHEMGFAREVAdRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
374-574 |
1.19e-33 |
|
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: 127.80 E-value: 1.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 374 FKNFNLTIK---DGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQniaeVTQDS--------LRRAISVVPQEPA 442
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT----VLFDSrkkinlppQQRKIGLVFQQYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 443 LF-HRSIRENIAYARPDATDEEVRDAAQkahalEFIDMLpeGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDEA 521
Cdd:cd03297 86 LFpHLNVRENLAFGLKRKRNREDRISVD-----ELLDLL--GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1083564009 522 TSALDSESEVAVQKALKELM--YGKTVIAIAHRLSTLRDM-SRILVLEHGTIQEDG 574
Cdd:cd03297 159 FSALDRALRLQLLPELKQIKknLNIPVIFVTHDLSEAEYLaDRIVVMEDGRLQYIG 214
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
353-578 |
1.22e-33 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 131.99 E-value: 1.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 353 VAKKGEIVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLllreydIAG------GAIKIDDQNIAEVT 426
Cdd:PRK09452 9 SSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRL------IAGfetpdsGRIMLDGQDITHVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 427 QDslRRAISVVPQEPALF-HRSIRENIAYA-----RPDA-TDEEVRDAAQKAHALEFIDMLPEgmntlvgergvKLSGGQ 499
Cdd:PRK09452 83 AE--NRHVNTVFQSYALFpHMTVFENVAFGlrmqkTPAAeITPRVMEALRMVQLEEFAQRKPH-----------QLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 500 RQRVAIARAILKDAPILILDEATSALDSESEVAVQKALKELM--YGKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTH 576
Cdd:PRK09452 150 QQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQrkLGITFVFVTHDQEEALTMSdRIVVMRDGRIEQDGTP 229
|
..
gi 1083564009 577 EE 578
Cdd:PRK09452 230 RE 231
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
344-582 |
2.30e-33 |
|
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: 128.53 E-value: 2.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 344 IDVENAQDLVAKKGEIVLDGISFAHEAVEVFK---------NFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGA 414
Cdd:cd03294 1 IKIKGLYKIFGKNPQKAFKLLAKGKSKEEILKktgqtvgvnDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 415 IKIDDQNIAEVTQDSL----RRAISVVPQEPALF-HRSIRENIAYARPDA-TDEEVRdAAQKAHALEFIDMlpEGM-NTL 487
Cdd:cd03294 81 VLIDGQDIAAMSRKELrelrRKKISMVFQSFALLpHRTVLENVAFGLEVQgVPRAER-EERAAEALELVGL--EGWeHKY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 488 VGErgvkLSGGQRQRVAIARAILKDAPILILDEATSALDSESEVAVQKALKEL--MYGKTVIAIAHRLS-TLRDMSRILV 564
Cdd:cd03294 158 PDE----LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLqaELQKTIVFITHDLDeALRLGDRIAI 233
|
250
....*....|....*...
gi 1083564009 565 LEHGTIQEDGTHEELLKN 582
Cdd:cd03294 234 MKDGRLVQVGTPEEILTN 251
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
361-568 |
4.74e-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: 4.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 361 LDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVtqdslRRAISVVPQe 440
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVPQ- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 441 palfhrsiRENIAYARPdATDEEV----------------RDAAQKA-HALEFIDMLpEGMNTLVGErgvkLSGGQRQRV 503
Cdd:cd03235 76 --------RRSIDRDFP-ISVRDVvlmglyghkglfrrlsKADKAKVdEALERVGLS-ELADRQIGE----LSGGQQQRV 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1083564009 504 AIARAILKDAPILILDEATSALDSESEVAVQKALKEL-MYGKTVIAIAHRLSTLRD-MSRILVLEHG 568
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEyFDRVLLLNRT 208
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
359-579 |
1.09e-32 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 125.94 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEA-VEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRA---I 434
Cdd:COG3638 3 LELRNLSKRYPGgTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrrrI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 435 SVVPQEPALFHR-SIRENI-----------AYARPDATDEEVRDAAQkahALEFIDMLPegmntLVGERGVKLSGGQRQR 502
Cdd:COG3638 83 GMIFQQFNLVPRlSVLTNVlagrlgrtstwRSLLGLFPPEDRERALE---ALERVGLAD-----KAYQRADQLSGGQQQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 503 VAIARAILKDAPILILDEATSALDSESEVAVQKALKELM--YGKTVIAIAHRLST-LRDMSRILVLEHGTIQEDGTHEEL 579
Cdd:COG3638 155 VAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAreDGITVVVNLHQVDLaRRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
377-570 |
3.74e-32 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 123.43 E-value: 3.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 377 FNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIaeVTQDSLRRAISVVPQEPALF-HRSIRENIAYA 455
Cdd:TIGR01277 17 FDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSH--TGLAPYQRPVSMLFQENNLFaHLTVRQNIGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 456 -RPD-----ATDEEVRDAAQKAHALEFIDMLPEgmntlvgergvKLSGGQRQRVAIARAILKDAPILILDEATSALDSES 529
Cdd:TIGR01277 95 lHPGlklnaEQQEKVVDAAQQVGIADYLDRLPE-----------QLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1083564009 530 EVAVQKALKELMYGK--TVIAIAHRLSTLRDM-SRILVLEHGTI 570
Cdd:TIGR01277 164 REEMLALVKQLCSERqrTLLMVTHHLSDARAIaSQIAVVSQGKI 207
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
359-583 |
1.34e-31 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 131.44 E-value: 1.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFaheavevfknfnlTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAISVVP 438
Cdd:PTZ00243 1324 LVLRGVSF-------------RIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIP 1390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 439 QEPALFHRSIRENIayaRP--DATDEEVRDAAQKAHALEFIDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKDAPIL 516
Cdd:PTZ00243 1391 QDPVLFDGTVRQNV---DPflEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGF 1467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083564009 517 IL-DEATSALDSESEVAVQKALKELMYGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGTHEELLKNS 583
Cdd:PTZ00243 1468 ILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNR 1535
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
358-590 |
4.20e-31 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 124.10 E-value: 4.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 358 EIVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLllreydIAG------GAIKIDDQNiAEVTQDSLR 431
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRI------IAGletpdsGRIVLNGRD-LFTNLPPRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 432 RAISVVPQEPALF-HRSIRENIAYArpdATDEEVRDAAQKAHALEFIDMLpeGMNTLVGERGVKLSGGQRQRVAIARAIL 510
Cdd:COG1118 75 RRVGFVFQHYALFpHMTVAENIAFG---LRVRPPSKAEIRARVEELLELV--QLEGLADRYPSQLSGGQRQRVALARALA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 511 KDAPILILDEATSALDSesevAVQKAL-KELM-----YGKTVIAIAH------RLStlrdmSRILVLEHGTIQEDGTHEE 578
Cdd:COG1118 150 VEPEVLLLDEPFGALDA----KVRKELrRWLRrlhdeLGGTTVFVTHdqeealELA-----DRVVVMNQGRIEQVGTPDE 220
|
250
....*....|..
gi 1083564009 579 LLKNSGTYATLW 590
Cdd:COG1118 221 VYDRPATPFVAR 232
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
377-589 |
1.12e-30 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 119.69 E-value: 1.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 377 FNLTIKDGERIGLVGKSGAGKSTLVSLllreydIAG------GAIKIDDQNIAEVTQDslRRAISVVPQEPALF-HRSIR 449
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNL------IAGfltpasGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFsHLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 450 ENIAYA-RP-----DATDEEVRDAAQKAHALEFIDMLPEgmntlvgergvKLSGGQRQRVAIARAILKDAPILILDEATS 523
Cdd:PRK10771 90 QNIGLGlNPglklnAAQREKLHAIARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1083564009 524 ALDSE---------SEVAVQKALKELMygktviaIAHRLS-TLRDMSRILVLEHGTIQEDGTHEELLKNSGTYATL 589
Cdd:PRK10771 159 ALDPAlrqemltlvSQVCQERQLTLLM-------VSHSLEdAARIAPRSLVVADGRIAWDGPTDELLSGKASASAL 227
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
375-582 |
1.65e-30 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 119.36 E-value: 1.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 375 KNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDslRRAISVVPQEPALF-HRSIRENIA 453
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 454 YA-----RPDAT-DEEVRDAAQKAHALEFIDMLPEgmntlvgergvKLSGGQRQRVAIARAILKDAPILILDEATSALDS 527
Cdd:cd03299 94 YGlkkrkVDKKEiERKVLEIAEMLGIDHLLNRKPE-----------TLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1083564009 528 ESEVAVQKALKELM--YGKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEELLKN 582
Cdd:cd03299 163 RTKEKLREELKKIRkeFGVTVLHVTHDFEEAWALAdKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
368-582 |
2.31e-30 |
|
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: 125.18 E-value: 2.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 368 HEAVevfKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDiAGGAIKIDDQNIAEVTQD---SLRRAISVVPQEP--A 442
Cdd:COG4172 299 VKAV---DGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRalrPLRRRMQVVFQDPfgS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 443 LFHR-----SIRENIAYARPDATDEEVRDAAQKAhaLEFIDMLPEGMNTLVGErgvkLSGGQRQRVAIARA-ILKdaP-I 515
Cdd:COG4172 375 LSPRmtvgqIIAEGLRVHGPGLSAAERRARVAEA--LEEVGLDPAARHRYPHE----FSGGQRQRIAIARAlILE--PkL 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1083564009 516 LILDEATSALDseseVAVQKA----LKELM--YGKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEELLKN 582
Cdd:COG4172 447 LVLDEPTSALD----VSVQAQildlLRDLQreHGLAYLFISHDLAVVRALAhRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
361-565 |
2.64e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 124.75 E-value: 2.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 361 LDGIS--FAheAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQniaEV----TQDSLRRAI 434
Cdd:COG1129 7 MRGISksFG--GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGE---PVrfrsPRDAQAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 435 SVVPQEPALF-HRSIRENIAYARPDATDEEVRDAAQKAHALEFIDMLpeGMN----TLVGErgvkLSGGQRQRVAIARAI 509
Cdd:COG1129 82 AIIHQELNLVpNLSVAENIFLGREPRRGGLIDWRAMRRRARELLARL--GLDidpdTPVGD----LSVAQQQLVEIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1083564009 510 LKDAPILILDEATSALdSESEV----AVQKALKELmyGKTVIAIAHRLSTLRDMS-RILVL 565
Cdd:COG1129 156 SRDARVLILDEPTASL-TEREVerlfRIIRRLKAQ--GVAIIYISHRLDEVFEIAdRVTVL 213
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
376-583 |
3.34e-30 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 127.16 E-value: 3.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 376 NFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIddqniaevtqdsLRRAISVVPQEPALFHRSIRENIAYA 455
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVAYVPQVSWIFNATVRDNILFG 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 456 RP-DATD-EEVRDAAQKAHALefiDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDEATSALDseSEVAV 533
Cdd:PLN03130 703 SPfDPERyERAIDVTALQHDL---DLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD--AHVGR 777
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1083564009 534 Q---KALKELMYGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGTHEELLKNS 583
Cdd:PLN03130 778 QvfdKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNG 830
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
359-579 |
5.31e-30 |
|
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: 118.05 E-value: 5.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAH-EAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRA---I 434
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrqI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 435 SVVPQEPALFHR-SIRENIAYARPDA-----------TDEEVRDAaqkAHALEFIDMLpegmnTLVGERGVKLSGGQRQR 502
Cdd:cd03256 81 GMIFQQFNLIERlSVLENVLSGRLGRrstwrslfglfPKEEKQRA---LAALERVGLL-----DKAYQRADQLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 503 VAIARAILKDAPILILDEATSALDSESEVAVQKALKEL--MYGKTVIAIAHRLSTLRD-MSRILVLEHGTIQEDGTHEEL 579
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
359-579 |
5.71e-30 |
|
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: 117.72 E-value: 5.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLllreydIAG------GAIKIDDQNIAEVtqDSLRR 432
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRL------IAGfetptsGEILLDGKDITNL--PPHKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 433 AISVVPQEPALF-HRSIRENIAYArpdATDEEVRDAAQKAHALEFIDMLpeGMNTLVGERGVKLSGGQRQRVAIARAILK 511
Cdd:cd03300 73 PVNTVFQNYALFpHLTVFENIAFG---LRLKKLPKAEIKERVAEALDLV--QLEGYANRKPSQLSGGQQQRVAIARALVN 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1083564009 512 DAPILILDEATSALDSESEVAVQKALKEL--MYGKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEEL 579
Cdd:cd03300 148 EPKVLLLDEPLGALDLKLRKDMQLELKRLqkELGITFVFVTHDQEEALTMSdRIAVMNKGKIQQIGTPEEI 218
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
318-587 |
1.23e-29 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 125.06 E-value: 1.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 318 FMINNISQIYSEAEEGLVAISQ-----AHEVIDVENAQDLVAKKGE---IVLDGISF--AHEAVEVFKNFNLTIKDGERI 387
Cdd:TIGR00957 588 FPLNILPMVISSIVQASVSLKRlriflSHEELEPDSIERRTIKPGEgnsITVHNATFtwARDLPPTLNGITFSIPEGALV 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 388 GLVGKSGAGKSTLVSLLLREYDIAGGAIkiddqniaevtqdSLRRAISVVPQEPALFHRSIRENIAYARPdATDEEVRDA 467
Cdd:TIGR00957 668 AVVGQVGCGKSSLLSALLAEMDKVEGHV-------------HMKGSVAYVPQQAWIQNDSLRENILFGKA-LNEKYYQQV 733
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 468 AQKAHALEFIDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDEATSALDSEsevaVQKALKE-------L 540
Cdd:TIGR00957 734 LEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH----VGKHIFEhvigpegV 809
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1083564009 541 MYGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGTHEELLKNSGTYA 587
Cdd:TIGR00957 810 LKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFA 856
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
372-570 |
1.62e-29 |
|
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: 116.09 E-value: 1.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 372 EVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQD--SLRRAISVVPQEPALF-HRSI 448
Cdd:cd03262 14 HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinELRQKVGMVFQQFNLFpHLTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 449 RENIAYA-------RPDATDEEVRDAAQKAHALEFIDMLPegmntlvgergVKLSGGQRQRVAIARAILKDAPILILDEA 521
Cdd:cd03262 94 LENITLApikvkgmSKAEAEERALELLEKVGLADKADAYP-----------AQLSGGQQQRVAIARALAMNPKVMLFDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1083564009 522 TSALDSESEVAVQKALKELMY-GKTVIAIAHRLSTLRDMS-RILVLEHGTI 570
Cdd:cd03262 163 TSALDPELVGEVLDVMKDLAEeGMTMVVVTHEMGFAREVAdRVIFMDDGRI 213
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
376-589 |
1.78e-29 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 124.70 E-value: 1.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 376 NFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYdiaggaikiddqNIAEVTQDSLRRAISVVPQEPALFHRSIRENIAYA 455
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISAMLGEL------------SHAETSSVVIRGSVAYVPQVSWIFNATVRENILFG 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 456 RPDATDEEVR--DAAQKAHALefiDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDEATSALDseSEVAV 533
Cdd:PLN03232 703 SDFESERYWRaiDVTALQHDL---DLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALD--AHVAH 777
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1083564009 534 Q---KALKELMYGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGTHEELLKNSGTYATL 589
Cdd:PLN03232 778 QvfdSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKL 836
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
376-570 |
1.82e-29 |
|
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: 115.97 E-value: 1.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 376 NFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDS---LRRAISVVPQEPALF-HRSIREN 451
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKIGVVFQDFRLLpDRNVYEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 452 IAYARpDATDEEVRDAAQK-AHALEFIDmLPEGMNTLVGErgvkLSGGQRQRVAIARAILKDAPILILDEATSALDSESE 530
Cdd:cd03292 99 VAFAL-EVTGVPPREIRKRvPAALELVG-LSHKHRALPAE----LSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1083564009 531 VAVQKALKEL-MYGKTVIAIAHRLSTLRDMS-RILVLEHGTI 570
Cdd:cd03292 173 WEIMNLLKKInKAGTTVVVATHAKELVDTTRhRVIALERGKL 214
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
361-582 |
4.03e-29 |
|
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: 115.22 E-value: 4.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 361 LDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEV-TQDSLRRAISVVPQ 439
Cdd:cd03224 3 VENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLpPHERARAGIGYVPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 440 EPALFHR-SIRENI---AYARPDATDEEVRDaaqkaHALEFIDMLPEGMNTLVGErgvkLSGGQRQRVAIARAILKDAPI 515
Cdd:cd03224 83 GRRIFPElTVEENLllgAYARRRAKRKARLE-----RVYELFPRLKERRKQLAGT----LSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1083564009 516 LILDEATSALdseSEVAVQ------KALKELmyGKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEELLKN 582
Cdd:cd03224 154 LLLDEPSEGL---APKIVEeifeaiRELRDE--GVTILLVEQNARFALEIAdRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
370-579 |
4.20e-29 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 115.86 E-value: 4.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 370 AVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSL---RRAISVVPQEPALFHR 446
Cdd:TIGR02315 14 GKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLrklRRRIGMIFQHYNLIER 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 447 -SIRENIAYARPdATDEEVRD------AAQKAHALEFIDMLpeGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILD 519
Cdd:TIGR02315 94 lTVLENVLHGRL-GYKPTWRSllgrfsEEDKERALSALERV--GLADKAYQRADQLSGGQQQRVAIARALAQQPDLILAD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1083564009 520 EATSALDSESEVAVQKALKELM--YGKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEEL 579
Cdd:TIGR02315 171 EPIASLDPKTSKQVMDYLKRINkeDGITVIINLHQVDLAKKYAdRIVGLKAGEIVFDGAPSEL 233
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
370-583 |
5.33e-29 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 115.19 E-value: 5.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 370 AVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNI--AEVTQDSLRRAISVVPQEPALF-HR 446
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQEAGMVFQQFYLFpHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 447 SIRENIAYARPDATDEEVRDAAQKAHALEFIDMLPEGMNTLVGErgvkLSGGQRQRVAIARAILKDAPILILDEATSALD 526
Cdd:PRK09493 93 TALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSE----LSGGQQQRVAIARALAVKPKLMLFDEPTSALD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1083564009 527 SESEVAVQKALKELM-YGKTVIAIAHRLSTLRDM-SRILVLEHGTIQEDGTHEELLKNS 583
Cdd:PRK09493 169 PELRHEVLKVMQDLAeEGMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIKNP 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
359-578 |
8.68e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 120.55 E-value: 8.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIddqniaevtQDSLRraISVVP 438
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL---------GETVK--IGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 439 QEPALFH--RSIRENIAYARPDATDEEVRDAAQkahalefiDML--PEGMNTLVGergvKLSGGQRQRVAIARAILKDAP 514
Cdd:COG0488 385 QHQEELDpdKTVLDELRDGAPGGTEQEVRGYLG--------RFLfsGDDAFKPVG----VLSGGEKARLALAKLLLSPPN 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083564009 515 ILILDEATSALDSESEVAVQKALKElmYGKTVIAIAH-R--LSTLRDmsRILVLEHGTIQE-DGTHEE 578
Cdd:COG0488 453 VLLLDEPTNHLDIETLEALEEALDD--FPGTVLLVSHdRyfLDRVAT--RILEFEDGGVREyPGGYDD 516
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
359-567 |
1.02e-28 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 113.34 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTqDSLRRAISVVP 438
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-EDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 439 QEPALF-HRSIRENIAYARpdATDEEVRDAAQKAHALEFIDmLPEGMNTLVGergvKLSGGQRQRVAIARAILKDAPILI 517
Cdd:COG4133 82 HADGLKpELTVRENLRFWA--ALYGLRADREAIDEALEAVG-LAGLADLPVR----QLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1083564009 518 LDEATSALDSESEVAVQKALKE-LMYGKTVIAIAHRLSTLRDMsRILVLEH 567
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAhLARGGAVLLTTHQPLELAAA-RVLDLGD 204
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
373-580 |
1.23e-28 |
|
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: 115.34 E-value: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 373 VFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGgAIKIDDQNIAEVTQDSLRRAISVVPQEPALFHRSIRENI 452
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEG-DIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 453 -AYARpdATDEEVRDAAQKAHALEFIDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDEATSALDSESEV 531
Cdd:cd03289 98 dPYGK--WSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQ 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1083564009 532 AVQKALKELMYGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGTHEELL 580
Cdd:cd03289 176 VIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLL 224
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
359-574 |
1.23e-28 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 113.44 E-value: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVEVFKNFNLTIKDGeRIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEvTQDSLRRAISVVP 438
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 439 QEPALFHR-SIRENIAYArpdATDEEVRDAAQKAHALEFIDMLpeGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILI 517
Cdd:cd03264 79 QEFGVYPNfTVREFLDYI---AWLKGIPSKEVKARVDEVLELV--NLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1083564009 518 LDEATSALDSESEVAVQKALKELMYGKTVIAIAHRLSTLRDM-SRILVLEHGTIQEDG 574
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
282-580 |
1.56e-28 |
|
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: 121.94 E-value: 1.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 282 LALLIIS-FQQGTATSGDfvlvfalISSVWRELTRIgFMINNISQIYSEAEEGLVAISQAHE-VIDVENAQDLVAKKGEI 359
Cdd:TIGR01271 1147 LAMNILStLQWAVNSSID-------VDGLMRSVSRV-FKFIDLPQEEPRPSGGGGKYQLSTVlVIENPHAQKCWPSGGQM 1218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 360 VLDGIS--FAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGgAIKIDDQNIAEVTQDSLRRAISVV 437
Cdd:TIGR01271 1219 DVQGLTakYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEG-EIQIDGVSWNSVTLQTWRKAFGVI 1297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 438 PQEPALFHRSIRENI-AYARpdATDEEVRDAAQKAHALEFIDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKDAPIL 516
Cdd:TIGR01271 1298 PQKVFIFSGTFRKNLdPYEQ--WSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKIL 1375
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1083564009 517 ILDEATSALDSESEVAVQKALKELMYGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGTHEELL 580
Cdd:TIGR01271 1376 LLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLL 1439
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
361-570 |
1.68e-28 |
|
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: 112.74 E-value: 1.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 361 LDGISFA-HEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTqdsLRRAISVVPQ 439
Cdd:cd03226 2 IENISFSyKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE---RRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 440 EP--ALFHRSIRENIAYARPDATDeevrDAAQKAHALEFIDMlpegmNTLVGERGVKLSGGQRQRVAIARAILKDAPILI 517
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKELDA----GNEQAETVLKDLDL-----YALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1083564009 518 LDEATSALDSESEVAVQKALKELM-YGKTVIAIAHRLSTLRDM-SRILVLEHGTI 570
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLAKVcDRVLLLANGAI 204
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
359-584 |
1.95e-28 |
|
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: 114.45 E-value: 1.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVEVF--KNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIaeVTQDSL---RRA 433
Cdd:TIGR04520 1 IEVENVSFSYPESEKPalKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDT--LDEENLweiRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 434 ISVVPQEP--ALFHRSIRENIAYA------RPDATDEEVRDAAQKAHALEFIDMLPEgmntlvgergvKLSGGQRQRVAI 505
Cdd:TIGR04520 79 VGMVFQNPdnQFVGATVEDDVAFGlenlgvPREEMRKRVDEALKLVGMEDFRDREPH-----------LLSGGQKQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 506 ARAILKDAPILILDEATSALDSESEVAVQKALKELM--YGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGT------HE 577
Cdd:TIGR04520 148 AGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTpreifsQV 227
|
....*..
