|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
16-506 |
0e+00 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 1013.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 16 MTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENGISMVHQ 95
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 96 ELNLVLQRSVMDNMWLGRYPTKGVFVDQEKMYLDTKAIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSYDAKIVIMDE 175
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 176 PTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQSLEGLDMDKIIAMMVGRSLNQRFP 255
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVGRSLTQRFP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 256 DRENKPGEVILEVRNLTSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANEA 335
Cdd:PRK10982 241 DKENKPGEVILEVRNLTSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 336 INNGFALVTEERRSTGIYAYLDIGFNSLISNIRNYKSKIGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGNQQKV 415
Cdd:PRK10982 321 INHGFALVTEERRSTGIYAYLDIGFNSLISNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGNQQKV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 416 IIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNGLVSGIVDTKTTTQ 495
Cdd:PRK10982 401 IIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTKTTTQ 480
|
490
....*....|.
gi 495051738 496 NEILRLASLHL 506
Cdd:PRK10982 481 NEILRLASLHL 491
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
11-503 |
0e+00 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 791.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 11 EYLLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENGI 90
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 91 SMVHQELNLVLQRSVMDNMWLGRYPTKGVFVDQEKMYLDTKAIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSYDAKI 170
Cdd:COG1129 82 AIIHQELNLVPNLSVAENIFLGREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 171 VIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQSLEGLDMDKIIAMMVGRSL 250
Cdd:COG1129 162 LILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMVGREL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 251 NQRFPDRENKPGEVILEVRNLTslRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNH 330
Cdd:COG1129 242 EDLFPKRAAAPGEVVLEVEGLS--VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 331 SANEAINNGFALVTEERRSTGIYAYLDIGFNSLISNIRNYkSKIGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGG 410
Cdd:COG1129 320 SPRDAIRAGIAYVPEDRKGEGLVLDLSIRENITLASLDRL-SRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVGNLSGG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 411 NQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNGLVSGIVDT 490
Cdd:COG1129 399 NQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDR 478
|
490
....*....|...
gi 495051738 491 KTTTQNEILRLAS 503
Cdd:COG1129 479 EEATEEAIMAAAT 491
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
11-502 |
0e+00 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 585.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 11 EYLLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDS--GSILFQGKEIDFHSAKEALEN 88
Cdd:PRK13549 3 EYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNIRDTERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 89 GISMVHQELNLVLQRSVMDNMWLGRYPTKGVFVDQEKMYLDTKAIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSYDA 168
Cdd:PRK13549 83 GIAIIHQELALVKELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 169 KIVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQSLEGLDMDKIIAMMVGR 248
Cdd:PRK13549 163 RLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITMMVGR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 249 SLNQRFPDRENKPGEVILEVRNLTSLR--QPSIR---DVSFDLHKGEILGIAGLVGAKRTDIVETLFGIRE-KSGGTISL 322
Cdd:PRK13549 243 ELTALYPREPHTIGEVILEVRNLTAWDpvNPHIKrvdDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 323 HGKKINNHSANEAINNGFALVTEERRSTGIYAYLDIGFNSLISNIRNYkSKIGLLDNSRMKSDTQWVIDSMRVKTPGHRT 402
Cdd:PRK13549 323 DGKPVKIRNPQQAIAQGIAMVPEDRKRDGIVPVMGVGKNITLAALDRF-TGGSRIDDAAELKTILESIQRLKVKTASPEL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 403 QIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK13549 402 AIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEG 481
|
490 500
....*....|....*....|
gi 495051738 483 LVSGIVDTKTTTQNEILRLA 502
Cdd:PRK13549 482 KLKGDLINHNLTQEQVMEAA 501
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
14-502 |
0e+00 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 556.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENGISMV 93
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 94 HQELNLVLQRSVMDNMWLGRYPTKGVFVDQEKMYLDTKAIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSYDAKIVIM 173
Cdd:PRK11288 85 YQELHLVPEMTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 174 DEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIAT-QSLEGLDMDKIIAMMVGRSLNQ 252
Cdd:PRK11288 165 DEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATfDDMAQVDRDQLVQAMVGREIGD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 253 RFPDRENKPGEVILEVRNLTS--LRQPsirdVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNH 330
Cdd:PRK11288 245 IYGYRPRPLGEVRLRLDGLKGpgLREP----ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 331 SANEAINNGFALVTEERRSTGIYAYLDIGFNSLISNIRNYKSKIGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGG 410
Cdd:PRK11288 321 SPRDAIRAGIMLCPEDRKAEGIIPVHSVADNINISARRHHLRAGCLINNRWEAENADRFIRSLNIKTPSREQLIMNLSGG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 411 NQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNGLVSGIVDT 490
Cdd:PRK11288 401 NQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELAR 480
|
490
....*....|..
gi 495051738 491 KTTTQNEILRLA 502
Cdd:PRK11288 481 EQATERQALSLA 492
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
13-502 |
0e+00 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 550.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENGISM 92
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 93 VHQELNLVLQRSVMDNMWLGRYPTKGV-FVDQEKMYLDTKAIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSYDAKIV 171
Cdd:PRK10762 84 IHQELNLIPQLTIAENIFLGREFVNRFgRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 172 IMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQSLEGLDMDKIIAMMVGRSLN 251
Cdd:PRK10762 164 IMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMMVGRKLE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 252 QRFPDRENKPGEVILEVRNLTSlrqPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHS 331
Cdd:PRK10762 244 DQYPRLDKAPGEVRLKVDNLSG---PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 332 ANEAINNGFALVTEERRSTGIYAYLDIGFNSLISNIRNYKSKIGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGN 411
Cdd:PRK10762 321 PQDGLANGIVYISEDRKRDGLVLGMSVKENMSLTALRYFSRAGGSLKHADEQQAVSDFIRLFNIKTPSMEQAIGLLSGGN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 412 QQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNGLVSGIVDTK 491
Cdd:PRK10762 401 QQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTRE 480
|
490
....*....|.
gi 495051738 492 TTTQNEILRLA 502
Cdd:PRK10762 481 QATQEKLMAAA 491
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
9-498 |
0e+00 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 542.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 9 SGEYLLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALEN 88
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 89 GISMVHQELNLVLQRSVMDNMWLGRYPTKGVFVDQEKMYLDTKAIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSYDA 168
Cdd:COG3845 81 GIGMVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 169 KIVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQSLEGLDMDKIIAMMVGR 248
Cdd:COG3845 161 RILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAELMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 249 SLNQRFPDRENKPGEVILEVRNLTSLR---QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGK 325
Cdd:COG3845 241 EVLLRVEKAPAEPGEVVLEVENLSVRDdrgVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 326 KINNHSANEAINNGFALVTEERRSTGIYAYLDIGFNSLISNIRNYK-SKIGLLDNSRMKSDTQWVIDSMRVKTPGHRTQI 404
Cdd:COG3845 321 DITGLSPRERRRLGVAYIPEDRLGRGLVPDMSVAENLILGRYRRPPfSRGGFLDRKAIRAFAEELIEEFDVRTPGPDTPA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 405 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:COG3845 401 RSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
490
....*....|....
gi 495051738 485 SGIVDTKTTTQNEI 498
Cdd:COG3845 481 VGEVPAAEATREEI 494
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
13-501 |
2.42e-178 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 510.10 E-value: 2.42e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDS--GSILFQGKEIDFHSAKEALENGI 90
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRFKDIRDSEALGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 91 SMVHQELNLVLQRSVMDNMWLGRYPTKGVFVDQEKMYLDTKAIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSYDAKI 170
Cdd:NF040905 81 VIIHQELALIPYLSIAENIFLGNERAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 171 VIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQSLEG--LDMDKIIAMMVGR 248
Cdd:NF040905 161 LILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDCRAdeVTEDRIIRGMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 249 SLNQRFPDRENKPGEVILEVRNLT------SLRQpSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGireKS-----G 317
Cdd:NF040905 241 DLEDRYPERTPKIGEVVFEVKNWTvyhplhPERK-VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFG---RSygrniS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 318 GTISLHGKKINNHSANEAINNGFALVTEERRSTGIYAYLDIGFNSLISNIRNYkSKIGLLDNSRMKSDTQWVIDSMRVKT 397
Cdd:NF040905 317 GTVFKDGKEVDVSTVSDAIDAGLAYVTEDRKGYGLNLIDDIKRNITLANLGKV-SRRGVIDENEEIKVAEEYRKKMNIKT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 398 PGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRIL 477
Cdd:NF040905 396 PSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIY 475
|
490 500
....*....|....*....|....
gi 495051738 478 VMSNGLVSGIVDTKTTTQNEILRL 501
Cdd:NF040905 476 VMNEGRITGELPREEASQERIMRL 499
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
13-505 |
4.50e-172 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 494.69 E-value: 4.50e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENGISM 92
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 93 VHQELNLVLQRSVMDNMWLGRYPTKGVF----VDQEKMYLDTKAIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSYDA 168
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGRHLTKKVCgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 169 KIVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQSLEGLDMDKIIAMMVGR 248
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLMVGR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 249 SLNQRFPDRE----NKPGEVILEVRNLTSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHG 324
Cdd:PRK09700 245 ELQNRFNAMKenvsNLAHETVFEVRNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 325 KKINNHSANEAINNGFALVTEERRSTGIYAYLDIGFNSLISN-IRN--YKSKIGLLDNSRMKSDTQWVIDSMRVKTPGHR 401
Cdd:PRK09700 325 KDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISRsLKDggYKGAMGLFHEVDEQRTAENQRELLALKCHSVN 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 402 TQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSN 481
Cdd:PRK09700 405 QNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCE 484
|
490 500
....*....|....*....|....*
gi 495051738 482 GLVSGIVD-TKTTTQNEILRLASLH 505
Cdd:PRK09700 485 GRLTQILTnRDDMSEEEIMAWALPQ 509
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
13-502 |
1.01e-154 |
|
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: 450.05 E-value: 1.01e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDS--GSILFQGKEIDFHSAKEALENGI 90
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 91 SMVHQELNLVLQRSVMDNMWLGRYPT-KGVFVDQEKMYLDTKAIFDELDIDIDPKAR-VGTLSVSQMQMIEIAKAFSYDA 168
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEITlPGGRMAYNAMYLRAKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 169 KIVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQSLEGLDMDKIIAMMVGR 248
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 249 SLNQRFPDRENKPGEVILEVRNLTSL-----RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIRE-KSGGTISL 322
Cdd:TIGR02633 241 EITSLYPHEPHEIGDVILEARNLTCWdvinpHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 323 HGKKINNHSANEAINNGFALVTEERRSTGIYAYLDIGFNSLISNIRNYkSKIGLLDNSRMKSDTQWVIDSMRVKTPGHRT 402
Cdd:TIGR02633 321 NGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGKNITLSVLKSF-CFKMRIDAAAELQIIGSAIQRLKVKTASPFL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 403 QIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:TIGR02633 400 PIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
490 500
....*....|....*....|
gi 495051738 483 LVSGIVDTKTTTQNEILRLA 502
Cdd:TIGR02633 480 KLKGDFVNHALTQEQVLAAA 499
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-502 |
2.44e-118 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 357.44 E-value: 2.44e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 4 NNTQSSGEYLLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAK 83
Cdd:PRK15439 2 QTSDTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 84 EALENGISMVHQELNLVLQRSVMDNMWLGRYPTKGvfvDQEKMyldtKAIFDELDIDIDPKARVGTLSVSQMQMIEIAKA 163
Cdd:PRK15439 82 KAHQLGIYLVPQEPLLFPNLSVKENILFGLPKRQA---SMQKM----KQLLAALGCQLDLDSSAGSLEVADRQIVEILRG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 164 FSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQSLEGLDMDKIIA 243
Cdd:PRK15439 155 LMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 244 MMVGRSLNQRFPD------------RENKPGEVILEVRNLTSlrqPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFG 311
Cdd:PRK15439 235 AITPAAREKSLSAsqklwlelpgnrRQQAAGAPVLTVEDLTG---EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 312 IREKSGGTISLHGKKINNHSANEAINNGFALVTEERRSTGIYAYLDIGFN--SLISNIRNYkskigLLDNSRMKSDTQWV 389
Cdd:PRK15439 312 LRPARGGRIMLNGKEINALSTAQRLARGLVYLPEDRQSSGLYLDAPLAWNvcALTHNRRGF-----WIKPARENAVLERY 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 390 IDSMRVKTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPEL 469
Cdd:PRK15439 387 RRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEI 466
|
490 500 510
....*....|....*....|....*....|...
gi 495051738 470 LGITDRILVMSNGLVSGIVDTKTTTQNEILRLA 502
Cdd:PRK15439 467 EQMADRVLVMHQGEISGALTGAAINVDTIMRLA 499
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-230 |
3.73e-85 |
|
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: 259.67 E-value: 3.73e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENGISMV 93
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 94 HQelnlvlqrsvmdnmwlgryptkgvfvdqekmyldtkaifdeldididpkarvgtLSVSQMQMIEIAKAFSYDAKIVIM 173
Cdd:cd03216 81 YQ------------------------------------------------------LSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495051738 174 DEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIAT 230
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
262-482 |
6.48e-81 |
|
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: 249.66 E-value: 6.48e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 262 GEVILEVRNLTslRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANEAINNGFA 341
Cdd:cd03215 1 GEPVLEVRGLS--VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 342 LVTEERRSTGIYAYLDIGFNSLISNIrnykskiglldnsrmksdtqwvidsmrvktpghrtqigsLSGGNQQKVIIGRWL 421
Cdd:cd03215 79 YVPEDRKREGLVLDLSVAENIALSSL---------------------------------------LSGGNQQKVVLARWL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495051738 422 LTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:cd03215 120 ARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
13-482 |
5.79e-61 |
|
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: 208.22 E-value: 5.79e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFPG--VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKD---SGSILFQGKEIDFHSAKEaLE 87
Cdd:COG1123 4 LLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL-RG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 88 NGISMVHQE----LNLVlqrSVMDNMWLGRYPTKgvfVDQEKMYLDTKAIFDELDIDIDPKARVGTLSVSQMQMIEIAKA 163
Cdd:COG1123 83 RRIGMVFQDpmtqLNPV---TVGDQIAEALENLG---LSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 164 FSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQS-LEGLDMDKI 241
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPpEEILAAPQA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 242 IAMMVGRSLNQRFPDRENKPGEVILEVRNLT-------SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIRE 314
Cdd:COG1123 237 LAAVPRLGAARGRAAPAAAAAEPLLEVRNLSkrypvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 315 KSGGTISLHGKKINNHSANEainngfalVTEERRSTGI-----YAYLD----IGfNSLISNIRNYkskiGLLDNSRMKSD 385
Cdd:COG1123 317 PTSGSILFDGKDLTKLSRRS--------LRELRRRVQMvfqdpYSSLNprmtVG-DIIAEPLRLH----GLLSRAERRER 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 386 TQWVIDsmRVK-TPGHRTQ-IGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-GKGIIII 462
Cdd:COG1123 384 VAELLE--RVGlPPDLADRyPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFI 461
|
490 500
....*....|....*....|
gi 495051738 463 SSEMPELLGITDRILVMSNG 482
Cdd:COG1123 462 SHDLAVVRYIADRVAVMYDG 481
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
14-230 |
1.86e-50 |
|
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: 172.24 E-value: 1.86e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENGISMV 93
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 94 HQELNLVLQRSVMDNMWLGRYPTKGVFVDQEKMYLDTKAIFDELD-----IDIDPKA--RVGTLSVSQMQMIEIAKAFSY 166
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTGSGLLLARARREEREARERAEellerVGLADLAdrPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495051738 167 DAKIVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIAT 230
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAE 224
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
10-230 |
8.04e-47 |
|
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: 163.29 E-value: 8.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 10 GEYLLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENG 89
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 90 ISMVHQELNLVLQRSVMDNMWLGRYPTKGVFVDQEKMYL-----DTKAIFDE----LD-IDIDPKA--RVGTLSVSQMQM 157
Cdd:COG0411 81 IARTFQNPRLFPELTVLENVLVAAHARLGRGLLAALLRLprarrEEREARERaeelLErVGLADRAdePAGNLSYGQQRR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495051738 158 IEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLK-ERGCGIVYISHKMEEIFQLCDEITILRDGQWIAT 230
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRdERGITILLIEHDMDLVMGLADRIVVLDFGRVIAE 234
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
13-236 |
1.45e-45 |
|
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: 159.64 E-value: 1.45e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeIDFHSAKEALENGISM 92
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDG--EDVRKEPREARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 93 VHQELNLVLQRSVMDNMwlgRY--PTKGVFVDQEKmyLDTKAIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSYDAKI 170
Cdd:COG4555 79 LPDERGLYDRLTVRENI---RYfaELYGLFDEELK--KRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495051738 171 VIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQSLEGL 236
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
14-236 |
1.65e-44 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 156.38 E-value: 1.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAkEALENgISMV 93
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPA-EVRRR-IGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 94 HQELNLVLQRSVMDNM-WLGRYptKGVFVDQEKMYLDtkAIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSYDAKIVI 172
Cdd:COG1131 79 PQEPALYPDLTVRENLrFFARL--YGLPRKEARERID--ELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495051738 173 MDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQSLEGL 236
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
14-226 |
1.68e-41 |
|
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: 146.39 E-value: 1.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeiDFHSAKEALENGISMV 93
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGK--DIKKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 94 HQELNLVLQRSVMDNMWLgrypTKGvfvdqekMyldtkaifdeldididpKARVGtlsvsqmqmieIAKAFSYDAKIVIM 173
Cdd:cd03230 79 PEEPSLYENLTVRENLKL----SGG-------M-----------------KQRLA-----------LAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495051738 174 DEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 226
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
15-226 |
2.53e-36 |
|
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: 133.75 E-value: 2.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 15 EMTNINKSFPG--VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEalengism 92
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKE-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 93 VHQELNLVLQRSvmDNMWLGryPTkgVF-----------VDQEKMYLDTKAIFDELDIDIDPKARVGTLSVSQMQMIEIA 161
Cdd:cd03225 73 LRRKVGLVFQNP--DDQFFG--PT--VEeevafglenlgLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495051738 162 KAFSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 226
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
14-226 |
5.51e-36 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 133.85 E-value: 5.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFP-GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDF--HSAKEALENGI 90
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlkGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 91 SMVHQELNLVLQRSVMDNMWLGRYPTK-------GVFVDQEKmyLDTKAIFDELDIDIDPKARVGTLSVSQMQMIEIAKA 163
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRRstwrslfGLFPKEEK--QRALAALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495051738 164 FSYDAKIVIMDEPTSSL---TEKEVNHLFKIIRklKERGCGIVYISHKMEEIFQLCDEITILRDGQ 226
Cdd:cd03256 159 LMQQPKLILADEPVASLdpaSSRQVMDLLKRIN--REEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-249 |
2.61e-35 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 137.84 E-value: 2.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 6 TQSSGEYLLEMTNINksfpGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEA 85
Cdd:COG1129 249 AAAPGEVVLEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDA 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 86 LENGISMV---HQELNLVLQRSVMDNM---WLGRYpTKGVFVDQEKMYLDTKAIFDELDIDI-DPKARVGTLSVSQMQMI 158
Cdd:COG1129 325 IRAGIAYVpedRKGEGLVLDLSIRENItlaSLDRL-SRGGLLDRRRERALAEEYIKRLRIKTpSPEQPVGNLSGGNQQKV 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 159 EIAKAFSYDAKIVIMDEPT-----SSLTEkevnhLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQSL 233
Cdd:COG1129 404 VLAKWLATDPKVLILDEPTrgidvGAKAE-----IYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDR 478
|
250
....*....|....*.