gi 1083564009 578 ELLKNSG 584
Cdd:TIGR04520 228 ELLKEIG 234
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
361-582 |
1.97e-28 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 115.98 E-value: 1.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 361 LDGISFaheavevfknfnlTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSL---RRAISVV 437
Cdd:COG4608 34 VDGVSF-------------DIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplRRRMQMV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 438 PQEP--ALFHR-----SIRENIAYARpDATDEEVRDAAQKAhaLEFIDMLPEGMNTLVGErgvkLSGGQRQRVAIARAIL 510
Cdd:COG4608 101 FQDPyaSLNPRmtvgdIIAEPLRIHG-LASKAERRERVAEL--LELVGLRPEHADRYPHE----FSGGQRQRIGIARALA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 511 KDAPILILDEATSALDseseVAVQkA-----LKELM--YGKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEELLKN 582
Cdd:COG4608 174 LNPKLIVCDEPVSALD----VSIQ-AqvlnlLEDLQdeLGLTYLFISHDLSVVRHISdRVAVMYLGKIVEIAPRDELYAR 248
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
359-553 |
3.73e-28 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 113.59 E-value: 3.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYD-IAG----GAIKIDDQNIAEVTQD--SLR 431
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDlIPGarveGEILLDGEDIYDPDVDvvELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 432 RAISVVPQEPALFHRSIRENIAYA-------RPDATDEEVRDAAQKAhAL--EFIDMLpegmntlvGERGVKLSGGQRQR 502
Cdd:COG1117 92 RRVGMVFQKPNPFPKSIYDNVAYGlrlhgikSKSELDEIVEESLRKA-ALwdEVKDRL--------KKSALGLSGGQQQR 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1083564009 503 VAIARAILKDAPILILDEATSALDSESEVAVQKALKELmygK---TVIAIAHRL 553
Cdd:COG1117 163 LCIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL---KkdyTIVIVTHNM 213
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
357-569 |
5.60e-28 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 118.37 E-value: 5.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 357 GEIVLDGISFAHEAVEV-FKNFNLTIKDGERIGLVGKSGAGKSTLvsllLREydIAG------GAIKIDDQniaevtQDS 429
Cdd:COG4178 361 GALALEDLTLRTPDGRPlLEDLSLSLKPGERLLITGPSGSGKSTL----LRA--IAGlwpygsGRIARPAG------ARV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 430 LrraisVVPQEPALFHRSIRENIAYARP--DATDEEVRDAAQKAHALEFIDMLPEGMNtlvgeRGVKLSGGQRQRVAIAR 507
Cdd:COG4178 429 L-----FLPQRPYLPLGTLREALLYPATaeAFSDAELREALEAVGLGHLAERLDEEAD-----WDQVLSLGEQQRLAFAR 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1083564009 508 AILKDAPILILDEATSALDSESEVAVQKALKELMYGKTVIAIAHRlSTLRDM-SRILVLEHGT 569
Cdd:COG4178 499 LLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR-STLAAFhDRVLELTGDG 560
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
355-582 |
2.08e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 111.62 E-value: 2.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 355 KKGEIVLDGISFAHEAVE--VFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRR 432
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 433 AISVVPQEP--ALFHRSIRENIAYA------RPDATDEEVRDAAQKAHALEFIDMLPEgmntlvgergvKLSGGQRQRVA 504
Cdd:PRK13632 84 KIGIIFQNPdnQFIGATVEDDIAFGlenkkvPPKKMKDIIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 505 IARAILKDAPILILDEATSALDSESEVAVQKALKEL--MYGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGTHEELLKN 582
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLrkTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
389-600 |
7.69e-27 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 111.43 E-value: 7.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 389 LVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDslRRAISVVPQEPALF-HRSIRENIAYA-RPDATDEEVRD 466
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH--LRHINMVFQSYALFpHMTVEENVAFGlKMRKVPRAEIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 467 AAQKAhALEFIDMlpegmNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDEATSALDSESEVAVQKALKELMY--GK 544
Cdd:TIGR01187 79 PRVLE-ALRLVQL-----EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEqlGI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1083564009 545 TVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEELlknsgtYATLWNHQAGGFLQE 600
Cdd:TIGR01187 153 TFVFVTHDQEEAMTMSdRIAIMRKGKIAQIGTPEEI------YEEPANLFVARFIGE 203
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
359-580 |
8.68e-27 |
|
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: 109.40 E-value: 8.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLRE-YDIAGGAIKIDDQNIAEVTQDSLRRAISVV 437
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlPPTYGNDVRLFGERRGGEDVWELRKRIGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 438 pqEPALfHRSIRENI---------AYA---RPDATDEEvrdaaQKAHALEFIDMLpeGMNTLVGERGVKLSGGQRQRVAI 505
Cdd:COG1119 84 --SPAL-QLRFPRDEtvldvvlsgFFDsigLYREPTDE-----QRERARELLELL--GLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083564009 506 ARAILKDAPILILDEATSALDSESEVAVQKALKELM--YGKTVIAIAHRLSTLRD-MSRILVLEHGTIQEDGTHEELL 580
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLAaeGAPTLVLVTHHVEEIPPgITHVLLLKDGRVVAAGPKEEVL 231
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
359-582 |
1.72e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 109.37 E-value: 1.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVevfKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAE--VTQDSLRRAISV 436
Cdd:PRK13637 11 IYMEGTPFEKKAL---DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDIRKKVGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 437 VPQEP--ALFHRSIRENIAYA--RPDATDEEVRDAAQKAHAL------EFIDMLPegmntlvgergVKLSGGQRQRVAIA 506
Cdd:PRK13637 88 VFQYPeyQLFEETIEKDIAFGpiNLGLSEEEIENRVKRAMNIvgldyeDYKDKSP-----------FELSGGQKRRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 507 RAILKDAPILILDEATSALDSESEVAVQKALKELM--YGKTVIAIAHrlsTLRDMS----RILVLEHGTIQEDGTHEELL 580
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHkeYNMTIILVSH---SMEDVAkladRIIVMNKGKCELQGTPREVF 233
|
..
gi 1083564009 581 KN 582
Cdd:PRK13637 234 KE 235
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
376-569 |
2.27e-26 |
|
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: 107.42 E-value: 2.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 376 NFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAI----KIDDQNIAEVTQDSLRRAISVVPQEPALFHRSIREN 451
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYSVAYAAQKPWLLNATVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 452 IAYARPdaTDEEVRDAAQKAHALE-FIDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDEATSALDSE-S 529
Cdd:cd03290 99 ITFGSP--FNKQRYKAVTDACSLQpDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1083564009 530 EVAVQKALKELMYG--KTVIAIAHRLSTLRDMSRILVLEHGT 569
Cdd:cd03290 177 DHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
361-571 |
3.18e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 112.47 E-value: 3.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 361 LDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIddqniaevtQDSLRraISVVPQE 440
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------PKGLR--IGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 441 PALF-HRSIRENI----------------AYARPDATDEEVRDAAQKAHALEFID----------ML------PEGMNTL 487
Cdd:COG0488 70 PPLDdDLTVLDTVldgdaelraleaeleeLEAKLAEPDEDLERLAELQEEFEALGgweaearaeeILsglgfpEEDLDRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 488 VGErgvkLSGGQRQRVAIARAILKDAPILILDEATSALDSESEVAVQKALKElmYGKTVIAIAH------RLSTlrdmsR 561
Cdd:COG0488 150 VSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKN--YPGTVLVVSHdryfldRVAT-----R 218
|
250
....*....|
gi 1083564009 562 ILVLEHGTIQ 571
Cdd:COG0488 219 ILELDRGKLT 228
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
362-579 |
3.54e-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: 108.41 E-value: 3.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 362 DGISFAH---EAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKiddqniaevtqDSLRraISVVP 438
Cdd:cd03291 38 NNLFFSNlclVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK-----------HSGR--ISFSS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 439 QEPALFHRSIRENIAYARpdATDEEVRDAAQKAHALEF-IDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILI 517
Cdd:cd03291 105 QFSWIMPGTIKENIIFGV--SYDEYRYKSVVKACQLEEdITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1083564009 518 LDEATSALD--SESEVaVQKALKELMYGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGTHEEL 579
Cdd:cd03291 183 LDSPFGYLDvfTEKEI-FESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
358-580 |
3.63e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 107.79 E-value: 3.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 358 EIVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAISVV 437
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 438 PQEPALFHR-SIRENIAYARP---------DATDEE-VRDAAQKAHALEFIDmlpegmntlvgERGVKLSGGQRQRVAIA 506
Cdd:PRK11231 82 PQHHLTPEGiTVRELVAYGRSpwlslwgrlSAEDNArVNQAMEQTRINHLAD-----------RRLTDLSGGQRQRAFLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1083564009 507 RAILKDAPILILDEATSALDSESEVAVQKALKEL-MYGKTVIAIAHRLS-TLRDMSRILVLEHGTIQEDGTHEELL 580
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELnTQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
354-574 |
5.60e-26 |
|
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: 105.91 E-value: 5.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 354 AKKGEIVLDGISFaheavevfknfnlTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRa 433
Cdd:cd03266 14 VKKTVQAVDGVSF-------------TVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 434 ISVVPQEPALFHR-SIRENIAYArpdATDEEVRDAAQKAHALEFIDMLpeGMNTLVGERGVKLSGGQRQRVAIARAILKD 512
Cdd:cd03266 80 LGFVSDSTGLYDRlTARENLEYF---AGLYGLKGDELTARLEELADRL--GMEELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1083564009 513 APILILDEATSALDSESEVAVQKALKELM-YGKTVIAIAHRLSTLRDM-SRILVLEHGTIQEDG 574
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLRaLGKCILFSTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
359-581 |
6.00e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 107.79 E-value: 6.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVE--VFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAISV 436
Cdd:PRK13635 6 IRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 437 VPQEP--ALFHRSIRENIAYA-------RPDATdEEVRDAAQKAHALEFIDMLPEgmntlvgergvKLSGGQRQRVAIAr 507
Cdd:PRK13635 86 VFQNPdnQFVGATVQDDVAFGlenigvpREEMV-ERVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAIA- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1083564009 508 AILKDAP-ILILDEATSALDSESEVAVQKALKEL--MYGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGTHEELLK 581
Cdd:PRK13635 153 GVLALQPdIIILDEATSMLDPRGRREVLETVRQLkeQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
359-574 |
7.81e-26 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 105.65 E-value: 7.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVEVfkNFNLTIKDGERIGLVGKSGAGKSTLVSLllreydIAG------GAIKIDDQNIAevTQDSLRR 432
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNL------IAGfetpqsGRVLINGVDVT--AAPPADR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 433 AISVVPQEPALF-HRSIRENIAYARPDAT--DEEVRDAAQKAHALEFIDMLpegMNTLVGErgvkLSGGQRQRVAIARAI 509
Cdd:cd03298 71 PVSMLFQENNLFaHLTVEQNVGLGLSPGLklTAEDRQAIEVALARVGLAGL---EKRLPGE----LSGGERQRVALARVL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083564009 510 LKDAPILILDEATSALDSESEVAVQKALKEL--MYGKTVIAIAHRLSTLRDM-SRILVLEHGTIQEDG 574
Cdd:cd03298 144 VRDKPVLLLDEPFAALDPALRAEMLDLVLDLhaETKMTVLMVTHQPEDAKRLaQRVVFLDNGRIAAQG 211
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
362-580 |
8.34e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 106.78 E-value: 8.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 362 DGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSL--RRAisVVPQ 439
Cdd:PRK13548 6 RNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELarRRA--VLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 440 EPAL-FHRSIRENIAYARPDATDEEVRDAAQKAHALEFIDMLPegmntLVGERGVKLSGGQRQRVAIARAIL------KD 512
Cdd:PRK13548 84 HSSLsFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAH-----LAGRDYPQLSGGEQQRVQLARVLAqlwepdGP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1083564009 513 APILILDEATSALDSESEVAVQKALKELMY--GKTVIAIAHRLS-TLRDMSRILVLEHGTIQEDGTHEELL 580
Cdd:PRK13548 159 PRWLLLDEPTSALDLAHQHHVLRLARQLAHerGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVL 229
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
363-600 |
1.08e-25 |
|
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: 106.81 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 363 GISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDS---LRRAISVVPQ 439
Cdd:TIGR02769 16 GLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrraFRRDVQLVFQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 440 E-PALFH--RSIRENIA-----YARPDATDEEVRdaaqKAHALEFIDMLPEGMNTLVGErgvkLSGGQRQRVAIARAILK 511
Cdd:TIGR02769 96 DsPSAVNprMTVRQIIGeplrhLTSLDESEQKAR----IAELLDMVGLRSEDADKLPRQ----LSGGQLQRINIARALAV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 512 DAPILILDEATSALDSESEVAVQKALKELM--YGKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEELLKNSgtyat 588
Cdd:TIGR02769 168 KPKLIVLDEAVSNLDMVLQAVILELLRKLQqaFGTAYLFITHDLRLVQSFCqRVAVMDKGQIVEECDVAQLLSFK----- 242
|
250
....*....|..
gi 1083564009 589 lwnHQAGGFLQE 600
Cdd:TIGR02769 243 ---HPAGRNLQS 251
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
364-582 |
3.19e-25 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 109.77 E-value: 3.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 364 ISFAHEA--VEVFKNFNLTIKDGERIGLVGKSGAGKS----TLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRR----A 433
Cdd:COG4172 14 VAFGQGGgtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 434 ISVVPQEP--AL--FH---RSIRENIAYARPdatdeeVRDAAQKAHALEFIDmlpegmntLVG----ERGVK-----LSG 497
Cdd:COG4172 94 IAMIFQEPmtSLnpLHtigKQIAEVLRLHRG------LSGAAARARALELLE--------RVGipdpERRLDayphqLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 498 GQRQRVAIARAILKDAPILILDEATSALDseseVAVQKALKELM------YGKTVIAIAHRLSTLRDMS-RILVLEHGTI 570
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPTTALD----VTVQAQILDLLkdlqreLGMALLLITHDLGVVRRFAdRVAVMRQGEI 235
|
250
....*....|..
gi 1083564009 571 QEDGTHEELLKN 582
Cdd:COG4172 236 VEQGPTAELFAA 247
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
378-595 |
4.96e-25 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 106.72 E-value: 4.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 378 NLTIKDGERIGLVGKSGAGKSTLVSLllreydIAG------GAIKIDDqniaEVTQDSL--------RRAISVVPQEPAL 443
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRA------IAGlerpdsGRIRLGG----EVLQDSArgiflpphRRRIGYVFQEARL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 444 F-HRSIRENIAYARpdatdeevRDAAQKAHALEF---IDMLpeGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILD 519
Cdd:COG4148 89 FpHLSVRGNLLYGR--------KRAPRAERRISFdevVELL--GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 520 EATSALDSES-------------EVA-----VQKALKELMygktviaiahRLSTlrdmsRILVLEHGTIQEDGTHEELLK 581
Cdd:COG4148 159 EPLAALDLARkaeilpylerlrdELDipilyVSHSLDEVA----------RLAD-----HVVLLEQGRVVASGPLAEVLS 223
|
250
....*....|....
gi 1083564009 582 NSGTYATLWNHQAG 595
Cdd:COG4148 224 RPDLLPLAGGEEAG 237
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
358-577 |
6.17e-25 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 103.94 E-value: 6.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 358 EIVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLL-LREYDIAGgAIKIDD------QNIAEVTQDSL 430
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLnLLETPDSG-QLNIAGhqfdfsQKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 431 RRAISVVPQEPALF-HRSIRENIAYArP----DATDEEVRDAAQKAHA----LEFIDMLPegmntlvgergVKLSGGQRQ 501
Cdd:COG4161 81 RQKVGMVFQQYNLWpHLTVMENLIEA-PckvlGLSKEQAREKAMKLLArlrlTDKADRFP-----------LHLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083564009 502 RVAIARAILKDAPILILDEATSALDSESEVAVQKALKELMY-GKTVIAIAHRLSTLRDM-SRILVLEHGTIQEDGTHE 577
Cdd:COG4161 149 RVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFARKVaSQVVYMEKGRIIEQGDAS 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
372-570 |
6.95e-25 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 102.24 E-value: 6.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 372 EVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLL--LREYDIAGGAIKIDDQNIaevTQDSLRRAISVVPQEPALF-HRSI 448
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPL---DKRSFRKIIGYVPQDDILHpTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 449 RENIAYArpdatdeevrdaaqkAHAlefidmlpegmntlvgeRGvkLSGGQRQRVAIARAILKDAPILILDEATSALDSE 528
Cdd:cd03213 100 RETLMFA---------------AKL-----------------RG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1083564009 529 SEVAVQKALKELMY-GKTVIAIAHRLSTL--RDMSRILVLEHGTI 570
Cdd:cd03213 146 SALQVMSLLRRLADtGRTIICSIHQPSSEifELFDKLLLLSQGRV 190
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
375-582 |
1.08e-24 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 102.90 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 375 KNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSL-RRAISVVPQEPALFHR-SIRENI 452
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIaRLGIGRTFQIPRLFPElTVLENV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 453 AYARPDATDE---------EVRDAAQKAH-ALEFIDmLPEGMNTLVGErgvkLSGGQRQRVAIARAILKDAPILILDEAT 522
Cdd:cd03219 97 MVAAQARTGSglllararrEEREARERAEeLLERVG-LADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDEPA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1083564009 523 SALDSESEVAVQKALKEL-MYGKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEELLKN 582
Cdd:cd03219 172 AGLNPEETEELAELIRELrERGITVLLVEHDMDVVMSLAdRVTVLDQGRVIAEGTPDEVRNN 233
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
378-580 |
1.51e-24 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 105.19 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 378 NLTIKDGERIGLVGKSGAGKSTLVSL---LLREYdiaGGAIKIDDqniaEVTQDSL--------RRAISVVPQEPALF-H 445
Cdd:TIGR02142 17 DFTLPGQGVTAIFGRSGSGKTTLIRLiagLTRPD---EGEIVLNG----RTLFDSRkgiflppeKRRIGYVFQEARLFpH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 446 RSIRENIAYARPDATDEEVRDAAQKahaleFIDMLpeGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDEATSAL 525
Cdd:TIGR02142 90 LSVRGNLRYGMKRARPSERRISFER-----VIELL--GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1083564009 526 DSESEVAVQKALKELM--YGKTVIAIAHRLS-TLRDMSRILVLEHGTIQEDGTHEELL 580
Cdd:TIGR02142 163 DDPRKYEILPYLERLHaeFGIPILYVSHSLQeVLRLADRVVVLEDGRVAAAGPIAEVW 220
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
359-570 |
2.39e-24 |
|
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: 99.81 E-value: 2.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVT-QDSLRRAISVV 437
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 438 PQepalfhrsireniayarpdatdeevrdaaqkahalefidmlpegmntlvgergvkLSGGQRQRVAIARAILKDAPILI 517
Cdd:cd03216 81 YQ-------------------------------------------------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1083564009 518 LDEATSALdSESEV----AVQKALKELmyGKTVIAIAHRLSTLRDMS-RILVLEHGTI 570
Cdd:cd03216 106 LDEPTAAL-TPAEVerlfKVIRRLRAQ--GVAVIFISHRLDEVFEIAdRVTVLRDGRV 160
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
359-577 |
3.55e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 101.63 E-value: 3.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLL-LRE------YDIAGGAI----KIDDQNIAEvtq 427
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnLLEmprsgtLNIAGNHFdfskTPSDKAIRE--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 428 dsLRRAISVVPQEPALF-HRSIRENIAYArPDATDEEVRDAAqKAHALEFIDMLPegMNTLVGERGVKLSGGQRQRVAIA 506
Cdd:PRK11124 80 --LRRNVGMVFQQYNLWpHLTVQQNLIEA-PCRVLGLSKDQA-LARAEKLLERLR--LKPYADRFPLHLSGGQQQRVAIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1083564009 507 RAILKDAPILILDEATSALDSESEVAVQKALKELM-YGKTVIAIAHRLSTLRDM-SRILVLEHGTIQEDGTHE 577
Cdd:PRK11124 154 RALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAeTGITQVIVTHEVEVARKTaSRVVYMENGHIVEQGDAS 226
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
359-582 |
3.70e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 102.37 E-value: 3.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAH-EAVEVFKNFNLTIKDGERIGLVGKSGAGKSTL---VSLLLREydiAGGAIKIDDQNIAEVTQ-DSLRRA 433
Cdd:PRK13644 2 IRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLalhLNGLLRP---QKGKVLVSGIDTGDFSKlQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 434 ISVVPQEP--ALFHRSIRENIAYARPDAT--DEEVRDAAQKAHAlefidmlPEGMNTLVGERGVKLSGGQRQRVAIARAI 509
Cdd:PRK13644 79 VGIVFQNPetQFVGRTVEEDLAFGPENLClpPIEIRKRVDRALA-------EIGLEKYRHRSPKTLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1083564009 510 LKDAPILILDEATSALDSESEVAVQKALKELM-YGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGTHEELLKN 582
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSGIAVLERIKKLHeKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSD 225
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
365-579 |
3.70e-24 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 108.07 E-value: 3.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 365 SFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKiddqniaevtqDSLRraISVVPQEPALF 444
Cdd:TIGR01271 433 NFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK-----------HSGR--ISFSPQTSWIM 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 445 HRSIRENIAYARpdATDEEVRDAAQKAHALEF-IDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDEATS 523
Cdd:TIGR01271 500 PGTIKDNIIFGL--SYDEYRYTSVIKACQLEEdIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1083564009 524 ALDSESEVAV-QKALKELMYGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGTHEEL 579
Cdd:TIGR01271 578 HLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
363-600 |
1.03e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 100.92 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 363 GISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVT---QDSLRRAISVVPQ 439
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 440 E-PALFH--RSIRENIAYARPDATDeeVRDAAQKAHALEFIDML---PEGMNTLVGErgvkLSGGQRQRVAIARAILKDA 513
Cdd:PRK10419 97 DsISAVNprKTVREIIREPLRHLLS--LDKAERLARASEMLRAVdldDSVLDKRPPQ----LSGGQLQRVCLARALAVEP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 514 PILILDEATSALDSESEVAVQKALKELM--YGKTVIAIAHRLSTL-RDMSRILVLEHGTIQEDGTHEELLKNSgtyatlw 590
Cdd:PRK10419 171 KLLILDEAVSNLDLVLQAGVIRLLKKLQqqFGTACLFITHDLRLVeRFCQRVMVMDNGQIVETQPVGDKLTFS------- 243
|
250
....*....|
gi 1083564009 591 nHQAGGFLQE 600
Cdd:PRK10419 244 -SPAGRVLQN 252
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
366-589 |
1.29e-23 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 106.40 E-value: 1.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 366 FAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIkiddqnIAEvtqdslrRAISVVPQEPALFH 445
Cdd:PTZ00243 668 FELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV------WAE-------RSIAYVPQQAWIMN 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 446 RSIRENIAYarpdaTDEEvrDAAQKAHA-----LEF-IDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILD 519
Cdd:PTZ00243 735 ATVRGNILF-----FDEE--DAARLADAvrvsqLEAdLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLD 807
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1083564009 520 EATSALDSE-SEVAVQKALKELMYGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGTHEELLKNSgTYATL 589
Cdd:PTZ00243 808 DPLSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS-LYATL 877
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
359-580 |
2.27e-23 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 99.39 E-value: 2.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAISVVP 438
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 439 QEPALFHR-SIRENIAYAR-------PDATDEEVRDAaqkahALEFIDMLPegmntLVGERGVKLSGGQRQRVAIARAIL 510
Cdd:COG4604 82 QENHINSRlTVRELVAFGRfpyskgrLTAEDREIIDE-----AIAYLDLED-----LADRYLDELSGGQRQRAFIAMVLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1083564009 511 KDAPILILDEATSALDSESEVAVQKALKELM--YGKTVIAIAHRL---STLRDmsRILVLEHGTIQEDGTHEELL 580
Cdd:COG4604 152 QDTDYVLLDEPLNNLDMKHSVQMMKLLRRLAdeLGKTVVIVLHDInfaSCYAD--HIVAMKDGRVVAQGTPEEII 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
351-580 |
3.66e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 102.23 E-value: 3.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 351 DLVAKKGEI-VLDGISfaheavevfknfnLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDS 429
Cdd:PRK09536 8 DLSVEFGDTtVLDGVD-------------LSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 430 LRRAISVVPQEPAL-FHRSIRENIA---------YARPDATDEE-VRDAAQKAHALEFIDmlpegmntlvgeRGV-KLSG 497
Cdd:PRK09536 75 ASRRVASVPQDTSLsFEFDVRQVVEmgrtphrsrFDTWTETDRAaVERAMERTGVAQFAD------------RPVtSLSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 498 GQRQRVAIARAILKDAPILILDEATSALDSESEVAVQKALKELM-YGKTVIAIAHRLS-TLRDMSRILVLEHGTIQEDGT 575
Cdd:PRK09536 143 GERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVdDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGP 222
|
....*
gi 1083564009 576 HEELL 580
Cdd:PRK09536 223 PADVL 227
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
376-582 |
3.89e-23 |
|
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: 98.96 E-value: 3.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 376 NFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSL-RRAISVVPQEPALFHR-SIRENI- 452
Cdd:COG0411 22 DVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIaRLGIARTFQNPRLFPElTVLENVl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 453 -------------AYARPDATDEEVRDAAQKA-HALEFIDMLPEgMNTLVGErgvkLSGGQRQRVAIARAILKDAPILIL 518
Cdd:COG0411 102 vaaharlgrgllaALLRLPRARREEREARERAeELLERVGLADR-ADEPAGN----LSYGQQRRLEIARALATEPKLLLL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083564009 519 DEATSAL-DSESEVAVQ--KALKELMyGKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEELLKN 582
Cdd:COG0411 177 DEPAAGLnPEETEELAEliRRLRDER-GITILLIEHDMDLVMGLAdRIVVLDFGRVIAEGTPAEVRAD 243
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
358-585 |
4.83e-23 |
|
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: 98.18 E-value: 4.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 358 EIVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLllreydIAG------GAIKIDDQniaEVTQDSLR 431
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRL------IAGlerpdsGTILFGGE---DATDVPVQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 432 -RAISVVPQEPALF-HRSIRENIAY---ARPDATDEEVRDAAQKAHALefIDMLpeGMNTLVGERGVKLSGGQRQRVAIA 506
Cdd:cd03296 73 eRNVGFVFQHYALFrHMTVFDNVAFglrVKPRSERPPEAEIRAKVHEL--LKLV--QLDWLADRYPAQLSGGQRQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 507 RAILKDAPILILDEATSALDSESEVAVQKALKELM--YGKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEELLKNS 583
Cdd:cd03296 149 RALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHdeLHVTTVFVTHDQEEALEVAdRVVVMNKGRIEQVGTPDEVYDHP 228
|
..