gi 495051738 234 EGLDMDKIIAMMVGRS 249
Cdd:COG1129 479 EEATEEAIMAAATGGA 494
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
13-229 |
4.24e-35 |
|
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: 131.70 E-value: 4.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKE-ALEngIS 91
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElARR--IA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 92 MVHQELNLVLQRSVMDNMWLGRYPTKGVF--VDQEkmylDTKAIFDELDI-DIDPKA--RVGTLSVSQMQMIEIAKAFSY 166
Cdd:COG1120 79 YVPQEPPAPFGLTVRELVALGRYPHLGLFgrPSAE----DREAVEEALERtGLEHLAdrPVDELSGGERQRVLIARALAQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495051738 167 DAKIVIMDEPTSSLtekEVNH---LFKIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWIA 229
Cdd:COG1120 155 EPPLLLLDEPTSHL---DLAHqleVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVA 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
14-226 |
5.67e-35 |
|
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: 130.25 E-value: 5.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENGISMV 93
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 94 HQELNLVLQRSVMDNMWLGRYPTKGVFVDQ--EKMYldtkAIFDELdididpKAR----VGTLSVSQMQMIEIAKAFSYD 167
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKArlERVY----ELFPRL------KERrkqlAGTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495051738 168 AKIVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 226
Cdd:cd03224 151 PKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
15-226 |
5.86e-35 |
|
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: 128.13 E-value: 5.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 15 EMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEaLENGISMVH 94
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE-LRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 95 QelnlvlqrsvmdnmwlgryptkgvfvdqekmyldtkaifdeldididpkarvgtLSVSQMQMIEIAKAFSYDAKIVIMD 174
Cdd:cd00267 80 Q------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495051738 175 EPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 226
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
14-226 |
1.53e-33 |
|
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: 126.09 E-value: 1.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfhSAKEALENGISMV 93
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV---TGVPPERRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 94 HQELNLVLQRSVMDNMwlgRYPTKGVFVDQEKMYLDTKAIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSYDAKIVIM 173
Cdd:cd03259 78 FQDYALFPHLTVAENI---AFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495051738 174 DEPTSSLTEKEVNHLFKIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQ 226
Cdd:cd03259 155 DEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGR 208
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
14-226 |
3.51e-33 |
|
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: 124.22 E-value: 3.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAK-EALENGISM 92
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 93 VHQELNLVLQRSVMDNMWLGryptkgvfvdqekmyldtkaifdeldididpkarvgtLSVSQMQMIEIAKAFSYDAKIVI 172
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG-------------------------------------LSGGQQQRVALARALAMDPDVLL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495051738 173 MDEPTSSLTEKEVNHLFKIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQ 226
Cdd:cd03229 124 LDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
13-226 |
4.10e-33 |
|
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: 125.70 E-value: 4.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFPG----VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALEN 88
Cdd:cd03257 1 LLEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 89 G--ISMVHQE----LNLVL--QRSVMDNMWLgryptKGVFVDQEKMyldtKAIFDELDIDIDPKARVGT-----LSVSQM 155
Cdd:cd03257 81 RkeIQMVFQDpmssLNPRMtiGEQIAEPLRI-----HGKLSKKEAR----KEAVLLLLVGVGLPEEVLNrypheLSGGQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495051738 156 QMIEIAKAFSYDAKIVIMDEPTSSL---TEKEVNHLFKIIRklKERGCGIVYISHKMEEIFQLCDEITILRDGQ 226
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALdvsVQAQILDLLKKLQ--EELGLTLLFITHDLGVVAKIADRVAVMYAGK 223
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
14-229 |
6.22e-33 |
|
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: 124.32 E-value: 6.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFhsakeALENGISMV 93
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI-----AARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 94 HQELNLVLQRSVMDNM-WLGRYptKGVFVDQEKMYLDTkaIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSYDAKIVI 172
Cdd:cd03269 76 PEERGLYPKMKVIDQLvYLAQL--KGLKKEEARRRIDE--WLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495051738 173 MDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIA 229
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVL 208
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
13-226 |
1.84e-32 |
|
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: 123.85 E-value: 1.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFPG----VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKE--AL 86
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 87 ENGISMVHQELNLVLQRSVMDNMwlgRYPTKGVFVDQEKMYLDTKAIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSY 166
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENV---ALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495051738 167 DAKIVIMDEPTSSLTEKEVNHLFKIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQ 226
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGE 218
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
14-226 |
2.07e-32 |
|
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: 123.60 E-value: 2.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFP-GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENgISM 92
Cdd:COG1122 1 IELENLSFSYPgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK-VGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 93 VHQ--ELNLVLqRSVMD-------NmwLGryptkgvfVDQEKMYLDTKAIFDELDIDiDPKAR-VGTLSVSQMQMIEIAK 162
Cdd:COG1122 80 VFQnpDDQLFA-PTVEEdvafgpeN--LG--------LPREEIRERVEEALELVGLE-HLADRpPHELSGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495051738 163 AFSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 226
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGR 211
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
14-229 |
6.77e-32 |
|
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: 121.84 E-value: 6.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPG--VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfHSAKEALENGIS 91
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI--RTDRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 92 MVHQELNLVLQRSVMDNMWL-GRYptKGVFVDQEKMylDTKAIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSYDAKI 170
Cdd:cd03263 79 YCPQFDALFDELTVREHLRFyARL--KGLPKSEIKE--EVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495051738 171 VIMDEPTSSLTEKEVNHLFKIIRKLKeRGCGIVYISHKMEEIFQLCDEITILRDGQWIA 229
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRC 212
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
29-178 |
1.20e-31 |
|
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: 118.90 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKeALENGISMVHQELNLVLQRSVMDN 108
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERK-SLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495051738 109 MWLGRYPTkgvFVDQEKMYLDTKAIFDELDIDIDPKARVG----TLSVSQMQMIEIAKAFSYDAKIVIMDEPTS 178
Cdd:pfam00005 80 LRLGLLLK---GLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
14-226 |
1.40e-31 |
|
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: 119.41 E-value: 1.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPG--VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfHSAKEALENGIS 91
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLR-DLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 92 MVHQELNLvLQRSVMDNMwlgryptkgvfvdqekmyldtkaifdeldididpkarvgtLSVSQMQMIEIAKAFSYDAKIV 171
Cdd:cd03228 80 YVPQDPFL-FSGTIRENI----------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495051738 172 IMDEPTSSL---TEKEVnhlFKIIRKLKeRGCGIVYISHKMEEIfQLCDEITILRDGQ 226
Cdd:cd03228 119 ILDEATSALdpeTEALI---LEALRALA-KGKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
15-222 |
1.53e-31 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 120.72 E-value: 1.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 15 EMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKealengISMVH 94
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR------IGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 95 QELNLVLQR--SVMDNMWLGRYPTKGVFVDQEKmylDTKAIFDE-LD-IDIDPKA--RVGTLSVSQMQMIEIAKAFSYDA 168
Cdd:cd03235 75 QRRSIDRDFpiSVRDVVLMGLYGHKGLFRRLSK---ADKAKVDEaLErVGLSELAdrQIGELSGGQQQRVLLARALVQDP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495051738 169 KIVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITIL 222
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-226 |
2.31e-31 |
|
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: 126.94 E-value: 2.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 8 SSGEYLLEMTNINKSFP-----GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSA 82
Cdd:COG1123 255 AAAEPLLEVRNLSKRYPvrgkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 83 KEALENG--ISMVHQE----LN--LVLQRSVMDNMWLGRYPTKGvfvdqekmylDTKAIFDEL--DIDIDPKA---RVGT 149
Cdd:COG1123 335 RSLRELRrrVQMVFQDpyssLNprMTVGDIIAEPLRLHGLLSRA----------ERRERVAELleRVGLPPDLadrYPHE 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495051738 150 LSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQ 226
Cdd:COG1123 405 LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLqRELGLTYLFISHDLAVVRYIADRVAVMYDGR 482
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
13-226 |
2.75e-31 |
|
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: 120.86 E-value: 2.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENGISM 92
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 93 VHQELNLVLQRSVMDNMWLGRYPTKGVFV---DQEKMYldtkAIFDELdididpKAR----VGTLSVSQMQMIEIAKAFS 165
Cdd:COG0410 83 VPEGRRIFPSLTVEENLLLGAYARRDRAEvraDLERVY----ELFPRL------KERrrqrAGTLSGGEQQMLAIGRALM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495051738 166 YDAKIVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 226
Cdd:COG0410 153 SRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGR 213
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
15-229 |
6.26e-31 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 117.92 E-value: 6.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 15 EMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENgISMVH 94
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK-IAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 95 QELNLVlqrsvmdnmwlgryptkgvfvdqekmyldtkaifdeldiDIDPKA--RVGTLSVSQMQMIEIAKAFSYDAKIVI 172
Cdd:cd03214 80 QALELL---------------------------------------GLAHLAdrPFNELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495051738 173 MDEPTSSLTEKEVNHLFKIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWIA 229
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVA 178
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
11-226 |
9.43e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 119.42 E-value: 9.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 11 EYLLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKealengI 90
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR------I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 91 SMVHQ--ELNLVLQRSVMDNMWLGRYPTKGVF--VDQEkmylDTKAIFDELD-IDIDPKA--RVGTLSVSQMQMIEIAKA 163
Cdd:COG1121 78 GYVPQraEVDWDFPITVRDVVLMGRYGRRGLFrrPSRA----DREAVDEALErVGLEDLAdrPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495051738 164 FSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 226
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGL 216
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
14-230 |
2.47e-30 |
|
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: 117.32 E-value: 2.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfhSAKEALENGISMV 93
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ--KNIEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 94 hQELNLVLQRSVMDNMwlgRYPTKGVFVDQEKMyldtKAIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSYDAKIVIM 173
Cdd:cd03268 79 -EAPGFYPNLTARENL---RLLARLLGIRKKRI----DEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495051738 174 DEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIAT 230
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
13-229 |
3.85e-30 |
|
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: 117.08 E-value: 3.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSF----PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeIDFHSAKEALEN 88
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPAEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 89 GISMVHQELNLVLQRSVMDNM-WLGR-YPTKGvfvDQEKMYLDTkaIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSY 166
Cdd:cd03266 79 RLGFVSDSTGLYDRLTARENLeYFAGlYGLKG---DELTARLEE--LADRLGMEELLDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495051738 167 DAKIVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIA 229
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVY 216
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
14-226 |
4.06e-30 |
|
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: 116.82 E-value: 4.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPG----VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALE-- 87
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 88 -NGISMVHQELNLVLQRSVMDNMWLGRYPTkGVFVDQEKMYLdtKAIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSY 166
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVELPLLLA-GVPKKERRERA--EELLERVGLGDRLNHYPSELSGGQQQRVAIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495051738 167 DAKIVIMDEPTSSL---TEKEVnhlFKIIRKL-KERGCGIVYISHKMeEIFQLCDEITILRDGQ 226
Cdd:cd03255 158 DPKIILADEPTGNLdseTGKEV---MELLRELnKEAGTTIVVVTHDP-ELAEYADRIIELRDGK 217
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
10-226 |
8.64e-30 |
|
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: 114.84 E-value: 8.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 10 GEYLLEMTNInkSFPGvkALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENG 89
Cdd:cd03215 1 GEPVLEVRGL--SVKG--AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 90 ISMV----HQELnLVLQRSVMDNMWLGRYptkgvfvdqekmyldtkaifdeldididpkarvgtLSVSQMQMIEIAKAFS 165
Cdd:cd03215 77 IAYVpedrKREG-LVLDLSVAENIALSSL-----------------------------------LSGGNQQKVVLARWLA 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495051738 166 YDAKIVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 226
Cdd:cd03215 121 RDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
14-226 |
9.97e-30 |
|
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: 123.41 E-value: 9.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPG--VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG---KEIDfhsaKEALEN 88
Cdd:COG2274 474 IELENVSFRYPGdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlRQID----PASLRR 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 89 GISMVHQELNLvLQRSVMDNMWLGRyPTkgvfVDQEKMY--LDTKAIFDelDIDIDPK---ARVG----TLSVSQMQMIE 159
Cdd:COG2274 550 QIGVVLQDVFL-FSGTIRENITLGD-PD----ATDEEIIeaARLAGLHD--FIEALPMgydTVVGeggsNLSGGQRQRLA 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495051738 160 IAKAFSYDAKIVIMDEPTSSL---TEKevnhlfKIIRKLKE--RGCGIVYISHKMEEIfQLCDEITILRDGQ 226
Cdd:COG2274 622 IARALLRNPRILILDEATSALdaeTEA------IILENLRRllKGRTVIIIAHRLSTI-RLADRIIVLDKGR 686
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
266-484 |
2.59e-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: 114.84 E-value: 2.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 266 LEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANEAINNGFALV 343
Cdd:cd03224 1 LEVENLNAGygKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 344 TEERRstgIYAYLdigfnSLISNIRnykskIGLLDnsRMKSDTQWVIDSM---------RVKTPGhrtqiGSLSGGNQQK 414
Cdd:cd03224 81 PEGRR---IFPEL-----TVEENLL-----LGAYA--RRRAKRKARLERVyelfprlkeRRKQLA-----GTLSGGEQQM 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495051738 415 VIIGRWLLTQPEILMLDEPTRG-----IDvgakfEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:cd03224 141 LAIARALMSRPKLLLLDEPSEGlapkiVE-----EIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRV 210
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
13-236 |
3.59e-29 |
|
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: 115.29 E-value: 3.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFP----GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdFHSAKEALEN 88
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV-TRRRRKAFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 89 GISMVHQE----LN--LVLQRSVMDNMWLGRYPtkgvfvdqekmylDTKAIFDEL--DIDIDPKAR---VGTLSVSQMQM 157
Cdd:COG1124 80 RVQMVFQDpyasLHprHTVDRILAEPLRIHGLP-------------DREERIAELleQVGLPPSFLdryPHQLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 158 IEIAKAFSYDAKIVIMDEPTSSL---TEKEVNHLFKIIRKlkERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQSLE 234
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALdvsVQAEILNLLKDLRE--ERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVA 224
|
..
gi 495051738 235 GL 236
Cdd:COG1124 225 DL 226
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-236 |
8.38e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 115.59 E-value: 8.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAK------EalE 87
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRrigylpE--E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 88 NGI--SMvhqelnlvlqrSVMDN-MWLGRYptKGvfVDQEKMYLDTKAIFDELDIDIDPKARVGTLSVSQMQMIEIAKAF 164
Cdd:COG4152 80 RGLypKM-----------KVGEQlVYLARL--KG--LSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495051738 165 SYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQSLEGL 236
Cdd:COG4152 145 LHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
13-226 |
1.61e-28 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 112.83 E-value: 1.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFP----GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfHSAKEA--- 85
Cdd:COG1136 4 LLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDI--SSLSERela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 86 ---LENgISMVHQELNLVLQRSVMDNMWLGRYPTKgvfVDQEKMYLDTKAIFDELDID--IDpkARVGTLSVSQMQMIEI 160
Cdd:COG1136 82 rlrRRH-IGFVFQFFNLLPELTALENVALPLLLAG---VSRKERRERARELLERVGLGdrLD--HRPSQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 161 AKAFSYDAKIVIMDEPTSSL---TEKEVnhlFKIIRKL-KERGCGIVYISHKmEEIFQLCDEITILRDGQ 226
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLdskTGEEV---LELLRELnRELGTTIVMVTHD-PELAARADRVIRLRDGR 221
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
10-247 |
1.66e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 118.21 E-value: 1.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 10 GEYLLEMTNIN-KSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALEN 88
Cdd:COG3845 254 GEVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 89 GISMVHQELN---LVLQRSVMDNMWLGRYPT----KGVFVDQEKMYLDTKAIFDELDIDI-DPKARVGTLSVSQMQMIEI 160
Cdd:COG3845 334 GVAYIPEDRLgrgLVPDMSVAENLILGRYRRppfsRGGFLDRKAIRAFAEELIEEFDVRTpGPDTPARSLSGGNQQKVIL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 161 AKAFSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQSLEGLDMDK 240
Cdd:COG3845 414 ARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEATREE 493
|
....*..
gi 495051738 241 IIAMMVG 247
Cdd:COG3845 494 IGLLMAG 500
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
261-484 |
2.35e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 112.88 E-value: 2.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 261 PGEVILEVRNLT-SL-RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSA------ 332
Cdd:COG1121 2 MMMPAIELENLTvSYgGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRrigyvp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 333 -NEAINNGFALVTEERRSTGIYayldigfnslisnirnykSKIGLLDNSRmKSDTQWVIDSM-RVKTPGHR-TQIGSLSG 409
Cdd:COG1121 82 qRAEVDWDFPITVRDVVLMGRY------------------GRRGLFRRPS-RADREAVDEALeRVGLEDLAdRPIGELSG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495051738 410 GNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:COG1121 143 GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
266-482 |
8.68e-28 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 110.92 E-value: 8.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 266 LEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSAneAINNGFALV 343
Cdd:COG1131 1 IEVRGLTKRygDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPA--EVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 344 TEErrsTGIYAYLdigfnSLISNIRNYKSKIGLlDNSRMKSDTQWVIDSMRVKTPGHRtQIGSLSGGNQQKVIIGRWLLT 423
Cdd:COG1131 79 PQE---PALYPDL-----TVRENLRFFARLYGL-PRKEARERIDELLELFGLTDAADR-KVGTLSGGMKQRLGLALALLH 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495051738 424 QPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKG 207
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
14-226 |
8.99e-28 |
|
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: 110.31 E-value: 8.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAK-EALENGISM 92
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNiNELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 93 VHQELNLVLQRSVMDNMWLGRYPTKGVFVDQ---------EKMYLDTKAifdeldididpKARVGTLSVSQMQMIEIAKA 163
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKGMSKAEaeeralellEKVGLADKA-----------DAYPAQLSGGQQQRVAIARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495051738 164 FSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 226
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
267-484 |
1.39e-27 |
|
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: 109.93 E-value: 1.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 267 EVRNLT-SL-RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSA-------NEAIN 337
Cdd:cd03235 1 EVEDLTvSYgGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKrigyvpqRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 338 NGFALVTEERRSTGIYayldigfnslisnirnykSKIGLLDNSRmKSDTQWVIDSM-RVKTPGHRT-QIGSLSGGNQQKV 415
Cdd:cd03235 81 RDFPISVRDVVLMGLY------------------GHKGLFRRLS-KADKAKVDEALeRVGLSELADrQIGELSGGQQQRV 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495051738 416 IIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
266-484 |
1.95e-27 |
|
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: 108.25 E-value: 1.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 266 LEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSanEAINNGFALV 343
Cdd:cd03230 1 IEVRNLSKRygKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP--EEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 344 TEErrsTGIYAYLdigfnSLISNIRnykskiglldnsrmksdtqwvidsmrvktpghrtqigsLSGGNQQKVIIGRWLLT 423
Cdd:cd03230 79 PEE---PSLYENL-----TVRENLK--------------------------------------LSGGMKQRLALAQALLH 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495051738 424 QPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:cd03230 113 DPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
14-226 |
1.37e-26 |
|
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: 107.27 E-value: 1.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIY-----QKDSGSILFQGKEI-DFHSAKEALE 87
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIyDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 88 NGISMVHQELNLvLQRSVMDNM----WLGRYPTKGVFVDQEKMYLDTKAIFDELdidiDPKARVGTLSVSQMQMIEIAKA 163
Cdd:cd03260 81 RRVGMVFQKPNP-FPGSIYDNVayglRLHGIKLKEELDERVEEALRKAALWDEV----KDRLHALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495051738 164 FSYDAKIVIMDEPTSSL----TEK-EvnhlfKIIRKLKERgCGIVYISHKMEEIFQLCDEITILRDGQ 226
Cdd:cd03260 156 LANEPEVLLLDEPTSALdpisTAKiE-----ELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGR 217
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
263-482 |
3.75e-26 |
|
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: 106.60 E-value: 3.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 263 EVILEVRNLTSLRQPS--IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANEAINNGF 340
Cdd:COG0410 1 MPMLEVENLHAGYGGIhvLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 341 ALVTEERRstgIYAYLdigfnSLISNIRnykskIGLLdNSRMKSDTQWVIDSM-----RVKTpgHRTQI-GSLSGGNQQK 414
Cdd:COG0410 81 GYVPEGRR---IFPSL-----TVEENLL-----LGAY-ARRDRAEVRADLERVyelfpRLKE--RRRQRaGTLSGGEQQM 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495051738 415 VIIGRWLLTQPEILMLDEPTRG-----IDvgakfEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:COG0410 145 LAIGRALMSRPKLLLLDEPSLGlapliVE-----EIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERG 212
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-229 |
1.34e-25 |
|
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: 104.59 E-value: 1.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPG--VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEaLENGIS 91
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD-LRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 92 MVHQELNLVLQrSVMDNMWLGRYPTKgvfvDQEKMYLDTKAIFDELdIDIDPKA---RVG----TLSVSQMQMIEIAKAF 164
Cdd:cd03245 82 YVPQDVTLFYG-TLRDNITLGAPLAD----DERILRAAELAGVTDF-VNKHPNGldlQIGergrGLSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495051738 165 SYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLKeRGCGIVYISHKMeEIFQLCDEITILRDGQWIA 229
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRP-SLLDLVDRIIVMDSGRIVA 218
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
14-226 |
2.60e-25 |
|
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: 103.49 E-value: 2.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKealENGISMV 93
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK---DRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 94 HQELNLVLQRSVMDNMwlgRYPTKGVFVDQEKMYLDTKAIFDELDID--IDPKARvgTLSVSQMQMIEIAKAFSYDAKIV 171
Cdd:cd03301 78 FQNYALYPHMTVYDNI---AFGLKLRKVPKDEIDERVREVAELLQIEhlLDRKPK--QLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495051738 172 IMDEPTSSLTEK-EVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 226
Cdd:cd03301 153 LMDEPLSNLDAKlRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQ 208
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
18-226 |
2.99e-25 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 103.11 E-value: 2.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 18 NINKSFP-GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfhSAKEALENgISMVHQE 96
Cdd:cd03226 4 NISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKS-IGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 97 LNLVLQR-SVMDNMWLGRYPTKGVFVDQEKmyldtkaIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSYDAKIVIMDE 175
Cdd:cd03226 80 VDYQLFTdSVREELLLGLKELDAGNEQAET-------VLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495051738 176 PTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 226
Cdd:cd03226 153 PTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGA 203
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
13-482 |
4.20e-25 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 109.17 E-value: 4.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSF----PGVKALDNVNLKVRPHSIHALMGENGAGKS-TLLKCLFGIYQK----DSGSILFQGKE---IDFH 80
Cdd:PRK10261 12 VLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAgglvQCDKMLLRRRSrqvIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 81 SAKEALENG-----ISMVHQE----LNLV------LQRSVMDNMWLGRyptkgvfvdqEKMYLDTKAIFDELDIdidPKA 145
Cdd:PRK10261 92 EQSAAQMRHvrgadMAMIFQEpmtsLNPVftvgeqIAESIRLHQGASR----------EEAMVEAKRMLDQVRI---PEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 146 RV------GTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKL-KERGCGIVYISHKMEEIFQLCDE 218
Cdd:PRK10261 159 QTilsrypHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAEIADR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 219 ITILRDGQWIATQSLEG-------------LDMDKIIAMMVGRSLNQRFP-------DRENK--------PGEVILEVRN 270
Cdd:PRK10261 239 VLVMYQGEAVETGSVEQifhapqhpytralLAAVPQLGAMKGLDYPRRFPlislehpAKQEPpieqdtvvDGEPILQVRN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 271 LTSlRQP--------------SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSAN--E 334
Cdd:PRK10261 319 LVT-RFPlrsgllnrvtrevhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 335 AINNGFALVTEERrstgiYAYLD----IGFnSLISNIRNYkskiGLLDNSRMKSDTQWVIDSMRVKtPGHRTQI-GSLSG 409
Cdd:PRK10261 398 ALRRDIQFIFQDP-----YASLDprqtVGD-SIMEPLRVH----GLLPGKAAAARVAWLLERVGLL-PEHAWRYpHEFSG 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495051738 410 GNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-GKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK10261 467 GQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLG 540
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
14-236 |
8.56e-25 |
|
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: 107.92 E-value: 8.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFP-GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfHSAKEALENGISM 92
Cdd:COG4988 337 IELEDVSFSYPgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLS-DLDPASWRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 93 VHQElNLVLQRSVMDNMWLGRyPTkgvfVDQEKM-------YLDT--KAIFDELDididpkARVG----TLSVSQMQMIE 159
Cdd:COG4988 416 VPQN-PYLFAGTIRENLRLGR-PD----ASDEELeaaleaaGLDEfvAALPDGLD------TPLGeggrGLSGGQAQRLA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 160 IAKAFSYDAKIVIMDEPTSSL---TEKEVnhlFKIIRKLKeRGCGIVYISHKMEEIfQLCDEITILRDGQWIATQSLEGL 236
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLdaeTEAEI---LQALRRLA-KGRTVILITHRLALL-AQADRILVLDDGRIVEQGTHEEL 558
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
19-226 |
9.34e-25 |
|
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: 103.49 E-value: 9.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 19 INKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALE---NGISMVHQ 95
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrKKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 96 ELNLVLQRSVMDNMWLGrYPTKGVfVDQEKMYLDTKAIfDELDIDIDPKARVGTLSVSQMQMIEIAKAFSYDAKIVIMDE 175
Cdd:cd03294 110 SFALLPHRTVLENVAFG-LEVQGV-PRAEREERAAEAL-ELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495051738 176 PTSSL---TEKEV-NHLFKIIRKLKERgcgIVYISHKMEEIFQLCDEITILRDGQ 226
Cdd:cd03294 187 AFSALdplIRREMqDELLRLQAELQKT---IVFITHDLDEALRLGDRIAIMKDGR 238
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
14-236 |
1.29e-24 |
|
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: 101.68 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfhsAKEALE--NGIS 91
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV----VREPREvrRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 92 MVHQELNLVLQRSVMDNM-WLGR-YPTKGVFVDQE-KMYLDTKAIFDELDididpkARVGTLSVSQMQMIEIAKAFSYDA 168
Cdd:cd03265 77 IVFQDLSVDDELTGWENLyIHARlYGVPGAERRERiDELLDFVGLLEAAD------RLVKTYSGGMRRRLEIARSLVHRP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495051738 169 KIVIMDEPTSSLTEKEVNHLFKIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWIATQSLEGL 236
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
267-482 |
6.44e-24 |
|
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: 99.46 E-value: 6.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 267 EVRNLT----SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANEAINN-GFA 341
Cdd:cd03225 1 ELKNLSfsypDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKvGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 342 L-----------VTEErrstgiyayldigfnsLISNIRNYKskiglLDNSRMKSDTQWVIDSMRVKTPGHRtQIGSLSGG 410
Cdd:cd03225 81 FqnpddqffgptVEEE----------------VAFGLENLG-----LPEEEIEERVEEALELVGLEGLRDR-SPFTLSGG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495051738 411 NQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:cd03225 139 QKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
8-225 |
1.03e-23 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 100.16 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 8 SSGEYLLEMTNINKSFP----GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAK 83
Cdd:COG1116 2 SAAAPALELRGVSKRFPtgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 84 ealengISMVHQELNLVLQRSVMDNMWLGRyPTKGVFVDQekmyldTKAIFDELdIDidpkaRVG----------TLSVS 153
Cdd:COG1116 82 ------RGVVFQEPALLPWLTVLDNVALGL-ELRGVPKAE------RRERAREL-LE-----LVGlagfedayphQLSGG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495051738 154 QMQMIEIAKAFSYDAKIVIMDEPTSSL---TEKEVNHLfkIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDG 225
Cdd:COG1116 143 MRQRVAIARALANDPEVLLMDEPFGALdalTRERLQDE--LLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
266-482 |
1.06e-23 |
|
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: 98.03 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 266 LEVRNLTSLR--QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANeainngfalV 343
Cdd:cd03229 1 LELKNVSKRYgqKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDE---------L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 344 TEERRSTGiYAYLDIGFNSLISNIRNykskIGLLdnsrmksdtqwvidsmrvktpghrtqigsLSGGNQQKVIIGRWLLT 423
Cdd:cd03229 72 PPLRRRIG-MVFQDFALFPHLTVLEN----IALG-----------------------------LSGGQQQRVALARALAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 424 QPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKGKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLqAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
14-234 |
2.03e-23 |
|
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: 98.73 E-value: 2.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKE--ALENGIS 91
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 92 MVHQELNLVLQRSVMDNMwlgRYPTKGVFVDQEKMYLD-TKAIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSYDAKI 170
Cdd:cd03261 81 MLFQSGALFDSLTVFENV---AFPLREHTRLSEEEIREiVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495051738 171 VIMDEPTSSL---TEKEVNHLfkiIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWIATQSLE 234
Cdd:cd03261 158 LLYDEPTAGLdpiASGVIDDL---IRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPE 222
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
266-486 |
2.04e-23 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 96.73 E-value: 2.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 266 LEVRNLTSlRQPSI---RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANEAINNGFAL 342
Cdd:cd03216 1 LELRGITK-RFGGVkalDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 343 VTEerrstgiyayldigfnslisnirnykskiglldnsrmksdtqwvidsmrvktpghrtqigsLSGGNQQKVIIGRWLL 422
Cdd:cd03216 80 VYQ-------------------------------------------------------------LSVGERQMVEIARALA 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495051738 423 TQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNGLVSG 486
Cdd:cd03216 99 RNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVG 162
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
14-226 |
2.07e-23 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 100.92 E-value: 2.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPG----VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKE--ALE 87
Cdd:COG1135 2 IELENLSKTFPTkggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElrAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 88 NGISMVHQELNLVLQRSVMDNMwlgRYPTKGVFVDQEkmylDTKAIFDEL-D-IDIDPKARV--GTLSVSQMQMIEIAKA 163
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENV---ALPLEIAGVPKA----EIRKRVAELlElVGLSDKADAypSQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495051738 164 FSYDAKIVIMDEPTSSL---TEKEVNHLFKIIRklKERGCGIVYISHKMEEIFQLCDEITILRDGQ 226
Cdd:COG1135 155 LANNPKVLLCDEATSALdpeTTRSILDLLKDIN--RELGLTIVLITHEMDVVRRICDRVAVLENGR 218
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
265-482 |
2.41e-23 |
|
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: 98.35 E-value: 2.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 265 ILEVRNLT------SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANEAinn 338
Cdd:cd03257 1 LLEVKNLSvsfptgGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 339 gfalvtEERRStgiyaylDIG------FNSLisnirnykskiglldNSRMKSDTQwVIDSMRVKTPGHRTQI-------- 404
Cdd:cd03257 78 ------KIRRK-------EIQmvfqdpMSSL---------------NPRMTIGEQ-IAEPLRIHGKLSKKEArkeavlll 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 405 ---------------GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-GKGIIIISSEMPE 468
Cdd:cd03257 129 lvgvglpeevlnrypHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGV 208
|
250
....*....|....