gi 1083564009 584 GT 585
Cdd:cd03296 229 AS 230
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
361-582 |
5.10e-23 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 98.13 E-value: 5.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 361 LDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEV-TQDSLRRAISVVPQ 439
Cdd:COG0410 6 VENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLpPHRIARLGIGYVPE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 440 EPALFHR-SIRENI---AYARpdatdeevRDAAQKAHALEFI-DMLPEgmntlVGER----GVKLSGGQRQRVAIARAIL 510
Cdd:COG0410 86 GRRIFPSlTVEENLllgAYAR--------RDRAEVRADLERVyELFPR-----LKERrrqrAGTLSGGEQQMLAIGRALM 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1083564009 511 KDAPILILDEATSALdseSEVAVQK---ALKELMY-GKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEELLKN 582
Cdd:COG0410 153 SRPKLLLLDEPSLGL---APLIVEEifeIIRRLNReGVTILLVEQNARFALEIAdRAYVLERGRIVLEGTAAELLAD 226
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
359-581 |
5.19e-23 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 100.56 E-value: 5.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLllreydIAG------GAIKIDDQniaEVTQDSLR- 431
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRL------VAGlekpteGQIFIDGE---DVTHRSIQq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 432 RAISVVPQEPALF-HRSIRENIAYA-----RPDatdEEVRDAAQKAhaLEFIDMlpEGMntlvGERGV-KLSGGQRQRVA 504
Cdd:PRK11432 78 RDICMVFQSYALFpHMSLGENVGYGlkmlgVPK---EERKQRVKEA--LELVDL--AGF----EDRYVdQISGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 505 IARAILKDAPILILDEATSALDSESEVAVQKALKELM--YGKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEELLK 581
Cdd:PRK11432 147 LARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQqqFNITSLYVTHDQSEAFAVSdTVIVMNKGKIMQIGSPQELYR 226
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
359-579 |
5.56e-23 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 100.87 E-value: 5.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVtqDSLRRAISVVP 438
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDV--PPAERGVGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 439 QEPALF-HRSIRENIAY----ARPDATD-----EEVRDAAQKAHALefidmlpegmntlvgERGVK-LSGGQRQRVAIAR 507
Cdd:PRK11000 82 QSYALYpHLSVAENMSFglklAGAKKEEinqrvNQVAEVLQLAHLL---------------DRKPKaLSGGQRQRVAIGR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1083564009 508 AILKDAPILILDEATSALDS----ESEVAVQKALKELmyGKTVIAIAH---RLSTLRDmsRILVLEHGTIQEDGTHEEL 579
Cdd:PRK11000 147 TLVAEPSVFLLDEPLSNLDAalrvQMRIEISRLHKRL--GRTMIYVTHdqvEAMTLAD--KIVVLDAGRVAQVGKPLEL 221
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
375-579 |
1.58e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 97.88 E-value: 1.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 375 KNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAISVVPQEP--ALFHRSIRENI 452
Cdd:PRK13650 24 NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPdnQFVGATVEDDV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 453 AYARPDA--TDEEVRDAAQkaHALEFIdmlpeGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDEATSALDSESE 530
Cdd:PRK13650 104 AFGLENKgiPHEEMKERVN--EALELV-----GMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGR 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1083564009 531 VAVQKALKELM--YGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGTHEEL 579
Cdd:PRK13650 177 LELIKTIKGIRddYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
375-579 |
1.98e-22 |
|
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: 96.03 E-value: 1.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 375 KNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEvTQDSLRRAISVVPQEPALFHR-SIRENIA 453
Cdd:cd03263 19 DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALFDElTVREHLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 454 -YAR----PDATDEEVrdAAQKAHALEfidmLPEGMNTLVGErgvkLSGGQRQRVAIARAILKDAPILILDEATSALDSE 528
Cdd:cd03263 98 fYARlkglPKSEIKEE--VELLLRVLG----LTDKANKRART----LSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1083564009 529 SEVAVQKALKELMYGKTVIaiahrLSTLrDM-------SRILVLEHGTIQEDGTHEEL 579
Cdd:cd03263 168 SRRAIWDLILEVRKGRSII-----LTTH-SMdeaealcDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
359-569 |
6.00e-22 |
|
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: 92.13 E-value: 6.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIaevtqdslrraISVVP 438
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVK-----------IGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 439 QepalfhrsireniayarpdatdeevrdaaqkahalefidmlpegmntlvgergvkLSGGQRQRVAIARAILKDAPILIL 518
Cdd:cd03221 70 Q-------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1083564009 519 DEATSALDSESEVAVQKALKElmYGKTVIAIAH-R--LSTLRDmsRILVLEHGT 569
Cdd:cd03221 95 DEPTNHLDLESIEALEEALKE--YPGTVILVSHdRyfLDQVAT--KIIELEDGK 144
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
375-551 |
6.09e-22 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 94.84 E-value: 6.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 375 KNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLrraisVVPQEPALFH-RSIRENIA 453
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 454 YA----RPDATDEEvrdaaQKAHALEFIDMLpeGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDEATSALDSES 529
Cdd:TIGR01184 77 LAvdrvLPDLSKSE-----RRAIVEEHIALV--GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180
....*....|....*....|....
gi 1083564009 530 EVAVQKALKELM--YGKTVIAIAH 551
Cdd:TIGR01184 150 RGNLQEELMQIWeeHRVTVLMVTH 173
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
372-574 |
7.05e-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: 93.82 E-value: 7.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 372 EVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEvTQDSLRRAISVVpQEPALF-HRSIRE 450
Cdd:cd03268 14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-NIEALRRIGALI-EAPGFYpNLTARE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 451 NIAYArpdATDEEVRDAAQKahalEFIDMLpeGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDEATSALDSESE 530
Cdd:cd03268 92 NLRLL---ARLLGIRKKRID----EVLDVV--GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1083564009 531 VAVQKALKELM-YGKTVIAIAHRLSTLRDM-SRILVLEHGTIQEDG 574
Cdd:cd03268 163 KELRELILSLRdQGITVLISSHLLSEIQKVaDRIGIINKGKLIEEG 208
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
361-526 |
1.00e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 93.70 E-value: 1.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 361 LDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYD---IAGGAIKIDDQNIAEVtqDSLRRAISVV 437
Cdd:COG4136 4 LENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRRLTAL--PAEQRRIGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 438 PQEPALF-HRSIRENIAYARPDATDEEVRDAaQKAHALEFIDMlpEGMntlvGERGVK-LSGGQRQRVAIARAILKDAPI 515
Cdd:COG4136 82 FQDDLLFpHLSVGENLAFALPPTIGRAQRRA-RVEQALEEAGL--AGF----ADRDPAtLSGGQRARVALLRALLAEPRA 154
|
170
....*....|.
gi 1083564009 516 LILDEATSALD 526
Cdd:COG4136 155 LLLDEPFSKLD 165
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
344-582 |
1.31e-21 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 94.43 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 344 IDVENaqdLVAK-KGEIVLDGIsfaheavevfknfNLTIKDGERIGLVGKSGAGKSTLV-SLLLREYDIAG----GAIKI 417
Cdd:PRK11264 4 IEVKN---LVKKfHGQTVLHGI-------------DLEVKPGEVVAIIGPSGSGKTTLLrCINLLEQPEAGtirvGDITI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 418 D-----DQNIAEVTQdsLRRAISVVPQEPALF-HRSIRENIAYArPDATDEEVRDAA-QKAHALefidMLPEGMNTLVGE 490
Cdd:PRK11264 68 DtarslSQQKGLIRQ--LRQHVGFVFQNFNLFpHRTVLENIIEG-PVIVKGEPKEEAtARAREL----LAKVGLAGKETS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 491 RGVKLSGGQRQRVAIARAILKDAPILILDEATSALDSESEVAVQKALKELMYGK-TVIAIAHRLSTLRDMS-RILVLEHG 568
Cdd:PRK11264 141 YPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARDVAdRAIFMDQG 220
|
250
....*....|....
gi 1083564009 569 TIQEDGTHEELLKN 582
Cdd:PRK11264 221 RIVEQGPAKALFAD 234
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
367-582 |
1.84e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 93.80 E-value: 1.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 367 AHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVT-QDSLRRAISVVPQEPALFH 445
Cdd:PRK10895 12 AYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYLPQEASIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 446 R-SIRENIAYA---RPDATDEEVRDAAQKAHALEFIDMLPEGMntlvgerGVKLSGGQRQRVAIARAILKDAPILILDEA 521
Cdd:PRK10895 92 RlSVYDNLMAVlqiRDDLSAEQREDRANELMEEFHIEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1083564009 522 TSALDSESEVAVQKALKELM-YGKTVIAIAHRL-STLRDMSRILVLEHGTIQEDGTHEELLKN 582
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
357-582 |
1.89e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 95.07 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 357 GEIVLDGISFAHEAVEVFK-----NFNLTIKDGERIGLVGKSGAGKSTLVSL----LLRE--YDIAGG-AIKIDDQNIAE 424
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPFEfkalnNTSLTFKKNKVTCVIGTTGSGKSTMIQLtnglIISEtgQTIVGDyAIPANLKKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 425 VTQdsLRRAISVVPQEP--ALFHRSIRENIAYArPDATDEEVRDAAQKAHALEFIDMLPEgmnTLVGERGVKLSGGQRQR 502
Cdd:PRK13645 85 VKR--LRKEIGLVFQFPeyQLFQETIEKDIAFG-PVNLGENKQEAYKKVPELLKLVQLPE---DYVKRSPFELSGGQKRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 503 VAIARAILKDAPILILDEATSALDSESEVAVQKALKEL--MYGKTVIAIAHRL-STLRDMSRILVLEHGTIQEDGTHEEL 579
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnkEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGSPFEI 238
|
...
gi 1083564009 580 LKN 582
Cdd:PRK13645 239 FSN 241
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
371-579 |
2.47e-21 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 95.68 E-value: 2.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 371 VEVFKNFNLTIKDGERIGLVGKSGAGKSTLvsllLR-----EyDIAGGAIKIDDQNIAEVtqDSLRRAISVVPQEPALF- 444
Cdd:PRK11650 17 TQVIKGIDLDVADGEFIVLVGPSGCGKSTL----LRmvaglE-RITSGEIWIGGRVVNEL--EPADRDIAMVFQNYALYp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 445 HRSIRENIAYA---R--PDAT-DEEVRDAAQkahALEFIDMLpegmntlvgERG-VKLSGGQRQRVAIARAILKDAPILI 517
Cdd:PRK11650 90 HMSVRENMAYGlkiRgmPKAEiEERVAEAAR---ILELEPLL---------DRKpRELSGGQRQRVAMGRAIVREPAVFL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1083564009 518 LDEATSALDSESEVAVQKALKELM--YGKTVIAIAH---RLSTLRDmsRILVLEHGTIQEDGTHEEL 579
Cdd:PRK11650 158 FDEPLSNLDAKLRVQMRLEIQRLHrrLKTTSLYVTHdqvEAMTLAD--RVVVMNGGVAEQIGTPVEV 222
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
371-551 |
3.25e-21 |
|
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: 92.50 E-value: 3.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 371 VEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQ----NIAEVTQD---SLRRA--------IS 435
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQASPReilALRRRtigyvsqfLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 436 VVPQEPA-------LFHRSIRENIAYARpdatdeevrdAAQKAHALEfidmLPEGM-----NTLvgergvklSGGQRQRV 503
Cdd:COG4778 104 VIPRVSAldvvaepLLERGVDREEARAR----------ARELLARLN----LPERLwdlppATF--------SGGEQQRV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1083564009 504 AIARAILKDAPILILDEATSALDSESEVAVQKALKELMY-GKTVIAIAH 551
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKArGTAIIGIFH 210
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
370-575 |
3.46e-21 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 95.25 E-value: 3.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 370 AVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSL--LLREYDiaGGAIKIDDQNIAEVTQDSLRRA---ISVVPQepalf 444
Cdd:PRK11153 17 TIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCinLLERPT--SGRVLVDGQDLTALSEKELRKArrqIGMIFQ----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 445 H------RSIRENIAYA-RPDATDEevrdAAQKAHALEFIDM--LPEGMNTLVGErgvkLSGGQRQRVAIARAILKDAPI 515
Cdd:PRK11153 90 HfnllssRTVFDNVALPlELAGTPK----AEIKARVTELLELvgLSDKADRYPAQ----LSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1083564009 516 LILDEATSALDSESEVAVQKALKEL--MYGKTVIAIAHRLSTLRDM-SRILVLEHGTIQEDGT 575
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDInrELGLTIVLITHEMDVVKRIcDRVAVIDAGRLVEQGT 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
359-579 |
5.21e-21 |
|
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: 96.80 E-value: 5.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLL--LREYDIAGGAI--------------------- 415
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 416 ------------KIDDQNIAEVTQDSLRRAISVVPQEP-ALF-HRSIRENIAYARPDAtDEEVRDAAQKAhaLEFIDM-- 479
Cdd:TIGR03269 81 pcpvcggtlepeEVDFWNLSDKLRRRIRKRIAIMLQRTfALYgDDTVLDNVLEALEEI-GYEGKEAVGRA--VDLIEMvq 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 480 LPEGMNTLVGErgvkLSGGQRQRVAIARAILKDAPILILDEATSALDSESEVAVQKALKELM--YGKTVIAIAHRLSTLR 557
Cdd:TIGR03269 158 LSHRITHIARD----LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSHWPEVIE 233
|
250 260
....*....|....*....|...
gi 1083564009 558 DMS-RILVLEHGTIQEDGTHEEL 579
Cdd:TIGR03269 234 DLSdKAIWLENGEIKEEGTPDEV 256
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
360-580 |
5.25e-21 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 92.87 E-value: 5.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 360 VLDGISfaheavevfknfnLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSL--RRAisVV 437
Cdd:COG4559 16 LLDDVS-------------LTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELarRRA--VL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 438 PQEPAL-FHRSIRENIAYARPDATDEEVRDAAQKAHALEFIDMLPegmntLVGERGVKLSGGQRQRVAIARAIL-----K 511
Cdd:COG4559 81 PQHSSLaFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAH-----LAGRSYQTLSGGEQQRVQLARVLAqlwepV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1083564009 512 DAP--ILILDEATSALDSESEVAVQKALKELMY-GKTVIAIAHRLS-TLRDMSRILVLEHGTIQEDGTHEELL 580
Cdd:COG4559 156 DGGprWLFLDEPTSALDLAHQHAVLRLARQLARrGGGVVAVLHDLNlAAQYADRILLLHQGRLVAQGTPEEVL 228
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
372-582 |
5.58e-21 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 92.72 E-value: 5.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 372 EVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQD-------------SLRRAISVVP 438
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadknqlrLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 439 QEPALF-HRSIRENIAYARPDA---TDEEVRDAAQKAHALEFIDMLPEGmntlvgERGVKLSGGQRQRVAIARAILKDAP 514
Cdd:PRK10619 99 QHFNLWsHMTVLENVMEAPIQVlglSKQEARERAVKYLAKVGIDERAQG------KYPVHLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 515 ILILDEATSALDSESEVAVQKALKELM-YGKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEELLKN 582
Cdd:PRK10619 173 VLLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGFARHVSsHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
373-574 |
6.41e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 96.31 E-value: 6.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 373 VFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDiAGGAIKIDDQNIAEVTQDSL---RRAISVVPQEP--ALFHR- 446
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPnsSLNPRl 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 447 ----SIRENIAYARPDATDEEvRDAAQKAhALEFIDMLPEGMNTLVGErgvkLSGGQRQRVAIARAILKDAPILILDEAT 522
Cdd:PRK15134 380 nvlqIIEEGLRVHQPTLSAAQ-REQQVIA-VMEEVGLDPETRHRYPAE----FSGGQRQRIAIARALILKPSLIILDEPT 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1083564009 523 SALDSESEVAVQKALKELM--YGKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDG 574
Cdd:PRK15134 454 SSLDKTVQAQILALLKSLQqkHQLAYLFISHDLHVVRALChQVIVLRQGEVVEQG 508
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
359-579 |
8.32e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 94.38 E-value: 8.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLllreydIAG------GAIKIDDQNIAEV-TQDslr 431
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRI------IAGlehqtsGHIRFHGTDVSRLhARD--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 432 RAISVVPQEPALF-HRSIRENIAYA--------RPDAtdeevrdAAQKAHALEFIDMLPegMNTLVGERGVKLSGGQRQR 502
Cdd:PRK10851 74 RKVGFVFQHYALFrHMTVFDNIAFGltvlprreRPNA-------AAIKAKVTQLLEMVQ--LAHLADRYPAQLSGGQKQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 503 VAIARAILKDAPILILDEATSALDSEsevaVQKALK--------ELMYgkTVIAIAHRLSTLRDMS-RILVLEHGTIQED 573
Cdd:PRK10851 145 VALARALAVEPQILLLDEPFGALDAQ----VRKELRrwlrqlheELKF--TSVFVTHDQEEAMEVAdRVVVMSQGNIEQA 218
|
....*.
gi 1083564009 574 GTHEEL 579
Cdd:PRK10851 219 GTPDQV 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
372-562 |
9.67e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 91.76 E-value: 9.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 372 EVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDI-----AGGAIKIDDQNIAEVTQDS--LRRAISVVPQEPALF 444
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLnpevtITGSIVYNGHNIYSPRTDTvdLRKEIGMVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 445 HRSIRENIAYA-RPDAT-DEEVRDAAQKAhALEFIDMLPEGMNTLvGERGVKLSGGQRQRVAIARAILKDAPILILDEAT 522
Cdd:PRK14239 99 PMSIYENVVYGlRLKGIkDKQVLDEAVEK-SLKGASIWDEVKDRL-HDSALGLSGGQQQRVCIARVLATSPKIILLDEPT 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1083564009 523 SALDSESEVAVQKALKELMYGKTVIAIAHrlsTLRDMSRI 562
Cdd:PRK14239 177 SALDPISAGKIEETLLGLKDDYTMLLVTR---SMQQASRI 213
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
375-553 |
1.12e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 92.15 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 375 KNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDI-----AGGAIKIDDQNI--AEVTQDSLRRAISVVPQEPALFHRS 447
Cdd:PRK14243 27 KNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPKS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 448 IRENIAY-ARPDA----TDEEVRDAAQKAhAL--EFIDMLPEGmntlvgerGVKLSGGQRQRVAIARAILKDAPILILDE 520
Cdd:PRK14243 107 IYDNIAYgARINGykgdMDELVERSLRQA-ALwdEVKDKLKQS--------GLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190
....*....|....*....|....*....|...
gi 1083564009 521 ATSALDSESEVAVQKALKELMYGKTVIAIAHRL 553
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
378-582 |
1.25e-20 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 93.23 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 378 NLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRA---ISVVPQEP--ALFHR-SIREN 451
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsdIQMIFQDPlaSLNPRmTIGEI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 452 IAYA----RPDATDEEVRDAAqKAHALEfIDMLPEGMNTLVGErgvkLSGGQRQRVAIARAILKDAPILILDEATSALDS 527
Cdd:PRK15079 121 IAEPlrtyHPKLSRQEVKDRV-KAMMLK-VGLLPNLINRYPHE----FSGGQCQRIGIARALILEPKLIICDEPVSALDV 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1083564009 528 ESEVAVQKALKELM--YGKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEELLKN 582
Cdd:PRK15079 195 SIQAQVVNLLQQLQreMGLSLIFIAHDLAVVKHISdRVLVMYLGHAVELGTYDEVYHN 252
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
376-585 |
2.11e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 93.36 E-value: 2.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 376 NFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTqdSLRRAISVVPQEPALF-HRSIRENIAY 454
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP--PYQRPINMMFQSYALFpHMTVEQNIAF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 455 -------ARPDATDEeVRDAAQKAHALEFIDMLPEgmntlvgergvKLSGGQRQRVAIARAILKDAPILILDEATSALDS 527
Cdd:PRK11607 115 glkqdklPKAEIASR-VNEMLGLVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDK 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1083564009 528 ESEVAVQKALKELM--YGKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEELLKNSGT 585
Cdd:PRK11607 183 KLRDRMQLEVVDILerVGVTCVMVTHDQEEAMTMAgRIAIMNRGKFVQIGEPEEIYEHPTT 243
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
359-581 |
2.29e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 91.35 E-value: 2.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVEVF--KNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAISV 436
Cdd:PRK13648 8 IVFKNVSFQYQSDASFtlKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 437 VPQEPA-LFHRSI-RENIAYARPD---ATDEEVRDAAQkahALEFIDMLPEGmntlvGERGVKLSGGQRQRVAIARAILK 511
Cdd:PRK13648 88 VFQNPDnQFVGSIvKYDVAFGLENhavPYDEMHRRVSE---ALKQVDMLERA-----DYEPNALSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1083564009 512 DAPILILDEATSALDSESEVAVQKALKELMYGK--TVIAIAHRLSTLRDMSRILVLEHGTIQEDGTHEELLK 581
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
359-568 |
2.37e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 90.87 E-value: 2.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAG-----GAIKIDDQNIAE--VTQDSLR 431
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYErrVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 432 RAISVVPQEPALFHRSIRENIAYA------RPDATDEEVRDAAQKAhalefIDMLPEGMNTLvGERGVKLSGGQRQRVAI 505
Cdd:PRK14258 88 RQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIVESALKD-----ADLWDEIKHKI-HKSALDLSGGQQQRLCI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1083564009 506 ARAILKDAPILILDEATSALDSESEVAVQKALKELMYGK--TVIAIAHRLSTLRDMSRILVLEHG 568
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSelTMVIVSHNLHQVSRLSDFTAFFKG 226
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
369-575 |
2.82e-20 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 90.19 E-value: 2.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 369 EAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLlreydiAG------GAIKIDDQNIAEVTQDSL----RRAISVVP 438
Cdd:COG4181 23 GELTILKGISLEVEAGESVAIVGASGSGKSTLLGLL------AGldrptsGTVRLAGQDLFALDEDARarlrARHVGFVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 439 QE----PALfhrSIRENIAYARPDATDeevRDAAQKAHAlefidMLPE-GMNTLVGERGVKLSGGQRQRVAIARAILKDA 513
Cdd:COG4181 97 QSfqllPTL---TALENVMLPLELAGR---RDARARARA-----LLERvGLGHRLDHYPAQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1083564009 514 PILILDEATSALDSESEVAVQKALKELM--YGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGT 575
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLFELNreRGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTA 229
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
375-568 |
3.02e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 94.32 E-value: 3.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 375 KNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQniaEVT----QDSLRRAISVVPQEPALFHR-SIR 449
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGK---PVRirspRDAIALGIGMVHQHFMLVPNlTVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 450 ENIAYARPD---------ATDEEVRDAAQKAHaLEfIDMlpegmNTLVGErgvkLSGGQRQRVAIARAILKDAPILILDE 520
Cdd:COG3845 99 ENIVLGLEPtkggrldrkAARARIRELSERYG-LD-VDP-----DAKVED----LSVGEQQRVEILKALYRGARILILDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1083564009 521 ATSALdSESEV----AVQKALKELmyGKTVIAIAHRLSTLRDMS-RILVLEHG 568
Cdd:COG3845 168 PTAVL-TPQEAdelfEILRRLAAE--GKSIIFITHKLREVMAIAdRVTVLRRG 217
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
359-584 |
3.40e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 91.01 E-value: 3.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVE--VFKNFNLTIKDGERIGLVGKSGAGKSTLVSL---LLREYDIAGGAIKIDDQNIAEVTQDSLRRA 433
Cdd:PRK13640 6 VEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLingLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 434 ISVVPQEP------ALFHRSIR---ENIAYARPDATdEEVRDAAQKAHALEFIDMLPEgmntlvgergvKLSGGQRQRVA 504
Cdd:PRK13640 86 VGIVFQNPdnqfvgATVGDDVAfglENRAVPRPEMI-KIVRDVLADVGMLDYIDSEPA-----------NLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 505 IArAILKDAP-ILILDEATSALDSESEVAVQKALKELMYGK--TVIAIAHRLSTLRDMSRILVLEHGTIQEDGT------ 575
Cdd:PRK13640 154 IA-GILAVEPkIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSpveifs 232
|
....*....
gi 1083564009 576 HEELLKNSG 584
Cdd:PRK13640 233 KVEMLKEIG 241
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
373-526 |
3.86e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 90.53 E-value: 3.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 373 VFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDslRRA--ISVVPQEPAL---FHRS 447
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEY--KRAkyIGRVFQDPMMgtaPSMT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 448 IREN--IAYARPD------ATDEEVRDAAQKahALEFIDM-LPEGMNTLVGergvKLSGGQRQRVAIARAILKDAPILIL 518
Cdd:COG1101 99 IEENlaLAYRRGKrrglrrGLTKKRRELFRE--LLATLGLgLENRLDTKVG----LLSGGQRQALSLLMATLTKPKLLLL 172
|
....*...