gi 495051738 469 LLGITDRILVMSNG 482
Cdd:cd03257 209 VAKIADRVAVMYAG 222
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
266-482 |
2.46e-23 |
|
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: 98.66 E-value: 2.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 266 LEVRNLT----SLRqpSIRDVSFDLHKGEILGIAGLVGAKRTdiveTLF----GIREKSGGTISLHGKKINNHSANEAIN 337
Cdd:cd03219 1 LEVRGLTkrfgGLV--ALDDVSFSVRPGEIHGLIGPNGAGKT----TLFnlisGFLRPTSGSVLFDGEDITGLPPHEIAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 338 NGFAlvteerRS---TGIYAYLDIGFNSLISNIRNYKSKIGLLDNSRMKSDTQ----WVIDsmRVKTPGHR-TQIGSLSG 409
Cdd:cd03219 75 LGIG------RTfqiPRLFPELTVLENVMVAAQARTGSGLLLARARREEREAReraeELLE--RVGLADLAdRPAGELSY 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495051738 410 GNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:cd03219 147 GQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQG 219
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
279-482 |
2.86e-23 |
|
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: 97.33 E-value: 2.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 279 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNhsaneainngfalvtEERRSTGIYAYLD- 357
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---------------KERRKSIGYVMQDv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 358 ---IGFNSLISNIRnykskIGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIgSLSGGNQQKVIIGRWLLTQPEILMLDEPT 434
Cdd:cd03226 81 dyqLFTDSVREELL-----LGLKELDAGNEQAETVLKDLDLYALKERHPL-SLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495051738 435 RGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:cd03226 155 SGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
267-482 |
3.14e-23 |
|
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: 95.77 E-value: 3.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 267 EVRNLT--SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSaneainngfalvt 344
Cdd:cd00267 1 EIENLSfrYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 345 eerrstgiyayldigfnslisnIRNYKSKIGLldnsrmksdtqwvidsmrvktpghrtqIGSLSGGNQQKVIIGRWLLTQ 424
Cdd:cd00267 68 ----------------------LEELRRRIGY---------------------------VPQLSGGQRQRVALARALLLN 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495051738 425 PEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:cd00267 99 PDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
9-230 |
4.14e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 98.52 E-value: 4.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 9 SGEYLLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALEN 88
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 89 GISMVHQELNLVLQRSVMDNMWL------------GRYPTKGvFVDQEKMYLDTKAIFdeLD-IDIDPKA--RVGTLSVS 153
Cdd:PRK11300 81 GVVRTFQHVRLFREMTVIENLLVaqhqqlktglfsGLLKTPA-FRRAESEALDRAATW--LErVGLLEHAnrQAGNLAYG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495051738 154 QMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLK-ERGCGIVYISHKMEEIFQLCDEITILRDGQWIAT 230
Cdd:PRK11300 158 QQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRnEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLAN 235
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
14-235 |
6.00e-23 |
|
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: 97.41 E-value: 6.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGVKaLDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFHSAKEalenGISM 92
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDItNLPPEKR----DISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 93 VHQELNLVLQRSVMDNMwlgRYPTKGVFVDQEKMYLDTKAIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSYDAKIVI 172
Cdd:cd03299 76 VPQNYALFPHMTVYKNI---AYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495051738 173 MDEPTSSLTEKEVNHLFKIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQSLEG 235
Cdd:cd03299 153 LDEPFSALDVRTKEKLREELKKIrKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEE 216
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
14-222 |
6.86e-23 |
|
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: 96.77 E-value: 6.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPG----VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKealeng 89
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 90 ISMVHQELNLVLQRSVMDNMWLGRyptKGVFVDQEkmylDTKAIFDELdididpKARVG----------TLSVSQMQMIE 159
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGL---ELQGVPKA----EARERAEEL------LELVGlsgfenayphQLSGGMRQRVA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495051738 160 IAKAFSYDAKIVIMDEPTSSLTE--KEV--NHLFKIIRklkERGCGIVYISHKMEEIFQLCDEITIL 222
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDAltREQlqEELLDIWR---ETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
14-229 |
7.78e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 98.72 E-value: 7.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENGIsmV 93
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGV--V 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 94 HQELNLVLQRSVMDNMWL-GRYptKGVFVDQEKMYLDTKAIFDELDIDIDpkARVGTLSVSQMQMIEIAKAFSYDAKIVI 172
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVfGRY--FGLSAAAARALVPPLLEFAKLENKAD--AKVGELSGGMKRRLTLARALVNDPDVLV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495051738 173 MDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIA 229
Cdd:PRK13537 162 LDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIA 218
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
13-207 |
8.14e-23 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 96.01 E-value: 8.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfHSAKEALENGISM 92
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI--RDAREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 93 VHQELNLVLQRSVMDN--MWLGRYptkGVFVDQEkmylDTKAIFDELDID--IDpkARVGTLSVSQMQMIEIAKAFSYDA 168
Cdd:COG4133 80 LGHADGLKPELTVRENlrFWAALY---GLRADRE----AIDEALEAVGLAglAD--LPVRQLSAGQKRRVALARLLLSPA 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 495051738 169 KIVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISH 207
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
15-225 |
8.15e-23 |
|
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: 96.91 E-value: 8.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 15 EMTNINKSF-PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSaKEALENGISMV 93
Cdd:cd03254 4 EFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS-RKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 94 HQElNLVLQRSVMDNMWLGRYPTKgvfvDQEKMYLDTKAIFDEL------DIDIDPKARVGTLSVSQMQMIEIAKAFSYD 167
Cdd:cd03254 83 LQD-TFLFSGTIMENIRLGRPNAT----DEEVIEAAKEAGAHDFimklpnGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495051738 168 AKIVIMDEPTSSL---TEKEVNhlfKIIRKLKERGCGIVyISHKMEEIfQLCDEITILRDG 225
Cdd:cd03254 158 PKILILDEATSNIdteTEKLIQ---EALEKLMKGRTSII-IAHRLSTI-KNADKILVLDDG 213
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
262-501 |
1.03e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 100.87 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 262 GEVILEVRNLTSlRQPSIR---DVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANEAINN 338
Cdd:COG3845 2 MPPALELRGITK-RFGGVVandDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 339 G-------FAL-----VTEerrstgiyayldigfnslisNIR--NYKSKIGLLDNSRMKSDTQWVIDSMRVKTPGHRTqI 404
Cdd:COG3845 81 GigmvhqhFMLvpnltVAE--------------------NIVlgLEPTKGGRLDRKAARARIRELSERYGLDVDPDAK-V 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 405 GSLSGGNQQKVIIGRWLLTQPEILMLDEPT-----RGIDvgakfEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVM 479
Cdd:COG3845 140 EDLSVGEQQRVEILKALYRGARILILDEPTavltpQEAD-----ELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVL 214
|
250 260
....*....|....*....|..
gi 495051738 480 SNGLVSGIVDTKTTTQNEILRL 501
Cdd:COG3845 215 RRGKVVGTVDTAETSEEELAEL 236
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
14-229 |
1.15e-22 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 96.46 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFHSAKEAlENGISM 92
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDItKLPMHKRA-RLGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 93 VHQELNLVLQRSVMDNMWL---GRYPTKgvfvdQEKMYLdTKAIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSYDAK 169
Cdd:cd03218 80 LPQEASIFRKLTVEENILAvleIRGLSK-----KEREEK-LEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 170 IVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIA 229
Cdd:cd03218 154 FLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLA 213
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
14-226 |
1.21e-22 |
|
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: 96.64 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfhSAKEALENGISMV 93
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA---TDVPVQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 94 HQELNLVLQRSVMDNMWLG-RYPTKGVFVDQEKMYLDTKAIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSYDAKIVI 172
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGlRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495051738 173 MDEPTSSLTEKEVNHLFKIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQ 226
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGR 214
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
14-225 |
1.90e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 99.15 E-value: 1.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENgISMV 93
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR-VASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 94 HQELNLVLQRSVMDNMWLGRYPTKGVFVDQEKMylDTKAI---FDELDIDIDPKARVGTLSVSQMQMIEIAKAFSYDAKI 170
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMGRTPHRSRFDTWTET--DRAAVeraMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495051738 171 VIMDEPTSSLtekEVNH---LFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDG 225
Cdd:PRK09536 161 LLLDEPTASL---DINHqvrTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADG 215
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
9-237 |
2.36e-22 |
|
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: 95.82 E-value: 2.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 9 SGEYLLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKE--AL 86
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 87 ENGISMVHQE------LnlvlqrSVMDNMwlgryptkgVFVDQEKMYLDTKAIFD---------ELDIDID--P------ 143
Cdd:COG1127 81 RRRIGMLFQGgalfdsL------TVFENV---------AFPLREHTDLSEAEIRElvleklelvGLPGAADkmPselsgg 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 144 -KARVGtlsvsqmqmieIAKAFSYDAKIVIMDEPTSSL---TEKEVNHLfkiIRKLKER-GCGIVYISHKMEEIFQLCDE 218
Cdd:COG1127 146 mRKRVA-----------LARALALDPEILLYDEPTAGLdpiTSAVIDEL---IRELRDElGLTSVVVTHDLDSAFAIADR 211
|
250
....*....|....*....
gi 495051738 219 ITILRDGQWIATQSLEGLD 237
Cdd:COG1127 212 VAVLADGKIIAEGTPEELL 230
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
14-222 |
2.48e-22 |
|
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: 100.05 E-value: 2.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGV-KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKeALENGISM 92
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAD-SWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 93 VHQeLNLVLQRSVMDNMWLGRYPTKGVFVDQ--EKMYLD--TKAIFDELDIDIDPKARvgTLSVSQMQMIEIAKAFSYDA 168
Cdd:TIGR02857 401 VPQ-HPFLFAGTIAENIRLARPDASDAEIREalERAGLDefVAALPQGLDTPIGEGGA--GLSGGQAQRLALARAFLRDA 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495051738 169 KIVIMDEPTSSL---TEKEVNhlfKIIRKLKERGCGIVyISHKmEEIFQLCDEITIL 222
Cdd:TIGR02857 478 PLLLLDEPTAHLdaeTEAEVL---EALRALAQGRTVLL-VTHR-LALAALADRIVVL 529
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
15-226 |
4.15e-22 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 97.18 E-value: 4.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 15 EMTNINKSFPG----VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKE--ALEN 88
Cdd:PRK11153 3 ELKNISKVFPQggrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 89 GISMVHQELNLVLQRSVMDNMWLgryPTKGVFVDQEKMyldtKAIFDELdididpKARVG----------TLSVSQMQMI 158
Cdd:PRK11153 83 QIGMIFQHFNLLSSRTVFDNVAL---PLELAGTPKAEI----KARVTEL------LELVGlsdkadrypaQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495051738 159 EIAKAFSYDAKIVIMDEPTSSL---TEKEVNHLFKII-RKLkerGCGIVYISHKMEEIFQLCDEITILRDGQ 226
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALdpaTTRSILELLKDInREL---GLTIVLITHEMDVVKRICDRVAVIDAGR 218
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
13-226 |
5.87e-22 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 97.09 E-value: 5.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfhSAKEALENGISM 92
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV---TGLPPEKRNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 93 VHQELNLVLQRSVMDNMwlgRYPTKGVFVDQEkmylDTKAIFDE-LD-IDIDPKA--RVGTLSVSQMQMIEIAKAFSYDA 168
Cdd:COG3842 82 VFQDYALFPHLTVAENV---AFGLRMRGVPKA----EIRARVAElLElVGLEGLAdrYPHQLSGGQQQRVALARALAPEP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495051738 169 KIVIMDEPTSSL-------TEKEvnhLFKIIRKLkergcGI--VYISHKMEEIFQLCDEITILRDGQ 226
Cdd:COG3842 155 RVLLLDEPLSALdaklreeMREE---LRRLQREL-----GItfIYVTHDQEEALALADRIAVMNDGR 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
263-484 |
6.45e-22 |
|
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: 98.82 E-value: 6.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 263 EVILEVRNLT----SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSG---GTISLHGKKINNHSANEa 335
Cdd:COG1123 2 TPLLEVRDLSvrypGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEAL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 336 INNGFALVTEERRS--TGIYAYLDIGFNslisnIRNykskiGLLDNSRMKSDTQWVIDSMRVKTPGHRtQIGSLSGGNQQ 413
Cdd:COG1123 81 RGRRIGMVFQDPMTqlNPVTVGDQIAEA-----LEN-----LGLSRAEARARVLELLEAVGLERRLDR-YPHQLSGGQRQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495051738 414 KVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-GKGIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:COG1123 150 RVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRI 221
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
13-229 |
8.74e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 94.19 E-value: 8.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENGISM 92
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 93 VHQELNLVLQRSVMDNMWLGRYPTKGVFVDQEKMYLDtkAIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSYDAKIVI 172
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRAN--ELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495051738 173 MDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIA 229
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIA 217
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
267-482 |
1.00e-21 |
|
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: 92.11 E-value: 1.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 267 EVRNLT-SLRQ-PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANEainngFAlvt 344
Cdd:cd03214 1 EVENLSvGYGGrTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKE-----LA--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 345 eerrstgiyayldigfnslisnirnykSKIGLLdnsrmksdTQwVIDSMRVKTPGHRtQIGSLSGGNQQKVIIGRWLLTQ 424
Cdd:cd03214 73 ---------------------------RKIAYV--------PQ-ALELLGLAHLADR-PFNELSGGERQRVLLARALAQE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495051738 425 PEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPEL-LGITDRILVMSNG 482
Cdd:cd03214 116 PPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLaARYADRVILLKDG 174
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
265-482 |
1.17e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 94.29 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 265 ILEVRNLtSLR---QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANEAINNG-- 339
Cdd:PRK11300 5 LLSVSGL-MMRfggLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGvv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 340 --FALVTEERRSTGIYayldigfNSLISNIRNYKSKI--GLL--------DNSRMKSDTQWvIDSMRVKTPGHRtQIGSL 407
Cdd:PRK11300 84 rtFQHVRLFREMTVIE-------NLLVAQHQQLKTGLfsGLLktpafrraESEALDRAATW-LERVGLLEHANR-QAGNL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495051738 408 SGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-GKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK11300 155 AYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
13-226 |
1.20e-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: 93.65 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFP-----GVK--ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILF--QGKEIDFHSAK 83
Cdd:COG4778 4 LLEVENLSKTFTlhlqgGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 84 E----AL-ENGISMVHQELNLVlqrsvmdnmwlGRYPTKGVF--------VDQEKMYLDTKAIFDELDI-----DIDPka 145
Cdd:COG4778 84 PreilALrRRTIGYVSQFLRVI-----------PRVSALDVVaepllergVDREEARARARELLARLNLperlwDLPP-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 146 rvGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSL--TEKEVnhLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILR 223
Cdd:COG4778 151 --ATFSGGEQQRVNIARGFIADPPLLLLDEPTASLdaANRAV--VVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVT 226
|
...
gi 495051738 224 DGQ 226
Cdd:COG4778 227 PFS 229
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
14-226 |
2.16e-21 |
|
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: 92.26 E-value: 2.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGVKALDNVNLKVrPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeIDFHSAKEALENGISMV 93
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDG--QDVLKQPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 94 HQELNLVLQRSVMDNM----WLGRYPTKgvfvdQEKMYLDtkAIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSYDAK 169
Cdd:cd03264 78 PQEFGVYPNFTVREFLdyiaWLKGIPSK-----EVKARVD--EVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495051738 170 IVIMDEPTSSLTEKEVNHLFKIIRKL-KERgcgIVYIS-HKMEEIFQLCDEITILRDGQ 226
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELgEDR---IVILStHIVEDVESLCNQVAVLNKGK 206
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
29-229 |
3.31e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 92.77 E-value: 3.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEaLENGISMVHQEL---------NL 99
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ-LARRLALLPQHHltpegitvrEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 100 V-LQRSVMDNMWlGRYPTKgvfvDQEKMyldTKAIfDELDIDIDPKARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTS 178
Cdd:PRK11231 97 VaYGRSPWLSLW-GRLSAE----DNARV---NQAM-EQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495051738 179 SLtekEVNH---LFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIA 229
Cdd:PRK11231 168 YL---DINHqveLMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMA 218
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
13-482 |
3.58e-21 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 96.68 E-value: 3.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFPG----VKALDNVNLKVRPHSIHALMGENGAGKS----TLLKCLFGIYQKDSGSILFQGKEIdFHSAKE 84
Cdd:COG4172 6 LLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDL-LGLSER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 85 ALE----NGISMVHQE----LN------------LVLQRSVMDNMWLGRyptkgvfvdqekmyldTKAIFDELDIDiDPK 144
Cdd:COG4172 85 ELRrirgNRIAMIFQEpmtsLNplhtigkqiaevLRLHRGLSGAAARAR----------------ALELLERVGIP-DPE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 145 ARVGT----LSVSQMQMIEIAKAFSYDAKIVIMDEPTSSL---TEKEVnhlFKIIRKLK-ERGCGIVYISHKMEEIFQLC 216
Cdd:COG4172 148 RRLDAyphqLSGGQRQRVMIAMALANEPDLLIADEPTTALdvtVQAQI---LDLLKDLQrELGMALLLITHDLGVVRRFA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 217 DEITILRDG---------------QWIATQSLegLDmdkiiammvgrSLNQRFPDRENKPGEVILEVRNLT--------S 273
Cdd:COG4172 225 DRVAVMRQGeiveqgptaelfaapQHPYTRKL--LA-----------AEPRGDPRPVPPDAPPLLEARDLKvwfpikrgL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 274 LRQPS-----IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIrEKSGGTISLHGKKINNHSANEainngfalvteerr 348
Cdd:COG4172 292 FRRTVghvkaVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRA-------------- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 349 stgiyayldigfnslisnIRNYKSKI--------GLLdNSRMkSDTQWVIDSMRVKTPG-----HRTQIGSL-------- 407
Cdd:COG4172 357 ------------------LRPLRRRMqvvfqdpfGSL-SPRM-TVGQIIAEGLRVHGPGlsaaeRRARVAEAleevgldp 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 408 ----------SGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-GKGIIIISSEmpelLG----I 472
Cdd:COG4172 417 aarhryphefSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHD----LAvvraL 492
|
570
....*....|
gi 495051738 473 TDRILVMSNG 482
Cdd:COG4172 493 AHRVMVMKDG 502
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
41-231 |
4.01e-21 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 91.40 E-value: 4.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 41 IHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEidfHSAKEALENGISMVHQELNLVLQRSVMDNMWLGRYPT-KGV 119
Cdd:cd03298 26 ITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVD---VTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGLSPGlKLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 120 FVDQEKMyldtKAIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKL-KER 198
Cdd:cd03298 103 AEDRQAI----EVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhAET 178
|
170 180 190
....*....|....*....|....*....|...
gi 495051738 199 GCGIVYISHKMEEIFQLCDEITILRDGQWIATQ 231
Cdd:cd03298 179 KMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
266-482 |
4.57e-21 |
|
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: 92.01 E-value: 4.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 266 LEVRNLT---SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTdiveTLF----GIREKSGGTISLHGKKINNHSANEAinn 338
Cdd:COG1122 1 IELENLSfsyPGGTPALDDVSLSIEKGEFVAIIGPNGSGKS----TLLrllnGLLKPTSGEVLVDGKDITKKNLREL--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 339 gfalvteeRRSTGI---YA---------YLDIGFnSLisniRNYKskiglLDNSRMKSDTQWVIDsmRVKTPGHRTQ-IG 405
Cdd:COG1122 74 --------RRKVGLvfqNPddqlfaptvEEDVAF-GP----ENLG-----LPREEIRERVEEALE--LVGLEHLADRpPH 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495051738 406 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:COG1122 134 ELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDG 210
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
14-501 |
4.93e-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: 96.02 E-value: 4.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGI--YQKDSGSIL-------------------- 71
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 72 --------FQGKEIDFHSAKEALENGIS-----MVHQELNLVLQRSVMDNMwLGRYPTKGvFVDQEKMYLDTKAI-FDEL 137
Cdd:TIGR03269 81 pcpvcggtLEPEEVDFWNLSDKLRRRIRkriaiMLQRTFALYGDDTVLDNV-LEALEEIG-YEGKEAVGRAVDLIeMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 138 DIDIDPKARvgTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKL-KERGCGIVYISHKMEEIFQLC 216
Cdd:TIGR03269 159 SHRITHIAR--DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEVIEDLS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 217 DEITILRDGQWIAtqslEGLDMDKIIAMMVGRSLNQRFpdRENKPGEVILEVRNLT----SLRQPSIR---DVSFDLHKG 289
Cdd:TIGR03269 237 DKAIWLENGEIKE----EGTPDEVVAVFMEGVSEVEKE--CEVEVGEPIIKVRNVSkryiSVDRGVVKavdNVSLEVKEG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 290 EILGIAGLVGAKRTDIVETLFGIREKSGGtislhgkKINNHSANEAIN---NGFALVTEERRSTGI-------YAYLDIg 359
Cdd:TIGR03269 311 EIFGIVGTSGAGKTTLSKIIAGVLEPTSG-------EVNVRVGDEWVDmtkPGPDGRGRAKRYIGIlhqeydlYPHRTV- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 360 fnslisnIRNYKSKIGL---LDNSRMKSdtqwVIdsmRVKTPGHRTQIG---------SLSGGNQQKVIIGRWLLTQPEI 427
Cdd:TIGR03269 383 -------LDNLTEAIGLelpDELARMKA----VI---TLKMVGFDEEKAeeildkypdELSEGERHRVALAQVLIKEPRI 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495051738 428 LMLDEPTRGIDVGAKFEIYQLIAELAKK-GKGIIIISSEMPELLGITDRILVMSNGLVSGIVDTKtttqnEILRL 501
Cdd:TIGR03269 449 VILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPE-----EIVEE 518
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
24-226 |
5.07e-21 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 96.39 E-value: 5.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 24 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfHSAKEALENGISMVHQElNLVLQR 103
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIR-DLTLESLRRQIGVVPQD-TFLFSG 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 104 SVMDNMWLGRyPTkgvfVDQEKMY------------------LDTkaifdeldididpkaRVG----TLSVSQMQMIEIA 161
Cdd:COG1132 429 TIRENIRYGR-PD----ATDEEVEeaakaaqahefiealpdgYDT---------------VVGergvNLSGGQRQRIAIA 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495051738 162 KAFSYDAKIVIMDEPTSSL---TEKEVnhlFKIIRKLKeRGCGIVYISHKMEEIfQLCDEITILRDGQ 226
Cdd:COG1132 489 RALLKDPPILILDEATSALdteTEALI---QEALERLM-KGRTTIVIAHRLSTI-RNADRILVLDDGR 551
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
13-226 |
6.68e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 91.48 E-value: 6.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENGISM 92
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 93 VHQELNLVLQRSVMDNMWLGryptkGVFVDQEKMYLDTKAIFDELDIDIDPKA-RVGTLSVSQMQMIEIAKAFSYDAKIV 171
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMG-----GFFAERDQFQERIKWVYELFPRLHERRIqRAGTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495051738 172 IMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 226
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGH 214
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
265-484 |
1.00e-20 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 90.50 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 265 ILEVRNLT------SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGkkINNHSANEAINN 338
Cdd:cd03266 1 MITADALTkrfrdvKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPAEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 339 GFALVTEerrSTGIYAYLdigfnSLISNIRNYKSKIGLlDNSRMKSDTQWVIDSMRVKTPGHRtQIGSLSGGNQQKVIIG 418
Cdd:cd03266 79 RLGFVSD---STGLYDRL-----TARENLEYFAGLYGL-KGDELTARLEELADRLGMEELLDR-RVGGFSTGMRQKVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495051738 419 RWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:cd03266 149 RALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
14-226 |
1.11e-20 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 93.21 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfhSAKEALENGISMV 93
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV---TDLPPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 94 HQelNLVL--QRSVMDNMwlgRYPTKgvfvdQEKMyldTKAIFDE-----LDI-DIDP--KARVGTLSVSQMQMIEIAKA 163
Cdd:COG3839 81 FQ--SYALypHMTVYENI---AFPLK-----LRKV---PKAEIDRrvreaAELlGLEDllDRKPKQLSGGQRQRVALGRA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495051738 164 FSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQ 226
Cdd:COG3839 148 LVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLhRRLGTTTIYVTHDQVEAMTLADRIAVMNDGR 211
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
13-210 |
1.23e-20 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 90.92 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEAL---ENG 89
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLirqEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 90 isMVHQELNLVLQRSVMDNMWLGRYPTKGVfvdqekmyldTKAIFDELDIDIdpKARVG----------TLSVSQMQMIE 159
Cdd:PRK09493 81 --MVFQQFYLFPHLTALENVMFGPLRVRGA----------SKEEAEKQAREL--LAKVGlaerahhypsELSGGQQQRVA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495051738 160 IAKAFSYDAKIVIMDEPTSSLtEKEVNH-LFKIIRKLKERGCGIVYISHKME 210
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSAL-DPELRHeVLKVMQDLAEEGMTMVIVTHEIG 197
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
16-484 |
1.24e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 94.75 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 16 MTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfhsakealengISMVHQ 95
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLR------------IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 96 ELNLVLQRSVMDNMWLGRYPTKGVFVDQEKMY---------------------------LDTKA--IFDELDI-DIDPKA 145
Cdd:COG0488 69 EPPLDDDLTVLDTVLDGDAELRALEAELEELEaklaepdedlerlaelqeefealggweAEARAeeILSGLGFpEEDLDR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 146 RVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTssltekevNHL----------FkiirkLKERGCGIVYISH-------- 207
Cdd:COG0488 149 PVSELSGGWRRRVALARALLSEPDLLLLDEPT--------NHLdlesiewleeF-----LKNYPGTVLVVSHdryfldrv 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 208 ----------------------------------KMEEIFQlcDEITILRDgqWI---------ATQS------LEglDM 238
Cdd:COG0488 216 atrileldrgkltlypgnysayleqraerleqeaAAYAKQQ--KKIAKEEE--FIrrfrakarkAKQAqsrikaLE--KL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 239 DKIIAMMVGRSLNQRFPDREnKPGEVILEVRNLtSLR---QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREK 315
Cdd:COG0488 290 EREEPPRRDKTVEIRFPPPE-RLGKKVLELEGL-SKSygdKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEP 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 316 SGGTISLhGKKINnhsaneainngFALVTEERrstgiyAYLDIGfNSLISNIRNYKSK------IGLLdnSRM--KSDTQ 387
Cdd:COG0488 368 DSGTVKL-GETVK-----------IGYFDQHQ------EELDPD-KTVLDELRDGAPGgteqevRGYL--GRFlfSGDDA 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 388 WvidsmrvktpghrTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKfeiyQLIAELAKKGKGIIIISSEMP 467
Cdd:COG0488 427 F-------------KPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETL----EALEEALDDFPGTVLLVSHDR 489
|
570
....*....|....*...
gi 495051738 468 ELL-GITDRILVMSNGLV 484
Cdd:COG0488 490 YFLdRVATRILEFEDGGV 507
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-226 |
2.16e-20 |
|
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: 89.66 E-value: 2.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 27 KALDNVNLKVR---PHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG-------KEIDFHSAKEalenGISMVHQE 96
Cdd:cd03297 8 KRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKINLPPQQR----KIGLVFQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 97 LNLVLQRSVMDNMWLGrYPTKGVFVDQEKMyldtKAIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEP 176
Cdd:cd03297 84 YALFPHLNVRENLAFG-LKRKRNREDRISV----DELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495051738 177 TSSLTEKEVNHLFKIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQ 226
Cdd:cd03297 159 FSALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
7-252 |
2.51e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 93.91 E-value: 2.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 7 QSSGEYLLEMTNInkSFPGVkalDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEAL 86
Cdd:PRK10762 251 KAPGEVRLKVDNL--SGPGV---NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 87 ENGISMVHQELN---LVLQRSVMDNMWLG--RYPTKGVFV---DQEKMYLDTkaiFDELdIDIDPKAR---VGTLSVSQM 155
Cdd:PRK10762 326 ANGIVYISEDRKrdgLVLGMSVKENMSLTalRYFSRAGGSlkhADEQQAVSD---FIRL-FNIKTPSMeqaIGLLSGGNQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 156 QMIEIAKAFSYDAKIVIMDEPTSSL---TEKEVnhlFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQS 232
Cdd:PRK10762 402 QKVAIARGLMTRPKVLILDEPTRGVdvgAKKEI---YQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFT 478
|
250 260
....*....|....*....|
gi 495051738 233 LEGLDMDKIIAMMVGRSLNQ 252
Cdd:PRK10762 479 REQATQEKLMAAAVGKLNRV 498
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
266-482 |
3.61e-20 |
|
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: 88.88 E-value: 3.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 266 LEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTIslhgkKINNHSANEAINNGFALV 343
Cdd:cd03269 1 LEVENVTKRfgRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEV-----LFDGKPLDIAARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 344 TEERrstGIYAYLDIGFNSL-ISNIRNYKskiglldnsrmKSDTQWVIDSM--RVKTPGHRTQ-IGSLSGGNQQKVIIGR 419
Cdd:cd03269 76 PEER---GLYPKMKVIDQLVyLAQLKGLK-----------KEEARRRIDEWleRLELSEYANKrVEELSKGNQQKVQFIA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495051738 420 WLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:cd03269 142 AVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
266-482 |
7.16e-20 |
|
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: 88.33 E-value: 7.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 266 LEVRNLT----SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHsaneainngfa 341
Cdd:cd03263 1 LQIRNLTktykKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTD----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 342 lVTEERRSTGIYAYLDIGFNSL--ISNIRNYkSKIGLLDNSRMKSDTQWVIDSMRVkTPGHRTQIGSLSGGNQQKVIIGR 419
Cdd:cd03263 70 -RKAARQSLGYCPQFDALFDELtvREHLRFY-ARLKGLPKSEIKEEVELLLRVLGL-TDKANKRARTLSGGMKRKLSLAI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495051738 420 WLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKGKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:cd03263 147 ALIGGPSVLLLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDG 208
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-230 |
7.67e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 88.82 E-value: 7.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKC---LFGIYQKD--SGSILFQGKEIdFHSAKEALEN 88
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYPEArvSGEVYLDGQDI-FKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 89 GISMVHQELNLVLQRSVMDNMWLGRYPTKGVFVDQE-----KMYLDTKAIFDELDIDIDPKArvGTLSVSQMQMIEIAKA 163
Cdd:PRK14247 83 RVQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKElqervRWALEKAQLWDEVKDRLDAPA--GKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495051738 164 FSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLKeRGCGIVYISHKMEEIFQLCDEITILRDGQWIAT 230
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELK-KDMTIVLVTHFPQQAARISDYVAFLYKGQIVEW 226
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
14-229 |
8.43e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 90.66 E-value: 8.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfhSAKEALENGISMV 93
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP--ARARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 94 HQELNLVLQRSVMDNMWL-GRYptKGVFVDQEKMYLDTKAIFDELDIDIDpkARVGTLSVSQMQMIEIAKAFSYDAKIVI 172
Cdd:PRK13536 120 PQFDNLDLEFTVRENLLVfGRY--FGMSTREIEAVIPSLLEFARLESKAD--ARVSDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495051738 173 MDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIA 229
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIA 252
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
14-225 |
1.12e-19 |
|
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: 88.06 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfhSAKEALENGISMV 93
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI---TNLPPHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 94 HQELNLVLQRSVMDNMwlgRYPTKGVFVDQEKMYLDTKAIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSYDAKIVIM 173
Cdd:cd03300 78 FQNYALFPHLTVFENI---AFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495051738 174 DEPTSSLTEKEVNHLFKIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDG 225
Cdd:cd03300 155 DEPLGALDLKLRKDMQLELKRLqKELGITFVFVTHDQEEALTMSDRIAVMNKG 207
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
31-249 |
2.16e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 90.88 E-value: 2.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 31 NVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENGIsmVH-----QELNLVLQRSV 105
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGL--VYlpedrQSSGLYLDAPL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 106 MDNMWLGRYPTKGVFVDQEKmyldTKAIFDE----LDIDI-DPKARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSL 180
Cdd:PRK15439 359 AWNVCALTHNRRGFWIKPAR----ENAVLERyrraLNIKFnHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495051738 181 TEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQwiATQSLEGLDM--DKIIAMMVGRS 249
Cdd:PRK15439 435 DVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGE--ISGALTGAAInvDTIMRLAFGEH 503
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
24-226 |
2.94e-19 |
|
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: 86.90 E-value: 2.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 24 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG---KEIDFHSAKEAlengISMVHQELNLv 100
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdiREVTLDSLRRA----IGVVPQDTVL- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 101 LQRSVMDNMWLGRyptkgVFVDQEKMYLDTKA--IFDEldIDIDPKA---RVG----TLSVSQMQMIEIAKAFSYDAKIV 171
Cdd:cd03253 87 FNDTIGYNIRYGR-----PDATDEEVIEAAKAaqIHDK--IMRFPDGydtIVGerglKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495051738 172 IMDEPTSSL---TEKEVnhlFKIIRKLKERGCGIVyISHKMEEIFQlCDEITILRDGQ 226
Cdd:cd03253 160 LLDEATSALdthTEREI---QAALRDVSKGRTTIV-IAHRLSTIVN-ADKIIVLKDGR 212
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
14-207 |
3.18e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 86.26 E-value: 3.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFP-GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKE--ALENGI 90
Cdd:COG2884 2 IRFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 91 SMVHQELNLVLQRSVMDN----MWLGRYPTKGVF--VDQ--EKMYLDTKAifdeldididpKARVGTLSVSQMQMIEIAK 162
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENvalpLRVTGKSRKEIRrrVREvlDLVGLSDKA-----------KALPHELSGGEQQRVAIAR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495051738 163 AFSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISH 207
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATH 195
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
266-500 |
3.57e-19 |
|
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: 86.40 E-value: 3.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 266 LEVRNLTSLR--QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANEAInngfalv 343
Cdd:cd03261 1 IELRGLTKSFggRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELY------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 344 tEERRSTGI---YAYLdigFNSL--ISNIrnyksKIGLLDNSRMKSDTQWVIDSMRVKTPGHRTQI----GSLSGGNQQK 414
Cdd:cd03261 74 -RLRRRMGMlfqSGAL---FDSLtvFENV-----AFPLREHTRLSEEEIREIVLEKLEAVGLRGAEdlypAELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 415 VIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAK-KGKGIIIISSEMPELLGITDRILVMSNGLV--SGIVDTK 491
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKeLGLTSIMVTHDLDTAFAIADRIAVLYDGKIvaEGTPEEL 224
|
....*....
gi 495051738 492 TTTQNEILR 500
Cdd:cd03261 225 RASDDPLVR 233
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
14-210 |
4.78e-19 |
|
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: 85.54 E-value: 4.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFP-GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFH-SAKEALENGI 90
Cdd:cd03292 1 IEFINVTKTYPnGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsDLRgRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 91 SMVHQELNLVLQRSVMDNMWLgryptkGVFVDQEKMYLDTKAIFDELD-IDIDPKARV--GTLSVSQMQMIEIAKAFSYD 167
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAF------ALEVTGVPPREIRKRVPAALElVGLSHKHRAlpAELSGGEQQRVAIARAIVNS 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495051738 168 AKIVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKME 210
Cdd:cd03292 155 PTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKE 197
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
10-230 |
5.43e-19 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 89.86 E-value: 5.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 10 GEYLLEMTNINKSFPGV-----KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQ-GKEIDFHSAK 83
Cdd:TIGR03269 276 GEPIIKVRNVSKRYISVdrgvvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKP 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 84 EALENG-----ISMVHQELNLVLQRSVMDNMwlgrypTKGVFVDQEKMYLDTKAIF--------DELDIDIDPKArVGTL 150
Cdd:TIGR03269 356 GPDGRGrakryIGILHQEYDLYPHRTVLDNL------TEAIGLELPDELARMKAVItlkmvgfdEEKAEEILDKY-PDEL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 151 SVSQMQMIEIAKAFSYDAKIVIMDEPTSSL---TEKEVNHlfKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQW 227
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMdpiTKVDVTH--SILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
...
gi 495051738 228 IAT 230
Cdd:TIGR03269 507 VKI 509
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
13-229 |
8.91e-19 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 85.91 E-value: 8.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFPGVKALDNVNLKVRPHSiH-ALMGENGAGKSTLLKCLFG-IYQKDSGSILFQGKEIDFHSAKEaLENGI 90
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGE-HwAILGPNGAGKSTLLSLITGdLPPTYGNDVRLFGERRGGEDVWE-LRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 91 SMVHQELNLVLQR--SVMDnMWL-GRYPTKGVFVD-QEKMYLDTKAIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSY 166
Cdd:COG1119 81 GLVSPALQLRFPRdeTVLD-VVLsGFFDSIGLYREpTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495051738 167 DAKIVIMDEPTSSLTEKEVNHLFKIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWIA 229
Cdd:COG1119 160 DPELLILDEPTAGLDLGARELLLALLDKLaAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVA 223
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
29-226 |
1.51e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 88.62 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSaKEALENGISMVHQElNLVLQRSVMDN 108
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS-HSVLRQGVAMVQQD-PVVLADTFLAN 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 109 MWLGRYptkgvfVDQEKMY--LDT-------KAIFDELDididpkARVG----TLSVSQMQMIEIAKAFSYDAKIVIMDE 175
Cdd:PRK10790 435 VTLGRD------ISEEQVWqaLETvqlaelaRSLPDGLY------TPLGeqgnNLSVGQKQLLALARVLVQTPQILILDE 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495051738 176 PTSSL---TEKEVNHLFKIIRKLKErgcgIVYISHKMEEIFQlCDEITILRDGQ 226
Cdd:PRK10790 503 ATANIdsgTEQAIQQALAAVREHTT----LVVIAHRLSTIVE-ADTILVLHRGQ 551
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
265-482 |
1.53e-18 |
|
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: 85.10 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 265 ILEVRNLT-SLRQPSI-RDVSFDLHKGEILGIAGLVGA-KRTdIVETLFGIREKSGGTISLHGKKINNHSANE---AInn 338
Cdd:COG1120 1 MLEAENLSvGYGGRPVlDDVSLSLPPGEVTALLGPNGSgKST-LLRALAGLLKPSSGEVLLDGRDLASLSRRElarRI-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 339 gfALVTEERRST-----------GIYAYLdigfnslisnirnykskiGLLDNSRmKSDTQWVIDSM-RVKTPGHRTQ-IG 405
Cdd:COG1120 78 --AYVPQEPPAPfgltvrelvalGRYPHL------------------GLFGRPS-AEDREAVEEALeRTGLEHLADRpVD 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495051738 406 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPEL-LGITDRILVMSNG 482
Cdd:COG1120 137 ELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLaARYADRLVLLKDG 214
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
14-226 |
1.93e-18 |
|
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: 82.65 E-value: 1.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGVKA--LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfHSAKEALENGIS 91
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIS-QWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 92 MVHQELNLvLQRSVMDNMwlgryptkgvfvdqekmyldtkaifdeldididpkarvgtLSVSQMQMIEIAKAFSYDAKIV 171
Cdd:cd03246 80 YLPQDDEL-FSGSIAENI----------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495051738 172 IMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIfQLCDEITILRDGQ 226
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETL-ASADRILVLEDGR 172
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
24-226 |
2.02e-18 |
|
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: 84.51 E-value: 2.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 24 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEaLENGISMVHQELNLvLQR 103
Cdd:cd03249 14 PDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRW-LRSQIGLVSQEPVL-FDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 104 SVMDNMWLGRYPTKgvfvDQEKMYLDTKAIFDELdIDIDPKA---RVG----TLSVSQMQMIEIAKAFSYDAKIVIMDEP 176
Cdd:cd03249 92 TIAENIRYGKPDAT----DEEVEEAAKKANIHDF-IMSLPDGydtLVGergsQLSGGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495051738 177 TSSL---TEKEVNHlfKIIRKLKERGCgiVYISHKMEEIfQLCDEITILRDGQ 226
Cdd:cd03249 167 TSALdaeSEKLVQE--ALDRAMKGRTT--IVIAHRLSTI-RNADLIAVLQNGQ 214
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
259-504 |
2.12e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 85.04 E-value: 2.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 259 NKPGEVILEVRNL----TSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANE 334
Cdd:PRK13632 1 IKNKSVMIKVENVsfsyPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 335 AINN-GFALVTEERRSTGIYAYLDIGFNslISNIRNYKSKIG-LLDNSRMKSDTQWVIDsmrvKTPGhrtqigSLSGGNQ 412
Cdd:PRK13632 81 IRKKiGIIFQNPDNQFIGATVEDDIAFG--LENKKVPPKKMKdIIDDLAKKVGMEDYLD----KEPQ------NLSGGQK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 413 QKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKG-KGIIIISSEMPELLgITDRILVMSNGLVSGIVDTK 491
Cdd:PRK13632 149 QRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPK 227
|
250
....*....|....
gi 495051738 492 TTTQN-EILRLASL 504
Cdd:PRK13632 228 EILNNkEILEKAKI 241
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
266-482 |
2.35e-18 |
|
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: 83.72 E-value: 2.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 266 LEVRNLTSLR--QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNhsaneainngfalV 343
Cdd:cd03259 1 LELKGLSKTYgsVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG-------------V 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 344 TEERRSTGI-------YAYLdigfnSLISNIRnykskIGLLDNSRMKSDTQ----WVIDSMRVKTPGHRTqIGSLSGGNQ 412
Cdd:cd03259 68 PPERRNIGMvfqdyalFPHL-----TVAENIA-----FGLKLRGVPKAEIRarvrELLELVGLEGLLNRY-PHELSGGQQ 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495051738 413 QKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-GKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:cd03259 137 QRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEG 207
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
11-255 |
2.45e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 85.28 E-value: 2.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 11 EYLLEMTNINKSFP-GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFhSAKEALE-- 87
Cdd:PRK13636 3 DYILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDY-SRKGLMKlr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 88 NGISMVHQEL-NLVLQRSVMDNMWLGRYPTKgvfVDQEKMYLDTKAIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSY 166
Cdd:PRK13636 82 ESVGMVFQDPdNQLFSASVYQDVSFGAVNLK---LPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 167 DAKIVIMDEPTSSLTEKEVNHLFKIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWIatqsLEGLDMDKIIAMM 245
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMqKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI----LQGNPKEVFAEKE 234
|
250
....*....|
gi 495051738 246 VGRSLNQRFP 255
Cdd:PRK13636 235 MLRKVNLRLP 244
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
14-229 |
3.33e-18 |
|
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: 82.36 E-value: 3.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPG--VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfHSAKEALENGIS 91
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV--SDLEKALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 92 MVHQELNLvLQRSVMDNmwLGRyptkgvfvdqekmyldtkaifdeldididpkarvgTLSVSQMQMIEIAKAFSYDAKIV 171
Cdd:cd03247 79 VLNQRPYL-FDTTLRNN--LGR-----------------------------------RFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495051738 172 IMDEPTSSL---TEKEVNHLFkiIRKLKERgcGIVYISHKMEEIFQLcDEITILRDGQWIA 229
Cdd:cd03247 121 LLDEPTVGLdpiTERQLLSLI--FEVLKDK--TLIWITHHLTGIEHM-DKILFLENGKIIM 176
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
14-225 |
4.06e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 83.87 E-value: 4.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEA-------- 85
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGqlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 86 ----LENGISMVHQELNLVLQRSVMDNMWLGRYPTKGVfvdqEKMYLDTKAIFDELDIDIDPKARVG---TLSVSQMQMI 158
Cdd:PRK10619 86 qlrlLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGL----SKQEARERAVKYLAKVGIDERAQGKypvHLSGGQQQRV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495051738 159 EIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDG 225
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQG 228
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
24-226 |
4.96e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 87.47 E-value: 4.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 24 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGK---EIDFHSakeaLENGISMVHQElNLV 100
Cdd:TIGR00958 492 PDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVplvQYDHHY----LHRQVALVGQE-PVL 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 101 LQRSVMDNMWLG--RYPTKGVFVDQEKMYLDTKAIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTS 178
Cdd:TIGR00958 567 FSGSVRENIAYGltDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495051738 179 SLtEKEVNHLFKIIRKLKERgcGIVYISHKMEEIfQLCDEITILRDGQ 226
Cdd:TIGR00958 647 AL-DAECEQLLQESRSRASR--TVLLIAHRLSTV-ERADQILVLKKGS 690
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
278-504 |
7.19e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 83.00 E-value: 7.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 278 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANEAINNGFALVTEERRstgIYAYLD 357
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRR---VFSRMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 358 IGFNSLISNIrnykskigLLDNSRMKSDTQWVIDsMRVKTPGHRTQ-IGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRG 436
Cdd:PRK11614 97 VEENLAMGGF--------FAERDQFQERIKWVYE-LFPRLHERRIQrAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495051738 437 IDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNGLVSgIVDT-KTTTQNEILRLASL 504
Cdd:PRK11614 168 LAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVV-LEDTgDALLANEAVRSAYL 235
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
266-482 |
9.50e-18 |
|
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: 82.38 E-value: 9.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 266 LEVRNLT-SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNhsaneainngfaLVT 344
Cdd:cd03299 1 LKVENLSkDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITN------------LPP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 345 EERRStgIYAYLDigfNSLISNIRNYKS-KIGLLDNSRMKS-DTQWVIDSMRVKTPGH--RTQIGSLSGGNQQKVIIGRW 420
Cdd:cd03299 69 EKRDI--SYVPQN---YALFPHMTVYKNiAYGLKKRKVDKKeIERKVLEIAEMLGIDHllNRKPETLSGGEQQRVAIARA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495051738 421 LLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-GKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:cd03299 144 LVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNG 206
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
232-482 |
9.83e-18 |
|
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: 86.43 E-value: 9.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 232 SLEGLDmdKIIAMMVGRSLNQRFPDRENKPGEVilEVRNLT----SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVE 307
Cdd:COG2274 444 ALERLD--DILDLPPEREEGRSKLSLPRLKGDI--ELENVSfrypGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLK 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 308 TLFGIREKSGGTISLHGKKINNHSANEainngfaLvteeRRSTGIY---AYLdigFN-SLISNIRNYKSKI--------- 374
Cdd:COG2274 520 LLLGLYEPTSGRILIDGIDLRQIDPAS-------L----RRQIGVVlqdVFL---FSgTIRENITLGDPDAtdeeiieaa 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 375 ---GLLDnsrmksdtqwVIDSMrvktP-GHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIY 446
Cdd:COG2274 586 rlaGLHD----------FIEAL----PmGYDTVVGeggsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIIL 651
|
250 260 270
....*....|....*....|....*....|....*.
gi 495051738 447 QLIAELAkKGKGIIIISSEmPELLGITDRILVMSNG 482
Cdd:COG2274 652 ENLRRLL-KGRTVIIIAHR-LSTIRLADRIIVLDKG 685
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
15-245 |
1.87e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 82.35 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 15 EMTNINKSFPGVK--ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEaLENGISM 92
Cdd:PRK13632 9 KVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE-IRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 93 VHQEL-NLVLQRSVMDNMWLGRYPTKgvfVDQEKMyldtKAIFDELD--------IDIDPKarvgTLSVSQMQMIEIAKA 163
Cdd:PRK13632 88 IFQNPdNQFIGATVEDDIAFGLENKK---VPPKKM----KDIIDDLAkkvgmedyLDKEPQ----NLSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 164 FSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLKERGCG-IVYISHKMEEIFqLCDEITILRDGQWIATQS-LEGLDMDKI 241
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKtLISITHDMDEAI-LADKVIVFSEGKLIAQGKpKEILNNKEI 235
|
....
gi 495051738 242 IAMM 245
Cdd:PRK13632 236 LEKA 239
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
29-229 |
1.88e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 82.36 E-value: 1.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHS-AKEALENGISMVHQELNLVLQRSVMD 107
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKrGLLALRQQVATVFQDPEQQIFYTDID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 108 NMWLGRYPTKGVFVDQEKMYLDTK-AIFDELDIDIDPkarVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVN 186
Cdd:PRK13638 97 SDIAFSLRNLGVPEAEITRRVDEAlTLVDAQHFRHQP---IQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495051738 187 HLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIA 229
Cdd:PRK13638 174 QMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILT 216
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
266-484 |
2.06e-17 |
|
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: 79.95 E-value: 2.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 266 LEVRNLT----SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANEAinngfa 341
Cdd:cd03246 1 LEVENVSfrypGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 342 lvteeRRSTGIYAYLDIGFN-SLISNIrnykskiglldnsrmksdtqwvidsmrvktpghrtqigsLSGGNQQKVIIGRW 420
Cdd:cd03246 75 -----GDHVGYLPQDDELFSgSIAENI---------------------------------------LSGGQRQRLGLARA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495051738 421 LLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEmPELLGITDRILVMSNGLV 484
Cdd:cd03246 111 LYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHR-PETLASADRILVLEDGRV 173
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
279-482 |
2.13e-17 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 81.16 E-value: 2.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 279 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGiREKSGGTISlhgkkinnhsaneainnGFALVTEERRSTG----IYA 354
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISG-RVEGGGTTS-----------------GQILFNGQPRKPDqfqkCVA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 355 YLDiGFNSLISN--IRNYKSKIGLLDNSRMKSDTQwviDSMRVKTPGHR----TQIG-----SLSGGNQQKVIIGRWLLT 423
Cdd:cd03234 85 YVR-QDDILLPGltVRETLTYTAILRLPRKSSDAI---RKKRVEDVLLRdlalTRIGgnlvkGISGGERRRVSIAVQLLW 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495051738 424 QPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKgIIIISSEMP--ELLGITDRILVMSNG 482
Cdd:cd03234 161 DPKVLILDEPTSGLDSFTALNLVSTLSQLARRNR-IVILTIHQPrsDLFRLFDRILLLSSG 220
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
14-209 |
3.14e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 81.33 E-value: 3.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDF-------HSAKEAL 86
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTarslsqqKGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 87 ENGISMVHQELNLVLQRSVMDNMWLGRYPTKGvfVDQEKMYLDTKAIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSY 166
Cdd:PRK11264 84 RQHVGFVFQNFNLFPHRTVLENIIEGPVIVKG--EPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495051738 167 DAKIVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKM 209
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEM 204
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
24-226 |
5.57e-17 |
|
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: 79.82 E-value: 5.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 24 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKeALENGISMVHQElNLVLQR 103
Cdd:cd03248 25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK-YLHSKVSLVGQE-PVLFAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 104 SVMDNM--WLGRYPTKGVFVDQEKMYLDTKAIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLT 181
Cdd:cd03248 103 SLQDNIayGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495051738 182 EKEVNHLFKIIRKLKERGCGIVyISHKMEEIfQLCDEITILRDGQ 226
Cdd:cd03248 183 AESEQQVQQALYDWPERRTVLV-IAHRLSTV-ERADQILVLDGGR 225
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
13-230 |
5.74e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 80.89 E-value: 5.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFP-GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFhSAKEALEngis 91
Cdd:PRK13639 1 ILETRDLKYSYPdGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKY-DKKSLLE---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 92 mVHQELNLVLQRSvmDNMWLGryPTkgvfVDQEKMY--LDTKAIFDELDIDI-DPKARVGT----------LSVSQMQMI 158
Cdd:PRK13639 76 -VRKTVGIVFQNP--DDQLFA--PT----VEEDVAFgpLNLGLSKEEVEKRVkEALKAVGMegfenkpphhLSGGQKKRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495051738 159 EIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIAT 230
Cdd:PRK13639 147 AIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKE 218
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
281-487 |
9.28e-17 |
|
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: 78.88 E-value: 9.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 281 DVSFDLhKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINnhSANEAINngfaLVTEERRstgiyayldIGF 360
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLF--DSRKKIN----LPPQQRK---------IGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 361 ----NSLISNIRNYKSKIGLLDNSRMKSDTQWV---IDSMRVKTPGHRtQIGSLSGGNQQKVIIGRWLLTQPEILMLDEP 433
Cdd:cd03297 80 vfqqYALFPHLNVRENLAFGLKRKRNREDRISVdelLDLLGLDHLLNR-YPAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495051738 434 TRGIDVGAKFEIYQLIAELAKKGKG-IIIISSEMPELLGITDRILVMSNGLVSGI 487
Cdd:cd03297 159 FSALDRALRLQLLPELKQIKKNLNIpVIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
261-484 |
9.75e-17 |
|
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: 82.88 E-value: 9.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 261 PGEVILEVRNLT---SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSAnEAIN 337
Cdd:COG4988 332 AGPPSIELEDVSfsyPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDP-ASWR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 338 NGFALVTEErrstgiyAYLdigFN-SLISNIRNYKSKI------------GLLDnsrmksdtqwVIDSMrvktP-GHRTQ 403
Cdd:COG4988 411 RQIAWVPQN-------PYL---FAgTIRENLRLGRPDAsdeeleaaleaaGLDE----------FVAAL----PdGLDTP 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 404 IGS----LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKGKGIIIISSEmPELLGITDRILVM 479
Cdd:COG4988 467 LGEggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHR-LALLAQADRILVL 544
|
....*
gi 495051738 480 SNGLV 484
Cdd:COG4988 545 DDGRI 549
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
266-492 |
1.13e-16 |
|
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: 79.15 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 266 LEVRNLTSLRQPS--IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIRE-----KSGGTISLHGKKINNHSANeainn 338
Cdd:cd03260 1 IELRDLNVYYGDKhaLKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVD----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 339 gfalVTEERRSTGI---YAYLdigFN-SLISNIRnYKSKI-GLLDNSRMKSDTQWVIDSM----RVKTpghRTQIGSLSG 409
Cdd:cd03260 76 ----VLELRRRVGMvfqKPNP---FPgSIYDNVA-YGLRLhGIKLKEELDERVEEALRKAalwdEVKD---RLHALGLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 410 GNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKgKGIIIISSEMPELLGITDRILVMSNGLVSGIVD 489
Cdd:cd03260 145 GQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGP 223
|
...
gi 495051738 490 TKT 492
Cdd:cd03260 224 TEQ 226
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-228 |
1.15e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 81.81 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 4 NNTQSSGEYLLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfhSAK 83
Cdd:PRK11607 10 AKTRKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL---SHV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 84 EALENGISMVHQELNLVLQRSVMDNMWLG----RYPTKGVFVDQEKMYldTKAIFDELdididPKARVGTLSVSQMQMIE 159
Cdd:PRK11607 87 PPYQRPINMMFQSYALFPHMTVEQNIAFGlkqdKLPKAEIASRVNEML--GLVHMQEF-----AKRKPHQLSGGQRQRVA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 160 IAKAFSYDAKIVIMDEPTSSLTEKEVNHL-FKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWI 228
Cdd:PRK11607 160 LARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
266-482 |
1.54e-16 |
|
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: 79.08 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 266 LEVRNLT------SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINN---------- 329
Cdd:COG1124 2 LEVRNLSvsygqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRrrrkafrrrv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 330 --------------HSANEAINNGFALVTEERRSTGIYAYLDigfnslisnirnyksKIGLldnsrmksdtqwvidsmrv 395
Cdd:COG1124 82 qmvfqdpyaslhprHTVDRILAEPLRIHGLPDREERIAELLE---------------QVGL------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 396 kTPGHRTQ-IGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKGKGIIIISSEMPELLGIT 473
Cdd:COG1124 128 -PPSFLDRyPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLC 206
|
....*....