gi 1083564009 519 DEATSALD 526
Cdd:COG1101 173 DEHTAALD 180
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
369-573 |
3.88e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 94.41 E-value: 3.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 369 EAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSL----RRAISVVPQEPALF 444
Cdd:PRK10535 19 EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 445 -HRSIRENIAYARPDATDEEvrdAAQKAHALEFIDMLpeGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDEATS 523
Cdd:PRK10535 99 sHLTAAQNVEVPAVYAGLER---KQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1083564009 524 ALDSESEVAVQKALKELM-YGKTVIAIAHRLSTLRDMSRILVLEHGTIQED 573
Cdd:PRK10535 174 ALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRN 224
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
361-581 |
3.95e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 90.62 E-value: 3.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 361 LDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAISVVPQE 440
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 441 -PALFHRSIRENIAYARPDATDEEVR-DAAQKAHALEFIDMLpeGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILIL 518
Cdd:PRK10575 94 lPAAEGMTVRELVAIGRYPWHGALGRfGAADREKVEEAISLV--GLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1083564009 519 DEATSALDSESEVAVQKALKEL--MYGKTVIAIAHRLS-TLRDMSRILVLEHGTIQEDGTHEELLK 581
Cdd:PRK10575 172 DEPTSALDIAHQVDVLALVHRLsqERGLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELMR 237
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
375-582 |
4.74e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 92.79 E-value: 4.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 375 KNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLR----RAISVVPQEPALF-HRSIR 449
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMpHMTVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 450 ENIAYARPDATdeeVRDAAQKAHALEFIDMLpeGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDEATSALDSES 529
Cdd:PRK10070 125 DNTAFGMELAG---INAEERREKALDALRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1083564009 530 EVAVQKALKELM--YGKTVIAIAHRL-STLRDMSRILVLEHGTIQEDGTHEELLKN 582
Cdd:PRK10070 200 RTEMQDELVKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
359-582 |
1.29e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 88.43 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLR------EYDIAGGAIkIDDQNIAEVTQDSLRR 432
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielypEARVSGEVY-LDGQDIFKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 433 AISVVPQEP-ALFHRSIRENIAYA--------RPDATDEEVRDAAQKAHALEfidmlpEGMNTLVGERGvKLSGGQRQRV 503
Cdd:PRK14247 83 RVQMVFQIPnPIPNLSIFENVALGlklnrlvkSKKELQERVRWALEKAQLWD------EVKDRLDAPAG-KLSGGQQQRL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 504 AIARAILKDAPILILDEATSALDSESEVAVQKALKELMYGKTVIAIAH-RLSTLRDMSRILVLEHGTIQEDGTHEELLKN 582
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREVFTN 235
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
373-580 |
1.40e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 88.57 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 373 VFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQ------NIAEVTQDSLRRAISVVPQEPALF-H 445
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFpH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 446 RSIRENIAYARPDATDEEVRDAAQ-KAHALEFIDMLPEGMNTLvGERGVKLSGGQRQRVAIARAILKDAPILILDEATSA 524
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKREIKKiVEECLRKVGLWKEVYDRL-NSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1083564009 525 LDSESEVAVQKALKELMYGKTVIAIAHR-LSTLRDMSRILVLEHGTIQEDGTHEELL 580
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNEIAIVIVSHNpQQVARVADYVAFLYNGELVEWGSSNEIF 240
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
343-589 |
1.50e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 89.76 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 343 VIDVENaqdL-----VAKKGE----IVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLlreydiAG- 412
Cdd:COG4586 1 IIEVEN---LsktyrVYEKEPglkgALKGLFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKML------TGi 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 413 -----GAIKIDDQNIAEVTQDSLRRaISVV------------PQEPALFHRSIreniaYARPDATDEEVRDaaqkahalE 475
Cdd:COG4586 72 lvptsGEVRVLGYVPFKRRKEFARR-IGVVfgqrsqlwwdlpAIDSFRLLKAI-----YRIPDAEYKKRLD--------E 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 476 FIDMLPEG--MNTLVgeRgvKLSGGQRQRVAIARAILKDAPILILDEATSALDSESEVAVQKALKEL--MYGKTVIAIAH 551
Cdd:COG4586 138 LVELLDLGelLDTPV--R--QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnrERGTTILLTSH 213
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1083564009 552 rlstlrDM-------SRILVLEHGTIQEDGTHEELLKNSGTYATL 589
Cdd:COG4586 214 ------DMddiealcDRVIVIDHGRIIYDGSLEELKERFGPYKTI 252
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
377-580 |
1.95e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 87.97 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 377 FNLTIKDGERIGLVGKSGAGKSTlvsLLLReydIAG-----GAIKIDDQNIAEVTQDSLRRAISVVPQE-PALFHRSIRE 450
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKST---LLAR---MAGllpgqGEILLNGRPLSDWSAAELARHRAYLSQQqSPPFAMPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 451 NIAYARPDATDEEVRDA--AQKAHALEFIDMLPEGMNTlvgergvkLSGGQRQRVAIARAILK-------DAPILILDEA 521
Cdd:COG4138 89 YLALHQPAGASSEAVEQllAQLAEALGLEDKLSRPLTQ--------LSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1083564009 522 TSALDSESEVAVQKALKEL-MYGKTVIAIAHRLS-TLRDMSRILVLEHGTIQEDGTHEELL 580
Cdd:COG4138 161 MNSLDVAQQAALDRLLRELcQQGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
363-590 |
1.97e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 88.68 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 363 GISFAHEAVevfKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDS----LRRAISVVP 438
Cdd:PRK13646 15 GTPYEHQAI---HDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKyirpVRKRIGMVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 439 Q--EPALFHRSIRENIAYArPDATDEEVRDAAQKAHALefidMLPEGMNTLVGERG-VKLSGGQRQRVAIARAILKDAPI 515
Cdd:PRK13646 92 QfpESQLFEDTVEREIIFG-PKNFKMNLDEVKNYAHRL----LMDLGFSRDVMSQSpFQMSGGQMRKIAIVSILAMNPDI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083564009 516 LILDEATSALDSESEVAVQKALKELMY--GKTVIAIAHRLSTL-RDMSRILVLEHGTIQEDGTHEELLkNSGTYATLW 590
Cdd:PRK13646 167 IVLDEPTAGLDPQSKRQVMRLLKSLQTdeNKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELF-KDKKKLADW 243
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
341-583 |
2.15e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 88.61 E-value: 2.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 341 HEVIDVENAQDLVAKKGEI-VLDGISFaheavevfknfnlTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDD 419
Cdd:PRK13642 2 NKILEVENLVFKYEKESDVnQLNGVSF-------------SITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 420 QNIAEVTQDSLRRAISVVPQEP--ALFHRSIRENIAYARPDATDEEVRDAAQKAHALEFIDMLpegmnTLVGERGVKLSG 497
Cdd:PRK13642 69 ELLTAENVWNLRRKIGMVFQNPdnQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNML-----DFKTREPARLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 498 GQRQRVAIARAILKDAPILILDEATSALDSESEVAVQKALKEL--MYGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGT 575
Cdd:PRK13642 144 GQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIkeKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAA 223
|
....*...
gi 1083564009 576 HEELLKNS 583
Cdd:PRK13642 224 PSELFATS 231
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
361-582 |
2.42e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 89.25 E-value: 2.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 361 LDGISFAHEAvevfknfnltikdGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAE---VTQDSLRRAISVV 437
Cdd:PRK11308 31 LDGVSFTLER-------------GKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadpEAQKLLRQKIQIV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 438 PQEP--ALFHRSIRENIaYARPDATDEEVRDAAQKAHALEfidmlpegMNTLVGERGVK-------LSGGQRQRVAIARA 508
Cdd:PRK11308 98 FQNPygSLNPRKKVGQI-LEEPLLINTSLSAAERREKALA--------MMAKVGLRPEHydryphmFSGGQRQRIAIARA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 509 ILKDAPILILDEATSALDseseVAVQKALKELM------YGKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEELLK 581
Cdd:PRK11308 169 LMLDPDVVVADEPVSALD----VSVQAQVLNLMmdlqqeLGLSYVFISHDLSVVEHIAdEVMVMYLGRCVEKGTKEQIFN 244
|
.
gi 1083564009 582 N 582
Cdd:PRK11308 245 N 245
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
363-579 |
2.93e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 91.27 E-value: 2.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 363 GISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLllreydIAG------GAIKIDDQNIAEVTQDSLRR-AIS 435
Cdd:PRK15439 16 SISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKI------IAGivppdsGTLEIGGNPCARLTPAKAHQlGIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 436 VVPQEPALF-HRSIRENIAYARPDATDEEVR------------DAAQKAHALEFIDmlpegmntlvgergvklsggqRQR 502
Cdd:PRK15439 90 LVPQEPLLFpNLSVKENILFGLPKRQASMQKmkqllaalgcqlDLDSSAGSLEVAD---------------------RQI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1083564009 503 VAIARAILKDAPILILDEATSALD-SESEVAVQKALKELMYGKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEEL 579
Cdd:PRK15439 149 VEILRGLMRDSRILILDEPTASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQLAdRISVMRDGTIALSGKTADL 227
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
371-570 |
5.10e-19 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 86.17 E-value: 5.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 371 VEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLL---LREYDIAGGAIKIDDQniaEVTQDSLRRAISVVPQEPALF-HR 446
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNGQ---PRKPDQFQKCVAYVRQDDILLpGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 447 SIRENIAYARPDATDEEVRDAAQKAhaLEFIDMLPEGMNTLVGERGVK-LSGGQRQRVAIARAILKDAPILILDEATSAL 525
Cdd:cd03234 97 TVRETLTYTAILRLPRKSSDAIRKK--RVEDVLLRDLALTRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1083564009 526 DSESEVAVQKALKELMY-GKTVIAIAH--RLSTLRDMSRILVLEHGTI 570
Cdd:cd03234 175 DSFTALNLVSTLSQLARrNRIVILTIHqpRSDLFRLFDRILLLSSGEI 222
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
368-574 |
6.28e-19 |
|
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: 86.23 E-value: 6.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 368 HEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDqNIAEVTQDSLRRAISVV---------- 437
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-LVPWKRRKKFLRRIGVVfgqktqlwwd 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 438 --PQEPALFHRSIreniaYARPDATDEEVRDaaqkahalEFIDMLPEG--MNTLVgeRgvKLSGGQRQRVAIARAILKDA 513
Cdd:cd03267 110 lpVIDSFYLLAAI-----YDLPPARFKKRLD--------ELSELLDLEelLDTPV--R--QLSLGQRMRAEIAAALLHEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1083564009 514 PILILDEATSALDSESEVAVQKALKELM--YGKTVIAIAHrlsTLRDM----SRILVLEHGTIQEDG 574
Cdd:cd03267 173 EILFLDEPTIGLDVVAQENIRNFLKEYNreRGTTVLLTSH---YMKDIealaRRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
369-588 |
7.58e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 87.98 E-value: 7.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 369 EAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVS----LLLREY-DIAGGAIKIDDQNIAEVTQDS-----------LRR 432
Cdd:PRK13631 37 NELVALNNISYTFEKNKIYFIIGNSGSGKSTLVThfngLIKSKYgTIQVGDIYIGDKKNNHELITNpyskkiknfkeLRR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 433 AISVVPQEP--ALFHRSIRENIAYArPDATDEEVRDAAQKAHalEFIDMLpeGMNTLVGERG-VKLSGGQRQRVAIARAI 509
Cdd:PRK13631 117 RVSMVFQFPeyQLFKDTIEKDIMFG-PVALGVKKSEAKKLAK--FYLNKM--GLDDSYLERSpFGLSGGQKRRVAIAGIL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 510 LKDAPILILDEATSALDSESEVAVQKALKEL-MYGKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEELLKNSGTYA 587
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDPKGEHEMMQLILDAkANNKTVFVITHTMEHVLEVAdEVIVMDKGKILKTGTPYEIFTDQHIIN 271
|
.
gi 1083564009 588 T 588
Cdd:PRK13631 272 S 272
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
376-583 |
8.56e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 87.19 E-value: 8.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 376 NFNLTIKDGERIGLVGKSGAGKSTLV----SLLLReydiAGGAIKIDDQNIAEVTQD----SLRRAISVVPQ--EPALFH 445
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMqhfnALLKP----SSGTITIAGYHITPETGNknlkKLRKKVSLVFQfpEAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 446 RSIRENIAYARPD--ATDEEVRDAAqkahaLEFIDMLpeGMNTLVGERG-VKLSGGQRQRVAIARAILKDAPILILDEAT 522
Cdd:PRK13641 101 NTVLKDVEFGPKNfgFSEDEAKEKA-----LKWLKKV--GLSEDLISKSpFELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1083564009 523 SALDSESEVAVQKALKELMY-GKTVIAIAHRLSTLRDMSR-ILVLEHGTIQEDGTHEELLKNS 583
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYQKaGHTVILVTHNMDDVAEYADdVLVLEHGKLIKHASPKEIFSDK 236
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
344-579 |
8.77e-19 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 85.50 E-value: 8.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 344 IDVENaqdLVAKKGEIvldgisfahEAVevfKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIA 423
Cdd:cd03265 1 IEVEN---LVKKYGDF---------EAV---RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 424 EVTQDsLRRAISVVPQEPALFHR-SIRENIA-YARPDATDEEVRDAaQKAHALEFIDMLpEGMNTLVGergvKLSGGQRQ 501
Cdd:cd03265 66 REPRE-VRRRIGIVFQDLSVDDElTGWENLYiHARLYGVPGAERRE-RIDELLDFVGLL-EAADRLVK----TYSGGMRR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 502 RVAIARAILKDAPILILDEATSALDSESEVAVQKALKELM--YGKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEE 578
Cdd:cd03265 139 RLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKeeFGMTILLTTHYMEEAEQLCdRVAIIDHGRIIAEGTPEE 218
|
.
gi 1083564009 579 L 579
Cdd:cd03265 219 L 219
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
371-574 |
8.93e-19 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 85.28 E-value: 8.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 371 VEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIddqniaevtqdslRRAISVVPQEPALFHRSI-- 448
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV-------------RGRVSSLLGLGGGFNPELtg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 449 RENIAY------ARPDATDEEVRDAAQKAHALEFIDmLPegmntlvgergVK-LSGGQRQRVAIARAILKDAPILILDEA 521
Cdd:cd03220 102 RENIYLngrllgLSRKEIDEKIDEIIEFSELGDFID-LP-----------VKtYSSGMKARLAFAIATALEPDILLIDEV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1083564009 522 TSALDSESEVAVQKALKELM-YGKTVIAIAHRLSTLRDM-SRILVLEHGTIQEDG 574
Cdd:cd03220 170 LAVGDAAFQEKCQRRLRELLkQGKTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
359-582 |
1.04e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 86.68 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVE------VFKNFNLTIKDGERIGLVGKSGAGKSTLV----SLLLReydiAGGAIKIDD------QNI 422
Cdd:PRK13633 5 IKCKNVSYKYESNEesteklALDDVNLEVKKGEFLVILGRNGSGKSTIAkhmnALLIP----SEGKVYVDGldtsdeENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 423 AEVtqdslRRAISVVPQEP--ALFHRSIRENIAYA------RPDATDEEVRDAAQKAHALEFIDMLPEgmntlvgergvK 494
Cdd:PRK13633 81 WDI-----RNKAGMVFQNPdnQIVATIVEEDVAFGpenlgiPPEEIRERVDESLKKVGMYEYRRHAPH-----------L 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 495 LSGGQRQRVAIARAILKDAPILILDEATSALDSESEVAVQKALKEL--MYGKTVIAIAHRLSTLRDMSRILVLEHGTIQE 572
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELnkKYGITIILITHYMEEAVEADRIIVMDSGKVVM 224
|
250
....*....|
gi 1083564009 573 DGTHEELLKN 582
Cdd:PRK13633 225 EGTPKEIFKE 234
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
368-581 |
1.06e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 85.90 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 368 HEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLllreydIAGgaikiddqnIAEVTQDSLRRAISVVPQ-EPAL-FH 445
Cdd:COG1134 36 REEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKL------IAG---------ILEPTSGRVEVNGRVSALlELGAgFH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 446 RSI--RENI-AYAR-----PDATDEEVRDAAQKAHALEFIDMlPegmntlvgergVK-LSGGQRQRVAIARAILKDAPIL 516
Cdd:COG1134 101 PELtgRENIyLNGRllglsRKEIDEKFDEIVEFAELGDFIDQ-P-----------VKtYSSGMRARLAFAVATAVDPDIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1083564009 517 ILDEATSALDSESEVAVQKALKELM-YGKTVIAIAHRLSTLRDM-SRILVLEHGTIQEDGTHEELLK 581
Cdd:COG1134 169 LVDEVLAVGDAAFQKKCLARIRELReSGRTVIFVSHSMGAVRRLcDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
370-582 |
1.41e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 86.68 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 370 AVEVFKNFNLTIKDGERIGLVGKSGAGKSTLV----SLLLREydiaGGAI--KIDDQNIAEVTQD--------------- 428
Cdd:PRK13651 19 ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIehlnALLLPD----TGTIewIFKDEKNKKKTKEkekvleklviqktrf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 429 -------SLRRAISVVPQ--EPALFHRSIRENIAYArpdATDEEVRDAAQKAHALEFIDM--LPEgmnTLVGERGVKLSG 497
Cdd:PRK13651 95 kkikkikEIRRRVGVVFQfaEYQLFEQTIEKDIIFG---PVSMGVSKEEAKKRAAKYIELvgLDE---SYLQRSPFELSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 498 GQRQRVAIARAILKDAPILILDEATSALDSESEVAVQKALKEL-MYGKTVIAIAHRL-STLRDMSRILVLEHGTIQEDGT 575
Cdd:PRK13651 169 GQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLdNVLEWTKRTIFFKDGKIIKDGD 248
|
....*..
gi 1083564009 576 HEELLKN 582
Cdd:PRK13651 249 TYDILSD 255
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
357-570 |
1.85e-18 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 83.25 E-value: 1.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 357 GEIVL--DGISFAHeaveVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNI-AEVTQDSLRRA 433
Cdd:cd03215 1 GEPVLevRGLSVKG----AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVtRRSPRDAIRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 434 ISVVPQEP---ALFH-RSIRENIAYARPdatdeevrdaaqkahalefidmlpegmntlvgergvkLSGGQRQRVAIARAI 509
Cdd:cd03215 77 IAYVPEDRkreGLVLdLSVAENIALSSL-------------------------------------LSGGNQQKVVLARWL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1083564009 510 LKDAPILILDEATSALDSESEVAVQKALKEL-MYGKTVIAIAHRLSTLRDMS-RILVLEHGTI 570
Cdd:cd03215 120 ARDPRVLILDEPTRGVDVGAKAEIYRLIRELaDAGKAVLLISSELDELLGLCdRILVMYEGRI 182
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
358-579 |
3.96e-18 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 87.93 E-value: 3.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 358 EIVLDGISFAHEAVEVFKNF-----NLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRR 432
Cdd:COG4615 327 TLELRGVTYRYPGEDGDEGFtlgpiDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQ 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 433 AISVVPQEPALFHRsireniAYARPDATDEEvrdaaqKAHALefIDMLpeGMNTLVGERG-----VKLSGGQRQRVAIAR 507
Cdd:COG4615 407 LFSAVFSDFHLFDR------LLGLDGEADPA------RAREL--LERL--ELDHKVSVEDgrfstTDLSQGQRKRLALLV 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 508 AILKDAPILILDEATSALDSEsevavqkaLKELMY----------GKTVIAIAH--RLSTLRDmsRILVLEHGTIQEDGT 575
Cdd:COG4615 471 ALLEDRPILVFDEWAADQDPE--------FRRVFYtellpelkarGKTVIAISHddRYFDLAD--RVLKMDYGKLVELTG 540
|
....
gi 1083564009 576 HEEL 579
Cdd:COG4615 541 PAAL 544
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
374-566 |
4.57e-18 |
|
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: 87.92 E-value: 4.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 374 FKNFNLT-----IKDGERIGLVGKSGAGKSTLVSLLlreydiaGGAIKIDDQNIAEvtqdSLRraISVVPQepalfhrsi 448
Cdd:COG1245 351 YGGFSLEveggeIREGEVLGIVGPNGIGKTTFAKIL-------AGVLKPDEGEVDE----DLK--ISYKPQ--------- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 449 reniaYARPDaTDEEVRDAAQKAHA---------LEFIDmlPEGMNTLVgERGVK-LSGGQRQRVAIARAILKDAPILIL 518
Cdd:COG1245 409 -----YISPD-YDGTVEEFLRSANTddfgssyykTEIIK--PLGLEKLL-DKNVKdLSGGELQRVAIAACLSRDADLYLL 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1083564009 519 DEATSALDSESEVAVQKALKELM--YGKTVIAIAHRLsTLRDM--SRILVLE 566
Cdd:COG1245 480 DEPSAHLDVEQRLAVAKAIRRFAenRGKTAMVVDHDI-YLIDYisDRLMVFE 530
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
372-551 |
6.27e-18 |
|
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: 87.30 E-value: 6.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 372 EVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLllreydIAGgaikIDDQNIAEVT-QDSLRraISVVPQEPAL-FHRSIR 449
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRI------MAG----VDKDFNGEARpQPGIK--VGYLPQEPQLdPTKTVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 450 ENI-------------------AYARPDA-------TDEEVRD--AAQKAHALEF-IDMLPEGMNTLVGERGV-KLSGGQ 499
Cdd:TIGR03719 87 ENVeegvaeikdaldrfneisaKYAEPDAdfdklaaEQAELQEiiDAADAWDLDSqLEIAMDALRCPPWDADVtKLSGGE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1083564009 500 RQRVAIARAILKDAPILILDEATSALDSESEVAVQKALKElmYGKTVIAIAH 551
Cdd:TIGR03719 167 RRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQE--YPGTVVAVTH 216
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
363-576 |
6.68e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 86.91 E-value: 6.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 363 GISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLL--LREYDIAGGAIKIDDQNI-AEVTQDSLRRAISVVPQ 439
Cdd:PRK13549 10 NITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLsgVYPHGTYEGEIIFEGEELqASNIRDTERAGIAIIHQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 440 EPALF-HRSIRENI----------------AYARPDATDEEVRdaaqkahalefIDMLPegmNTLVGErgvkLSGGQRQR 502
Cdd:PRK13549 90 ELALVkELSVLENIflgneitpggimdydaMYLRAQKLLAQLK-----------LDINP---ATPVGN----LGLGQQQL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1083564009 503 VAIARAILKDAPILILDEATSALdSESEVAVQKA-LKELM-YGKTVIAIAHRLSTLRDMS-RILVLehgtiqEDGTH 576
Cdd:PRK13549 152 VEIAKALNKQARLLILDEPTASL-TESETAVLLDiIRDLKaHGIACIYISHKLNEVKAISdTICVI------RDGRH 221
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
357-577 |
7.83e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 85.27 E-value: 7.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 357 GEIVLDGISFaheavevfknfnlTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQdSLRRAISV 436
Cdd:PRK13536 53 DKAVVNGLSF-------------TVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARAR-LARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 437 VPQEPAL-FHRSIRENIA----YARPDATDEEvrdaAQKAHALEFIdMLPEGMNTLVGErgvkLSGGQRQRVAIARAILK 511
Cdd:PRK13536 119 VPQFDNLdLEFTVRENLLvfgrYFGMSTREIE----AVIPSLLEFA-RLESKADARVSD----LSGGMKRRLTLARALIN 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1083564009 512 DAPILILDEATSALDSESEVAVQKALKELM-YGKTVIAIAHRLSTL-RDMSRILVLEHG-TIQEDGTHE 577
Cdd:PRK13536 190 DPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHFMEEAeRLCDRLCVLEAGrKIAEGRPHA 258
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
372-585 |
9.71e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 83.59 E-value: 9.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 372 EVFKNFNLTIKDGERIGLVGKSGAGKSTL---VSLLLR----EYDIAGGAIKIDDQNIAEVtqdslRRAISVVPQEP--A 442
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLflhFNGILKptsgEVLIKGEPIKYDKKSLLEV-----RKTVGIVFQNPddQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 443 LFHRSIRENIAYA------RPDATDEEVRDAAQKAHALEFIDMLPEgmntlvgergvKLSGGQRQRVAIARAILKDAPIL 516
Cdd:PRK13639 91 LFAPTVEEDVAFGplnlglSKEEVEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1083564009 517 ILDEATSALDSESEVAVQKALKEL-MYGKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEELLKNSGT 585
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVYAdKVYVMSDGKIIKEGTPKEVFSDIET 230
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
369-551 |
1.25e-17 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 82.99 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 369 EAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLllreydIAG------GAIKIDDQniaEVTQDSLRRAisVVPQEPA 442
Cdd:COG4525 18 QPQPALQDVSLTIESGEFVVALGASGCGKTTLLNL------IAGflapssGEITLDGV---PVTGPGADRG--VVFQKDA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 443 LFH-RSIRENIAYARPDATdeeVRDAAQKAHALEFIdmlpegmnTLVGERGV------KLSGGQRQRVAIARAILKDAPI 515
Cdd:COG4525 87 LLPwLNVLDNVAFGLRLRG---VPKAERRARAEELL--------ALVGLADFarrriwQLSGGMRQRVGIARALAADPRF 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 1083564009 516 LILDEATSALDSESEVAVQKALKEL--MYGKTVIAIAH 551
Cdd:COG4525 156 LLMDEPFGALDALTREQMQELLLDVwqRTGKGVFLITH 193
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
358-583 |
1.34e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 83.53 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 358 EIVLDGISFAHEAVEVF-----KNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQD---- 428
Cdd:PRK13634 2 DITFQKVEHRYQYKTPFerralYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkklk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 429 SLRRAISVVPQ--EPALFHRSIRENIAYArpdATDEEVRDAAQKAHALEFIDMLpeGMNTLVGERG-VKLSGGQRQRVAI 505
Cdd:PRK13634 82 PLRKKVGIVFQfpEHQLFEETVEKDICFG---PMNFGVSEEDAKQKAREMIELV--GLPEELLARSpFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 506 ARAILKDAPILILDEATSALDSESevavQKALKELMY------GKTVIAIAHrlsTLRDMSR----ILVLEHGTIQEDGT 575
Cdd:PRK13634 157 AGVLAMEPEVLVLDEPTAGLDPKG----RKEMMEMFYklhkekGLTTVLVTH---SMEDAARyadqIVVMHKGTVFLQGT 229
|
....*...
gi 1083564009 576 HEELLKNS 583
Cdd:PRK13634 230 PREIFADP 237
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
367-565 |
1.64e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 80.74 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 367 AHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLlreydiaGGAIKiddQNIAEVTQDSLRRaISVVPQ---EPAL 443
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVL-------AGVLR---PTSGTVRRAGGAR-VAYVPQrseVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 444 FHRSIRENIA---------YARPDATDEEVRDaaqkaHALEFIdmlpeGMNTLVGERGVKLSGGQRQRVAIARAILKDAP 514
Cdd:NF040873 70 LPLTVRDLVAmgrwarrglWRRLTRDDRAAVD-----DALERV-----GLADLAGRQLGELSGGQRQRALLAQGLAQEAD 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1083564009 515 ILILDEATSALDSESEVAVQKALKELMY-GKTVIAIAHRLSTLRDMSRILVL 565
Cdd:NF040873 140 LLLLDEPTTGLDAESRERIIALLAEEHArGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
361-526 |
1.77e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 81.68 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 361 LDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAISVVPQE 440
Cdd:PRK10247 10 LQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 441 PALFHRSIRENIAYA---RPDATDEE--VRDAAQKAhalefidmLPEgmnTLVGERGVKLSGGQRQRVAIARAILKDAPI 515
Cdd:PRK10247 90 PTLFGDTVYDNLIFPwqiRNQQPDPAifLDDLERFA--------LPD---TILTKNIAELSGGEKQRISLIRNLQFMPKV 158
|
170
....*....|.
gi 1083564009 516 LILDEATSALD 526
Cdd:PRK10247 159 LLLDEITSALD 169
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
359-567 |
2.15e-17 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 79.89 E-value: 2.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVEVF-KNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIddqniaevtqdSLRRAISVV 437
Cdd:cd03223 1 IELENLSLATPDGRVLlKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM-----------PEGEDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 438 PQEPALFHRSIRENIAYARPDAtdeevrdaaqkahalefidmlpegmntlvgergvkLSGGQRQRVAIARAILKDAPILI 517
Cdd:cd03223 70 PQRPYLPLGTLREQLIYPWDDV-----------------------------------LSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1083564009 518 LDEATSALDSESEVAVQKALKELmyGKTVIAIAHRLSTLRDMSRILVLEH 567
Cdd:cd03223 115 LDEATSALDEESEDRLYQLLKEL--GITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
362-580 |
3.55e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.96 E-value: 3.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 362 DGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAISVVPQE- 440
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNa 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 441 --PALFhrSIRENIAYAR----PDATD--EEVRDAAQKAhalefidMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKD 512
Cdd:PRK10253 91 ttPGDI--TVQELVARGRyphqPLFTRwrKEDEEAVTKA-------MQATGITHLADQSVDTLSGGQRQRAWIAMVLAQE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1083564009 513 APILILDEATSALDSESEVAVQKALKEL--MYGKTVIAIAHRLS-TLRDMSRILVLEHGTIQEDGTHEELL 580
Cdd:PRK10253 162 TAIMLLDEPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
373-583 |
5.24e-17 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 80.66 E-value: 5.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 373 VFKNFNLTIKDGERIGLVGKSGAGKSTLVslllreYDIAG------GAIKIDDQNIAEVTQDslRRA---ISVVPQEPAL 443
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTF------YMIVGlvkpdsGKILLDGQDITKLPMH--KRArlgIGYLPQEASI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 444 FHR-SIRENIAYARPDATDeevrDAAQKAHALEfiDMLPE-GMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDEA 521
Cdd:cd03218 87 FRKlTVEENILAVLEIRGL----SKKEREEKLE--ELLEEfHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1083564009 522 TSALDSESEVAVQKALKELMYGKTVIAIA-HRLS-TLRDMSRILVLEHGTIQEDGTHEELLKNS 583
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
378-572 |
9.19e-17 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 83.48 E-value: 9.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 378 NLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAISVVPQEPALFHRSIreniayarp 457
Cdd:PRK10522 343 NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLL--------- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 458 dATDEEVRDAAQKAHALEFIDMlpEGMNTLVGER--GVKLSGGQRQRVAIARAILKDAPILILDEATSALDSE-SEVAVQ 534
Cdd:PRK10522 414 -GPEGKPANPALVEKWLERLKM--AHKLELEDGRisNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHfRREFYQ 490
|
170 180 190
....*....|....*....|....*....|....*....
gi 1083564009 535 KALKELM-YGKTVIAIAHRLSTLRDMSRILVLEHGTIQE 572
Cdd:PRK10522 491 VLLPLLQeMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
372-579 |
1.15e-16 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 79.49 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 372 EVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEV-TQDSLRRAISVVPQEPALFHR-SIR 449
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLpPHERARAGIAYVPQGREIFPRlTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 450 ENI---AYARPDatdeevRDAAQKAHALEFIDMLPEgmntLVGERGVKLSGGQRQRVAIARAILKDAPILILDEATSALD 526
Cdd:TIGR03410 94 ENLltgLAALPR------RSRKIPDEIYELFPVLKE----MLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQ 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1083564009 527 SeSEVA-VQKALKEL--MYGKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEEL 579
Cdd:TIGR03410 164 P-SIIKdIGRVIRRLraEGGMAILLVEQYLDFARELAdRYYVMERGRVVASGAGDEL 219
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
377-584 |
1.24e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 79.98 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 377 FNLTIKDGERIGLVGKSGAGKSTLVSLllreydIAG-----GAIKIDDQNIAEVTQDSL--RRAIsVVPQEPALFHRSIR 449
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLAR------MAGllpgsGSIQFAGQPLEAWSAAELarHRAY-LSQQQTPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 450 ENIAYARPDATDEEVRDAA--QKAHALEFIDMLPEGMNTlvgergvkLSGGQRQRVAIARAILKDAP-------ILILDE 520
Cdd:PRK03695 88 QYLTLHQPDKTRTEAVASAlnEVAEALGLDDKLGRSVNQ--------LSGGEWQRVRLAAVVLQVWPdinpagqLLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1083564009 521 ATSALDSESEVAVQKALKEL-MYGKTVIAIAHRLS-TLRDMSRILVLEHGTIQEDGTHEELLKNSG 584
Cdd:PRK03695 160 PMNSLDVAQQAALDRLLSELcQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
354-581 |
1.53e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 82.76 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 354 AKKGEIVL--DGISfaheAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVT-QDSL 430
Cdd:COG1129 250 AAPGEVVLevEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSpRDAI 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 431 RRAISVVP---QEPALF-HRSIRENIAYARPD--ATDEEVRDAAQKAHALEFIDML---PEGMNTLVGErgvkLSGGQRQ 501
Cdd:COG1129 326 RAGIAYVPedrKGEGLVlDLSIRENITLASLDrlSRGGLLDRRRERALAEEYIKRLrikTPSPEQPVGN----LSGGNQQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 502 RVAIARAILKDAPILILDEATSALDSESEVAVQKALKEL-MYGKTVIAIAHRLSTLRDMS-RILVLEHGTIQ-----EDG 574
Cdd:COG1129 402 KVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELaAEGKAVIVISSELPELLGLSdRILVMREGRIVgeldrEEA 481
|
....*..
gi 1083564009 575 THEELLK 581
Cdd:COG1129 482 TEEAIMA 488
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
359-569 |
1.54e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 82.52 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVT-QDSLRRAISVV 437
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhKLAAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 438 PQEPALFHR-SIRENIAYAR---------PDATDEEVRdaaQKAHALEFIDMLPEGMNTLVGErgvkLSGGQRQRVAIAR 507
Cdd:PRK09700 86 YQELSVIDElTVLENLYIGRhltkkvcgvNIIDWREMR---VRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1083564009 508 AILKDAPILILDEATSAL-DSESE--VAVQKALKElmYGKTVIAIAHRLSTLRDM-SRILVLEHGT 569
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLtNKEVDylFLIMNQLRK--EGTAIVYISHKLAEIRRIcDRYTVMKDGS 222
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
372-551 |
1.71e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 78.38 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 372 EVFKNFNLTIKDGERIGLVGKSGAGKSTL---VSLLLReydIAGGAIKIDDQNI-----AEVT-----QDSLRRAISVvp 438
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLlrlIAGLLP---PAAGTIKLDGGDIddpdvAEAChylghRNAMKPALTV-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 439 qepalfhrsiRENIAY-ARPDATDEEVRDAAQKAHALEFIDMLPEGMntlvgergvkLSGGQRQRVAIARAILKDAPILI 517
Cdd:PRK13539 91 ----------AENLEFwAAFLGGEELDIAAALEAVGLAPLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWI 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 1083564009 518 LDEATSALDSESevavQKALKELMY-----GKTVIAIAH 551
Cdd:PRK13539 151 LDEPTAALDAAA----VALFAELIRahlaqGGIVIAATH 185
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
378-579 |
1.88e-16 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 80.92 E-value: 1.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 378 NLTIKDGERIGLVGKSGAGKS----TLVSLLLREYDIAGGAI---------------KIDDQNIAEVTQD---SLRRAIS 435
Cdd:PRK09473 36 NFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRIGGSATfngreilnlpekelnKLRAEQISMIFQDpmtSLNPYMR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 436 VVPQ--EPALFHRSIRENIAYarpdatDEEVR--DAAQKAHALEFIDMLPEgmntlvgergvKLSGGQRQRVAIARAILK 511
Cdd:PRK09473 116 VGEQlmEVLMLHKGMSKAEAF------EESVRmlDAVKMPEARKRMKMYPH-----------EFSGGMRQRVMIAMALLC 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1083564009 512 DAPILILDEATSALDseseVAVQKALKELM------YGKTVIAIAHRLSTLRDM-SRILVLEHGTIQEDGTHEEL 579
Cdd:PRK09473 179 RPKLLIADEPTTALD----VTVQAQIMTLLnelkreFNTAIIMITHDLGVVAGIcDKVLVMYAGRTMEYGNARDV 249
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
364-580 |
2.23e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 82.16 E-value: 2.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 364 ISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLR-------EYDIAGGAIKIDDQNIAEVTQDSLRRAISV 436
Cdd:TIGR03269 290 ISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGvleptsgEVNVRVGDEWVDMTKPGPDGRGRAKRYIGI 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 437 VPQEPALF-HRSIRENIAyarpDATDEEVRD--AAQKA-HALEFIDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKD 512
Cdd:TIGR03269 370 LHQEYDLYpHRTVLDNLT----EAIGLELPDelARMKAvITLKMVGFDEEKAEEILDKYPDELSEGERHRVALAQVLIKE 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1083564009 513 APILILDEATSALDSESEVAVQ----KALKELmyGKTVIAIAHRLSTLRDM-SRILVLEHGTIQEDGTHEELL 580
Cdd:TIGR03269 446 PRIVILDEPTGTMDPITKVDVThsilKAREEM--EQTFIIVSHDMDFVLDVcDRAALMRDGKIVKIGDPEEIV 516
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
381-581 |
2.85e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 82.40 E-value: 2.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 381 IKDGERIGLVGKSGAGKSTLVSLL--------LREYDIAGGAIKIDDQNIaevtqdslrRAISVVPQEPALF--HRSIRE 450
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALafrspkgvKGSGSVLLNGMPIDAKEM---------RAISAYVQQDDLFipTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 451 NIAY-AR---PDATDEEVRDAAQKahalEFIDM--LPEGMNTLVGERGVK--LSGGQRQRVAIARAILKDAPILILDEAT 522
Cdd:TIGR00955 119 HLMFqAHlrmPRRVTKKEKRERVD----EVLQAlgLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1083564009 523 SALDSESEVAVQKALKEL-MYGKTVIAIAHR-LSTLRDM-SRILVLEHGTIQEDGTHEELLK 581
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLaQKGKTIICTIHQpSSELFELfDKIILMAEGRVAYLGSPDQAVP 256
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
380-551 |
3.92e-16 |
|
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: 78.22 E-value: 3.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 380 TIKDGERIGLVGKSGAGKSTLVSLLlreydiaGGAIKIDDQNIaevtqDSLRRAISVVPQepalfhrsireniaYARPDa 459
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKML-------AGVLKPDEGDI-----EIELDTVSYKPQ--------------YIKAD- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 460 TDEEVRDAAQKAHALEFID-------MLPEGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDEATSALDSESEVA 532
Cdd:cd03237 74 YEGTVRDLLSSITKDFYTHpyfkteiAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLM 153
|
170 180
....*....|....*....|.
gi 1083564009 533 VQKALKELMYG--KTVIAIAH 551
Cdd:cd03237 154 ASKVIRRFAENneKTAFVVEH 174
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
378-579 |
4.29e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 78.52 E-value: 4.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 378 NLTIKDGERIGLVGKSGAGKSTLV---SLLLREYDIAGGAIKI---DDQNIAEVTQD--SLRRAISVVPQEPALFHR-SI 448
Cdd:PRK09984 24 DLNIHHGEMVALLGPSGSGKSTLLrhlSGLITGDKSAGSHIELlgrTVQREGRLARDirKSRANTGYIFQQFNLVNRlSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 449 RENIAYARPDATD---EEVR--DAAQKAHALEFIDMLpeGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDEATS 523
Cdd:PRK09984 104 LENVLIGALGSTPfwrTCFSwfTREQKQRALQALTRV--GMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1083564009 524 ALDSESEVAVQKALKELMY--GKTVIAIAHRLS-TLRDMSRILVLEHGTIQEDGTHEEL 579
Cdd:PRK09984 182 SLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
377-589 |
4.29e-16 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 82.37 E-value: 4.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 377 FNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIaEVTQDSLRRAISVVPQEPALFHR-SIRENIAYA 455
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 456 rpdatdEEVRDAAQKAHALEFIDMLPE-GMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDEATSALDSESEVAVQ 534
Cdd:TIGR01257 1028 ------AQLKGRSWEEAQLEMEAMLEDtGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1083564009 535 KALKELMYGKTVIAIAHRLSTLRDM-SRILVLEHGTIQEDGThEELLKN---SGTYATL 589
Cdd:TIGR01257 1102 DLLLKYRSGRTIIMSTHHMDEADLLgDRIAIISQGRLYCSGT-PLFLKNcfgTGFYLTL 1159
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
374-566 |
5.04e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 81.39 E-value: 5.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 374 FKNFNL-----TIKDGERIGLVGKSGAGKSTLVSLLlreydiaGGAIKIDDQNI-AEVTqdslrraISVVPQepalfhrs 447
Cdd:PRK13409 350 LGDFSLeveggEIYEGEVIGIVGPNGIGKTTFAKLL-------AGVLKPDEGEVdPELK-------ISYKPQ-------- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 448 ireniaYARPDaTDEEVRD----AAQKAHA----LEFIDmlPEGMNTLVgERGVK-LSGGQRQRVAIARAILKDAPILIL 518
Cdd:PRK13409 408 ------YIKPD-YDGTVEDllrsITDDLGSsyykSEIIK--PLQLERLL-DKNVKdLSGGELQRVAIAACLSRDADLYLL 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1083564009 519 DEATSALDSESEVAVQKALKELM--YGKTVIAIAHRLSTLRDMS-RILVLE 566
Cdd:PRK13409 478 DEPSAHLDVEQRLAVAKAIRRIAeeREATALVVDHDIYMIDYISdRLMVFE 528
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
376-581 |
5.06e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 79.01 E-value: 5.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 376 NFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDS----LRRAISVVPQEP--ALFHRSIR 449
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikpVRKKVGVVFQFPesQLFEETVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 450 ENIAYARPD---ATDEEVRDAAQKahaLEFIdmlpeGMNTLVGERG-VKLSGGQRQRVAIARAILKDAPILILDEATSAL 525
Cdd:PRK13643 104 KDVAFGPQNfgiPKEKAEKIAAEK---LEMV-----GLADEFWEKSpFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1083564009 526 DSESEVAVQKALKEL-MYGKTVIAIAHRLSTLRDMSR-ILVLEHGTIQEDGTHEELLK 581
Cdd:PRK13643 176 DPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADYADyVYLLEKGHIISCGTPSDVFQ 233
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
343-577 |
6.34e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 78.69 E-value: 6.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 343 VIDVENAQDLVAKKgeIVLDGISFaheavevfknfnlTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNI 422
Cdd:PRK13537 7 PIDFRNVEKRYGDK--LVVDGLSF-------------HVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 423 AEVTQDSlRRAISVVPQ----EPALfhrSIRENI-AYARP-DATDEEVRDAAQKAhaLEFIDmLPEGMNTLVGErgvkLS 496
Cdd:PRK13537 72 PSRARHA-RQRVGVVPQfdnlDPDF---TVRENLlVFGRYfGLSAAAARALVPPL--LEFAK-LENKADAKVGE----LS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 497 GGQRQRVAIARAILKDAPILILDEATSALDSESEVAVQKALKELM-YGKTVIAIAHRLSTL-RDMSRILVLEHG-TIQED 573
Cdd:PRK13537 141 GGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAeRLCDRLCVIEEGrKIAEG 220
|
....
gi 1083564009 574 GTHE 577
Cdd:PRK13537 221 APHA 224
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
359-573 |
7.07e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 77.80 E-value: 7.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDslrraISVVP 438
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARED-----TRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 439 QEPALFH-RSIRENIAYA-RPDAtdeevRDAAQKAhaLEFIdmlpeGMNTLVGERGVKLSGGQRQRVAIARAILKDAPIL 516
Cdd:PRK11247 88 QDARLLPwKKVIDNVGLGlKGQW-----RDAALQA--LAAV-----GLADRANEWPAALSGGQKQRVALARALIHRPGLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 517 ILDEATSALDSESEVAVQKALKEL--MYGKTVIAIAHRLSTLRDMS-RILVLEHGTIQED 573
Cdd:PRK11247 156 LLDEPLGALDALTRIEMQDLIESLwqQHGFTVLLVTHDVSEAVAMAdRVLLIEEGKIGLD 215
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
343-580 |
1.43e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 77.08 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 343 VIDVENAQdLVAKKGEIVLDGISfaheavevfknfnLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNI 422
Cdd:PRK13647 4 IIEVEDLH-FRYKDGTKALKGLS-------------LSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 423 AEVTQDSLRRAISVVPQEP--ALFHRSIRENIAYA------RPDATDEEVRDAAQKAHALEFIDMLPEgmntlvgergvK 494
Cdd:PRK13647 70 NAENEKWVRSKVGLVFQDPddQVFSSTVWDDVAFGpvnmglDKDEVERRVEEALKAVRMWDFRDKPPY-----------H 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 495 LSGGQRQRVAIARAILKDAPILILDEATSALDSESEVAVQKALKEL-MYGKTVIAIAHRLS-TLRDMSRILVLEHGTIQE 572
Cdd:PRK13647 139 LSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLA 218
|
....*...
gi 1083564009 573 DGTHEELL 580
Cdd:PRK13647 219 EGDKSLLT 226
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
372-551 |
1.66e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 79.78 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 372 EVFKNFNLTIKDGERIGLVGKSGAGKSTLvsllLReydIAGGaikIDDQNIAEVT-QDSLRraISVVPQEPALFH-RSIR 449
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTL----LR---IMAG---VDKEFEGEARpAPGIK--VGYLPQEPQLDPeKTVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 450 ENI-------------------AYARPDA-TDE------EVRD--AAQKAHALE-FIDM------LPEGmNTLVGergvK 494
Cdd:PRK11819 89 ENVeegvaevkaaldrfneiyaAYAEPDAdFDAlaaeqgELQEiiDAADAWDLDsQLEIamdalrCPPW-DAKVT----K 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1083564009 495 LSGGQRQRVAIARAILKDAPILILDEATSALDSESeVA-VQKALKElmYGKTVIAIAH 551
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES-VAwLEQFLHD--YPGTVVAVTH 218
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
366-582 |
1.84e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 76.80 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 366 FAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLlreydiAG------GAIKIDD------------QNIAEVTQ 427
Cdd:COG4167 21 FRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKML------AGiieptsGEILINGhkleygdykyrcKHIRMIFQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 428 D---SL--RRAISVVPQEPALFHrsireniayarpdaTDEEVRDAAQKAHA-LEFIDMLPEGMNTLVGErgvkLSGGQRQ 501
Cdd:COG4167 95 DpntSLnpRLNIGQILEEPLRLN--------------TDLTAEEREERIFAtLRLVGLLPEHANFYPHM----LSSGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 502 RVAIARAILKDAPILILDEATSALDseseVAVQKALKELM------YGKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDG 574
Cdd:COG4167 157 RVALARALILQPKIIIADEALAALD----MSVRSQIINLMlelqekLGISYIYVSQHLGIVKHISdKVLVMHQGEVVEYG 232
|
....*...
gi 1083564009 575 THEELLKN 582
Cdd:COG4167 233 KTAEVFAN 240
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
374-559 |
2.35e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 79.08 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 374 FKNFNL-TIKDGERIGLVGKSGAGKSTLVSLL-------LREYDiaggaikiDDQNIAEVT--------QDSLRR----A 433
Cdd:PRK13409 88 FKLYGLpIPKEGKVTGILGPNGIGKTTAVKILsgelipnLGDYE--------EEPSWDEVLkrfrgtelQNYFKKlyngE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 434 ISVV--PQE----PALFHRSIRENIayarpDATDEE-VRDaaqkahalEFIDMLpeGMNTLVgERGVK-LSGGQRQRVAI 505
Cdd:PRK13409 160 IKVVhkPQYvdliPKVFKGKVRELL-----KKVDERgKLD--------EVVERL--GLENIL-DRDISeLSGGELQRVAI 223
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1083564009 506 ARAILKDAPILILDEATSALDSESEVAVQKALKELMYGKTVIAIAHRLSTLrDM 559
Cdd:PRK13409 224 AAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDLAVL-DY 276
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
361-553 |
2.46e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.80 E-value: 2.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 361 LDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIA-EVTQDSLRRAISVVPQ 439
Cdd:PRK11288 7 FDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGVAIIYQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 440 E----PALfhrSIRENIAYARPDATDEEVRDAAQKAHALEFIDMLpeGMNTLVGERGVKLSGGQRQRVAIARAILKDAPI 515
Cdd:PRK11288 87 ElhlvPEM---TVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHL--GVDIDPDTPLKYLSIGQRQMVEIAKALARNARV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1083564009 516 LILDEATSALDS-ESEV--AVQKALKElmYGKTVIAIAHRL 553
Cdd:PRK11288 162 IAFDEPTSSLSArEIEQlfRVIRELRA--EGRVILYVSHRM 200
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
359-575 |
2.86e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 76.32 E-value: 2.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVEVFK-----NFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQD----S 429
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEgralfDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkdikQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 430 LRRAISVVPQ--EPALFHRSIRENIAYARPD--ATDEEVRDAAQKAHALEFIDmlpegmNTLVGERGVKLSGGQRQRVAI 505
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1083564009 506 ARAILKDAPILILDEATSALDSesevavqKALKELMY--------GKTVIAIAHRLSTLRDMSR-ILVLEHGTIQEDGT 575
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDP-------KGRKELMTlfkklhqsGMTIVLVTHLMDDVANYADfVYVLEKGKLVLSGK 228
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
371-582 |
4.17e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 78.36 E-value: 4.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 371 VEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQ---DSLRRAISVVPQEPalfHRS 447
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPgklQALRRDIQFIFQDP---YAS 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 448 I--RENIAYArpdaTDEEVR-------DAAQK--AHALEFIDMLPEGMNTLVGErgvkLSGGQRQRVAIARAILKDAPIL 516
Cdd:PRK10261 414 LdpRQTVGDS----IMEPLRvhgllpgKAAAArvAWLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVI 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1083564009 517 ILDEATSALDSESEVAVQKALKELM--YGKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEELLKN 582
Cdd:PRK10261 486 IADEAVSALDVSIRGQIINLLLDLQrdFGIAYLFISHDMAVVERIShRVAVMYLGQIVEIGPRRAVFEN 554
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
372-575 |
4.19e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 74.85 E-value: 4.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 372 EVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDS---LR-RAISVVPQepalFHR- 446
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRnQKLGFIYQ----FHHl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 447 ----SIRENIAYarPDATDEEVRDAAQKaHALEfidMLPE-GMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDEA 521
Cdd:PRK11629 99 lpdfTALENVAM--PLLIGKKKPAEINS-RALE---MLAAvGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1083564009 522 TSALDSESEVAVQKALKEL--MYGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGT 575
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELnrLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
359-579 |
4.92e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 75.92 E-value: 4.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGI--SFA-HEAVevfKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIaevtQDSLRRAIS 435
Cdd:COG4152 2 LELKGLtkRFGdKTAV---DDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL----DPEDRRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 436 VVPQEPALFHR-SIRENIAY-AR----PDAtdeevrDAAQKAHA-LEFIDmLPEGMNTLVGErgvkLSGGQRQRVAIARA 508
Cdd:COG4152 75 YLPEERGLYPKmKVGEQLVYlARlkglSKA------EAKRRADEwLERLG-LGDRANKKVEE----LSKGNQQKVQLIAA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1083564009 509 ILKDAPILILDEATSALDSeseVAVQ---KALKELMY-GKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEEL 579
Cdd:COG4152 144 LLHDPELLILDEPFSGLDP---VNVEllkDVIRELAAkGTTVIFSSHQMELVEELCdRIVIINKGRKVLSGSVDEI 216
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
372-551 |
5.09e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 75.26 E-value: 5.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 372 EVFKNFNLTIKDGERIGLVGKSGAGKSTLVS-----LLLREYDIAGGAIKIDDQNI--AEVTQDSLRRAISVVPQEPALF 444
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrlLELNEEARVEGEVRLFGRNIysPDVDPIEVRREVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 445 -HRSIRENIA-------YARP-DATDEEVRDAAQKAhalefidMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKDAPI 515
Cdd:PRK14267 98 pHLTIYDNVAigvklngLVKSkKELDERVEWALKKA-------ALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKI 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 1083564009 516 LILDEATSALDSESEVAVQKALKELMYGKTVIAIAH 551
Cdd:PRK14267 171 LLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
369-581 |
5.51e-15 |
|
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: 73.72 E-value: 5.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 369 EAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLL--REYDIAGGAIKIDDQNIAEV-TQDSLRRAISVVPQEPALFh 445
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghPKYEVTEGEILFKGEDITDLpPEERARLGIFLAFQYPPEI- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 446 rsireniayarpdatdEEVRdaaqkahalefidmlpegMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDEATSAL 525
Cdd:cd03217 90 ----------------PGVK------------------NADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1083564009 526 DSESEVAVQKALKELM-YGKTVIAIAH--RLSTLRDMSRILVLEHGTIQEDGTHEELLK 581
Cdd:cd03217 136 DIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKELALE 194
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
371-579 |
6.10e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 75.22 E-value: 6.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 371 VEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAISVVPQEP--ALFHRSI 448
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 449 RENIAYARPDATDEEVRDAAQKAHALEFIdmlpeGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDEATSALDSE 528
Cdd:PRK13652 97 EQDIAFGPINLGLDEETVAHRVSSALHML-----GLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQ 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1083564009 529 SEVAVQKALKEL--MYGKTVIAIAHRLSTLRDMSR-ILVLEHGTIQEDGTHEEL 579
Cdd:PRK13652 172 GVKELIDFLNDLpeTYGMTVIFSTHQLDLVPEMADyIYVMDKGRIVAYGTVEEI 225
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
374-559 |
1.06e-14 |
|
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: 77.13 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 374 FKNFNL-TIKDGERIGLVGKSGAGKSTLVSLL-------LREYDiaggaikiDDQNIAEVT--------QDSLRR----A 433
Cdd:COG1245 88 FRLYGLpVPKKGKVTGILGPNGIGKSTALKILsgelkpnLGDYD--------EEPSWDEVLkrfrgtelQDYFKKlangE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 434 ISVV--PQepalfhrsireNIAYArPDATDEEVRDAAQKAH----ALEFIDMLpeGMNTLVgERGVK-LSGGQRQRVAIA 506
Cdd:COG1245 160 IKVAhkPQ-----------YVDLI-PKVFKGTVRELLEKVDergkLDELAEKL--GLENIL-DRDISeLSGGELQRVAIA 224
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1083564009 507 RAILKDAPILILDEATSALDSESEVAVQKALKELM-YGKTVIAIAHRLSTLrDM 559
Cdd:COG1245 225 AALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAeEGKYVLVVEHDLAIL-DY 277
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
360-568 |
1.31e-14 |
|
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: 73.08 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 360 VLDGISFaheavevfknfnlTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIaevtQDSLRRAISVVPQ 439
Cdd:cd03269 15 ALDDISF-------------SVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL----DIAARNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 440 EPALF-HRSIRENIAYarpdatdeevrdAAQ-----KAHALEFIDMLPE--GMNTLVGERGVKLSGGQRQRVAIARAILK 511
Cdd:cd03269 78 ERGLYpKMKVIDQLVY------------LAQlkglkKEEARRRIDEWLErlELSEYANKRVEELSKGNQQKVQFIAAVIH 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1083564009 512 DAPILILDEATSALDSESEVAVQKALKELM-YGKTVIAIAHRLSTLRDM-SRILVLEHG 568
Cdd:cd03269 146 DPELLILDEPFSGLDPVNVELLKDVIRELArAGKTVILSTHQMELVEELcDRVLLLNKG 204
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
372-520 |
1.33e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 73.52 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 372 EVFKNFNLTIKDGERIGLVGKSGAGKSTLVslllreYDIAG------GAIKIDDQNIaevTQDSL-RRA---ISVVPQEP 441
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTTF------YMIVGlvkpdsGRIFLDGEDI---THLPMhKRArlgIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 442 ALFHR-SIRENIAYARpdatdeEVR--DAAQKAHALEfiDMLPE-GMNTLVGERGVKLSGGQRQRVAIARAILKDAPILI 517
Cdd:COG1137 88 SIFRKlTVEDNILAVL------ELRklSKKEREERLE--ELLEEfGITHLRKSKAYSLSGGERRRVEIARALATNPKFIL 159
|
...