gi 495051738 474 DRILVMSNG 482
Cdd:COG1124 207 DRVAVMQNG 215
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
13-229 |
1.74e-16 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 79.39 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEalengism 92
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWE-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 93 vhqelnLVLQRSVM-------------DNMWLGRYPtkgVFVDQEKmylDTKAIFDELdididpkARVG----------T 149
Cdd:COG4559 73 ------LARRRAVLpqhsslafpftveEVVALGRAP---HGSSAAQ---DRQIVREAL-------ALVGlahlagrsyqT 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 150 LSVSQMQMIEIAKAF-------SYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITIL 222
Cdd:COG4559 134 LSGGEQQRVQLARVLaqlwepvDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLL 213
|
....*..
gi 495051738 223 RDGQWIA 229
Cdd:COG4559 214 HQGRLVA 220
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
266-484 |
1.81e-16 |
|
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: 78.30 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 266 LEVRNLT------SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTdiveTLF----GIREKSGGTISLHGKKINNHSANEa 335
Cdd:cd03255 1 IELKNLSktygggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKS----TLLnilgGLDRPTSGEVRVDGTDISKLSEKE- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 336 inngfaLVTEERRSTG-IY-AYLDIGFNSLISNIRnykskIGLLDNSRMKSDTQWVIDSM--RVKTPGHRTQ-IGSLSGG 410
Cdd:cd03255 76 ------LAAFRRRHIGfVFqSFNLLPDLTALENVE-----LPLLLAGVPKKERRERAEELleRVGLGDRLNHyPSELSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495051738 411 NQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-GKGIIIISSEmPELLGITDRILVMSNGLV 484
Cdd:cd03255 145 QQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
15-226 |
2.10e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 78.97 E-value: 2.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 15 EMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfHSAKEALENGISMVH 94
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVA-TTPSRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 95 QELNLVLQRSVMDNMWLGRYP-TKG-------VFVDQEKMYLDTKAIFDE-LDididpkarvgTLSVSQMQMIEIAKAFS 165
Cdd:COG4604 82 QENHINSRLTVRELVAFGRFPySKGrltaedrEIIDEAIAYLDLEDLADRyLD----------ELSGGQRQRAFIAMVLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495051738 166 YDAKIVIMDEPTSSLTEKEVNHLFKIIRKL-KERGCGIVYISHkmeEI-FQLC--DEITILRDGQ 226
Cdd:COG4604 152 QDTDYVLLDEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLH---DInFASCyaDHIVAMKDGR 213
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
25-236 |
2.37e-16 |
|
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: 78.43 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 25 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEaLENGISMVHQELNLvLQRS 104
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAS-LRRQIGLVSQDVFL-FNDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 105 VMDNMwlgRYPTKGvfVDQEKMYLDTKA-----IFDELDIDIDPK--ARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPT 177
Cdd:cd03251 92 VAENI---AYGRPG--ATREEVEEAARAanaheFIMELPEGYDTVigERGVKLSGGQRQRIAIARALLKDPPILILDEAT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495051738 178 SSL---TEKEVNhlfKIIRKLKERGCGIVyISHKMEEIFQlCDEITILRDGQWIATQSLEGL 236
Cdd:cd03251 167 SALdteSERLVQ---AALERLMKNRTTFV-IAHRLSTIEN-ADRIVVLEDGKIVERGTHEEL 223
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
281-487 |
3.02e-16 |
|
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: 80.16 E-value: 3.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 281 DVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSAneainnGFALVTEERR------STGIYA 354
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRK------GIFLPPEKRRigyvfqEARLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 355 YLdigfnSLISNIR-NYKSKIGLLDNSRMKSDTQWV-IDSMRVKTPGhrtqigSLSGGNQQKVIIGRWLLTQPEILMLDE 432
Cdd:TIGR02142 89 HL-----SVRGNLRyGMKRARPSERRISFERVIELLgIGHLLGRLPG------RLSGGEKQRVAIGRALLSSPRLLLMDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495051738 433 PTRGIDVGAKFEIYQLIAELAKK-GKGIIIISSEMPELLGITDRILVMSNGLVSGI 487
Cdd:TIGR02142 158 PLAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAA 213
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
263-482 |
3.86e-16 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 79.38 E-value: 3.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 263 EVILEVRNLT-SLRQP-----SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSG---GTISLHGKKINN---H 330
Cdd:PRK09473 10 DALLDVKDLRvTFSTPdgdvtAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNlpeK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 331 SANEAINNGFALVTEERRsTGIYAYLDIGfNSLISNIRNYK--SKIGLLDNS-RMksdtqwvIDSmrVKTPGHRTQIG-- 405
Cdd:PRK09473 90 ELNKLRAEQISMIFQDPM-TSLNPYMRVG-EQLMEVLMLHKgmSKAEAFEESvRM-------LDA--VKMPEARKRMKmy 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 406 --SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-GKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK09473 159 phEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAG 238
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
25-226 |
4.09e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 77.22 E-value: 4.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 25 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEA--LENGISMVHQELNLVLQ 102
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVpfLRRQIGMIFQDHHLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 103 RSVMDNMWLgryPTKGVFVDQEKMYLDTKAIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTE 182
Cdd:PRK10908 94 RTVYDNVAI---PLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495051738 183 KEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 226
Cdd:PRK10908 171 ALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
28-226 |
4.30e-16 |
|
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: 77.53 E-value: 4.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 28 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFhSAKEALENGISMVHQElNLVLQRSVMD 107
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLAL-ADPAWLRRQVGVVLQE-NVLFNRSIRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 108 NMWLGRYPTKGVFVDQEKMYLDTKAIFDELDIDIDP--KARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSL-TEKE 184
Cdd:cd03252 95 NIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTivGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALdYESE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495051738 185 VNhlfkIIRKLKE--RGCGIVYISHKMEEIfQLCDEITILRDGQ 226
Cdd:cd03252 175 HA----IMRNMHDicAGRTVIIIAHRLSTV-KNADRIIVMEKGR 213
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
13-225 |
4.59e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 77.82 E-value: 4.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAkealENGIsm 92
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA----ERGV-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 93 VHQELNLVLQRSVMDNMWLGrYPTKGvfVDQEKMYLDTKAIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSYDAKIVI 172
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNVAFG-LQLAG--VEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495051738 173 MDEPTSSL---TEKEVNHLfkIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDG 225
Cdd:PRK11248 152 LDEPFGALdafTREQMQTL--LLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
261-482 |
4.84e-16 |
|
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: 80.97 E-value: 4.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 261 PGEVILEVRNLT----SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSAnEAI 336
Cdd:COG4987 329 PGGPSLELEDVSfrypGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDE-DDL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 337 NNGFALVTEErrstgiyAYLdigFN-SLISNIRnykskIGLLDnsrmKSDTQwVIDSMR-------VKTP--GHRTQIGS 406
Cdd:COG4987 408 RRRIAVVPQR-------PHL---FDtTLRENLR-----LARPD----ATDEE-LWAALErvglgdwLAALpdGLDTWLGE 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 407 ----LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKGKGIIIISSEmPELLGITDRILVMSNG 482
Cdd:COG4987 468 ggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHR-LAGLERMDRILVLEDG 545
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
280-482 |
4.98e-16 |
|
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: 76.80 E-value: 4.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 280 RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANeainngfalVTEERRSTGI------- 352
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKN---------INELRQKVGMvfqqfnl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 353 YAYLDIGFNSLISNI--------------RNYKSKIGLLDnsrmKSDtqwvidsmrvKTPGHrtqigsLSGGNQQKVIIG 418
Cdd:cd03262 88 FPHLTVLENITLAPIkvkgmskaeaeeraLELLEKVGLAD----KAD----------AYPAQ------LSGGQQQRVAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495051738 419 RWLLTQPEILMLDEPTRGID---VGakfEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:cd03262 148 RALAMNPKVMLFDEPTSALDpelVG---EVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
266-482 |
5.33e-16 |
|
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: 75.50 E-value: 5.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 266 LEVRNLT----SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANEAINNgFA 341
Cdd:cd03228 1 IEFKNVSfsypGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 342 LVTEErrstgiyAYLdigFN-SLISNIrnykskiglldnsrmksdtqwvidsmrvktpghrtqigsLSGGNQQKVIIGRW 420
Cdd:cd03228 80 YVPQD-------PFL---FSgTIRENI---------------------------------------LSGGQRQRIAIARA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495051738 421 LLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKGKGIIIISSEMpELLGITDRILVMSNG 482
Cdd:cd03228 111 LLRDPPILILDEATSALDPETEALILEALRALA-KGKTVIVIAHRL-STIRDADRIIVLDDG 170
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
14-210 |
7.19e-16 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 76.98 E-value: 7.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHS---AKE--ALEN 88
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKtpsDKAirELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 89 GISMVHQELNLVLQRSVMDNmwLGRYPTKGVFVDQEKMYLDTKAIFDELDIDidPKARVGTLSVS--QMQMIEIAKAFSY 166
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQN--LIEAPCRVLGLSKDQALARAEKLLERLRLK--PYADRFPLHLSggQQQRVAIARALMM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495051738 167 DAKIVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKME 210
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVE 202
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
18-226 |
9.51e-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: 80.83 E-value: 9.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 18 NINKSFP--GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfhSAKEALENGISMVHQ 95
Cdd:TIGR01257 933 NLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE--TNLDAVRQSLGMCPQ 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 96 ELNLVLQRSVMDNMwLGRYPTKGvfVDQEKMYLDTKAIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSYDAKIVIMDE 175
Cdd:TIGR01257 1011 HNILFHHLTVAEHI-LFYAQLKG--RSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDE 1087
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495051738 176 PTSSLTEKEVNHLFKIIRKLKErGCGIVYISHKMEEIFQLCDEITILRDGQ 226
Cdd:TIGR01257 1088 PTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGR 1137
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
266-482 |
1.15e-15 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 75.62 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 266 LEVRNLTSLR--QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSAneainngfalv 343
Cdd:COG4619 1 LELEGLSFRVggKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPP----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 344 TEERRSTgiyAYL----DIGFNSLISNIRN-YKSKIGLLDNSRMKSDTQwvidsmRVKTPGH--RTQIGSLSGGNQQKVI 416
Cdd:COG4619 70 PEWRRQV---AYVpqepALWGGTVRDNLPFpFQLRERKFDRERALELLE------RLGLPPDilDKPVERLSGGERQRLA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495051738 417 IGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKGKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:COG4619 141 LIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
261-500 |
1.27e-15 |
|
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: 76.17 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 261 PGEVILEVRNLTSLR--QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANEAinn 338
Cdd:COG1127 1 MSEPMIEVRNLTKSFgdRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKEL--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 339 gfalvTEERRSTGI---YAYLdigFNSL--ISNIRnykskIGLLDNSRMKSDTqwvIDSM------RVKTPGHRTQ-IGS 406
Cdd:COG1127 78 -----YELRRRIGMlfqGGAL---FDSLtvFENVA-----FPLREHTDLSEAE---IRELvlekleLVGLPGAADKmPSE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 407 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGID-VGAKfEIYQLIAELAKK-GKGIIIISSEMPELLGITDRILVMSNG-- 482
Cdd:COG1127 142 LSGGMRKRVALARALALDPEILLYDEPTAGLDpITSA-VIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGki 220
|
250
....*....|....*...
gi 495051738 483 LVSGIVDTKTTTQNEILR 500
Cdd:COG1127 221 IAEGTPEELLASDDPWVR 238
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
3-226 |
1.56e-15 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 75.65 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 3 SNNTQSSGEYLLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGK---EIDF 79
Cdd:cd03220 12 TYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvssLLGL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 80 HSAkealengismVHQELnlvlqrSVMDNMWL-GRYptKGVFVDQEKMYLDTKAIFDELDIDIDpkARVGTLSvSQMQM- 157
Cdd:cd03220 92 GGG----------FNPEL------TGRENIYLnGRL--LGLSRKEIDEKIDEIIEFSELGDFID--LPVKTYS-SGMKAr 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495051738 158 IEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 226
Cdd:cd03220 151 LAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGK 219
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
11-243 |
1.69e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 76.70 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 11 EYLLEMTNINKSFP-GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEaLENG 89
Cdd:PRK13647 2 DNIIEVEDLHFRYKdGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKW-VRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 90 ISMVHQEL-NLVLQRSVMDNMWLGrypTKGVFVDQEKMYLDTKAIFDELDI-DIDPKARVgTLSVSQMQMIEIAKAFSYD 167
Cdd:PRK13647 81 VGLVFQDPdDQVFSSTVWDDVAFG---PVNMGLDKDEVERRVEEALKAVRMwDFRDKPPY-HLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495051738 168 AKIVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQSLEGLDMDKIIA 243
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVE 232
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
14-225 |
1.79e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 77.82 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKealENGISMV 93
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR---DRKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 94 HQELNLVLQRSVMDNMWLG-------RYPTKGVfVDQEKMYLDTKAIFDELdIDIDPkarvGTLSVSQMQMIEIAKAFSY 166
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAFGltvlprrERPNAAA-IKAKVTQLLEMVQLAHL-ADRYP----AQLSGGQKQRVALARALAV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 167 DAKIVIMDEPTSSLTEKEVNHLFKIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDG 225
Cdd:PRK10851 154 EPQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQG 213
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
26-226 |
1.79e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 75.89 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 26 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeidfHSAKeaLENGISMvHQELnlvlqrSV 105
Cdd:COG1134 39 FWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR----VSAL--LELGAGF-HPEL------TG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 106 MDNMWL-GR---YPTKgvfvdqekmylDTKAIFDELdID-------ID-PkarVGTLSvSQMQM-IEIAKAFSYDAKIVI 172
Cdd:COG1134 106 RENIYLnGRllgLSRK-----------EIDEKFDEI-VEfaelgdfIDqP---VKTYS-SGMRArLAFAVATAVDPDILL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495051738 173 MDEPTS----SLTEKevnhLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 226
Cdd:COG1134 170 VDEVLAvgdaAFQKK----CLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGR 223
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
13-235 |
2.54e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 76.18 E-value: 2.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFP-GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFHSAKEalengi 90
Cdd:PRK13644 1 MIRLENVSYSYPdGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgDFSKLQG------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 91 smVHQELNLVLQRSvmDNMWLGRYPTKGVFVDQEKMYLDTKAIFDELDIDIdpkARVG----------TLSVSQMQMIEI 160
Cdd:PRK13644 75 --IRKLVGIVFQNP--ETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRAL---AEIGlekyrhrspkTLSGGQGQCVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495051738 161 AKAFSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIfQLCDEITILRDGQWIatqsLEG 235
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKIV----LEG 217
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
26-229 |
3.44e-15 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 75.06 E-value: 3.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 26 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkEIDFHSAKEALENgISMVH-QELNLVLQRS 104
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-LVPWKRRKKFLRR-IGVVFgQKTQLWWDLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 105 VMDNMWLGR--YptkGVFVDQEKMYLDtkAIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTE 182
Cdd:cd03267 112 VIDSFYLLAaiY---DLPPARFKKRLD--ELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495051738 183 KEVNHLFKIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWIA 229
Cdd:cd03267 187 VAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLY 234
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
263-482 |
3.50e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 76.38 E-value: 3.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 263 EVILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHsANEAinngf 340
Cdd:PRK13537 5 VAPIDFRNVEKRygDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSR-ARHA----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 341 alvteeRRSTGI---YAYLDIGFnSLISNIRNYKSKIGLlDNSRMKSDTQWVIDSMRVKTPGHrTQIGSLSGGNQQKVII 417
Cdd:PRK13537 79 ------RQRVGVvpqFDNLDPDF-TVRENLLVFGRYFGL-SAAAARALVPPLLEFAKLENKAD-AKVGELSGGMKRRLTL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495051738 418 GRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK13537 150 ARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
278-482 |
3.56e-15 |
|
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: 74.71 E-value: 3.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 278 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGtislhgkkinnhsanEAINNGFALVTEE---RRSTGI-- 352
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSG---------------RATVAGHDVVREPrevRRRIGIvf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 353 -YAYLD---IGFNSLISNIRNYKSKiglldNSRMKSDTQWVIDSMRVKTPGHRtQIGSLSGGNQQKVIIGRWLLTQPEIL 428
Cdd:cd03265 80 qDLSVDdelTGWENLYIHARLYGVP-----GAERRERIDELLDFVGLLEAADR-LVKTYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495051738 429 MLDEPTRGIDVGAKFEIYQLIAELAKK-GKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHG 208
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
13-252 |
3.83e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 75.43 E-value: 3.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGS---ILFQGKEIDfHSAKEALENG 89
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshIELLGRTVQ-REGRLARDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 90 ISMVH-----QELNLVLQRSVMDNMWLGRYPTKGV-------FVDQEKMylDTKAIFDELDIDIDPKARVGTLSVSQMQM 157
Cdd:PRK09984 83 KSRANtgyifQQFNLVNRLSVLENVLIGALGSTPFwrtcfswFTREQKQ--RALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 158 IEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWIATQSLEGL 236
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
|
250
....*....|....*.
gi 495051738 237 DMDKIIAMMvgRSLNQ 252
Cdd:PRK09984 241 DNERFDHLY--RSINR 254
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
27-228 |
3.89e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 75.64 E-value: 3.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 27 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALEN---GISMVHQ--ELNLvL 101
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKlrkKVSLVFQfpEAQL-F 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 102 QRSVMDNMWLGryPTKGVFVDQE-----KMYLDTKAIFDELdIDIDPKarvgTLSVSQMQMIEIAKAFSYDAKIVIMDEP 176
Cdd:PRK13641 100 ENTVLKDVEFG--PKNFGFSEDEakekaLKWLKKVGLSEDL-ISKSPF----ELSGGQMRRVAIAGVMAYEPEILCLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495051738 177 TSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWI 228
Cdd:PRK13641 173 AAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1-229 |
4.07e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 75.21 E-value: 4.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 1 MVSNNTQSSGEYLLEmtNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLfGIYQKDS-GSILFQGKEIDF 79
Cdd:PRK10575 1 MQEYTNHSDTTFALR--NVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQPPSeGEILLDAQPLES 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 80 HSAKeALENGISMVHQELNLVLQRSVMDNMWLGRYPTKGVF-----VDQEKMyldTKAIfdeLDIDIDPKAR--VGTLSV 152
Cdd:PRK10575 78 WSSK-AFARKVAYLPQQLPAAEGMTVRELVAIGRYPWHGALgrfgaADREKV---EEAI---SLVGLKPLAHrlVDSLSG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495051738 153 SQMQMIEIAKAFSYDAKIVIMDEPTSSL-TEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIA 229
Cdd:PRK10575 151 GERQRAWIAMLVAQDSRCLLLDEPTSALdIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIA 228
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
33-236 |
4.39e-15 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 74.41 E-value: 4.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 33 NLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEidfHSAKEALENGISMVHQELNLVLQRSVMDNMWLG 112
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD---LTALPPAERPVSMLFQENNLFPHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 113 RYPtkgvfvdqeKMYL---DTKAIFDELdididpkARVG----------TLSVSQMQMIEIAKAFSYDAKIVIMDEPTSS 179
Cdd:COG3840 96 LRP---------GLKLtaeQRAQVEQAL-------ERVGlaglldrlpgQLSGGQRQRVALARCLVRKRPILLLDEPFSA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495051738 180 L---TEKEVNHLfkiIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQSLEGL 236
Cdd:COG3840 160 LdpaLRQEMLDL---VDELcRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
265-479 |
4.45e-15 |
|
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: 76.25 E-value: 4.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 265 ILEVRNL-TSLRQPS-----IRDVSFDLHKGEILGIAG------------LVGakrtdivetLFGIREKSGGTISLHGKK 326
Cdd:COG0444 1 LLEVRNLkVYFPTRRgvvkaVDGVSFDVRRGETLGLVGesgsgkstlaraILG---------LLPPPGITSGEILFDGED 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 327 INNHSAneainngfalvtEERRStgiYAYLDIG------FNSLisnirNYKSKIG-----LLDNSRMKSDTQW---VIDS 392
Cdd:COG0444 72 LLKLSE------------KELRK---IRGREIQmifqdpMTSL-----NPVMTVGdqiaePLRIHGGLSKAEArerAIEL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 393 M-RVKTPGHRTQIGS----LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-GKGIIIISSEM 466
Cdd:COG0444 132 LeRVGLPDPERRLDRypheLSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDL 211
|
250
....*....|...
gi 495051738 467 PELLGITDRILVM 479
Cdd:COG0444 212 GVVAEIADRVAVM 224
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
276-482 |
5.02e-15 |
|
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: 74.58 E-value: 5.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 276 QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANE-AINNGFalvteerRSTGIYA 354
Cdd:cd03300 13 FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKrPVNTVF-------QNYALFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 355 YLDIGfnsliSNIrNYKSKIGLLDNSRMKSDTQWVIDSMRVKTPGHRtQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPT 434
Cdd:cd03300 86 HLTVF-----ENI-AFGLRLKKLPKAEIKERVAEALDLVQLEGYANR-KPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495051738 435 RGIDV----GAKFEIYQLIAELakkGKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:cd03300 159 GALDLklrkDMQLELKRLQKEL---GITFVFVTHDQEEALTMSDRIAVMNKG 207
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
29-228 |
5.50e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 74.70 E-value: 5.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKC---LFGIYQ---KDSGSILFQGKEIdFHSAKEALENGISMVHQELNLVLQ 102
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVlnrLIEIYDskiKVDGKVLYFGKDI-FQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 103 RSVMDNMwlgRYPTKGVFVDQEKmylDTKAIFDEL--------DIDIDPKARVGTLSVSQMQMIEIAKAFSYDAKIVIMD 174
Cdd:PRK14246 105 LSIYDNI---AYPLKSHGIKEKR---EIKKIVEEClrkvglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495051738 175 EPTSSLTEKEVNHLFKIIRKLKERgCGIVYISHKMEEIFQLCDEITILRDGQWI 228
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
20-228 |
5.86e-15 |
|
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: 73.35 E-value: 5.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 20 NKSFPGVKA-LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFG--IYQKDSGSILFQGKEIDFHSAKEALengismvhqe 96
Cdd:cd03213 15 SSPSKSGKQlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSFRKII---------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 97 lnlvlqrsvmdnmwlgryptkgVFVDQEKMYLDTKAIFDELDIdidpKARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEP 176
Cdd:cd03213 85 ----------------------GYVPQDDILHPTLTVRETLMF----AAKLRGLSGGERKRVSIALELVSNPSLLFLDEP 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495051738 177 TSSLTEKEVNHLFKIIRKLKERGCGIVYISHK-MEEIFQLCDEITILRDGQWI 228
Cdd:cd03213 139 TSGLDSSSALQVMSLLRRLADTGRTIICSIHQpSSEIFELFDKLLLLSQGRVI 191
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
266-484 |
5.89e-15 |
|
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: 74.12 E-value: 5.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 266 LEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNhsaneainngfaLV 343
Cdd:cd03218 1 LRAENLSKRygKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITK------------LP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 344 TEERRSTGIyAYL---DIGFNSLI--SNIRNYKSKIGLLDNSRMKSDTQWV----IDSMRvKTPGhrtqiGSLSGGNQQK 414
Cdd:cd03218 69 MHKRARLGI-GYLpqeASIFRKLTveENILAVLEIRGLSKKEREEKLEELLeefhITHLR-KSKA-----SSLSGGERRR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 415 VIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:cd03218 142 VEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKV 211
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
28-226 |
7.20e-15 |
|
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: 73.68 E-value: 7.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 28 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfHSAKEALENGISMVHQElNLVLQRSVMD 107
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDIS-KIGLHDLRSRISIIPQD-PVLFSGTIRS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 108 NM-WLGRYPTKGVFVDQEKMYLdtKAIFDELDIDIDPKARVG--TLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSL---T 181
Cdd:cd03244 97 NLdPFGEYSDEELWQALERVGL--KEFVESLPGGLDTVVEEGgeNLSVGQRQLLCLARALLRKSKILVLDEATASVdpeT 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495051738 182 EKevnHLFKIIRKlKERGCGIVYISHKMEEIFQlCDEITILRDGQ 226
Cdd:cd03244 175 DA---LIQKTIRE-AFKDCTVLTIAHRLDTIID-SDRILVLDKGR 214
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
6-217 |
7.47e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 74.43 E-value: 7.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 6 TQSSGEYLLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKC------LFGIYQKDsGSILFQGKEI-D 78
Cdd:PRK14243 3 TLNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndLIPGFRVE-GKVTFHGKNLyA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 79 FHSAKEALENGISMVHQELNlVLQRSVMDNMWLGRYpTKGVFVDQEKMY---LDTKAIFDEldidIDPKARVGTLSVS-- 153
Cdd:PRK14243 82 PDVDPVEVRRRIGMVFQKPN-PFPKSIYDNIAYGAR-INGYKGDMDELVersLRQAALWDE----VKDKLKQSGLSLSgg 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495051738 154 QMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLKERGCgIVYISHKMEEIFQLCD 217
Cdd:PRK14243 156 QQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYT-IIIVTHNMQQAARVSD 218
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
266-484 |
7.99e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 74.70 E-value: 7.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 266 LEVRNLTSLRQP-------SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANeainn 338
Cdd:PRK13637 3 IKIENLTHIYMEgtpfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVK----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 339 gfalVTEERRSTGIY------------AYLDIGFNSliSNIRNYKSKIglldNSRMKSDTQWV---IDSMRVKTPGhrtq 403
Cdd:PRK13637 78 ----LSDIRKKVGLVfqypeyqlfeetIEKDIAFGP--INLGLSEEEI----ENRVKRAMNIVgldYEDYKDKSPF---- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 404 igSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSE-MPELLGITDRILVMSNG 482
Cdd:PRK13637 144 --ELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHsMEDVAKLADRIIVMNKG 221
|
..