gi 1083564009 518 LDE 520
Cdd:COG1137 160 LDE 162
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
361-582 |
1.33e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 73.76 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 361 LDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAE-VTQDSLRRAISVVPQ 439
Cdd:PRK11614 8 FDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKIMREAVAIVPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 440 EPALFHR-SIRENIAYARPDATDEEVRDAAQKAHalefiDMLPEGMNTLVgERGVKLSGGQRQRVAIARAILKDAPILIL 518
Cdd:PRK11614 88 GRRVFSRmTVEENLAMGGFFAERDQFQERIKWVY-----ELFPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPRLLLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1083564009 519 DEATSALDSESEVAVQKALKELMY-GKTVIAIAHRLS-TLRDMSRILVLEHGTIQEDGTHEELLKN 582
Cdd:PRK11614 162 DEPSLGLAPIIIQQIFDTIEQLREqGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLAN 227
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
364-581 |
1.35e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 76.82 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 364 ISFAHEAVEV--FKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQ----------NIAEVTQDSLR 431
Cdd:PRK10261 20 IAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELSEQSAAQMR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 432 RA----ISVVPQEPAL-------FHRSIRENIAYARPDATDEEVRDAAQkahALEFIdMLPEGmNTLVGERGVKLSGGQR 500
Cdd:PRK10261 100 HVrgadMAMIFQEPMTslnpvftVGEQIAESIRLHQGASREEAMVEAKR---MLDQV-RIPEA-QTILSRYPHQLSGGMR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 501 QRVAIARAILKDAPILILDEATSALDSESEVAVQKALKELMYGKT--VIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHE 577
Cdd:PRK10261 175 QRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIAdRVLVMYQGEAVETGSVE 254
|
....
gi 1083564009 578 ELLK 581
Cdd:PRK10261 255 QIFH 258
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
354-579 |
1.60e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 76.22 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 354 AKKGEIVL--DGISFA-HEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSL 430
Cdd:COG3845 251 AEPGEVVLevENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRER 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 431 RRA-ISVVPQEPalfHR-------SIRENIA----YARPDATDEEVRDAAQKAHALEFI---DMLPEGMNTLVGergvKL 495
Cdd:COG3845 331 RRLgVAYIPEDR---LGrglvpdmSVAENLIlgryRRPPFSRGGFLDRKAIRAFAEELIeefDVRTPGPDTPAR----SL 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 496 SGGQRQRVAIARAILKDAPILILDEATSALDSESEVAVQKALKELMY-GKTVIAIAHRLSTLRDMS-RILVLEHGTI--- 570
Cdd:COG3845 404 SGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDaGAAVLLISEDLDEILALSdRIAVMYEGRIvge 483
|
250
....*....|.
gi 1083564009 571 --QEDGTHEEL 579
Cdd:COG3845 484 vpAAEATREEI 494
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
361-565 |
1.63e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 73.58 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 361 LDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQniaEVTQDSLRRAisVVPQE 440
Cdd:PRK11248 4 ISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK---PVEGPGAERG--VVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 441 PALFH-RSIRENIAYARPDA--TDEEVRDAAQKAhaLEFIDMlpEGmntlVGERGV-KLSGGQRQRVAIARAILKDAPIL 516
Cdd:PRK11248 79 EGLLPwRNVQDNVAFGLQLAgvEKMQRLEIAHQM--LKKVGL--EG----AEKRYIwQLSGGQRQRVGIARALAANPQLL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1083564009 517 ILDEATSALDSESEVAVQKALKELMY--GKTVIAIAHRLSTLRDMSRILVL 565
Cdd:PRK11248 151 LLDEPFGALDAFTREQMQTLLLKLWQetGKQVLLITHDIEEAVFMATELVL 201
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
352-551 |
2.50e-14 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 72.14 E-value: 2.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 352 LVAKKGEIVLDGISFAHEAvevfknfnltikdGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVtQDSLR 431
Cdd:cd03231 7 TCERDGRALFSGLSFTLAA-------------GEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQ-RDSIA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 432 RAISVVPQEPALFHR-SIRENIAYARPDATDEEVRDAAQKAHALEFIDmLPEGmntlvgergvKLSGGQRQRVAIARAIL 510
Cdd:cd03231 73 RGLLYLGHAPGIKTTlSVLENLRFWHADHSDEQVEEALARVGLNGFED-RPVA----------QLSAGQQRRVALARLLL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1083564009 511 KDAPILILDEATSALDSESEVAVQKALK-ELMYGKTVIAIAH 551
Cdd:cd03231 142 SGRPLWILDEPTTALDKAGVARFAEAMAgHCARGGMVVLTTH 183
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
376-573 |
2.59e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 75.60 E-value: 2.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 376 NFNLTIKDGERIGLVGKSGAGKSTLVSLL-----LREYDiagGAIKIDDQ-----NIAevtqDSLRRAISVVPQEPALF- 444
Cdd:NF040905 19 DVNLSVREGEIHALCGENGAGKSTLMKVLsgvypHGSYE---GEILFDGEvcrfkDIR----DSEALGIVIIHQELALIp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 445 HRSIRENIAYARPDATDEEVRDAAQKAHALEFIDM--LPEGMNTLVGERGVklsgGQRQRVAIARAILKDAPILILDEAT 522
Cdd:NF040905 92 YLSIAENIFLGNERAKRGVIDWNETNRRARELLAKvgLDESPDTLVTDIGV----GKQQLVEIAKALSKDVKLLILDEPT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1083564009 523 SAL-DSESEvavqkALKELM-----YGKTVIAIAHRL----------STLRDMSRI--LVLEHGTIQED 573
Cdd:NF040905 168 AALnEEDSA-----ALLDLLlelkaQGITSIIISHKLneirrvadsiTVLRDGRTIetLDCRADEVTED 231
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
54-325 |
4.71e-14 |
|
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: 72.97 E-value: 4.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 54 FLPYVYKIVVDGIQTQGtaevvsfiVFWSIVYVSAFLFFATIFR-LSSFLGVRGISRAVESTAYpALR----DYLQKHSH 128
Cdd:cd07346 17 ALPLLTKLLIDDVIPAG--------DLSLLLWIALLLLLLALLRaLLSYLRRYLAARLGQRVVF-DLRrdlfRHLQRLSL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 129 RFFSGNFAGGLNAKEIQVGGGMRNLLHEAIWTVTATAIGLLVTTGLMFSVDVRagVTFVTLIV--VIILCNLPLFKWQGG 206
Cdd:cd07346 88 SFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWK--LTLVALLLlpLYVLILRYFRRRIRK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 207 IARMHAKAIAKIRGVSIDALTNMRAVHSFAQGSQELSRLTETLEDARVIGVKKSDVAQYILIINTIIILLAVSGILALLI 286
Cdd:cd07346 166 ASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGG 245
|
250 260 270
....*....|....*....|....*....|....*....
gi 1083564009 287 ISFQQGTATSGDFVLVFALISSVWRELTRIGFMINNISQ 325
Cdd:cd07346 246 YLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQ 284
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
376-582 |
4.74e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 72.33 E-value: 4.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 376 NFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVT-QDSLRRAISVVPQEPALF---------- 444
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPgHQIARMGVVRTFQHVRLFremtvienll 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 445 ---HRSIRENI--------AYARPDatdeevRDAAQKA-HALEFIDMLPegmntLVGERGVKLSGGQRQRVAIARAILKD 512
Cdd:PRK11300 103 vaqHQQLKTGLfsgllktpAFRRAE------SEALDRAaTWLERVGLLE-----HANRQAGNLAYGQQRRLEIARCMVTQ 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1083564009 513 APILILDEATSALDSESEVAVQKALKELM--YGKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEELLKN 582
Cdd:PRK11300 172 PEILMLDEPAAGLNPKETKELDELIAELRneHNVTVLLIEHDMKLVMGISdRIYVVNQGTPLANGTPEEIRNN 244
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
348-581 |
5.25e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 72.55 E-value: 5.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 348 NAQDL-VAKKGEIVLDGISfaheavevfknfnLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAG--------GAIKID 418
Cdd:PRK13547 3 TADHLhVARRHRAILRDLS-------------LRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 419 DQNIAEVTQDSLRRAISVVPQ--EPAlFHRSIRENIAYA------RPDATDEEVRDAAQKAHALefidmlpEGMNTLVGE 490
Cdd:PRK13547 70 GEPLAAIDAPRLARLRAVLPQaaQPA-FAFSAREIVLLGrypharRAGALTHRDGEIAWQALAL-------AGATALVGR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 491 RGVKLSGGQRQRVAIARAILK---------DAPILILDEATSALDSESE----VAVQKALKELMYGktVIAIAHRLS-TL 556
Cdd:PRK13547 142 DVTTLSGGELARVQFARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQhrllDTVRRLARDWNLG--VLAIVHDPNlAA 219
|
250 260
....*....|....*....|....*
gi 1083564009 557 RDMSRILVLEHGTIQEDGTHEELLK 581
Cdd:PRK13547 220 RHADRIAMLADGAIVAHGAPADVLT 244
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
374-577 |
5.34e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.61 E-value: 5.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 374 FKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLrraISVVPQEPAL---FHRSIRE 450
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSEEVdwsFPVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 451 NIAYAR---------PDATDEEVRDAaqkahALEFIDMLpEGMNTLVGErgvkLSGGQRQRVAIARAILKDAPILILDEA 521
Cdd:PRK15056 100 VVMMGRyghmgwlrrAKKRDRQIVTA-----ALARVDMV-EFRHRQIGE----LSGGQKKRVFLARAIAQQGQVILLDEP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1083564009 522 TSALDSESEVAVQKALKELM-YGKTVIAIAHRLSTLRDMSRILVLEHGTIQEDGTHE 577
Cdd:PRK15056 170 FTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTE 226
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
369-580 |
9.16e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 72.19 E-value: 9.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 369 EAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQD--SLRRAISVVPQEP--ALF 444
Cdd:PRK13636 17 DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlmKLRESVGMVFQDPdnQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 445 HRSIRENIAYARPDAT--DEEVRDAAQKAhalefidMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDEAT 522
Cdd:PRK13636 97 SASVYQDVSFGAVNLKlpEDEVRKRVDNA-------LKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1083564009 523 SALDSESEVAVQKALKELM--YGKTVIAIAHRLSTLR-DMSRILVLEHGTIQEDGTHEELL 580
Cdd:PRK13636 170 AGLDPMGVSEIMKLLVEMQkeLGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
344-551 |
1.26e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 73.83 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 344 IDVENAqdlvAKKGEIV--LDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKID--- 418
Cdd:PRK11147 307 MQVEEA----SRSGKIVfeMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGtkl 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 419 -----DQNIAEVTQDslrraisvvpqepalfhRSIRENIAYARpdatdEEVRDAAQKAHALEFI-DML--PEGMNTLVGe 490
Cdd:PRK11147 383 evayfDQHRAELDPE-----------------KTVMDNLAEGK-----QEVMVNGRPRHVLGYLqDFLfhPKRAMTPVK- 439
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1083564009 491 rgvKLSGGQRQRVAIARAILKDAPILILDEATSALDSES-EVavqkaLKELM--YGKTVIAIAH 551
Cdd:PRK11147 440 ---ALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETlEL-----LEELLdsYQGTVLLVSH 495
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
372-568 |
1.70e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 69.90 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 372 EVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDS---LRRAISVVPQEPALF-HRS 447
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHLLmDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 448 IRENIAYAR--PDATDEEVRdaAQKAHALEFIDMLPEGMNTlvgerGVKLSGGQRQRVAIARAILKDAPILILDEATSAL 525
Cdd:PRK10908 96 VYDNVAIPLiiAGASGDDIR--RRVSAALDKVGLLDKAKNF-----PIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1083564009 526 DSESEVAVQKALKEL-MYGKTVIAIAHRLSTL-RDMSRILVLEHG 568
Cdd:PRK10908 169 DDALSEGILRLFEEFnRVGVTVLMATHDIGLIsRRSYRMLTLSDG 213
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
359-584 |
2.97e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 72.23 E-value: 2.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIK-IDDQNIAEVTQDSlrraISVV 437
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKwSENANIGYYAQDH----AYDF 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 438 PQEPALFhrsirENIAYARPDATDEE-VR----------DAAQKAhalefidmlpegmntlvgergVK-LSGGQRQRVAI 505
Cdd:PRK15064 396 ENDLTLF-----DWMSQWRQEGDDEQaVRgtlgrllfsqDDIKKS---------------------VKvLSGGEKGRMLF 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 506 ARAILKDAPILILDEATSALDSESEVAVQKALKelMYGKTVIAIAH-R--LSTLrdMSRIL-VLEHGTIQEDGTHEELLK 581
Cdd:PRK15064 450 GKLMMQKPNVLVMDEPTNHMDMESIESLNMALE--KYEGTLIFVSHdRefVSSL--ATRIIeITPDGVVDFSGTYEEYLR 525
|
...
gi 1083564009 582 NSG 584
Cdd:PRK15064 526 SQG 528
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
363-580 |
6.26e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 71.27 E-value: 6.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 363 GISFAHEAVE--VFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLR-------EYdiAGGAIKIDDQNIAEVTQDSLRRA 433
Cdd:PRK15134 12 SVAFRQQQTVrtVVNDVSLQIEAGETLALVGESGSGKSVTALSILRllpsppvVY--PSGDIRFHGESLLHASEQTLRGV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 434 ----ISVVPQEPAL-----------------FHRSIRENIAYARPDATDEEV--RDAAQKAHAlefidmLPEgmntlvge 490
Cdd:PRK15134 90 rgnkIAMIFQEPMVslnplhtlekqlyevlsLHRGMRREAARGEILNCLDRVgiRQAAKRLTD------YPH-------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 491 rgvKLSGGQRQRVAIARAILKDAPILILDEATSALDSESEVAVQKALKELM--YGKTVIAIAHRLSTLRDMS-RILVLEH 567
Cdd:PRK15134 156 ---QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQqeLNMGLLFITHNLSIVRKLAdRVAVMQN 232
|
250
....*....|...
gi 1083564009 568 GTIQEDGTHEELL 580
Cdd:PRK15134 233 GRCVEQNRAATLF 245
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
363-580 |
7.31e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 69.27 E-value: 7.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 363 GISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTL---VSLLLREYDIA----GGAIKIDDQNIAevtqdSLRRAIS 435
Cdd:PRK13638 6 DLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLfmnLSGLLRPQKGAvlwqGKPLDYSKRGLL-----ALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 436 VVPQEP--ALFHRSIRENIAYARPDATDEEVRDAAQKAHALefidmlpegmnTLVGERGVK------LSGGQRQRVAIAR 507
Cdd:PRK13638 81 TVFQDPeqQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEAL-----------TLVDAQHFRhqpiqcLSHGQKKRVAIAG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1083564009 508 AILKDAPILILDEATSALDSESEVAVQKALKELM-YGKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEELL 580
Cdd:PRK13638 150 ALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVaQGNHVIISSHDIDLIYEISdAVYVLRQGQILTHGAPGEVF 224
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
47-307 |
1.02e-12 |
|
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: 68.82 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 47 IGETVVSFLPYVYKIVVDGIQTQGTAEVVSfIVFWSIVYVSAFLFFATIFRLSSFLGVRGISRAVEstaypALRDYLQKH 126
Cdd:pfam00664 10 LSGAISPAFPLVLGRILDVLLPDGDPETQA-LNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSR-----RLRRKLFKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 127 SHR----FFSGNFAGGLNA---KEIQVgggMRNLLHEAIWTVTATAIGLLVTTGLMFSVDVRagVTFVTLIVV--IILCN 197
Cdd:pfam00664 84 ILRqpmsFFDTNSVGELLSrltNDTSK---IRDGLGEKLGLLFQSLATIVGGIIVMFYYGWK--LTLVLLAVLplYILVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 198 LPLFKWQGGIARMHAKAIAKIRGVSIDALTNMRAVHSFAQGSQELSRLTETLEDARVIGVKKSDVAQYILIINTIIILLA 277
Cdd:pfam00664 159 AVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLS 238
|
250 260 270
....*....|....*....|....*....|
gi 1083564009 278 VSGILALLIISFQQGTATSGDFVLVFALIS 307
Cdd:pfam00664 239 YALALWFGAYLVISGELSVGDLVAFLSLFA 268
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
363-572 |
1.04e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 68.64 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 363 GISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSL---RRAISVVPQ 439
Cdd:PRK11831 12 GVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSMLFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 440 EPALF-HRSIRENIAYArpdatdeeVRDAAQkahalefidmLPEG------MNTL--VGERGV------KLSGGQRQRVA 504
Cdd:PRK11831 92 SGALFtDMNVFDNVAYP--------LREHTQ----------LPAPllhstvMMKLeaVGLRGAaklmpsELSGGMARRAA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1083564009 505 IARAILKDAPILILDEATSALDSESEVAVQKALKELMY--GKTVIAIAHRLS---TLRDMSRIL----VLEHGTIQE 572
Cdd:PRK11831 154 LARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPevlSIADHAYIVadkkIVAHGSAQA 230
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
361-576 |
1.13e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 70.62 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 361 LDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAG--GAIKIDDQNI-AEVTQDSLRRAISVV 437
Cdd:TIGR02633 4 MKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLkASNIRDTERAGIVII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 438 PQEPALFHR-SIRENIAYARPDATDEEVRDAAQ---KAHALEFIDMLPEGMNTL-VGERGvklsGGQRQRVAIARAILKD 512
Cdd:TIGR02633 84 HQELTLVPElSVAENIFLGNEITLPGGRMAYNAmylRAKNLLRELQLDADNVTRpVGDYG----GGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1083564009 513 APILILDEATSAL-DSESEVAVQ--KALKElmYGKTVIAIAHRLSTLRDMSRILvlehgTIQEDGTH 576
Cdd:TIGR02633 160 ARLLILDEPSSSLtEKETEILLDiiRDLKA--HGVACVYISHKLNEVKAVCDTI-----CVIRDGQH 219
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
372-529 |
2.30e-12 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 66.23 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 372 EVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEvTQDSLRRAISVVPQEPALFHR-SIRE 450
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE-QRDEPHENILYLGHLPGLKPElSALE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 451 NIAYARPD--ATDEEVRDAAQKAHALEFIDmLPEGmntlvgergvKLSGGQRQRVAIARAILKDAPILILDEATSALDSE 528
Cdd:TIGR01189 93 NLHFWAAIhgGAQRTIEDALAAVGLTGFED-LPAA----------QLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
.
gi 1083564009 529 S 529
Cdd:TIGR01189 162 G 162
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
336-554 |
2.58e-12 |
|
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: 69.78 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 336 AISQAHEVIDVENAQDLVAKKGEIVLD--GISFAH------EAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLRE 407
Cdd:TIGR00954 422 RVEEIESGREGGRNSNLVPGRGIVEYQdnGIKFENiplvtpNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGEL 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 408 YDIAGGAIKIDDQNiaevtqdslrrAISVVPQEPALFHRSIRENIAYarPDATDEEVRDAAQKAhalEFIDMLPEGMNTL 487
Cdd:TIGR00954 502 WPVYGGRLTKPAKG-----------KLFYVPQRPYMTLGTLRDQIIY--PDSSEDMKRRGLSDK---DLEQILDNVQLTH 565
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1083564009 488 VGERGVK----------LSGGQRQRVAIARAILKDAPILILDEATSALDSESEVAVQKALKElmYGKTVIAIAHRLS 554
Cdd:TIGR00954 566 ILEREGGwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHRKS 640
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
361-553 |
3.04e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.26 E-value: 3.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 361 LDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQniaEVT----QDSLRRAISV 436
Cdd:PRK10762 7 LKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGK---EVTfngpKSSQEAGIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 437 VPQEPALF-HRSIRENIAYARpdatdEEV--------RDAAQKAHALEFIDMLPEGMNTLVGErgvkLSGGQRQRVAIAR 507
Cdd:PRK10762 84 IHQELNLIpQLTIAENIFLGR-----EFVnrfgridwKKMYAEADKLLARLNLRFSSDKLVGE----LSIGEQQMVEIAK 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1083564009 508 AILKDAPILILDEATSAL-DSESEvAVQKALKELM-YGKTVIAIAHRL 553
Cdd:PRK10762 155 VLSFESKVIIMDEPTDALtDTETE-SLFRVIRELKsQGRGIVYISHRL 201
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
367-582 |
3.38e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 68.01 E-value: 3.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 367 AHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLreydiagGAIK-----------IDDQNIAEVTQDSLR---- 431
Cdd:COG4170 16 PQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAIC-------GITKdnwhvtadrfrWNGIDLLKLSPRERRkiig 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 432 RAISVVPQEP-------ALFHRSIRENIayarPDATDEEV---RDAAQKAHALEF-----IDMLPEGMNTLVGErgvkLS 496
Cdd:COG4170 89 REIAMIFQEPsscldpsAKIGDQLIEAI----PSWTFKGKwwqRFKWRKKRAIELlhrvgIKDHKDIMNSYPHE----LT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 497 GGQRQRVAIARAILKDAPILILDEATSALDSESEVAVQKALKEL--MYGKTVIAIAHRLSTLRDMS-RILVLEHGTIQED 573
Cdd:COG4170 161 EGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLnqLQGTSILLISHDLESISQWAdTITVLYCGQTVES 240
|
....*....
gi 1083564009 574 GTHEELLKN 582
Cdd:COG4170 241 GPTEQILKS 249
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
372-577 |
3.56e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 66.63 E-value: 3.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 372 EVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLL--REYDIAGGAIKIDDQNIAEVTQDslRRA---ISVVPQEP----- 441
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghPKYEVTSGSILLDGEDILELSPD--ERAragIFLAFQYPveipg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 442 ---ALFHRSIRENIAYARPDATD--EEVRDAAQKahaLEF-IDMLpegmntlvgERGV--KLSGGQRQRVAIARAILKDA 513
Cdd:COG0396 92 vsvSNFLRTALNARRGEELSAREflKLLKEKMKE---LGLdEDFL---------DRYVneGFSGGEKKRNEILQMLLLEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1083564009 514 PILILDEATSALDSESEVAVQKALKELMY-GKTVIAIAH--RLSTLRDMSRILVLEHGTIQEDGTHE 577
Cdd:COG0396 160 KLAILDETDSGLDIDALRIVAEGVNKLRSpDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGKE 226
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
373-552 |
3.87e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.14 E-value: 3.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 373 VFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREY--DIAGGAIKIDDQNIaevtqdslrraisvvPQEpalfhRSIRE 450
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF---------------GRE-----ASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 451 NIaYARPDATDeevrdaaqkahALEFIDMLPEGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDEATSALDSES- 529
Cdd:COG2401 105 AI-GRKGDFKD-----------AVELLNAVGLSDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTa 172
|
170 180
....*....|....*....|....*.
gi 1083564009 530 -EVA--VQKALKELmyGKTVIAIAHR 552
Cdd:COG2401 173 kRVArnLQKLARRA--GITLVVATHH 196
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
370-594 |
4.24e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 66.65 E-value: 4.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 370 AVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLreyDIA-------GGAIKIDDQNIAEvtqDSLR-RAISVVPQEP 441
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAAL---GILpagvrqtAGRVLLDGKPVAP---CALRgRKIATIMQNP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 442 ALFHRSIRENIAYARPD-ATDEEVRDAAQKAHALEFIDMlpEGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDE 520
Cdd:PRK10418 89 RSAFNPLHTMHTHARETcLALGKPADDATLTAALEAVGL--ENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 521 ATSALDSESEVAVQKALKELM--YGKTVIAIAHRLSTL-RDMSRILVLEHGTIQEDGTHEELLKNSG---TYATLWNHQA 594
Cdd:PRK10418 167 PTTDLDVVAQARILDLLESIVqkRALGMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETLFNAPKhavTRSLVSAHLA 246
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
359-553 |
4.46e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 66.29 E-value: 4.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 359 IVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLreydiagGAIKIDDQNIAEvtQDSLRraISVVP 438
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVL-------GLVAPDEGVIKR--NGKLR--IGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 439 QE-------PALFHRSIReniayARPDATDEEVRDAAQKAHALEFIDMLPEgmntlvgergvKLSGGQRQRVAIARAILK 511
Cdd:PRK09544 74 QKlyldttlPLTVNRFLR-----LRPGTKKEDILPALKRVQAGHLIDAPMQ-----------KLSGGETQRVLLARALLN 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1083564009 512 DAPILILDEATSALDSESEVA----VQKALKELMYGktVIAIAHRL 553
Cdd:PRK09544 138 RPQLLVLDEPTQGVDVNGQVAlydlIDQLRRELDCA--VLMVSHDL 181
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
384-559 |
5.43e-12 |
|
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: 63.93 E-value: 5.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 384 GERIGLVGKSGAGKSTLVSLLLREYDIAGGAIK-IDDQNIAEVTQDSLRraisvvpqepalfhrsireniayarpdatde 462
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIyIDGEDILEEVLDQLL------------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 463 evrdaaqkahalefidmlpegmNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDEATSALDSESEVAVQKAL----- 537
Cdd:smart00382 51 ----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrll 108
|
170 180
....*....|....*....|....
gi 1083564009 538 --KELMYGKTVIAIAHRLSTLRDM 559
Cdd:smart00382 109 llLKSEKNLTVILTTNDEKDLGPA 132
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
357-582 |
5.56e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 66.66 E-value: 5.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 357 GEIVLDGISFAHEAVEVfknfnltikdgerIGLVGKSGAGKSTLVSLLLREYD-----------IAGGAIKIDDQNIAEv 425
Cdd:PRK14271 33 GKTVLDQVSMGFPARAV-------------TSLMGPTGSGKTTFLRTLNRMNDkvsgyrysgdvLLGGRSIFNYRDVLE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 426 tqdsLRRAISVVPQEPALFHRSIRENI---AYARPDATDEEVRDAAQkAHALEFidMLPEGMNTLVGERGVKLSGGQRQR 502
Cdd:PRK14271 99 ----FRRRVGMLFQRPNPFPMSIMDNVlagVRAHKLVPRKEFRGVAQ-ARLTEV--GLWDAVKDRLSDSPFRLSGGQQQL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 503 VAIARAILKDAPILILDEATSALDSESEVAVQKALKELMYGKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEELLK 581
Cdd:PRK14271 172 LCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISdRAALFFDGRLVEEGPTEQLFS 251
|
.
gi 1083564009 582 N 582
Cdd:PRK14271 252 S 252
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
356-580 |
6.34e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.11 E-value: 6.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 356 KGEIVLDGISFAHEAVEvfkNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVT-QDSLRRAI 434
Cdd:PRK10762 253 PGEVRLKVDNLSGPGVN---DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpQDGLANGI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 435 SVVPQEPA----LFHRSIRENIAYArpdATDEEVRDAAQKAHALE------FIDML----PeGMNTLVGErgvkLSGGQR 500
Cdd:PRK10762 330 VYISEDRKrdglVLGMSVKENMSLT---ALRYFSRAGGSLKHADEqqavsdFIRLFniktP-SMEQAIGL----LSGGNQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 501 QRVAIARAILKDAPILILDEATSALDseseVAVQKALKELMY-----GKTVIAIAHRLSTLRDMS-RILVLEHGTIQ--- 571
Cdd:PRK10762 402 QKVAIARGLMTRPKVLILDEPTRGVD----VGAKKEIYQLINqfkaeGLSIILVSSEMPEVLGMSdRILVMHEGRISgef 477
|
250
....*....|.
gi 1083564009 572 --EDGTHEELL 580
Cdd:PRK10762 478 trEQATQEKLM 488
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
384-568 |
7.52e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 68.37 E-value: 7.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 384 GERIGLVGKSGAGKSTLVSLLLREYDIAG--GAIKIDDQNIaevTQDSLRRaISVVPQEPALF-HRSIRENIAYAR---- 456
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKP---TKQILKR-TGFVTQDDILYpHLTVRETLVFCSllrl 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 457 PDATDEEVRDAAQKAHALEFidMLPEGMNTLVGE---RGVklSGGQRQRVAIARAILKDAPILILDEATSALDSESEVAV 533
Cdd:PLN03211 170 PKSLTKQEKILVAESVISEL--GLTKCENTIIGNsfiRGI--SGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRL 245
|
170 180 190
....*....|....*....|....*....|....*...
gi 1083564009 534 QKALKELMY-GKTVIAIAHRLST--LRDMSRILVLEHG 568
Cdd:PLN03211 246 VLTLGSLAQkGKTIVTSMHQPSSrvYQMFDSVLVLSEG 283
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
374-569 |
7.86e-12 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 65.85 E-value: 7.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 374 FKNFNLTI-KDGERIGLVGKSGAGKSTLVSLL--------------------LREYdiAGGAIkiddQN-IAEVTQDSLR 431
Cdd:cd03236 15 FKLHRLPVpREGQVLGLVGPNGIGKSTALKILagklkpnlgkfddppdwdeiLDEF--RGSEL----QNyFTKLLEGDVK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 432 RAISvvPQEPALFhrsireniayarPDATDEEVRDAAQKAHALEFIDMLPEGMN-TLVGERGV-KLSGGQRQRVAIARAI 509
Cdd:cd03236 89 VIVK--PQYVDLI------------PKAVKGKVGELLKKKDERGKLDELVDQLElRHVLDRNIdQLSGGELQRVAIAAAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1083564009 510 LKDAPILILDEATSALDSESEVAVQKALKELM-YGKTVIAIAHRLSTLRDMSRILVLEHGT 569
Cdd:cd03236 155 ARDADFYFFDEPSSYLDIKQRLNAARLIRELAeDDNYVLVVEHDLAVLDYLSDYIHCLYGE 215
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
366-580 |
1.09e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 65.58 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 366 FAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDD------------QNIAEVTQD---SL 430
Cdd:PRK15112 21 FRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfgdysyrsQRIRMIFQDpstSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 431 --RRAISVVPQEPalfhrsIRENIAYarpDATDEEVRDAAqkahALEFIDMLPEGMNTLVGergvKLSGGQRQRVAIARA 508
Cdd:PRK15112 101 npRQRISQILDFP------LRLNTDL---EPEQREKQIIE----TLRQVGLLPDHASYYPH----MLAPGQKQRLGLARA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1083564009 509 ILKDAPILILDEATSALDSESEVAVQKALKELM--YGKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEELL 580
Cdd:PRK15112 164 LILRPKVIIADEALASLDMSMRSQLINLMLELQekQGISYIYVTQHLGMMKHISdQVLVMHQGEVVERGSTADVL 238
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
381-568 |
1.20e-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: 63.80 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 381 IKDGERIGLVGKSGAGKSTLVSLLL--REYDIAGGAIKIDDQNIAEvtqdSLRRAISVVPQEPALFhrsireniayarPD 458
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLAgrKTAGVITGEILINGRPLDK----NFQRSTGYVEQQDVHS------------PN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 459 ATdeeVRDAaqkahaLEFIDMLpegmntlvgeRGvkLSGGQRQRVAIARAILKDAPILILDEATSALDSESEVAVQKALK 538
Cdd:cd03232 94 LT---VREA------LRFSALL----------RG--LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLK 152
|
170 180 190
....*....|....*....|....*....|...
gi 1083564009 539 EL-MYGKTVIAIAHRLS--TLRDMSRILVLEHG 568
Cdd:cd03232 153 KLaDSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
379-573 |
1.66e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 64.42 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 379 LTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQD---SLR-RAISVVPQE----PALfhrSIRE 450
Cdd:PRK10584 31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRaKHVGFVFQSfmliPTL---NALE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 451 NI---AYARPDatdeevRDAAQKAHALEFIDMLpeGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDEATSALDS 527
Cdd:PRK10584 108 NVelpALLRGE------SSRQSRNGAKALLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1083564009 528 ESEVAVQKALKELM--YGKTVIAIAHRLSTLRDMSRILVLEHGTIQED 573
Cdd:PRK10584 180 QTGDKIADLLFSLNreHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
376-572 |
2.09e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 66.73 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 376 NFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKI-DDQNIAEVTQDSlrRAISVvpqePALFH-----RSIR 449
Cdd:PRK10636 19 NATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFpGNWQLAWVNQET--PALPQ----PALEYvidgdREYR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 450 E-----NIAYARPD----ATDEEVRDAAQ----KAHALEFIDMLpeGMNTLVGERGVK-LSGGQRQRVAIARAILKDAPI 515
Cdd:PRK10636 93 QleaqlHDANERNDghaiATIHGKLDAIDawtiRSRAASLLHGL--GFSNEQLERPVSdFSGGWRMRLNLAQALICRSDL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1083564009 516 LILDEATSALDSESEVAVQKALKElmYGKTVIAIAHRlstlRD-----MSRILVLEHGTIQE 572
Cdd:PRK10636 171 LLLDEPTNHLDLDAVIWLEKWLKS--YQGTLILISHD----RDfldpiVDKIIHIEQQSLFE 226
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
376-568 |
2.09e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.90 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 376 NFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKID-DQNIAEVTQDSLRRA-------ISVVPQEPAlfhRS 447
Cdd:PRK11147 21 NAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEqDLIVARLQQDPPRNVegtvydfVAEGIEEQA---EY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 448 IRENIAYARPDATDEEVRDAAQKAHALEFID-----MLPEGMNTLVGERGV-------KLSGGQRQRVAIARAILKDAPI 515
Cdd:PRK11147 98 LKRYHDISHLVETDPSEKNLNELAKLQEQLDhhnlwQLENRINEVLAQLGLdpdaalsSLSGGWLRKAALGRALVSNPDV 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1083564009 516 LILDEATSALDSESEVAVQKALKElmYGKTVIAIAHRLSTLRDM-SRILVLEHG 568
Cdd:PRK11147 178 LLLDEPTNHLDIETIEWLEGFLKT--FQGSIIFISHDRSFIRNMaTRIVDLDRG 229
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
363-574 |
2.31e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 66.29 E-value: 2.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 363 GISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIA-EVTQDSLRRAISVVPQEP 441
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 442 ALF-HRSIRENIAYARPDAT------DEEVRDAAQKAHALEfIDMLPEgmntlvgERGVKLSGGQRQRVAIARAILKDAP 514
Cdd:PRK10982 83 NLVlQRSVMDNMWLGRYPTKgmfvdqDKMYRDTKAIFDELD-IDIDPR-------AKVATLSVSQMQMIEIAKAFSYNAK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1083564009 515 ILILDEATSALdSESEV----AVQKALKElmYGKTVIAIAHRlstlrdMSRILVL-EHGTIQEDG 574
Cdd:PRK10982 155 IVIMDEPTSSL-TEKEVnhlfTIIRKLKE--RGCGIVYISHK------MEEIFQLcDEITILRDG 210
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
372-577 |
3.56e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 63.89 E-value: 3.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 372 EVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLRE--YDIAGGAIKIDDQNIAEVTQDSL-RRAISVVPQEP------- 441
Cdd:CHL00131 21 EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPEERaHLGIFLAFQYPieipgvs 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 442 -ALFHRsirenIAYarpdatdeevrDAAQKAH------ALEFIDMLPE-----GMNTLVGERGVK--LSGGQRQRVAIAR 507
Cdd:CHL00131 101 nADFLR-----LAY-----------NSKRKFQglpeldPLEFLEIINEklklvGMDPSFLSRNVNegFSGGEKKRNEILQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1083564009 508 AILKDAPILILDEATSALDSESEVAVQKALKELM-YGKTVIAIAH--RLSTLRDMSRILVLEHGTIQEDGTHE 577
Cdd:CHL00131 165 MALLDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGDAE 237
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
381-568 |
3.69e-11 |
|
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: 62.20 E-value: 3.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 381 IKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDdqniaevtqdslRRAISVVPQEpalfhrsireniayarpdat 460
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWD------------GITPVYKPQY-------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 461 deevrdaaqkahalefidmlpegmntlvgergVKLSGGQRQRVAIARAILKDAPILILDEATSALDSESEVAVQKALKEL 540
Cdd:cd03222 70 --------------------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170 180 190
....*....|....*....|....*....|
gi 1083564009 541 -MYG-KTVIAIAHRLSTLRDMSRILVLEHG 568
Cdd:cd03222 118 sEEGkKTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
391-526 |
8.86e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 63.74 E-value: 8.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 391 GKSGAGKSTLVSLllreydIAG------GAIKIDDQNIAEVTQD-SL---RRAISVVPQEPALF-HRSIRENIAY--ARP 457
Cdd:PRK11144 31 GRSGAGKTSLINA------ISGltrpqkGRIVLNGRVLFDAEKGiCLppeKRRIGYVFQDARLFpHYKVRGNLRYgmAKS 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1083564009 458 DatdeevrdaaqKAHALEFIDMLpeGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDEATSALD 526
Cdd:PRK11144 105 M-----------VAQFDKIVALL--GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
376-579 |
4.22e-10 |
|
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: 62.15 E-value: 4.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 376 NFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIA-GGAIKIDDQNIAEVT-QDSLRRAISVVPQE-------PALfhr 446
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNpAQAIRAGIAMVPEDrkrhgivPIL--- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 447 SIRENIAYA---------RPDATDEE--VRDAAQKAHALEFIDMLPEGmntlvgergvKLSGGQRQRVAIARAILKDAPI 515
Cdd:TIGR02633 355 GVGKNITLSvlksfcfkmRIDAAAELqiIGSAIQRLKVKTASPFLPIG----------RLSGGNQQKAVLAKMLLTNPRV 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1083564009 516 LILDEATSALDSESEVAVQKALKELMY-GKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEEL 579
Cdd:TIGR02633 425 LILDEPTRGVDVGAKYEIYKLINQLAQeGVAIIVVSSELAEVLGLSdRVLVIGEGKLKGDFVNHAL 490
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
371-539 |
1.06e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 61.66 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 371 VEVFKNFNLTIKDGERIGLVGKSGAGKSTLvsLLLREYDIAGGAIKIDdqniAEVTQDSLRRAiSVVPQEPA-------- 442
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTL--LKTIASNTDGFHIGVE----GVITYDGITPE-EIKKHYRGdvvynaet 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 443 ---LFHRSIRENIAYA--------RPDATDEEVRdAAQKAHALEFIDMLPEGMNTLVGE---RGVklSGGQRQRVAIARA 508
Cdd:TIGR00956 147 dvhFPHLTVGETLDFAarcktpqnRPDGVSREEY-AKHIADVYMATYGLSHTRNTKVGNdfvRGV--SGGERKRVSIAEA 223
|
170 180 190
....*....|....*....|....*....|.
gi 1083564009 509 ILKDAPILILDEATSALDSESEVAVQKALKE 539
Cdd:TIGR00956 224 SLGGAKIQCWDNATRGLDSATALEFIRALKT 254
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
381-568 |
1.66e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.89 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 381 IKDGERIGLVGKSGAGKSTLVSLLLREYDiaGGAIKIDDQNIAEVTQD-SLRRAISVVPQEPA-LFHRSIRENI---AYA 455
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLAERVT--TGVITGGDRLVNGRPLDsSFQRSIGYVQQQDLhLPTSTVRESLrfsAYL 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 456 RPDAtdeEVRDAAQKAHALEFIDMLpeGMNT----LVGERGVKLSGGQRQRVAIA-RAILKDAPILILDEATSALDSESE 530
Cdd:TIGR00956 864 RQPK---SVSKSEKMEYVEEVIKLL--EMESyadaVVGVPGEGLNVEQRKRLTIGvELVAKPKLLLFLDEPTSGLDSQTA 938
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1083564009 531 VAVQKALKELM-YGKTVIAIAHRLST--LRDMSRILVLEHG 568
Cdd:TIGR00956 939 WSICKLMRKLAdHGQAILCTIHQPSAilFEEFDRLLLLQKG 979
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
374-574 |
2.33e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 58.40 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 374 FKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQ-----NIAEVTQDSLRRAI----SVVPQEPALF 444
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAERRRLLrtewGFVHQHPRDG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 445 HR---SIRENIAyARPDATDE----EVRDAAqkAHALEFIDMLPEGMNTLVGergvKLSGGQRQRVAIARAiLKDAPILI 517
Cdd:PRK11701 102 LRmqvSAGGNIG-ERLMAVGArhygDIRATA--GDWLERVEIDAARIDDLPT----TFSGGMQQRLQIARN-LVTHPRLV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1083564009 518 L-DEATSALDseseVAVQKALKELMYGKT------VIAIAHRLSTLRDMS-RILVLEHGTIQEDG 574
Cdd:PRK11701 174 FmDEPTGGLD----VSVQARLLDLLRGLVrelglaVVIVTHDLAVARLLAhRLLVMKQGRVVESG 234
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
376-579 |
2.49e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.94 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 376 NFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIA-GGAIKIDDQNIA-EVTQDSLRRAISVVPQE-------PALfhr 446
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGKPVKiRNPQQAIAQGIAMVPEDrkrdgivPVM--- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 447 SIRENIAYARPD--ATDEEVRDAAQKAHALEFID---------MLPEGmntlvgergvKLSGGQRQRVAIARAILKDAPI 515
Cdd:PRK13549 357 GVGKNITLAALDrfTGGSRIDDAAELKTILESIQrlkvktaspELAIA----------RLSGGNQQKAVLAKCLLLNPKI 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1083564009 516 LILDEATSALDSESEVAVQKALKELM-YGKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEEL 579
Cdd:PRK13549 427 LILDEPTRGIDVGAKYEIYKLINQLVqQGVAIIVISSELPEVLGLSdRVLVMHEGKLKGDLINHNL 492
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
375-581 |
3.61e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.41 E-value: 3.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 375 KNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQ-DSLRRAISVVPQ---EPALFHR-SIR 449
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAVKKGMAYITEsrrDNGFFPNfSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 450 ENIAYARP--------------DATDEEVRDAAQKAHALEFidmlpEGMNTLVGErgvkLSGGQRQRVAIARAILKDAPI 515
Cdd:PRK09700 360 QNMAISRSlkdggykgamglfhEVDEQRTAENQRELLALKC-----HSVNQNITE----LSGGNQQKVLISKWLCCCPEV 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1083564009 516 LILDEATSALDSESEVAVQKALKELM-YGKTVIAIAHRLSTLRDM-SRILVLEHGTI------QEDGTHEELLK 581
Cdd:PRK09700 431 IIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELPEIITVcDRIAVFCEGRLtqiltnRDDMSEEEIMA 504
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
375-568 |
7.83e-09 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 55.73 E-value: 7.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 375 KNFNLTIKDGERIGLVGKSGAGKSTLVSLL---LREYDIAGGAIKIDDQNIAEVTQdSLRRAISVVPQEPALFhrsiren 451
Cdd:cd03233 24 KDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYKEFAE-KYPGEIIYVSEEDVHF------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 452 iayarPDATDEEVRDAAQKAHALEFIdmlpegmntlvgeRGVklSGGQRQRVAIARAILKDAPILILDEATSALDSESEV 531
Cdd:cd03233 96 -----PTLTVRETLDFALRCKGNEFV-------------RGI--SGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1083564009 532 AVQKALKEL--MYGKTVIAIAHRLS-TLRDM-SRILVLEHG 568
Cdd:cd03233 156 EILKCIRTMadVLKTTTFVSLYQASdEIYDLfDKVLVLYEG 196
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
373-537 |
1.04e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.58 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 373 VFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLlreydiAG------GAIKIDDQNIAEVtQDSLRRAIsvvpqepaLF-- 444
Cdd:PRK13538 16 LFSGLSFTLNAGELVQIEGPNGAGKTSLLRIL------AGlarpdaGEVLWQGEPIRRQ-RDEYHQDL--------LYlg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 445 HR-------SIRENIAYARP---DATDEEVRDAAQKAHALEFIDmLPEGmntlvgergvKLSGGQRQRVAIARAILKDAP 514
Cdd:PRK13538 81 HQpgiktelTALENLRFYQRlhgPGDDEALWEALAQVGLAGFED-VPVR----------QLSAGQQRRVALARLWLTRAP 149
|
170 180
....*....|....*....|...
gi 1083564009 515 ILILDEATSALDSESeVAVQKAL 537
Cdd:PRK13538 150 LWILDEPFTAIDKQG-VARLEAL 171
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
372-570 |
1.47e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.37 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 372 EVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLL--LREydIAGGAIKIDDQNI-AEVTQDSLRRAISVVP---QEPALF- 444
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLygLRP--ARGGRIMLNGKEInALSTAQRLARGLVYLPedrQSSGLYl 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 445 HRSIRENI---AYARPDATDEEVRDAA---QKAHALefidmlpeGMNTLVGERGVK-LSGGQRQRVAIARAILKDAPILI 517
Cdd:PRK15439 355 DAPLAWNVcalTHNRRGFWIKPARENAvleRYRRAL--------NIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQLLI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1083564009 518 LDEATSALDSESEVAVQKALKELM-YGKTVIAIAHRLSTLRDMS-RILVLEHGTI 570
Cdd:PRK15439 427 VDEPTRGVDVSARNDIYQLIRSIAaQNVAVLFISSDLEEIEQMAdRVLVMHQGEI 481
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
363-528 |
2.83e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.47 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 363 GISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNiaeVTQDSLRRAISVVPQEPA 442
Cdd:PRK13543 16 ALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT---ATRGDRSRFMAYLGHLPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 443 LFHR-SIRENIAYArpdatdeevrDAAQKAHALEfidmLPEGMNTLVGERGV------KLSGGQRQRVAIARAILKDAPI 515
Cdd:PRK13543 93 LKADlSTLENLHFL----------CGLHGRRAKQ----MPGSALAIVGLAGYedtlvrQLSAGQKKRLALARLWLSPAPL 158
|
170
....*....|...
gi 1083564009 516 LILDEATSALDSE 528
Cdd:PRK13543 159 WLLDEPYANLDLE 171
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
56-325 |
2.97e-08 |
|
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: 55.58 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 56 PYVYKIVVDGIQTQGTAEVVSFIVFWsIVYVsAFLFFATIF-RLSSFLGVRGISRAVESTAYPALRdYLQKHSHRFFSGN 134
Cdd:cd18582 16 PFLLKYAVDALSAPASALLAVPLLLL-LAYG-LARILSSLFnELRDALFARVSQRAVRRLALRVFR-HLHSLSLRFHLSR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 135 FAGGLNaKEIQVGG-GMRNLLHEAIWTVTATAIGLLVTTGLMFSV--DVRAGVTFVTLIVVIILcNLPLFKWQGGIARMH 211
Cdd:cd18582 93 KTGALS-RAIERGTrGIEFLLRFLLFNILPTILELLLVCGILWYLygWSYALITLVTVALYVAF-TIKVTEWRTKFRREM 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 212 AKAIAKIRGVSIDALTNMRAVHSFAQGSQELSRLTETLEDARVIGVKKSDVAQYILIINTIIILLAVSGILALLIISFQQ 291
Cdd:cd18582 171 NEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIGQALIISLGLTAIMLLAAQGVVA 250
|
250 260 270
....*....|....*....|....*....|....
gi 1083564009 292 GTATSGDFVLVFALISSVWRELTRIGFMINNISQ 325
Cdd:cd18582 251 GTLTVGDFVLVNTYLLQLYQPLNFLGFVYREIRQ 284
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
377-578 |
1.37e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.15 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 377 FNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIA-EVTQDSLRRAISVVP----QEPALFHRSIREN 451
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRDAIRAGIMLCPedrkAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 452 IAY-ARPDATDEE--VRDAAQKAHALEFIDML----PEGmNTLVGergvKLSGGQRQRVAIARAILKDAPILILDEATSA 524
Cdd:PRK11288 352 INIsARRHHLRAGclINNRWEAENADRFIRSLniktPSR-EQLIM----NLSGGNQQKAILGRWLSEDMKVILLDEPTRG 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 525 LDseseVAVQKALKELMY-----GKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEE 578
Cdd:PRK11288 427 ID----VGAKHEIYNVIYelaaqGVAVLFVSSDLPEVLGVAdRIVVMREGRIAGELAREQ 482
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
380-581 |
4.29e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 52.05 E-value: 4.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 380 TIKDGERIGLVGKSGAGKS--TLVSLLLREY--DIAGGAIKIDDQNIAEVTQDSLRR----AISVVPQEPAlfhRSIreN 451
Cdd:PRK11022 29 SVKQGEVVGIVGESGSGKSvsSLAIMGLIDYpgRVMAEKLEFNGQDLQRISEKERRNlvgaEVAMIFQDPM---TSL--N 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 452 IAYARPDATDEEVR---DAAQKAHALEFIDMLpegmnTLVG------ERGV---KLSGGQRQRVAIARAILKDAPILILD 519
Cdd:PRK11022 104 PCYTVGFQIMEAIKvhqGGNKKTRRQRAIDLL-----NQVGipdpasRLDVyphQLSGGMSQRVMIAMAIACRPKLLIAD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1083564009 520 EATSALDseseVAVQKALKELMY------GKTVIAIAHRLSTLRDMS-RILVLEHGTIQEDGTHEELLK 581
Cdd:PRK11022 179 EPTTALD----VTIQAQIIELLLelqqkeNMALVLITHDLALVAEAAhKIIVMYAGQVVETGKAHDIFR 243
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
371-580 |
7.46e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 51.34 E-value: 7.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 371 VEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLL----REYDIAGGAIKIDDQNIAEVTQDSLRRAI----SVVPQEPA 442
Cdd:PRK15093 20 VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICgvtkDNWRVTADRMRFDDIDLLRLSPRERRKLVghnvSMIFQEPQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 443 LF---HRSIRENIAYARPDATDEE---VRDAAQKAHALEFIDMLP-EGMNTLVGERGVKLSGGQRQRVAIARAILKDAPI 515
Cdd:PRK15093 100 SCldpSERVGRQLMQNIPGWTYKGrwwQRFGWRKRRAIELLHRVGiKDHKDAMRSFPYELTEGECQKVMIAIALANQPRL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083564009 516 LILDEATSALDSESEVAVQKALKELMY--GKTVIAIAHRLSTLRDM-SRILVLEHGTIQEDGTHEELL 580
Cdd:PRK15093 180 LIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLSQWaDKINVLYCGQTVETAPSKELV 247
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
168-260 |
8.11e-07 |
|
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: 51.00 E-value: 8.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 168 LLVTTGLMFSVDVR-AGVTFVTLIVVIILcnlplFKWQGGIARMHAK----AIAKIRGVSIDALTNMRAVHSFAQGSQEL 242
Cdd:cd18572 124 LVGGLAFMFSLSWRlTLLAFITVPVIALI-----TKVYGRYYRKLSKeiqdALAEANQVAEEALSNIRTVRSFATEEREA 198
|
90
....*....|....*...