gi 495051738 483 LV 484
Cdd:PRK13637 222 KC 223
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
265-484 |
9.82e-15 |
|
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: 73.38 E-value: 9.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 265 ILEVRNLT------SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSaneainn 338
Cdd:cd03258 1 MIELKNVSkvfgdtGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLS------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 339 GFALVtEERRSTG-IYAyldiGFNSLISniRNYKSKIGL---LDNSRMKSDTQWVIDSMRVKTPGHRTQI--GSLSGGNQ 412
Cdd:cd03258 74 GKELR-KARRRIGmIFQ----HFNLLSS--RTVFENVALpleIAGVPKAEIEERVLELLELVGLEDKADAypAQLSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495051738 413 QKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-GKGIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
14-229 |
1.31e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 73.14 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEID----FHSAKEalenG 89
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIThlpmHKRARL----G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 90 ISMVHQE------LnlvlqrSVMDNMWL---GRYPTKgvfvDQEKMYLDtkAIFDELDIDIDPKARVGTLSVSQMQMIEI 160
Cdd:COG1137 80 IGYLPQEasifrkL------TVEDNILAvleLRKLSK----KEREERLE--ELLEEFGITHLRKSKAYSLSGGERRRVEI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495051738 161 AKAFSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIA 229
Cdd:COG1137 148 ARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLA 216
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
12-234 |
1.43e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 74.07 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 12 YLLEMTNINKSFPG-VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEalengi 90
Cdd:PRK13652 2 HLIETRDLCYSYSGsKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIRE------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 91 smVHQELNLVLQRSvmDNMWLGRYPTKGVFVDQEKMYLDTKAIFDELDIDI------DPKARV-GTLSVSQMQMIEIAKA 163
Cdd:PRK13652 76 --VRKFVGLVFQNP--DDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALhmlgleELRDRVpHHLSGGEKKRVAIAGV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495051738 164 FSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWIATQSLE 234
Cdd:PRK13652 152 IAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVE 223
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
14-234 |
1.87e-14 |
|
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: 72.17 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGI--YQKDSGSILFQGKEIDFHSAKEALENGIS 91
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 92 MVHQelnlvlqrsvmdnmwlgrYPTK--GVFVDQEKMYLDtkaifdeldididpkarVGtLSVSQMQMIEIAKAFSYDAK 169
Cdd:cd03217 81 LAFQ------------------YPPEipGVKNADFLRYVN-----------------EG-FSGGEKKRNEILQLLLLEPD 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495051738 170 IVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKmEEIFQLC--DEITILRDGQWIATQSLE 234
Cdd:cd03217 125 LAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHY-QRLLDYIkpDRVHVLYDGRIVKSGDKE 190
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
276-482 |
1.92e-14 |
|
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: 72.62 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 276 QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSaneainngfalVTEERRSTGiYAY 355
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD-----------PADLRRNIG-YVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 356 LDIG--FNSLISNI---RNYKSKIGLLDNSRMKSDTQWVIDSMRvktpGHRTQIG----SLSGGNQQKVIIGRWLLTQPE 426
Cdd:cd03245 85 QDVTlfYGTLRDNItlgAPLADDERILRAAELAGVTDFVNKHPN----GLDLQIGergrGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495051738 427 ILMLDEPTRGIDVGAKFEIYQLIAELAkKGKGIIIISSEMPeLLGITDRILVMSNG 482
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPS-LLDLVDRIIVMDSG 214
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
279-434 |
2.08e-14 |
|
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: 70.37 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 279 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSAneainngfalvTEERRSTGiYAYLDI 358
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDER-----------KSLRKEIG-YVFQDP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 359 GFNSLISNIRN--YKSKIGLLDNSRMKSDTQWVIDSMRVKTPGHRT---QIGSLSGGNQQKVIIGRWLLTQPEILMLDEP 433
Cdd:pfam00005 69 QLFPRLTVRENlrLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
.
gi 495051738 434 T 434
Cdd:pfam00005 149 T 149
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
255-482 |
2.13e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 75.66 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 255 PDRENKPGEVILEVRNLT------SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISlHGKKIN 328
Cdd:PRK10261 2 PHSDELDARDVLAVENLNiafmqeQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQ-CDKMLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 329 NHSANEAINNGFALVTEERRSTG-----IYAYLDIGFNSLISNIRNYKSKIGL---LDNSRMKSDTQWVIDSMRVktPGH 400
Cdd:PRK10261 81 RRRSRQVIELSEQSAAQMRHVRGadmamIFQEPMTSLNPVFTVGEQIAESIRLhqgASREEAMVEAKRMLDQVRI--PEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 401 RTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-GKGIIIISSEMPELLGITDR 475
Cdd:PRK10261 159 QTILSryphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADR 238
|
....*..
gi 495051738 476 ILVMSNG 482
Cdd:PRK10261 239 VLVMYQG 245
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
13-221 |
2.24e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 72.44 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAkEALENGISM 92
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP-EIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 93 VHQELNLvLQRSVMDNM---WLGRYPTKgvfvdQEKMYLDTKAIFdELDIDIDPKaRVGTLSVSQMQMIEIAKAFSYDAK 169
Cdd:PRK10247 86 CAQTPTL-FGDTVYDNLifpWQIRNQQP-----DPAIFLDDLERF-ALPDTILTK-NIAELSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495051738 170 IVIMDEPTSSLTE---KEVNHLfkIIRKLKERGCGIVYISHKMEEIFQLCDEITI 221
Cdd:PRK10247 158 VLLLDEITSALDEsnkHNVNEI--IHRYVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
262-482 |
2.57e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 73.73 E-value: 2.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 262 GEVILEVRNLTSL---RQP----SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANE 334
Cdd:PRK13631 18 DDIILRVKNLYCVfdeKQEnelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 335 AINNGFAL-----VTEERRSTGI------YAYL------DIGFNSLISNIRNYKSKiglldnsrmkSDTQWVIDSMRVKT 397
Cdd:PRK13631 98 ELITNPYSkkiknFKELRRRVSMvfqfpeYQLFkdtiekDIMFGPVALGVKKSEAK----------KLAKFYLNKMGLDD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 398 PGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRIL 477
Cdd:PRK13631 168 SYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVI 247
|
....*
gi 495051738 478 VMSNG 482
Cdd:PRK13631 248 VMDKG 252
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
13-186 |
2.92e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 75.38 E-value: 2.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFPGVK-ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSaKEALENGIS 91
Cdd:PRK13657 334 AVEFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT-RASLRRNIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 92 MVHQELNLvLQRSVMDNMWLGRyPTkgvfVDQEKMYLDTKAI----F-----DELDIDIDPKARvgTLSVSQMQMIEIAK 162
Cdd:PRK13657 413 VVFQDAGL-FNRSIEDNIRVGR-PD----ATDEEMRAAAERAqahdFierkpDGYDTVVGERGR--QLSGGERQRLAIAR 484
|
170 180
....*....|....*....|....*..
gi 495051738 163 AFSYDAKIVIMDEPTSSL---TEKEVN 186
Cdd:PRK13657 485 ALLKDPPILILDEATSALdveTEAKVK 511
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
30-484 |
3.46e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 74.74 E-value: 3.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 30 DNVNLKVRPHSIHALMGENGAGKST-------LLKCLFGIYQkdSGSILFQGKEIdFHSAKEALE----NGISMVHQE-- 96
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSVtalsilrLLPSPPVVYP--SGDIRFHGESL-LHASEQTLRgvrgNKIAMIFQEpm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 97 --LN------------LVLQRSvmdnmwLGRYPTKGvfvdqekmyldtkAIFDELDididpkaRVG-------------T 149
Cdd:PRK15134 103 vsLNplhtlekqlyevLSLHRG------MRREAARG-------------EILNCLD-------RVGirqaakrltdyphQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 150 LSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLK-ERGCGIVYISHKMEEIFQLCDEITILRDGQWI 228
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQqELNMGLLFITHNLSIVRKLADRVAVMQNGRCV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 229 ATQSLEGL-------DMDKIIAmmvgrSLNQRFPDRENKPGEVILEVRNLT---SLRQPSIR----------DVSFDLHK 288
Cdd:PRK15134 237 EQNRAATLfsapthpYTQKLLN-----SEPSGDPVPLPEPASPLLDVEQLQvafPIRKGILKrtvdhnvvvkNISFTLRP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 289 GEILGIAGLVGA-KRTDIVETLFGIRekSGGTISLHGKKINNHSANEainngfaLVTEERRstgiyayLDIGF---NSLI 364
Cdd:PRK15134 312 GETLGLVGESGSgKSTTGLALLRLIN--SQGEIWFDGQPLHNLNRRQ-------LLPVRHR-------IQVVFqdpNSSL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 365 SNIRNYKSKI--GLLDNSRMKS---DTQWVIDSM---------RVKTPGhrtqigSLSGGNQQKVIIGRWLLTQPEILML 430
Cdd:PRK15134 376 NPRLNVLQIIeeGLRVHQPTLSaaqREQQVIAVMeevgldpetRHRYPA------EFSGGQRQRIAIARALILKPSLIIL 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 495051738 431 DEPTRGIDVGAKFEIYQLIAELAKKGK-GIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:PRK15134 450 DEPTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQVIVLRQGEV 504
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
26-236 |
3.86e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 73.20 E-value: 3.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 26 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG-----KEIDFhsAKEalengISMVHQelnlv 100
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpfkRRKEF--ARR-----IGVVFG----- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 101 lQRS-------VMDNMWLGRyptkgvfvdqeKMYLDTKAIF----DELD--IDIDPKAR--VGTLSVSQ-MQMiEIAKAF 164
Cdd:COG4586 103 -QRSqlwwdlpAIDSFRLLK-----------AIYRIPDAEYkkrlDELVelLDLGELLDtpVRQLSLGQrMRC-ELAAAL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495051738 165 SYDAKIVIMDEPTSSL---TEKEVNHLFKIIRklKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQSLEGL 236
Cdd:COG4586 170 LHRPKILFLDEPTIGLdvvSKEAIREFLKEYN--RERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEEL 242
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
272-482 |
3.94e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 72.94 E-value: 3.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 272 TSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANEAINngfalvtEERRSTG 351
Cdd:PRK13641 16 TPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLK-------KLRKKVS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 352 I---YAYLDIGFNSLISNIRNYKSKIGLLDNSRMKSDTQWV-----IDSMRVKTPGhrtqigSLSGGNQQKVIIGRWLLT 423
Cdd:PRK13641 89 LvfqFPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLkkvglSEDLISKSPF------ELSGGQMRRVAIAGVMAY 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495051738 424 QPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK13641 163 EPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHG 221
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
13-264 |
4.34e-14 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 75.44 E-value: 4.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFPGVK--ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfhsakeaLENgI 90
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--------LTN-I 2007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 91 SMVHQELNLVLQRSVMDNMWLGR-----YPT-KGVFVDQ-EKMyldTKAIFDELDIDIDPKARVGTLSVSQMQMIEIAKA 163
Cdd:TIGR01257 2008 SDVHQNMGYCPQFDAIDDLLTGRehlylYARlRGVPAEEiEKV---ANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIA 2084
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 164 FSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQSLEGLDMD---- 239
Cdd:TIGR01257 2085 LIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKfgdg 2164
|
250 260 270
....*....|....*....|....*....|...
gi 495051738 240 KIIAMMVGRSLNQRFPD--------RENKPGEV 264
Cdd:TIGR01257 2165 YIVTMKIKSPKDDLLPDlnpveqffQGNFPGSV 2197
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-226 |
5.05e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 74.50 E-value: 5.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 25 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGI--YQkdsGSILFQG---KEIDFHSAKEALengiSMVHQELNL 99
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFlpYQ---GSLKINGielRELDPESWRKHL----SWVGQNPQL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 100 vLQRSVMDNMWLGRYPTKGVFVDQ--EKMYLD--TKAIFDELDIDIdpKARVGTLSVSQMQMIEIAKAFSYDAKIVIMDE 175
Cdd:PRK11174 435 -PHGTLRDNVLLGNPDASDEQLQQalENAWVSefLPLLPQGLDTPI--GDQAAGLSVGQAQRLALARALLQPCQLLLLDE 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495051738 176 PTSSL---TEKevnhlfKIIRKLKE--RGCGIVYISHKMEEIFQlCDEITILRDGQ 226
Cdd:PRK11174 512 PTASLdahSEQ------LVMQALNAasRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQ 560
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-226 |
5.83e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 73.44 E-value: 5.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 4 NNTQSSGEYLLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfhsak 83
Cdd:PRK09452 5 NKQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 84 ealeNGISMVHQELNLVLQR-------SVMDNMWLGRYPTKGVFVDQEKMYLDTKAIFdELDIDIDPKARvgTLSVSQMQ 156
Cdd:PRK09452 79 ----THVPAENRHVNTVFQSyalfphmTVFENVAFGLRMQKTPAAEITPRVMEALRMV-QLEEFAQRKPH--QLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495051738 157 MIEIAKAFSYDAKIVIMDEPTSSLTEK-------EVNHLfkiIRKLkerGCGIVYISHKMEEIFQLCDEITILRDGQ 226
Cdd:PRK09452 152 RVAIARAVVNKPKVLLLDESLSALDYKlrkqmqnELKAL---QRKL---GITFVFVTHDQEEALTMSDRIVVMRDGR 222
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
27-226 |
9.65e-14 |
|
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: 70.13 E-value: 9.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 27 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfHSAKEALENGISMVHQELNLvLQRSVM 106
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIS-TIPLEDLRSSLTIIPQDPTL-FSGTIR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 107 DNmwlgryptkgvfVDQEKMYLDTKaIFDELDIdidpKARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVN 186
Cdd:cd03369 100 SN------------LDPFDEYSDEE-IYGALRV----SEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495051738 187 HLFKIIRKLKErGCGIVYISHKMEEIFQlCDEITILRDGQ 226
Cdd:cd03369 163 LIQKTIREEFT-NSTILTIAHRLRTIID-YDKILVMDAGE 200
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
13-229 |
1.20e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 70.96 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEaLENGISM 92
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAE-LARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 93 VHQELNLVLQRSVMDNMWLGRYPtkGVFVDQEKMYLDTKAIfdeldididpkARVG----------TLSVSQMQMIEIAK 162
Cdd:PRK13548 81 LPQHSSLSFPFTVEEVVAMGRAP--HGLSRAEDDALVAAAL-----------AQVDlahlagrdypQLSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495051738 163 AF------SYDAKIVIMDEPTSSLTEKEVNHLFKIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWIA 229
Cdd:PRK13548 148 VLaqlwepDGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVA 221
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
265-489 |
1.21e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 71.29 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 265 ILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINnhsanEAINNGFAL 342
Cdd:COG4152 1 MLELKGLTKRfgDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-----PEDRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 343 VTEERrstGIYAYLDIG-----FNSL--------ISNIRNYKSKIGLLDNSRMKsdtqwvidsmrvktpghrtqIGSLSG 409
Cdd:COG4152 76 LPEER---GLYPKMKVGeqlvyLARLkglskaeaKRRADEWLERLGLGDRANKK--------------------VEELSK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 410 GNQQKV-IIGRwLLTQPEILMLDEPTRGID-VGAKfEIYQLIAELAKKGKgIIIISS---EMPELLgiTDRILVMSNG-- 482
Cdd:COG4152 133 GNQQKVqLIAA-LLHDPELLILDEPFSGLDpVNVE-LLKDVIRELAAKGT-TVIFSShqmELVEEL--CDRIVIINKGrk 207
|
....*..
gi 495051738 483 LVSGIVD 489
Cdd:COG4152 208 VLSGSVD 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
13-226 |
1.88e-13 |
|
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: 72.41 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFPG-----------VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIyQKDSGSILFQGKEIDFHS 81
Cdd:COG4172 275 LLEARDLKVWFPIkrglfrrtvghVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 82 AKE--ALENGISMVHQ-------------------------ELNL---------VLQRSVMDNMWLGRYPTKgvfvdqek 125
Cdd:COG4172 354 RRAlrPLRRRMQVVFQdpfgslsprmtvgqiiaeglrvhgpGLSAaerrarvaeALEEVGLDPAARHRYPHE-------- 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 126 myldtkaifdeldididpkarvgtLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSL---TEKEVNHLFkiiRKL-KERGCG 201
Cdd:COG4172 426 ------------------------FSGGQRQRIAIARALILEPKLLVLDEPTSALdvsVQAQILDLL---RDLqREHGLA 478
|
250 260
....*....|....*....|....*
gi 495051738 202 IVYISHKMEEIFQLCDEITILRDGQ 226
Cdd:COG4172 479 YLFISHDLAVVRALAHRVMVMKDGK 503
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-228 |
1.92e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.40 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 9 SGEYLLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFqGKEIDfhsakealen 88
Cdd:COG0488 311 LGKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK---------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 89 gISMVHQEL-NLVLQRSVMDNMWLGRYPTKGVFV------------DQEKmyldtkaifdeldididpkaRVGTLSV--- 152
Cdd:COG0488 380 -IGYFDQHQeELDPDKTVLDELRDGAPGGTEQEVrgylgrflfsgdDAFK--------------------PVGVLSGgek 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 153 SQMQMieiAKAFSYDAKIVIMDEPTssltekevNHL--------------FKiirklkerGCgIVYISHKMEEIFQLCDE 218
Cdd:COG0488 439 ARLAL---AKLLLSPPNVLLLDEPT--------NHLdietlealeealddFP--------GT-VLLVSHDRYFLDRVATR 498
|
250
....*....|
gi 495051738 219 ITILRDGQWI 228
Cdd:COG0488 499 ILEFEDGGVR 508
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
14-226 |
1.99e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 71.67 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfhsAKEALEN-GISM 92
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV----THRSIQQrDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 93 VHQELNLVLQRSVMDNMwlgRYPTKGVFVDQEKMYLDTKAIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSYDAKIVI 172
Cdd:PRK11432 83 VFQSYALFPHMSLGENV---GYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495051738 173 MDEPTSSLTEKEVNHLFKIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQ 226
Cdd:PRK11432 160 FDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGK 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
266-484 |
2.18e-13 |
|
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: 69.21 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 266 LEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANEainNGFALV 343
Cdd:cd03301 1 VELENVTKRfgNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD---RDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 344 TEerrSTGIYAYLdigfnSLISNIRnykskIGLldnsRMKSDTQWVIDSmRVKTPGHRTQIG--------SLSGGNQQKV 415
Cdd:cd03301 78 FQ---NYALYPHM-----TVYDNIA-----FGL----KLRKVPKDEIDE-RVREVAELLQIEhlldrkpkQLSGGQRQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 416 IIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-GKGIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:cd03301 140 ALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
27-228 |
2.37e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 70.58 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 27 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfHSAKEALengISMVHQELNLVLQrsvm 106
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIT-HKTKDKY---IRPVRKRIGMVFQ---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 107 dnmwlgrYPTKGVF---VDQE--------KMYLD-TKAIFDELDIDIDPKARVGTLSVSQM---QM--IEIAKAFSYDAK 169
Cdd:PRK13646 93 -------FPESQLFedtVEREiifgpknfKMNLDeVKNYAHRLLMDLGFSRDVMSQSPFQMsggQMrkIAIVSILAMNPD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 170 IVIMDEPTSSLTEKEVNHLFKIIRKLK-ERGCGIVYISHKMEEIFQLCDEITILRDGQWI 228
Cdd:PRK13646 166 IIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIV 225
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
27-228 |
2.39e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 70.54 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 27 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEAlengISMVHQELNLVLQ---- 102
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKD----IKQIRKKVGLVFQfpes 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 103 ----RSVMDNMWLGRY-----PTKGVFVDQEKMYLdtKAIFDELdIDIDPKarvgTLSVSQMQMIEIAKAFSYDAKIVIM 173
Cdd:PRK13649 97 qlfeETVLKDVAFGPQnfgvsQEEAEALAREKLAL--VGISESL-FEKNPF----ELSGGQMRRVAIAGILAMEPKILVL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495051738 174 DEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWI 228
Cdd:PRK13649 170 DEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
28-232 |
2.45e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 70.21 E-value: 2.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 28 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGS---ILFQGKEIDfhsakealENGISMVHQELNLVLQRS 104
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLT--------AKTVWDIREKVGIVFQNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 105 vmDNMWLGRYPTKGVF-------VDQEKMYLDTKAIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPT 177
Cdd:PRK13640 94 --DNQFVGATVGDDVAfglenraVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDEST 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495051738 178 SSLTEKEVNHLFKIIRKL-KERGCGIVYISHKMEEIfQLCDEITILRDGQWIATQS 232
Cdd:PRK13640 172 SMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGS 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
406-484 |
2.48e-13 |
|
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: 68.73 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 406 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIII----SSEMPELLgitDRILVMSN 481
Cdd:cd03213 111 GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSihqpSSEIFELF---DKLLLLSQ 187
|
...
gi 495051738 482 GLV 484
Cdd:cd03213 188 GRV 190
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
267-484 |
3.49e-13 |
|
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: 69.59 E-value: 3.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 267 EVRNLTSLRqPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANEAIN---NGFALV 343
Cdd:cd03294 29 EILKKTGQT-VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrKKISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 344 TEerrSTGIYAYLdigfnSLISNIRNYKSKIGLLDNSRMKSDTQwVIDSMRVKTPGHRtQIGSLSGGNQQKVIIGRWLLT 423
Cdd:cd03294 108 FQ---SFALLPHR-----TVLENVAFGLEVQGVPRAEREERAAE-ALELVGLEGWEHK-YPDELSGGMQQRVGLARALAV 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495051738 424 QPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKGKGIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:cd03294 178 DPDILLMDEAFSALDPLIRREMQDELLRLqAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
265-489 |
3.67e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 69.57 E-value: 3.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 265 ILEVRNLTSLRQPSI--RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKkinnhsaNEAINNGFAL 342
Cdd:PRK11701 6 LLSVRGLTKLYGPRKgcRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMR-------DGQLRDLYAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 343 VTEERR------------------STGIYAYLDIGFNSLISNIRNYKskiglldNSRMKSdTQWVidsMRVKTPGHRT-- 402
Cdd:PRK11701 79 SEAERRrllrtewgfvhqhprdglRMQVSAGGNIGERLMAVGARHYG-------DIRATA-GDWL---ERVEIDAARIdd 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 403 QIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKGKGIIIISSEM--PELLgiTDRILVM 479
Cdd:PRK11701 148 LPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLavARLL--AHRLLVM 225
|
250
....*....|..
gi 495051738 480 SNGLV--SGIVD 489
Cdd:PRK11701 226 KQGRVveSGLTD 237
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
265-495 |
3.89e-13 |
|
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: 69.45 E-value: 3.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 265 ILEVRNLT-----------SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKIN--NHS 331
Cdd:TIGR02769 2 LLEVRDVThtyrtgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYqlDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 332 ANEAINNGFALVTEE-------RRSTGiyayldigfNSLISNIRNYKSkiglLDNSRMKSDTQWVIDSMRVKTPGHRTQI 404
Cdd:TIGR02769 82 QRRAFRRDVQLVFQDspsavnpRMTVR---------QIIGEPLRHLTS----LDESEQKARIAELLDMVGLRSEDADKLP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 405 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKGKGIIIISSEMPELLGITDRILVMSNGl 483
Cdd:TIGR02769 149 RQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLqQAFGTAYLFITHDLRLVQSFCQRVAVMDKG- 227
|
250
....*....|..
gi 495051738 484 vsGIVDTKTTTQ 495
Cdd:TIGR02769 228 --QIVEECDVAQ 237
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
27-232 |
3.97e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 70.04 E-value: 3.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 27 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI--DFHSAKEA--LENGISMVHQ--ELNLv 100
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpaNLKKIKEVkrLRKEIGLVFQfpEYQL- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 101 LQRSVMDNMWLGryPTKgVFVDQEKMYLDTKAIFDELDIDIDPKARVG-TLSVSQMQMIEIAKAFSYDAKIVIMDEPTSS 179
Cdd:PRK13645 104 FQETIEKDIAFG--PVN-LGENKQEAYKKVPELLKLVQLPEDYVKRSPfELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495051738 180 LTEKEVNHLFKIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQS 232
Cdd:PRK13645 181 LDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-234 |
4.12e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 69.30 E-value: 4.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDS-----GSILFQGKEI-DFHSAKEALE 87
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 88 NGISMVHQELNLvLQRSVMDNM-----WLGRYPtKGVFVDQEKMYLDTKAIFDELDIDIDPKARvgTLSVSQMQMIEIAK 162
Cdd:PRK14258 88 RQVSMVHPKPNL-FPMSVYDNVaygvkIVGWRP-KLEIDDIVESALKDADLWDEIKHKIHKSAL--DLSGGQQQRLCIAR 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495051738 163 AFSYDAKIVIMDEPTSSL---TEKEVNHLFKIIRKLKErgCGIVYISHKMEEIFQLCDEITILRDGQWIATQSLE 234
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLdpiASMKVESLIQSLRLRSE--LTMVIVSHNLHQVSRLSDFTAFFKGNENRIGQLVE 236
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
263-486 |
4.28e-13 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 68.53 E-value: 4.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 263 EVILEVRNLT------SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTdiveTLF----GIREKSGGTISLHGKKINNHSA 332
Cdd:COG1136 2 SPLLELRNLTksygtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKS----TLLnilgGLDRPTSGEVLIDGQDISSLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 333 NEAinngfalvTEERRSTgiyayldIGF-----NsLIS------NIRnykskIGL-LDNSRMKSDTQWVIDSM-RVKTPG 399
Cdd:COG1136 78 REL--------ARLRRRH-------IGFvfqffN-LLPeltaleNVA-----LPLlLAGVSRKERRERARELLeRVGLGD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 400 HRTQ-IGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-GKGIIIISSEmPELLGITDRIL 477
Cdd:COG1136 137 RLDHrPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHD-PELAARADRVI 215
|
....*....