gi 1083564009 243 SRLTETLEDARVIGVKKS 260
Cdd:cd18572 199 RRYERALDKALKLSVRQA 216
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
369-565 |
2.26e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.40 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 369 EAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLL--REYDIAGGAIKIDDQNIAEVT-QDSLRRAISVVPQEPA--- 442
Cdd:PRK09580 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSpEDRAGEGIFMAFQYPVeip 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 443 -----LFH-------RSIRENIAYARPDATD--EEvrdaaqKAHALEF-IDMLPEGMNtlvgergVKLSGGQRQRVAIAR 507
Cdd:PRK09580 92 gvsnqFFLqtalnavRSYRGQEPLDRFDFQDlmEE------KIALLKMpEDLLTRSVN-------VGFSGGEKKRNDILQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1083564009 508 AILKDAPILILDEATSALDSEsevavqkALKelmygktviAIAHRLSTLRDMSRILVL 565
Cdd:PRK09580 159 MAVLEPELCILDESDSGLDID-------ALK---------IVADGVNSLRDGKRSFII 200
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
343-555 |
2.69e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 50.32 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 343 VIDVENaqdlVAKK-GEIVLdgisfaheavevFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQ- 420
Cdd:TIGR03719 322 VIEAEN----LTKAfGDKLL------------IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETv 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 421 NIAEVTQdslrraisvvpqepalfhrsIRENIAyarPDATD-EEVRDAaqkahaLEFIDMLPEGMNT------------- 486
Cdd:TIGR03719 386 KLAYVDQ--------------------SRDALD---PNKTVwEEISGG------LDIIKLGKREIPSrayvgrfnfkgsd 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083564009 487 ---LVGErgvkLSGGQRQRVAIARAILKDAPILILDEATSALDSESEVAVQKALKElmYGKTVIAIAH------RLST 555
Cdd:TIGR03719 437 qqkKVGQ----LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLN--FAGCAVVISHdrwfldRIAT 508
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
381-579 |
3.12e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 50.40 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 381 IKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQ----NIAEVTQDslrraISVVPQEPALFHR-SIRENI-AY 454
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsiltNISDVHQN-----MGYCPQFDAIDDLlTGREHLyLY 2036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 455 AR----PDATDEEVRDAAQKAHALEFIdmlpegMNTLVGergvKLSGGQRQRVAIARAILKDAPILILDEATSALDSESE 530
Cdd:TIGR01257 2037 ARlrgvPAEEIEKVANWSIQSLGLSLY------ADRLAG----TYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQAR 2106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1083564009 531 VAVQKALKELMY-GKTVIAIAHRLSTLRDM-SRILVLEHGTIQEDGTHEEL 579
Cdd:TIGR01257 2107 RMLWNTIVSIIReGRAVVLTSHSMEECEALcTRLAIMVKGAFQCLGTIQHL 2157
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
54-316 |
3.35e-06 |
|
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: 49.10 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 54 FLPYVYKIVVDGIQTQGTAEVVSFIVFWsIVYVSAFLFFATIFRLSSF--LGVRGISRavestaypaLRDYLQKHSHR-- 129
Cdd:cd18557 14 LLPYLIGRLIDTIIKGGDLDVLNELALI-LLAIYLLQSVFTFVRYYLFniAGERIVAR---------LRRDLFSSLLRqe 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 130 --FFSGNFAGGLNAK---EIQVgggmrnlLHEAIWTVTATAIG----LLVTTGLMFSVDVRagVTFVTLIVVIILcnLPL 200
Cdd:cd18557 84 iaFFDKHKTGELTSRlssDTSV-------LQSAVTDNLSQLLRnilqVIGGLIILFILSWK--LTLVLLLVIPLL--LIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 201 FKWQGGIARMHAKAI----AKIRGVSIDALTNMRAVHSFAQGSQELSRLTETLEDARVIGVKKSdvaqyILIINTIIILL 276
Cdd:cd18557 153 SKIYGRYIRKLSKEVqdalAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKA-----LANALFQGITS 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1083564009 277 AVSGILALLIISF-----QQGTATSGD--------FVLVFAL--ISSVWRELTRI 316
Cdd:cd18557 228 LLIYLSLLLVLWYggylvLSGQLTVGEltsfilytIMVASSVggLSSLLADIMKA 282
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
313-560 |
7.17e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.13 E-value: 7.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 313 LTRIGFMINNISQIYSEAEEGLVAISQAHEVIDveNAQDLVAKKGEIVLDGISFAHEAVEVFKNFNltiKDGERIGLVGK 392
Cdd:PRK01156 621 IREIENEANNLNNKYNEIQENKILIEKLRGKID--NYKKQIAEIDSIIPDLKEITSRINDIEDNLK---KSRKALDDAKA 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 393 SGAGKSTLVSLLLReyDIAGGAIKIDDQNIAEVTQDSLRRAISVVPQEPALFHRS-IRENIAYARPDATDEEVRDAAQKA 471
Cdd:PRK01156 696 NRARLESTIEILRT--RINELSDRINDINETLESMKKIKKAIGDLKRLREAFDKSgVPAMIRKSASQAMTSLTRKYLFEF 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 472 HaLEFIDM-LPEGMNTLVGERGV-----KLSGGQRQ------RVAIARAILKDAPILILDEATSALDSESEVA----VQK 535
Cdd:PRK01156 774 N-LDFDDIdVDQDFNITVSRGGMvegidSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNlkdiIEY 852
|
250 260
....*....|....*....|....*
gi 1083564009 536 ALKELMYGKTVIAIAHRlstlRDMS 560
Cdd:PRK01156 853 SLKDSSDIPQVIMISHH----RELL 873
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
373-581 |
7.69e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.63 E-value: 7.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 373 VFKNFNLTIKDGERIGLVGKSGAGKSTL-VSLLLREY--DIAGGAIK----ID--------DQNIAEVTQDslRRAISVV 437
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYgrNISGTVFKdgkeVDvstvsdaiDAGLAYVTED--RKGYGLN 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 438 PQEpalfhrSIRENIAYARPDA--------TDEEVRDAAQKAHAlefidmlpegMNTL---VGERGVKLSGGQRQRVAIA 506
Cdd:NF040905 353 LID------DIKRNITLANLGKvsrrgvidENEEIKVAEEYRKK----------MNIKtpsVFQKVGNLSGGNQQKVVLS 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 507 RAILKDAPILILDEATSALDSESEVAVQKALKELM-YGKTVIAIAHRLSTLRDMS-RILVLEHGTI-----QEDGTHEEL 579
Cdd:NF040905 417 KWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAaEGKGVIVISSELPELLGMCdRIYVMNEGRItgelpREEASQERI 496
|
..
gi 1083564009 580 LK 581
Cdd:NF040905 497 MR 498
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
373-551 |
9.17e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.70 E-value: 9.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 373 VFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYD-IAGGAIKIDDQNIAEVTQ---DSLRraisvVPQEPALFhrsi 448
Cdd:PLN03073 524 LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQpSSGTVFRSAKVRMAVFSQhhvDGLD-----LSSNPLLY---- 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 449 renIAYARPDATDEEVRdaaqkAHALEFidmlpeGMN-TLVGERGVKLSGGQRQRVAIARAILKDAPILILDEATSALDS 527
Cdd:PLN03073 595 ---MMRCFPGVPEQKLR-----AHLGSF------GVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDL 660
|
170 180
....*....|....*....|....
gi 1083564009 528 ESEVAVQKALkeLMYGKTVIAIAH 551
Cdd:PLN03073 661 DAVEALIQGL--VLFQGGVLMVSH 682
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
358-551 |
9.65e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.70 E-value: 9.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 358 EIVLDGISFAHEAVEVFKNFNLTIKDGERIGLVGKSGAGKSTLV---------------SLLLREYDIAGgaikiDDQNI 422
Cdd:PLN03073 177 DIHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLrymamhaidgipkncQILHVEQEVVG-----DDTTA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 423 AEVTQDS-------LRRAISVVPQEPALFHRSIRENIAYARPDATDEEVRDA--AQKAHALEFIDML---PEGMNTLVG- 489
Cdd:PLN03073 252 LQCVLNTdiertqlLEEEAQLVAQQRELEFETETGKGKGANKDGVDKDAVSQrlEEIYKRLELIDAYtaeARAASILAGl 331
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 490 --------ERGVKLSGGQRQRVAIARAILKDAPILILDEATSALDSESEVAVQKALkeLMYGKTVIAIAH 551
Cdd:PLN03073 332 sftpemqvKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSH 399
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
389-554 |
1.03e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 48.69 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 389 LVGKSGAGKSTLVSLLL-REydiAGGAIKIDDQniaevtqdslrraISVVPQEPALFHR---------------SIRENI 452
Cdd:PLN03140 911 LMGVSGAGKTTLMDVLAgRK---TGGYIEGDIR-------------ISGFPKKQETFARisgyceqndihspqvTVRESL 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 453 AYARPDATDEEVrdaaQKAHALEFIDMLPEGM------NTLVGERGVK-LSGGQRQRVAIARAILKDAPILILDEATSAL 525
Cdd:PLN03140 975 IYSAFLRLPKEV----SKEEKMMFVDEVMELVeldnlkDAIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1050
|
170 180 190
....*....|....*....|....*....|
gi 1083564009 526 DSESEVAVQKALKELM-YGKTVIAIAHRLS 554
Cdd:PLN03140 1051 DARAAAIVMRTVRNTVdTGRTVVCTIHQPS 1080
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
373-567 |
1.45e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.86 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 373 VFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIK----IDDQNIAEVTQDSLRraisvvPQEPALFHrsi 448
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGlakgIKLGYFAQHQLEFLR------ADESPLQH--- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 449 renIAYARPDATDEEVRDAAQkahALEFidmlpegMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDEATSALDSE 528
Cdd:PRK10636 398 ---LARLAPQELEQKLRDYLG---GFGF-------QGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLD 464
|
170 180 190
....*....|....*....|....*....|....*....
gi 1083564009 529 SEVAVQKALKElmYGKTVIAIAHRLSTLRDMSRILVLEH 567
Cdd:PRK10636 465 MRQALTEALID--FEGALVVVSHDRHLLRSTTDDLYLVH 501
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
378-583 |
1.87e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.32 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 378 NLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQNIAEVTQDSLRRAISVVPQepalfhrsiRENIAYARP 457
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQ---------RNNTDMLSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 458 DATD----------EEVRDAAQKAH-ALEFidmlpeGMNTLVGERGVKLSGGQRQRVAIARAILKDAPILILDEATSALD 526
Cdd:PRK10938 94 GEDDtgrttaeiiqDEVKDPARCEQlAQQF------GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1083564009 527 SESEVAVQKALKELMYGK-TVIAIAHRLSTLRD-MSRILVLEHGTIQEDGTHEELLKNS 583
Cdd:PRK10938 168 VASRQQLAELLASLHQSGiTLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQA 226
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
376-526 |
2.65e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.93 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 376 NFNLTIKDGERIGLVGKSGAGKSTLVSLLLREY------DIA------GGAIKIDD--QNIAEVTqDSL----RRAISVV 437
Cdd:PRK10938 278 NLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHpqgysnDLTlfgrrrGSGETIWDikKHIGYVS-SSLhldyRVSTSVR 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 438 PQEPALFHRSIreNIAYARPDAtdeevrdaaQKAHALEFIDMLpeGMNTLVGERGVK-LSGGQRQRVAIARAILKDAPIL 516
Cdd:PRK10938 357 NVILSGFFDSI--GIYQAVSDR---------QQKLAQQWLDIL--GIDKRTADAPFHsLSWGQQRLALIVRALVKHPTLL 423
|
170
....*....|
gi 1083564009 517 ILDEATSALD 526
Cdd:PRK10938 424 ILDEPLQGLD 433
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
429-584 |
8.55e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.11 E-value: 8.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 429 SLRRAISVvpQEPALFHR----SIRENIaYARPDATDEEVRDAaqKAHALEFIDMLpeGMNTLVGERGVKLSGGQRQRVA 504
Cdd:NF000106 82 ALRRTIG*--HRPVR*GRresfSGRENL-YMIGR*LDLSRKDA--RARADELLERF--SLTEAAGRAAAKYSGGMRRRLD 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 505 IARAILKDAPILILDEATSALDSESEVAVQKALKELMY-GKTVIAIAHRLSTLRDMSRIL-VLEHGTIQEDGTHEELLKN 582
Cdd:NF000106 155 LAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRdGATVLLTTQYMEEAEQLAHELtVIDRGRVIADGKVDELKTK 234
|
..
gi 1083564009 583 SG 584
Cdd:NF000106 235 VG 236
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
375-569 |
1.15e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 43.08 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 375 KNFNLTIKDGERIGLVGKSGAGKSTLVSlllreydiaggaikiddQNIAEVTQDSLRRAISVVPQEPALF----HRSIRE 450
Cdd:cd03238 12 QNLDVSIPLNVLVVVTGVSGSGKSTLVN-----------------EGLYASGKARLISFLPKFSRNKLIFidqlQFLIDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 451 NIAYARPDatdeevrdaaQKahalefidmlpegMNTLvgergvklSGGQRQRVAIARAILKDAP--ILILDEATSALDSE 528
Cdd:cd03238 75 GLGYLTLG----------QK-------------LSTL--------SGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQ 123
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1083564009 529 SEVAVQKALKELMY-GKTVIAIAHRLSTLRDMSRILVLEHGT 569
Cdd:cd03238 124 DINQLLEVIKGLIDlGNTVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
47-325 |
2.11e-04 |
|
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: 43.37 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 47 IGETVVSFL-PYVYKIVVDGIqTQGTAEVVSFIVFWSIVYvsAFLFFatifrLSSFLG-VRGIS-RAVESTAYPALR--- 120
Cdd:cd18560 6 ILGKACNVLaPLFLGRAVNAL-TLAKVKDLESAVTLILLY--ALLRF-----SSKLLKeLRSLLyRRVQQNAYRELSlkt 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 121 -DYLQKHSHRFFSGNFAGGLNAKEIQVGGGMRNLLHEAIWTVTATAIGLLVTTGLMFSVDVR--AGVTFVTLIVVIILcN 197
Cdd:cd18560 78 fAHLHSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVPTLLELIVVSVVFAFHFGAwlALIVFLSVLLYGVF-T 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 198 LPLFKWQGGIARMHAKAIAKIRGVSIDALTNMRAVHSFAQGSQELSRLTETLEDARVIGVKKSDVAQYILIINTIIILLA 277
Cdd:cd18560 157 IKVTEWRTKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQLIIQLG 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1083564009 278 VSGILALLIISFQQGTATSGDFVLVFALISSVWRELTRIGFMINNISQ 325
Cdd:cd18560 237 LTLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQ 284
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
54-325 |
3.10e-04 |
|
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: 43.17 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 54 FLPYVYKIVVDGIQTQG-TAEVVSFIVFWSIvyvsAFLFFATIFRLSSFLGVRGISRAVESTaypaLR----DYLQKHSH 128
Cdd:cd18541 17 LIPRIIGRAIDALTAGTlTASQLLRYALLIL----LLALLIGIFRFLWRYLIFGASRRIEYD----LRndlfAHLLTLSP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 129 RFFSGNFAGGL--------NAkeiqvgggMRNLLHEAIWTVTATAIGLLVTTGLMFSVDVRagVTFVTLIVVIILcnLPL 200
Cdd:cd18541 89 SFYQKNRTGDLmaratndlNA--------VRMALGPGILYLVDALFLGVLVLVMMFTISPK--LTLIALLPLPLL--ALL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 201 FKWQGGiaRMHAK------AIAKIRGVSIDALTNMRAVHSFAQGSQELSRLTETLEDArvigVKKS-DVAQYilIINTII 273
Cdd:cd18541 157 VYRLGK--KIHKRfrkvqeAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEY----VEKNlRLARV--DALFFP 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1083564009 274 ILLAVSGILALLIISF-----QQGTATSGDFV--------LVFALISsvwreltrIGFMINNISQ 325
Cdd:cd18541 229 LIGLLIGLSFLIVLWYggrlvIRGTITLGDLVafnsylgmLIWPMMA--------LGWVINLIQR 285
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
368-419 |
3.92e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 43.00 E-value: 3.92e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1083564009 368 HEAVEVFKNFnltIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDD 419
Cdd:PRK01889 182 GEGLDVLAAW---LSGGKTVALLGSSGVGKSTLVNALLGEEVQKTGAVREDD 230
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
342-551 |
5.96e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.80 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 342 EVIDVENaqdlVAKK-GEIVLdgisfaheavevFKNFNLTIKDGERIGLVGKSGAGKSTLVSLLLREYDIAGGAIKIDDQ 420
Cdd:PRK11819 323 KVIEAEN----LSKSfGDRLL------------IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGET 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 421 -NIAEVTQDslrraisvvpqepalfhrsiRENIAyarPDATD-EEVRDAaqkahaLEFIDMLPEGMNT------------ 486
Cdd:PRK11819 387 vKLAYVDQS--------------------RDALD---PNKTVwEEISGG------LDIIKVGNREIPSrayvgrfnfkgg 437
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1083564009 487 ----LVGErgvkLSGGQRQRVAIARAILKDAPILILDEATSALDSESEVAVQKALKElmYGKTVIAIAH 551
Cdd:PRK11819 438 dqqkKVGV----LSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLE--FPGCAVVISH 500
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
495-586 |
6.91e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.41 E-value: 6.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 495 LSGGQRQRVAIARAILKDAPILILDEATSALDSESEVAVQKALKELMY-GKTVIAIAHRLSTLRDMS-RILVLEHGTI-- 570
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKkDKGIIIISSEMPELLGITdRILVMSNGLVag 471
|
90
....*....|....*....
gi 1083564009 571 ---QEDGTHEELLKNSGTY 586
Cdd:PRK10982 472 ivdTKTTTQNEILRLASLH 490
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
56-325 |
7.59e-04 |
|
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: 41.65 E-value: 7.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 56 PYVYKIVVDGIQTQGTAEVvsfivfwsIVYVSAFLFFATIFR-LSSFLGVRGISRAVESTAYpALRDYLQKH----SHRF 130
Cdd:cd18542 19 PLLIRRIIDSVIGGGLREL--------LWLLALLILGVALLRgVFRYLQGYLAEKASQKVAY-DLRNDLYDHlqrlSFSF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 131 FSGNFAGGLnakeIQVGGG----MRNLLHEAIWTVTATAIGLLVTTGLMFSVDVRagVTFVTLIVVIILcnlplfkwqGG 206
Cdd:cd18542 90 HDKARTGDL----MSRCTSdvdtIRRFLAFGLVELVRAVLLFIGALIIMFSINWK--LTLISLAIIPFI---------AL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 207 IARMHAKAIAKIRGVSIDA-----------LTNMRAVHSFAQGSQELSRLTETLEDARVIGVKKSDV-AQYiliintIII 274
Cdd:cd18542 155 FSYVFFKKVRPAFEEIREQegelntvlqenLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLlAKY------WPL 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1083564009 275 LLAVSGILALLIISF-----QQGTATSGDFVLVFALISSVWRELTRIGFMINNISQ 325
Cdd:cd18542 229 MDFLSGLQIVLVLWVggylvINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSR 284
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
375-553 |
8.41e-04 |
|
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: 41.45 E-value: 8.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 375 KNFNLTIKDGERIGLVGKSGAGKSTLVSLLL---------------REYDIAGGAIKIDdqNIAEVTQDSLRRAISVVPQ 439
Cdd:cd03271 12 KNIDVDIPLGVLTCVTGVSGSGKSSLINDTLypalarrlhlkkeqpGNHDRIEGLEHID--KVIVIDQSPIGRTPRSNPA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 440 EPALFHRSIRE-----------------------NIAyarpDATDEEVRDAaqkahaLEFIDMLPEGMNTL--------- 487
Cdd:cd03271 90 TYTGVFDEIRElfcevckgkrynretlevrykgkSIA----DVLDMTVEEA------LEFFENIPKIARKLqtlcdvglg 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1083564009 488 ---VGERGVKLSGGQRQRVAIARAILKDAP---ILILDEATSALDSESEVAVQKALKELMY-GKTVIAIAHRL 553
Cdd:cd03271 160 yikLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNL 232
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
483-526 |
9.03e-04 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 41.51 E-value: 9.03e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1083564009 483 GMNTLVGERGVKLSGGQRQRVAIA--RAIL--KDAPILILDEATSALD 526
Cdd:cd03273 155 NMGGVWKESLTELSGGQRSLVALSliLALLlfKPAPMYILDEVDAALD 202
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
56-258 |
1.32e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 40.96 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 56 PYVYKIVVDGIQTQGTAEVVSFIVFWSIvyvsAFLFFATIfrLSSFLG-VRG--ISRAVESTAYP---ALRDYLQKHSHR 129
Cdd:cd18563 19 PYLTKILIDDVLIQLGPGGNTSLLLLLV----LGLAGAYV--LSALLGiLRGrlLARLGERITADlrrDLYEHLQRLSLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 130 FFSGNFAGGLNAKEIQVGGGMRNLLHEAIWTVTATAIGLLVTTGLMFSVDVRagVTFVTLIVVIILCNLPLFKWQggiaR 209
Cdd:cd18563 93 FFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWK--LALLVLIPVPLVVWGSYFFWK----K 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1083564009 210 MHA------KAIAKIRGVSIDALTNMRAVHSFAQGSQELSRLTETLEDARVIGVK 258
Cdd:cd18563 167 IRRlfhrqwRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIR 221
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
493-553 |
1.35e-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: 39.65 E-value: 1.35e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1083564009 493 VKLSGGQRQRVAIARAI----LKDAPILILDEATSALDSESEVAVQKALKELMYGK-TVIAIAHRL 553
Cdd:cd03227 76 LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGaQVIVITHLP 141
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
482-541 |
2.11e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.90 E-value: 2.11e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1083564009 482 EGMNTLVGERGVKLSGGQRQ------RVAIARAILKDAPILILDEATSALDSESevaVQKALKELM 541
Cdd:cd03240 103 GESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEN---IEESLAEII 165
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
378-526 |
2.96e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.88 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 378 NLTIKDGERIGLVGKSGAGKST----LVSLLlreyDIAGGAIK-----IDDQNIAevtqdsLRRAISVVPQEPALFHR-S 447
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTtmkmLTGLL----PASEGEAWlfgqpVDAGDIA------TRRRVGYMSQAFSLYGElT 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 448 IRENIA-YAR-----PDATDEEVRDAAQKAHALEFIDMLPEGmntlvgergvkLSGGQRQRVAIARAILKDAPILILDEA 521
Cdd:NF033858 356 VRQNLElHARlfhlpAAEIAARVAEMLERFDLADVADALPDS-----------LPLGIRQRLSLAVAVIHKPELLILDEP 424
|
....*
gi 1083564009 522 TSALD 526
Cdd:NF033858 425 TSGVD 429
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
47-258 |
6.35e-03 |
|
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: 38.95 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 47 IGETVVS-FLPYVYKIVVDGIQTQGtaevvsfIVFWSIVYVSAFLFFATIFR-LSSFLgvrgISRAVESTAYpALRDYLQ 124
Cdd:cd18551 9 LLGTAASlAQPLLVKNLIDALSAGG-------SSGGLLALLVALFLLQAVLSaLSSYL----LGRTGERVVL-DLRRRLW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 125 KH----SHRFFSGNFAGGLNAKEIQVGGGMRNLLHEAIWTVTATAIGLLVTTGLMFSVDVR-AGVTFVTlIVVIILCNLP 199
Cdd:cd18551 77 RRllrlPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVlTLVTLAV-VPLAFLIILP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1083564009 200 LFKWQGGIARMHAKAIAKIRGVSIDALTNMRAVHSFAQGSQELSRLTETLEDARVIGVK 258
Cdd:cd18551 156 LGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLK 214
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
180-260 |
7.04e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 38.99 E-value: 7.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 180 VRAGVTFVTLIVV----------IILCNLPLFKWQGGI-ARMHAKAIAKIR-------GVSIDALTNMRAVHSFAQGSQE 241
Cdd:cd18577 129 IQSLSTFIAGFIIafiyswkltlVLLATLPLIAIVGGImGKLLSKYTKKEQeayakagSIAEEALSSIRTVKAFGGEEKE 208
|
90
....*....|....*....
gi 1083564009 242 LSRLTETLEDARVIGVKKS 260
Cdd:cd18577 209 IKRYSKALEKARKAGIKKG 227
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
118-264 |
8.42e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 38.62 E-value: 8.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 118 ALRDYLQKHSHRFFSGNFAGGLNAKEIQVGGGMRNLLHEAIWTVTATAIGLLVTTGLMFSVDVRagvtfVTLIVVIIlcn 197
Cdd:cd18550 77 QLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWR-----LALLSLVL--- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083564009 198 LPLFKWqggIARMHAKAIAKIRGVSIDALTNMRA-------------VHSFAQGSQELSRLTETLEDARVIGVKKSDVAQ 264
Cdd:cd18550 149 LPLFVL---PTRRVGRRRRKLTREQQEKLAELNSimqetlsvsgallVKLFGREDDEAARFARRSRELRDLGVRQALAGR 225
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
495-563 |
8.80e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 39.18 E-value: 8.80e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1083564009 495 LSGGQRQRVAIA--RAIL--KDAPILILDEATSALDSESEVAVQKALKELMYGKTVIAIAHRLSTLRDMSRIL 563
Cdd:pfam02463 1078 LSGGEKTLVALAliFAIQkyKPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLV 1150
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
386-436 |
9.93e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 36.44 E-value: 9.93e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1083564009 386 RIGLVGKSGAGKSTLVSLLLREYDIAGgaikiddqNIAEVTQDSLRRAISV 436
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGAKAIVS--------DYPGTTRDPNEGRLEL 43
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