gi 495051738 478 VMSNGLVSG 486
Cdd:COG1136 216 RLRDGRIVS 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
276-482 |
4.41e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 70.24 E-value: 4.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 276 QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINnhsaneainngfALVTEERRSTGI--- 352
Cdd:PRK13536 54 KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP------------ARARLARARIGVvpq 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 353 YAYLDIGFnSLISNIRNYKSKIGLldNSRmksDTQWVIDSM----RVKTPGHrTQIGSLSGGNQQKVIIGRWLLTQPEIL 428
Cdd:PRK13536 122 FDNLDLEF-TVRENLLVFGRYFGM--STR---EIEAVIPSLlefaRLESKAD-ARVSDLSGGMKRRLTLARALINDPQLL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495051738 429 MLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK13536 195 ILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
266-484 |
4.77e-13 |
|
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: 68.21 E-value: 4.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 266 LEVRNLtSLR-----QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKInnhsaneainnGF 340
Cdd:cd03369 7 IEVENL-SVRyapdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI-----------ST 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 341 ALVTEERRSTGIYAYLDIGFNSLI-SNirnykskiglLDNSRMKSDTQwVIDSMRVKTPGHrtqigSLSGGNQQKVIIGR 419
Cdd:cd03369 75 IPLEDLRSSLTIIPQDPTLFSGTIrSN----------LDPFDEYSDEE-IYGALRVSEGGL-----NLSQGQRQLLCLAR 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495051738 420 WLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKGKGIIIISSEMPELLGItDRILVMSNGLV 484
Cdd:cd03369 139 ALLKRPRVLVLDEATASIDYATDALIQKTIREEF-TNSTILTIAHRLRTIIDY-DKILVMDAGEV 201
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
278-496 |
5.69e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.14 E-value: 5.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 278 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNH---------SANEAINNGFALVTEERR 348
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAlqknlvayvPQSEEVDWSFPVLVEDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 349 STGIYAYLdigfnslisnirnykskiGLLDNSRmKSDTQWVIDSM-RVKTPGHR-TQIGSLSGGNQQKVIIGRWLLTQPE 426
Cdd:PRK15056 102 MMGRYGHM------------------GWLRRAK-KRDRQIVTAALaRVDMVEFRhRQIGELSGGQKKRVFLARAIAQQGQ 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495051738 427 ILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITD-RILVMSNGLVSGIVDTKTTTQN 496
Cdd:PRK15056 163 VILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDyTVMVKGTVLASGPTETTFTAEN 233
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
266-479 |
6.06e-13 |
|
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: 70.78 E-value: 6.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 266 LEVRNLTSL---RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKI---NNHSANEAInng 339
Cdd:TIGR02857 322 LEFSGVSVAypgRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLadaDADSWRDQI--- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 340 fALVTEerrSTGIYAyldigfNSLISNIRNYKS--KIGLLDNSRMKSDTQWVIDSMRvktPGHRTQIGS----LSGGNQQ 413
Cdd:TIGR02857 399 -AWVPQ---HPFLFA------GTIAENIRLARPdaSDAEIREALERAGLDEFVAALP---QGLDTPIGEggagLSGGQAQ 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495051738 414 KVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKGKGIIIISSEmPELLGITDRILVM 479
Cdd:TIGR02857 466 RLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHR-LALAALADRIVVL 529
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-236 |
6.74e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 68.97 E-value: 6.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQK-----DSGSILFQGKEIDFHSAKEALEN 88
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRDVLEFRR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 89 GISMVHQELNlVLQRSVMDNMWLGRYPTKgvFVDQEKMYLDTKAIFDELDIDIDPKARVGT----LSVSQMQMIEIAKAF 164
Cdd:PRK14271 102 RVGMLFQRPN-PFPMSIMDNVLAGVRAHK--LVPRKEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495051738 165 SYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLKERgCGIVYISHKMEEIFQLCDEITILRDGQWIATQSLEGL 236
Cdd:PRK14271 179 AVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
28-225 |
7.44e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 68.62 E-value: 7.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 28 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEalengismVHQELNLVLQRSvmD 107
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEK--------LRKHIGIVFQNP--D 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 108 NMWLGRYPTKGV-------FVDQEKMYLDTKAIFDELDI----DIDPKArvgtLSVSQMQMIEIAKAFSYDAKIVIMDEP 176
Cdd:PRK13648 94 NQFVGSIVKYDVafglenhAVPYDEMHRRVSEALKQVDMleraDYEPNA----LSGGQKQRVAIAGVLALNPSVIILDEA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495051738 177 TSSLTEKEVNHLFKIIRKLK-ERGCGIVYISHKMEEIFQlCDEITILRDG 225
Cdd:PRK13648 170 TSMLDPDARQNLLDLVRKVKsEHNITIISITHDLSEAME-ADHVIVMNKG 218
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
27-267 |
7.61e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 68.99 E-value: 7.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 27 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSIlfqgKEIDFHSAKEALENGISMVHQELNLVLQ---- 102
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKV----TVGDIVVSSTSKQKEIKPVRKKVGVVFQfpes 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 103 ----RSVMDNMWLG-------RYPTKGVFVDQEKMYLDTKAIFDELDIDidpkarvgtLSVSQMQMIEIAKAFSYDAKIV 171
Cdd:PRK13643 96 qlfeETVLKDVAFGpqnfgipKEKAEKIAAEKLEMVGLADEFWEKSPFE---------LSGGQMRRVAIAGILAMEPEVL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 172 IMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIA--TQSLEGLDMDKIIAMMVGRS 249
Cdd:PRK13643 167 VLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIIScgTPSDVFQEVDFLKAHELGVP 246
|
250
....*....|....*...
gi 495051738 250 LNQRFPDRENKPGEVILE 267
Cdd:PRK13643 247 KATHFADQLQKTGAVTFE 264
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
25-230 |
7.73e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 68.76 E-value: 7.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 25 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeidfhSAKEAL-ENGISMVHQ--ELNLVL 101
Cdd:PRK15056 19 GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQ-----PTRQALqKNLVAYVPQseEVDWSF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 102 QRSVMDNMWLGRYPTKGVF-VDQEKMYLDTKAIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSL 180
Cdd:PRK15056 94 PVLVEDVVMMGRYGHMGWLrRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495051738 181 TEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDeITILRDGQWIAT 230
Cdd:PRK15056 174 DVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLAS 222
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
404-482 |
7.85e-13 |
|
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: 69.74 E-value: 7.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 404 IGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKG-IIIISSEMPELLGITDRILVMSNG 482
Cdd:COG4148 131 PATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIpILYVSHSLDEVARLADHVVLLEQG 210
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
266-482 |
1.02e-12 |
|
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: 67.22 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 266 LEVRNLTSL--RQPSIRDVSFDLHKGeILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHsaneainngfalV 343
Cdd:cd03264 1 LQLENLTKRygKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQ------------P 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 344 TEERRSTGiyaYL--DIGFnslISNIR-----NYKSKIGLLDNSRMKSDTQWVIDsmRVKTPGHRTQ-IGSLSGGNQQKV 415
Cdd:cd03264 68 QKLRRRIG---YLpqEFGV---YPNFTvreflDYIAWLKGIPSKEVKARVDEVLE--LVNLGDRAKKkIGSLSGGMRRRV 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495051738 416 IIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKkgKGIIIISSEMPE-LLGITDRILVMSNG 482
Cdd:cd03264 140 GIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEdVESLCNQVAVLNKG 205
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
11-228 |
1.39e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 67.49 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 11 EYLLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKD-----SGSILFQGKEIdfHSAKE- 84
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNI--YSPRTd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 85 --ALENGISMVHQELNlVLQRSVMDNMWLGrYPTKGVfvdQEKMYLDT--------KAIFDELDiDIDPKARVGtLSVSQ 154
Cdd:PRK14239 81 tvDLRKEIGMVFQQPN-PFPMSIYENVVYG-LRLKGI---KDKQVLDEavekslkgASIWDEVK-DRLHDSALG-LSGGQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495051738 155 MQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLKERGCgIVYISHKMEEIFQLCDEITILRDGQWI 228
Cdd:PRK14239 154 QQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYT-MLLVTRSMQQASRISDRTGFFLDGDLI 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
27-226 |
1.54e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 68.15 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 27 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKealengISMVHQELNLVLQrsvm 106
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVK------LSDIRKKVGLVFQ---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 107 dnmwlgrYPTKGVF----------------VDQEKMYLDTKAIFDELDIDIDPKARVG--TLSVSQMQMIEIAKAFSYDA 168
Cdd:PRK13637 91 -------YPEYQLFeetiekdiafgpinlgLSEEEIENRVKRAMNIVGLDYEDYKDKSpfELSGGQKRRVAIAGVVAMEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495051738 169 KIVIMDEPTSSLTEKEVNHLFKIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQ 226
Cdd:PRK13637 164 KILILDEPTAGLDPKGRDEILNKIKELhKEYNMTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
279-484 |
1.79e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 67.30 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 279 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKIN---NHSANEAINNGFALVTEERRSTGIYAY 355
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrDKDGQLKVADKNQLRLLRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 356 LDI-GFNSLISNIrnYKSKIGLLDNSRMKSDTQWVI--------DSMRVKTPGHrtqigsLSGGNQQKVIIGRWLLTQPE 426
Cdd:PRK10619 101 FNLwSHMTVLENV--MEAPIQVLGLSKQEARERAVKylakvgidERAQGKYPVH------LSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495051738 427 ILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:PRK10619 173 VLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
275-477 |
1.97e-12 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 65.72 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 275 RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKK----INNHSAneaINNGFALVTEERRST 350
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGArvayVPQRSE---VPDSLPLTVRDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 351 GIYAyldigfnslisnirnyksKIGLLDNSRmKSDTQWVIDSM-RVKTPG--HRtQIGSLSGGNQQKVIIGRWLLTQPEI 427
Cdd:NF040873 81 GRWA------------------RRGLWRRLT-RDDRAAVDDALeRVGLADlaGR-QLGELSGGQRQRALLAQGLAQEADL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495051738 428 LMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRIL 477
Cdd:NF040873 141 LLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVL 190
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
21-226 |
2.08e-12 |
|
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: 65.95 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 21 KSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeidfhsakealenGISMVHQE---L 97
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------------SIAYVSQEpwiQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 98 NlvlqRSVMDNMWLGRYptkgvfVDQEKmYLDT-KAIFDELDIDIDPKA---RVG----TLSVSQMQMIEIAKAFSYDAK 169
Cdd:cd03250 79 N----GTIRENILFGKP------FDEER-YEKViKACALEPDLEILPDGdltEIGekgiNLSGGQKQRISLARAVYSDAD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495051738 170 IVIMDEPTSSLTEKEVNHLFK--IIRKLKERGCgIVYISHKMEEIFQlCDEITILRDGQ 226
Cdd:cd03250 148 IYLLDDPLSAVDAHVGRHIFEncILGLLLNNKT-RILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
18-229 |
2.31e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 68.52 E-value: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 18 NINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfhsAKEALENGISMVHQEL 97
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN---DVPPAERGVGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 98 NLVLQRSVMDNMWLGrypTKGVFVDQEKMYLDTKAIFDELD----IDIDPKArvgtLSVSQMQMIEIAKAFSYDAKIVIM 173
Cdd:PRK11000 85 ALYPHLSVAENMSFG---LKLAGAKKEEINQRVNQVAEVLQlahlLDRKPKA----LSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495051738 174 DEPTSSLTEK-EVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILrDGQWIA 229
Cdd:PRK11000 158 DEPLSNLDAAlRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVL-DAGRVA 213
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
14-207 |
2.38e-12 |
|
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: 68.93 E-value: 2.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPG-VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeIDFHSAKE-ALENGIS 91
Cdd:TIGR02868 335 LELRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDG--VPVSSLDQdEVRRRVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 92 MVHQELNLvLQRSVMDNMWLGRyPTkgvfVDQEKMYL---------DTKAIFDELDIDIDPKARvgTLSVSQMQMIEIAK 162
Cdd:TIGR02868 413 VCAQDAHL-FDTTVRENLRLAR-PD----ATDEELWAalervgladWLRALPDGLDTVLGEGGA--RLSGGERQRLALAR 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495051738 163 AFSYDAKIVIMDEPTSSL---TEKEVNH-LFKIirklkERGCGIVYISH 207
Cdd:TIGR02868 485 ALLADAPILLLDEPTEHLdaeTADELLEdLLAA-----LSGRTVVLITH 528
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
279-482 |
2.63e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 66.46 E-value: 2.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 279 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANEAINNGFALVTEErrsTGIYAYLDI 358
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQE---ASIFRRLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 359 gFNSLISNIRNYKSkiglLDNSRMKSDTQWVIDSMRVKtpgH-RTQIG-SLSGGNQQKVIIGRWLLTQPEILMLDEPTRG 436
Cdd:PRK10895 96 -YDNLMAVLQIRDD----LSAEQREDRANELMEEFHIE---HlRDSMGqSLSGGERRRVEIARALAANPKFILLDEPFAG 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495051738 437 IDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK10895 168 VDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQG 213
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
30-229 |
3.03e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 66.93 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 30 DNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENgISMVHQELNLVLQRSVMDNM 109
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-IGLLAQNATTPGDITVQELV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 110 WLGRYPTKGVFVDQEKMylDTKAIFDELD---IDIDPKARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVN 186
Cdd:PRK10253 103 ARGRYPHQPLFTRWRKE--DEEAVTKAMQatgITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495051738 187 HLFKIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWIA 229
Cdd:PRK10253 181 DLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVA 224
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
26-226 |
3.23e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 67.62 E-value: 3.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 26 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIyQKDSGSI-----LFQGKEIDFHSAKEALE---NGISMVHQEl 97
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHVtadrfRWNGIDLLKLSPRERRKiigREIAMIFQE- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 98 nlvlQRSVMDnmwlgryPTKGVFvDQEKMYLDTKAI--------FDELDIDIDPKARVGT-------------LSVSQMQ 156
Cdd:COG4170 98 ----PSSCLD-------PSAKIG-DQLIEAIPSWTFkgkwwqrfKWRKKRAIELLHRVGIkdhkdimnsypheLTEGECQ 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495051738 157 MIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQ 226
Cdd:COG4170 166 KVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLnQLQGTSILLISHDLESISQWADTITVLYCGQ 236
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
265-486 |
3.34e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 66.21 E-value: 3.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 265 ILEVRNLT-SLRQ-PSIRDVSFDLHKGEILGIAGLVGAKRTdiveTLF----GIREKSGGTISLHGKKINNHSANEAINN 338
Cdd:COG1137 3 TLEAENLVkSYGKrTVVKDVSLEVNQGEIVGLLGPNGAGKT----TTFymivGLVKPDSGRIFLDGEDITHLPMHKRARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 339 GFALVTEE----RRST---GIYAYLDIGFNSlisnirnyKSKI-----GLLDNSRmksdtqwvIDSMRvKTPGHrtqigS 406
Cdd:COG1137 79 GIGYLPQEasifRKLTvedNILAVLELRKLS--------KKEReerleELLEEFG--------ITHLR-KSKAY-----S 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 407 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGID---VGakfEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNG- 482
Cdd:COG1137 137 LSGGERRRVEIARALATNPKFILLDEPFAGVDpiaVA---DIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGk 213
|
....*
gi 495051738 483 -LVSG 486
Cdd:COG1137 214 vLAEG 218
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
12-77 |
3.48e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 66.59 E-value: 3.48e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495051738 12 YLLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFG--IYQKDSGSILFQGKEI 77
Cdd:CHL00131 6 PILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESI 73
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-236 |
3.51e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 68.70 E-value: 3.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 3 SNNTQSSGEYLLEMTNINKSFPG--VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFH 80
Cdd:PRK11160 328 TTSTAAADQVSLTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADY 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 81 SaKEALENGISMVHQELNLvLQRSVMDNMWLGRyPTKgvfvDQEKMY-------LDTKAIFDE-LDIDIDPKARvgTLSV 152
Cdd:PRK11160 408 S-EAALRQAISVVSQRVHL-FSATLRDNLLLAA-PNA----SDEALIevlqqvgLEKLLEDDKgLNAWLGEGGR--QLSG 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 153 SQMQMIEIAKAFSYDAKIVIMDEPTSSL---TEKEVNHLfkiirkLKERGCG--IVYISHKMEEIFQLcDEITILRDGQW 227
Cdd:PRK11160 479 GEQRRLGIARALLHDAPLLLLDEPTEGLdaeTERQILEL------LAEHAQNktVLMITHRLTGLEQF-DRICVMDNGQI 551
|
....*....
gi 495051738 228 IATQSLEGL 236
Cdd:PRK11160 552 IEQGTHQEL 560
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
277-482 |
3.98e-12 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 65.82 E-value: 3.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 277 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHG----KKINNHSANEAINNGfalvteeRRSTGI 352
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlvpwKRRKKFLRRIGVVFG-------QKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 353 YaylDI----GFNsLISNIRNykskiglLDNSRMKSDTQWVIDSMRVkTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEIL 428
Cdd:cd03267 108 W---DLpvidSFY-LLAAIYD-------LPPARFKKRLDELSELLDL-EELLDTPVRQLSLGQRMRAEIAAALLHEPEIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495051738 429 MLDEPTRGIDVGAKFEIYQLIAEL-AKKGKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:cd03267 176 FLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKG 230
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
266-484 |
4.42e-12 |
|
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: 65.82 E-value: 4.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 266 LEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANEAiNNGF--- 340
Cdd:cd03296 3 IEVRNVSKRfgDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER-NVGFvfq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 341 --ALVteeRRSTgiyAYLDIGFNSLISNIRNYKSKiglldnSRMKSDTQWVIDSMRVKTPGHR--TQigsLSGGNQQKVI 416
Cdd:cd03296 82 hyALF---RHMT---VFDNVAFGLRVKPRSERPPE------AEIRAKVHELLKLVQLDWLADRypAQ---LSGGQRQRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495051738 417 IGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-GKGIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
266-484 |
4.53e-12 |
|
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: 66.05 E-value: 4.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 266 LEVRNLtSLRQPS----IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINN--HSANEA---- 335
Cdd:cd03256 1 IEVENL-SKTYPNgkkaLKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlkGKALRQlrrq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 336 ---INNGFALVteERRS------TGIYAYLDI-----GFNSLISNIRNYK--SKIGLLDNSRMKSDTqwvidsmrvktpg 399
Cdd:cd03256 80 igmIFQQFNLI--ERLSvlenvlSGRLGRRSTwrslfGLFPKEEKQRALAalERVGLLDKAYQRADQ------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 400 hrtqigsLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKgKGI-IIISSEMPEL-LGITDRIL 477
Cdd:cd03256 145 -------LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINRE-EGItVIVSLHQVDLaREYADRIV 216
|
....*..
gi 495051738 478 VMSNGLV 484
Cdd:cd03256 217 GLKDGRI 223
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
405-484 |
4.72e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 67.21 E-value: 4.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 405 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGK-GIIIISSEMPELLGITDRILVMSNGL 483
Cdd:PRK11144 127 GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINiPILYVSHSLDEILRLADRVVVLEQGK 206
|
.
gi 495051738 484 V 484
Cdd:PRK11144 207 V 207
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
265-506 |
4.81e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 66.25 E-value: 4.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 265 ILEVRNLtSLRQP----SIRDVSFDLHKGEILGIAGLVGAKRTdiveTLF----GIREKSGGTISLHGKKI--NNHSANE 334
Cdd:PRK13639 1 ILETRDL-KYSYPdgteALKGINFKAEKGEMVALLGPNGAGKS----TLFlhfnGILKPTSGEVLIKGEPIkyDKKSLLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 335 AI-----------NNGFALVTEErrstgiyaylDIGFNSLisNIRNYKSKIglldNSRMKSDTQWVIDSMRVKTPGHRtq 403
Cdd:PRK13639 76 VRktvgivfqnpdDQLFAPTVEE----------DVAFGPL--NLGLSKEEV----EKRVKEALKAVGMEGFENKPPHH-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 404 igsLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNG- 482
Cdd:PRK13639 138 ---LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGk 214
|
250 260
....*....|....*....|....
gi 495051738 483 LVSGIVDTKTTTQNEILRLASLHL 506
Cdd:PRK13639 215 IIKEGTPKEVFSDIETIRKANLRL 238
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
13-231 |
5.56e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 66.25 E-value: 5.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFPGV---------KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDF--HS 81
Cdd:PRK10419 3 LLNVSGLSHHYAHGglsgkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 82 AKEALENGISMVHQE-LNLV-LQRSVmdnMWLGRYPTKGVF-VDQEKMYLDTKAIFDELDIDI-DPKARVGTLSVSQMQM 157
Cdd:PRK10419 83 QRKAFRRDIQMVFQDsISAVnPRKTV---REIIREPLRHLLsLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495051738 158 IEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWIATQ 231
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQ 234
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
404-482 |
5.96e-12 |
|
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: 65.49 E-value: 5.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 404 IGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKG-KGIIIIS---SEMPEllGITdRILVM 479
Cdd:COG1119 140 FGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVThhvEEIPP--GIT-HVLLL 216
|
...
gi 495051738 480 SNG 482
Cdd:COG1119 217 KDG 219
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-209 |
6.34e-12 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 65.83 E-value: 6.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 4 NNTQSSGEYLLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIY-----QKDSGSILFQGKEId 78
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlipgARVEGEILLDGEDI- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 79 fHSAK---EALENGISMVHQELNLvLQRSVMDNMWLG----RYPTKGVfVDQ--EKmYLDTKAIFDELdididpKARVGT 149
Cdd:COG1117 81 -YDPDvdvVELRRRVGMVFQKPNP-FPKSIYDNVAYGlrlhGIKSKSE-LDEivEE-SLRKAALWDEV------KDRLKK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495051738 150 ----LSVSQMQMIEIAKAFSYDAKIVIMDEPTSSL----TEkevnhlfKI---IRKLKERgCGIVYISHKM 209
Cdd:COG1117 151 salgLSGGQQQRLCIARALAVEPEVLLMDEPTSALdpisTA-------KIeelILELKKD-YTIVIVTHNM 213
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-77 |
6.67e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 65.88 E-value: 6.67e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495051738 14 LEMTNINKSF-PG----VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI 77
Cdd:COG1101 2 LELKNLSKTFnPGtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV 70
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
14-228 |
8.74e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 67.35 E-value: 8.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPG--VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKeALENGIS 91
Cdd:PRK11176 342 IEFRNVTFTYPGkeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLA-SLRNQVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 92 MVHQELNLvLQRSVMDNMwlgRYPTKGVFVDQE-----KMYLDTKAIfDELDIDIDpkARVG----TLSVSQMQMIEIAK 162
Cdd:PRK11176 421 LVSQNVHL-FNDTIANNI---AYARTEQYSREQieeaaRMAYAMDFI-NKMDNGLD--TVIGengvLLSGGQRQRIAIAR 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495051738 163 AFSYDAKIVIMDEPTSSL-TEKEvNHLFKIIRKLKERGCGIVyISHKMEEIFQlCDEITILRDGQWI 228
Cdd:PRK11176 494 ALLRDSPILILDEATSALdTESE-RAIQAALDELQKNRTSLV-IAHRLSTIEK-ADEILVVEDGEIV 557
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
13-226 |
1.01e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 67.04 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFPGVK-----------ALDNVNLKVRPHSIHALMGENGAGKST----LLKCLfgiyqKDSGSILFQGKEI 77
Cdd:PRK15134 275 LLDVEQLQVAFPIRKgilkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 78 DFHSAKEAL--ENGISMVHQELNLVL--QRSVMDNMWLG---RYPTKGVFVDQEKMyldtKAIFDELDIDIDPKARV-GT 149
Cdd:PRK15134 350 HNLNRRQLLpvRHRIQVVFQDPNSSLnpRLNVLQIIEEGlrvHQPTLSAAQREQQV----IAVMEEVGLDPETRHRYpAE 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495051738 150 LSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQ 226
Cdd:PRK15134 426 FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGE 503
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
266-484 |
1.22e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 66.40 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 266 LEVRNLTSLR--QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANEAinngfalv 343
Cdd:PRK09536 4 IDVSDLSVEFgdTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAA-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 344 teERRSTGIYAYLDIGFNSLISNI----RN-YKSKIGLLDNSrmksDTQWVIDSM-RVKTPGHRTQ-IGSLSGGNQQKVI 416
Cdd:PRK09536 76 --SRRVASVPQDTSLSFEFDVRQVvemgRTpHRSRFDTWTET----DRAAVERAMeRTGVAQFADRpVTSLSGGERQRVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495051738 417 IGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
24-225 |
1.35e-11 |
|
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: 64.27 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 24 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEA-LENGISMVH-QELNLVL 101
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrSRNRYSVAYaAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 102 QRSVMDNMWLGRYPTKgvfvDQEKMYLDTKAIfdELDIDIDP---KARVG----TLSVSQMQMIEIAKAFSYDAKIVIMD 174
Cdd:cd03290 92 NATVEENITFGSPFNK----QRYKAVTDACSL--QPDIDLLPfgdQTEIGergiNLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495051738 175 EPTSSLTEKEVNHLFK--IIRKLKERGCGIVYISHKMEEIFQlCDEITILRDG 225
Cdd:cd03290 166 DPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
21-228 |
1.39e-11 |
|
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: 63.82 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 21 KSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGI---YQKDSGSILFQGkeidfHSAKEALEngismvhqel 97
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegNVSVEGDIHYNG-----IPYKEFAE---------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 98 nlvlqrsvmdnmwlgRYPTKGVFVDQEKMYLDTKAIFDELDIDIDPK--ARVGTLSVSQMQMIEIAKAFSYDAKIVIMDE 175
Cdd:cd03233 80 ---------------KYPGEIIYVSEEDVHFPTLTVRETLDFALRCKgnEFVRGISGGERKRVSIAEALVSRASVLCWDN 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495051738 176 PTSSLTEKEVNHLFKIIRKL--KERGCGIVYISHKMEEIFQLCDEITILRDGQWI 228
Cdd:cd03233 145 STRGLDSSTALEILKCIRTMadVLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
276-484 |
1.49e-11 |
|
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: 64.17 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 276 QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNhsaneainngfalVTEE--RRSTGIY 353
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIRE-------------VTLDslRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 354 AYLDIGFNSLIS-NIRnYkskiGLLDnsrmKSDTQWV-------IDSMRVKTP-GHRTQIGS----LSGGNQQKVIIGRW 420
Cdd:cd03253 81 PQDTVLFNDTIGyNIR-Y----GRPD----ATDEEVIeaakaaqIHDKIMRFPdGYDTIVGErglkLSGGEKQRVAIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495051738 421 LLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKGKGIIIISSEMPELLGiTDRILVMSNGLV 484
Cdd:cd03253 152 ILKNPPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIVN-ADKIIVLKDGRI 213
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
226-482 |
1.81e-11 |
|
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: 66.96 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 226 QWIATQSLEGL-DMDKIIAmmvgrSLNQRFPDRENKPGevILEVRNLTSL----RQPSIRDVSFDLHKGEILGIAGLVGA 300
Cdd:TIGR01257 1904 RWIAEPAKEPIfDEDDDVA-----EERQRIISGGNKTD--ILRLNELTKVysgtSSPAVDRLCVGVRPGECFGLLGVNGA 1976
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 301 KRTDIVETLFGIREKSGGTISLHGKKINNHSANEAINNGFA--------LVTEeRRSTGIYAYLdigfnslisniRNYKS 372
Cdd:TIGR01257 1977 GKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCpqfdaiddLLTG-REHLYLYARL-----------RGVPA 2044
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 373 KiglldnsRMKSDTQWVIDSMRVKTPGHRTQiGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAEL 452
Cdd:TIGR01257 2045 E-------EIEKVANWSIQSLGLSLYADRLA-GTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSI 2116
|
250 260 270
....*....|....*....|....*....|
gi 495051738 453 AKKGKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:TIGR01257 2117 IREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
26-225 |
2.89e-11 |
|
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: 63.06 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 26 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKD---SGSILFQGKEIDFHSAKEAlengISMVHQELNLVLQ 102
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPDQFQKC----VAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 103 RSV------MDNMWLGRYPTKGVfvdQEKMyldtKAIFDELDIDIDPKA--RVGTLSVSQMQMIEIAKAFSYDAKIVIMD 174
Cdd:cd03234 96 LTVretltyTAILRLPRKSSDAI---RKKR----VEDVLLRDLALTRIGgnLVKGISGGERRRVSIAVQLLWDPKVLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495051738 175 EPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHK-MEEIFQLCDEITILRDG 225
Cdd:cd03234 169 EPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQpRSDLFRLFDRILLLSSG 220
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
261-463 |
3.56e-11 |
|
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: 65.46 E-value: 3.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 261 PGEVILEVRNLTSLR---QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGkkINNHSANEAIN 337
Cdd:TIGR02868 330 LGKPTLELRDLSAGYpgaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDG--VPVSSLDQDEV 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 338 NGFALVTEERrstgiyAYL---DIGFNSLISN-------IRNYKSKIGLLDnsrmksdtqWVidsmRVKTPGHRTQIG-- 405
Cdd:TIGR02868 408 RRRVSVCAQD------AHLfdtTVRENLRLARpdatdeeLWAALERVGLAD---------WL----RALPDGLDTVLGeg 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 406 --SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAElAKKGKGIIIIS 463
Cdd:TIGR02868 469 gaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLIT 527
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
29-225 |
4.00e-11 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 62.26 E-value: 4.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGiyQKDSGSIlfqgkeidfhsakealENGISMVHQELNLVLQRSVMdn 108
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVI----------------TGEILINGRPLDKNFQRSTG-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 109 mwlgryptkgvFVDQEKMYLDTKAIFDELDIdidpKARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHL 188
Cdd:cd03232 83 -----------YVEQQDVHSPNLTVREALRF----SALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNI 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 495051738 189 FKIIRKLKERGCGIV-YISHKMEEIFQLCDEITILRDG 225
Cdd:cd03232 148 VRFLKKLADSGQAILcTIHQPSASIFEKFDRLLLLKRG 185
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
266-489 |
4.13e-11 |
|
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: 62.49 E-value: 4.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 266 LEVRNLT------SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTdiveTLF----GIREKSGGTISLHGKKINNHSAnea 335
Cdd:cd03293 1 LEVRNVSktygggGGAVTALEDISLSVEEGEFVALVGPSGCGKS----TLLriiaGLERPTSGEVLVDGEPVTGPGP--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 336 innGFALVTEErrstgiYAYLDigFNSLISNIRnykskIGLLDNSRMKSDTQWVIDSM--RVKTPGHRTQ-IGSLSGGNQ 412
Cdd:cd03293 74 ---DRGYVFQQ------DALLP--WLTVLDNVA-----LGLELQGVPKAEARERAEELleLVGLSGFENAyPHQLSGGMR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 413 QKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKGKGIIIISSEMPELLGITDRILVMSN--GLVSGIVD 489
Cdd:cd03293 138 QRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAEVE 217
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
9-225 |
4.68e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 65.52 E-value: 4.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 9 SGEYLLEMTNINKSFPgVKA-----LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGiyQKDSGSILFQGKEIDFHSAK 83
Cdd:TIGR00956 755 SGEDIFHWRNLTYEVK-IKKekrviLNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVITGGDRLVNGRPLD 831
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 84 EALENGISMVHQELNLVLQRSVMDNMWLG---RYPTKgvFVDQEKM-YLDtkAIFDELDIDIDPKARVGT----LSVSQM 155
Cdd:TIGR00956 832 SSFQRSIGYVQQQDLHLPTSTVRESLRFSaylRQPKS--VSKSEKMeYVE--EVIKLLEMESYADAVVGVpgegLNVEQR 907
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495051738 156 QMIEIAKAFSYDAK-IVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKME-EIFQLCDEITILRDG 225
Cdd:TIGR00956 908 KRLTIGVELVAKPKlLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSaILFEEFDRLLLLQKG 979
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
276-482 |
4.83e-11 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 65.19 E-value: 4.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 276 QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANEAINNgFALVTEErrstgiyAY 355
Cdd:COG1132 353 RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQ-IGVVPQD-------TF 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 356 LdigFN-SLISNIRnykskIGLLDNSRmksdtQWVIDSMRV--------KTP-GHRTQIG----SLSGGNQQKVIIGRWL 421
Cdd:COG1132 425 L---FSgTIRENIR-----YGRPDATD-----EEVEEAAKAaqahefieALPdGYDTVVGergvNLSGGQRQRIAIARAL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495051738 422 LTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKGKGIIIIS---SempellgiT----DRILVMSNG 482
Cdd:COG1132 492 LKDPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAhrlS--------TirnaDRILVLDDG 550
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
276-474 |
5.45e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 63.13 E-value: 5.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 276 QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSG-----GTISLHGKKINNHSAN-EAINNGFALVTEERRS 349
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVNlNRLRRQVSMVHPKPNL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 350 TGIYAYLDIGFNSLISNIRNyKSKIGLLDNSRMKSDTQWviDSMRVKTpgHRTQIgSLSGGNQQKVIIGRWLLTQPEILM 429
Cdd:PRK14258 100 FPMSVYDNVAYGVKIVGWRP-KLEIDDIVESALKDADLW--DEIKHKI--HKSAL-DLSGGQQQRLCIARALAVKPKVLL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495051738 430 LDEPTRGIDVGAKFEIYQLIAELAKKGK-GIIIISSEMPELLGITD 474
Cdd:PRK14258 174 MDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNLHQVSRLSD 219
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
284-484 |
6.21e-11 |
|
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: 62.13 E-value: 6.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 284 FDLH--KGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKkinNHSANEAINNGFALVTEErrsTGIYAYLDIGFN 361
Cdd:cd03298 17 FDLTfaQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV---DVTAAPPADRPVSMLFQE---NNLFAHLTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 362 slisnirnykskIGLLDNSRMKSDTQwviDSMRVKTPGHRTQI--------GSLSGGNQQKVIIGRWLLTQPEILMLDEP 433
Cdd:cd03298 91 ------------VGLGLSPGLKLTAE---DRQAIEVALARVGLaglekrlpGELSGGERQRVALARVLVRDKPVLLLDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495051738 434 TRGIDVGAKFEIYQLIAEL-AKKGKGIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:cd03298 156 FAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
13-235 |
7.52e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 62.14 E-value: 7.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFPGVK----ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHS--AKEAL 86
Cdd:PRK11629 5 LLQCDNLCKRYQEGSvqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 87 ENG-ISMVHQELNLVLQRSVMDN----MWLGRYPTKGVfvdQEKMYLDTKAIfdelDIDIDPKARVGTLSVSQMQMIEIA 161
Cdd:PRK11629 85 RNQkLGFIYQFHHLLPDFTALENvampLLIGKKKPAEI---NSRALEMLAAV----GLEHRANHRPSELSGGERQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495051738 162 KAFSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLKER-GCGIVYISHKMEEIFQLCDEITiLRDGQWIATQSLEG 235
Cdd:PRK11629 158 RALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLqGTAFLVVTHDLQLAKRMSRQLE-MRDGRLTAELSLMG 231
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
266-482 |
7.79e-11 |
|
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: 60.79 E-value: 7.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 266 LEVRNLT----SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKInnHSANEAINNGFA 341
Cdd:cd03247 1 LSINNVSfsypEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV--SDLEKALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 342 LVTEErrstgiyAYLdigFN-SLISNIrnykskiglldnsrmksdtqwvidsmrvktpGHRtqigsLSGGNQQKVIIGRW 420
Cdd:cd03247 79 VLNQR-------PYL---FDtTLRNNL-------------------------------GRR-----FSGGERQRLALARI 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495051738 421 LLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKGKGIIIISSempELLGIT--DRILVMSNG 482
Cdd:cd03247 113 LLQDAPIVLLDEPTVGLDPITERQLLSLIFEVL-KDKTLIWITH---HLTGIEhmDKILFLENG 172
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
277-484 |
7.91e-11 |
|
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: 62.10 E-value: 7.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 277 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSaNEAINNGFALVTEERRSTGiyayl 356
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE-HKYLHSKVSLVGQEPVLFA----- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 357 digfNSLISNIrnyksKIGLLDNSRM-------KSDTQWVIDSMRvktPGHRTQIGS----LSGGNQQKVIIGRWLLTQP 425
Cdd:cd03248 102 ----RSLQDNI-----AYGLQSCSFEcvkeaaqKAHAHSFISELA---SGYDTEVGEkgsqLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495051738 426 EILMLDEPTRGIDVGAKFEIYQLIAElAKKGKGIIIISSEMpELLGITDRILVMSNGLV 484
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQALYD-WPERRTVLVIAHRL-STVERADQILVLDGGRI 226
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
13-208 |
8.66e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.50 E-value: 8.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfhsakealeNGISM 92
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK---------KDLCT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 93 VHQELNLVLQRSVMD-NMWLgryptkgvfvdQEKMYLDTKaiFDELDIDIDPKARV-----------GTLSVSQMQMIEI 160
Cdd:PRK13540 72 YQKQLCFVGHRSGINpYLTL-----------RENCLYDIH--FSPGAVGITELCRLfslehlidypcGLLSSGQKRQVAL 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495051738 161 AKAFSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHK 208
Cdd:PRK13540 139 LRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
266-467 |
9.95e-11 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 61.35 E-value: 9.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 266 LEVRNLTSLR--QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKInnHSANEAINNGFALV 343
Cdd:cd03231 1 LEADELTCERdgRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL--DFQRDSIARGLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 344 TEErrsTGIYAYLdigfnSLISNIRNYKSkigllDNSRmksDTQW-VIDSMRVKTPGHRTqIGSLSGGNQQKVIIGRWLL 422
Cdd:cd03231 79 GHA---PGIKTTL-----SVLENLRFWHA-----DHSD---EQVEeALARVGLNGFEDRP-VAQLSAGQQRRVALARLLL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495051738 423 TQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGkGIIIISSEMP 467
Cdd:cd03231 142 SGRPLWILDEPTTALDKAGVARFAEAMAGHCARG-GMVVLTTHQD 185
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
277-495 |
1.06e-10 |
|
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: 61.86 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 277 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANEaINNGFALVTEErrstgiyAYL 356
Cdd:cd03251 16 PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAS-LRRQIGLVSQD-------VFL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 357 digFNSLI-SNIRnykskIGLLDNSRMKsdtqwVIDSMRV--------KTP-GHRTQIGS----LSGGNQQKVIIGRWLL 422
Cdd:cd03251 88 ---FNDTVaENIA-----YGRPGATREE-----VEEAARAanahefimELPeGYDTVIGErgvkLSGGQRQRIAIARALL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495051738 423 TQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKGKGIIIISSEMPELLGItDRILVMSNGlvsGIVDTKTTTQ 495
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRLSTIENA-DRIVVLEDG---KIVERGTHEE 222
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
13-180 |
1.10e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 62.25 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKE---IDFHSAKEA---- 85
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlRDLYALSEAerrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 86 ---LENGIsmVHQ--ELNLVLQRSVMDN-----MWLG--RYptkGVFVDQEKMYLDTKAIfDELDIDIDPkarvGTLSVS 153
Cdd:PRK11701 86 llrTEWGF--VHQhpRDGLRMQVSAGGNigerlMAVGarHY---GDIRATAGDWLERVEI-DAARIDDLP----TTFSGG 155
|
170 180
....*....|....*....|....*..
gi 495051738 154 QMQMIEIAKAFSYDAKIVIMDEPTSSL 180
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGL 182
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
31-234 |
1.14e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 62.97 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 31 NVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeIDFHSakealENGISM---------VHQELNLVL 101
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGR-VLFDA-----EKGICLppekrrigyVFQDARLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 102 QRSVMDNMwlgRYPTKGVFVDQekmyldtkaiFDELD--IDIDP--KARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPT 177
Cdd:PRK11144 90 HYKVRGNL---RYGMAKSMVAQ----------FDKIValLGIEPllDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495051738 178 SSLT---EKEV-NHLFKIIRKLKergCGIVYISHKMEEIFQLCDEITILRDGQWIATQSLE 234
Cdd:PRK11144 157 ASLDlprKRELlPYLERLAREIN---IPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLE 214
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-228 |
1.18e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 61.78 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 11 EYLLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQ-----KDSGSILFQGKEIdFHSAKEA 85
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNI-YSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 86 LE--NGISMVHQELNLVLQRSVMDNMWLGRYPTKGVFVDQE-----KMYLDTKAIFDELDIDIDPKArvGTLSVSQMQMI 158
Cdd:PRK14267 81 IEvrREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKEldervEWALKKAALWDEVKDRLNDYP--SNLSGGQRQRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 159 EIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLKERgCGIVYISHKMEEIFQLCDEITILRDGQWI 228
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLI 227
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
263-482 |
1.21e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 62.34 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 263 EVILEVRNLT----SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSaneainn 338
Cdd:PRK13635 3 EEIIRVEHISfrypDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEET------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 339 gfalVTEERRSTGIY------------AYLDIGFNslisnirnykskiglLDNSRMKSDT-----QWVIDSMRVKTPGHR 401
Cdd:PRK13635 76 ----VWDVRRQVGMVfqnpdnqfvgatVQDDVAFG---------------LENIGVPREEmvervDQALRQVGMEDFLNR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 402 tQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKGKGIIIISsempellgIT-------- 473
Cdd:PRK13635 137 -EPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQL-KEQKGITVLS--------IThdldeaaq 206
|
250
....*....|
gi 495051738 474 -DRILVMSNG 482
Cdd:PRK13635 207 aDRVIVMNKG 216
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
277-484 |
1.24e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 62.31 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 277 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANEAINN--GFALVTEERRSTGIYA 354
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKlvGIVFQNPETQFVGRTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 355 YLDIGF---NSLISNIRNYKskigLLDnsRMKSDTQwvIDSMRVKTPGhrtqigSLSGGNQQKVIIGRWLLTQPEILMLD 431
Cdd:PRK13644 96 EEDLAFgpeNLCLPPIEIRK----RVD--RALAEIG--LEKYRHRSPK------TLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495051738 432 EPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPElLGITDRILVMSNGLV 484
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKI 213
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
407-477 |
1.28e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 61.67 E-value: 1.28e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495051738 407 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-GKGIIIISSEMPELLGITDRIL 477
Cdd:PRK09544 121 LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVL 192
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
278-484 |
1.40e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 62.08 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 278 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSaneainngfalVTEERRSTGIYayLD 357
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDN-----------FEKLRKHIGIV--FQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 358 IGFNSLISNIRNYKSKIGLLDNS----RMKSDTQWVI-DSMRVKTPGHRTQigSLSGGNQQKVIIGRWLLTQPEILMLDE 432
Cdd:PRK13648 91 NPDNQFVGSIVKYDVAFGLENHAvpydEMHRRVSEALkQVDMLERADYEPN--ALSGGQKQRVAIAGVLALNPSVIILDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495051738 433 PTRGIDVGAKFEIYQLIAEL-AKKGKGIIIISSEMPELLGiTDRILVMSNGLV 484
Cdd:PRK13648 169 ATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAME-ADHVIVMNKGTV 220
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
29-226 |
1.46e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 62.06 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEaLENGISMVHQEL-NLVLQRSVMD 107
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWD-IRHKIGMVFQNPdNQFVGATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 108 NMWLGrYPTKGVFVDQEKMYLDTK-AIFDELDIDIDPKARvgtLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVN 186
Cdd:PRK13650 102 DVAFG-LENKGIPHEEMKERVNEAlELVGMQDFKEREPAR---LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 495051738 187 HLFKIIRKLKER-GCGIVYISHKMEEIfQLCDEITILRDGQ 226
Cdd:PRK13650 178 ELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQ 217
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
14-238 |
1.63e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 61.62 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILfqGKEIDFHSAKEalenGISMV 93
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL--AGTAPLAEARE----DTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 94 HQELNLVLQRSVMDNMWLGrypTKGVFVDQEKMYLDTKAIFDeldididpkaRVG----TLSVSQMQMIEIAKAFSYDAK 169
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGLG---LKGQWRDAALQALAAVGLAD----------RANewpaALSGGQKQRVALARALIHRPG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495051738 170 IVIMDEP---TSSLTEKEVNHLfkIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWiatqsleGLDM 238
Cdd:PRK11247 154 LLLLDEPlgaLDALTRIEMQDL--IESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI-------GLDL 216
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
250-482 |
2.19e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 62.16 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 250 LNQRFPDRENKPGEV---ILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHG 324
Cdd:PRK11607 1 MNDAIPRPQAKTRKAltpLLEIRNLTKSfdGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 325 KKINNHSA-NEAINNGFalvteerRSTGIYAYL----DIGFNslISNIRNYKSKIglldNSRMKSDTQWVIDSMRVKTPG 399
Cdd:PRK11607 81 VDLSHVPPyQRPINMMF-------QSYALFPHMtveqNIAFG--LKQDKLPKAEI----ASRVNEMLGLVHMQEFAKRKP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 400 HRtqigsLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEI-YQLIAELAKKGKGIIIISSEMPELLGITDRILV 478
Cdd:PRK11607 148 HQ-----LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAI 222
|
....
gi 495051738 479 MSNG 482
Cdd:PRK11607 223 MNRG 226
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
279-484 |
2.28e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 63.14 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 279 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKS---GGTISLHGKKINnhsaneainngfalvteERRSTGIYAY 355
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPID-----------------AKEMRAISAY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 356 L---DIGFNSLisNIRNYKSKIGLLdnsRMKSDT---------QWVIDSMRVKTPGHrTQIG------SLSGGNQQKVII 417
Cdd:TIGR00955 104 VqqdDLFIPTL--TVREHLMFQAHL---RMPRRVtkkekrervDEVLQALGLRKCAN-TRIGvpgrvkGLSGGERKRLAF 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495051738 418 GRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIII----SSEMPELLgitDRILVMSNGLV 484
Cdd:TIGR00955 178 ASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTihqpSSELFELF---DKIILMAEGRV 245
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
24-236 |
2.53e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.46 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 24 PGVK-ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfhsakeaLENGISMVHQELNLVLQ 102
Cdd:PLN03232 1246 PGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDV--------AKFGLTDLRRVLSIIPQ 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 103 RSVMDNMWL-------GRYPTKGVFVDQEKMYLdtKAIFDELDIDIDPKARVG--TLSVSQMQMIEIAKAFSYDAKIVIM 173
Cdd:PLN03232 1318 SPVLFSGTVrfnidpfSEHNDADLWEALERAHI--KDVIDRNPFGLDAEVSEGgeNFSVGQRQLLSLARALLRRSKILVL 1395
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495051738 174 DEPTSSLTEKEVNHLFKIIRKlKERGCGIVYISHKMEEIFQlCDEITILRDGQWIATQSLEGL 236
Cdd:PLN03232 1396 DEATASVDVRTDSLIQRTIRE-EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQEL 1456
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
10-207 |
2.89e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 62.65 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 10 GEYLLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFqGKEIDFHS---AKEAL 86
Cdd:TIGR03719 319 GDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLAYvdqSRDAL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 87 ENGISmVHQELN------LVLQRSVMDNMWLGRYPTKGvfVDQEKmyldtkaifdeldididpkaRVGTLSVSQMQMIEI 160
Cdd:TIGR03719 398 DPNKT-VWEEISggldiiKLGKREIPSRAYVGRFNFKG--SDQQK--------------------KVGQLSGGERNRVHL 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495051738 161 AKAFSYDAKIVIMDEPTSSLtekEVNHLfkiiRKLKER-----GCGIVyISH 207
Cdd:TIGR03719 455 AKTLKSGGNVLLLDEPTNDL---DVETL----RALEEAllnfaGCAVV-ISH 498
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
27-247 |
3.83e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 60.80 E-value: 3.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 27 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFH-SAKE--ALENGISMVHQ--ELNLvL 101
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGkKNKKlkPLRKKVGIVFQfpEHQL-F 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 102 QRSVMDNMWLGryPTKgvF-VDQEKMYLDTKAIFDELDIDIDPKARVG-TLSVSQMQMIEIAKAFSYDAKIVIMDEPTSS 179
Cdd:PRK13634 100 EETVEKDICFG--PMN--FgVSEEDAKQKAREMIELVGLPEELLARSPfELSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495051738 180 LTEKEVNHLFKIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQSLEGL--DMDKIIAMMVG 247
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIfaDPDELEAIGLD 246
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
261-482 |
3.93e-10 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 60.49 E-value: 3.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 261 PGEVILEVRNLT------SLRQPSIRDVSFDLHKGE---ILG------------IAGLVGAkrtdivetlfgirekSGGT 319
Cdd:COG1116 3 AAAPALELRGVSkrfptgGGGVTALDDVSLTVAAGEfvaLVGpsgcgkstllrlIAGLEKP---------------TSGE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 320 ISLHGKKINNHSANEAI---------------NNGFAL-----VTEERRSTgIYAYLDigfnslisnirnyksKIGLLD- 378
Cdd:COG1116 68 VLVDGKPVTGPGPDRGVvfqepallpwltvldNVALGLelrgvPKAERRER-ARELLE---------------LVGLAGf 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 379 -NSRmksdtqwvidsmrvktPGhrtqigSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKG 456
Cdd:COG1116 132 eDAY----------------PH------QLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETG 189
|
250 260
....*....|....*....|....*...
gi 495051738 457 KGIIIISSEMPE--LLGitDRILVMSNG 482
Cdd:COG1116 190 KTVLFVTHDVDEavFLA--DRVVVLSAR 215
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
266-500 |
4.43e-10 |
|
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: 60.01 E-value: 4.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 266 LEVRNLTSLR---QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSaneainngfal 342
Cdd:cd03295 1 IEFENVTKRYgggKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQD----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 343 VTEERRSTGiYAYLDIGFNSLISNIRNYKSKIGLLDNSRMKSDTqwvidsmRVKT--------PGHRTQ--IGSLSGGNQ 412
Cdd:cd03295 70 PVELRRKIG-YVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRE-------RADEllalvgldPAEFADryPHELSGGQQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 413 QKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-GKGIIIISSEMPELLGITDRILVMSNGLVSgIVDTK 491
Cdd:cd03295 142 QRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIV-QVGTP 220
|
....*....
gi 495051738 492 tttqNEILR 500
Cdd:cd03295 221 ----DEILR 225
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
14-70 |
4.93e-10 |
|
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: 57.84 E-value: 4.93e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 495051738 14 LEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSI 70
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV 57
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
265-484 |
5.90e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 60.03 E-value: 5.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 265 ILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANEaINNGFAL 342
Cdd:PRK11231 2 TLRTENLTVGygTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ-LARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 343 -----VTEErrstgiyaylDIGFNSLISNIRN-YKSKIGlldnsRMKSDtqwviDSMRVKTPGHRTQI--------GSLS 408
Cdd:PRK11231 81 lpqhhLTPE----------GITVRELVAYGRSpWLSLWG-----RLSAE-----DNARVNQAMEQTRInhladrrlTDLS 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495051738 409 GGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:PRK11231 141 GGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHV 216
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
26-242 |
6.83e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 60.25 E-value: 6.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 26 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSI----LFQGKEIDFHSAKEA-----------LENGI 90
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELITNpyskkiknfkeLRRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 91 SMVHQ--ELNL---VLQRSVM---DNMWLGRYPTKgvfvDQEKMYLDtKAIFDELDIDIDPKArvgtLSVSQMQMIEIAK 162
Cdd:PRK13631 119 SMVFQfpEYQLfkdTIEKDIMfgpVALGVKKSEAK----KLAKFYLN-KMGLDDSYLERSPFG----LSGGQKRRVAIAG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 163 AFSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQSLEGLDMDKII 242
Cdd:PRK13631 190 ILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQHI 269
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
266-482 |
6.96e-10 |
|
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: 61.27 E-value: 6.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 266 LEVRNLT----SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSAnEAINNGFA 341
Cdd:TIGR02203 331 VEFRNVTfrypGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTL-ASLRRQVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 342 LVTEErrstgiyAYLdigFNSLISNIRNYkSKIGLLDNSRMKS-----DTQWVIDSMrvktP-GHRTQIGS----LSGGN 411
Cdd:TIGR02203 410 LVSQD-------VVL---FNDTIANNIAY-GRTEQADRAEIERalaaaYAQDFVDKL----PlGLDTPIGEngvlLSGGQ 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495051738 412 QQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKGKGIIIISSEMPELLGiTDRILVMSNG 482
Cdd:TIGR02203 475 RQRLAIARALLKDAPILILDEATSALDNESERLVQAALERL-MQGRTTLVIAHRLSTIEK-ADRIVVMDDG 543
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
9-226 |
7.43e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 60.82 E-value: 7.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 9 SGEYLLEMTNINKsfpGVKaldNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALE- 87
Cdd:PRK10070 30 SKEQILEKTGLSL---GVK---DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 88 --NGISMVHQELNLVLQRSVMDNMWLGRYPTKGVFVDQEKMYLDTkaiFDELDIDIDPKARVGTLSVSQMQMIEIAKAFS 165
Cdd:PRK10070 104 rrKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDA---LRQVGLENYAHSYPDELSGGMRQRVGLARALA 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495051738 166 YDAKIVIMDEPTSSL-----TEKEvNHLFKIIRKLKERgcgIVYISHKMEEIFQLCDEITILRDGQ 226
Cdd:PRK10070 181 INPDILLMDEAFSALdplirTEMQ-DELVKLQAKHQRT---IVFISHDLDEAMRIGDRIAIMQNGE 242
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
281-482 |
7.71e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 59.26 E-value: 7.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 281 DVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINnHSANEAINNGFALvteeRRSTG-------IY 353
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFD-FSKTPSDKAIREL----RRNVGmvfqqynLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 354 AYLdigfnSLISNIRNYKSKIGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIgSLSGGNQQKVIIGRWLLTQPEILMLDEP 433
Cdd:PRK11124 95 PHL-----TVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPL-HLSGGQQQRVAIARALMMEPQVLLFDEP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495051738 434 TRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK11124 169 TAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENG 217
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
277-482 |
8.43e-10 |
|
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: 58.78 E-value: 8.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 277 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANEaINNGFALVTEErrsTGIYAyl 356
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKS-LRSMIGVVLQD---TFLFS-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 357 digfNSLISNIRnykskiglLDNSRMKsDTQWVIDSMRVK--------TPGHRTQIG----SLSGGNQQKVIIGRWLLTQ 424
Cdd:cd03254 91 ----GTIMENIR--------LGRPNAT-DEEVIEAAKEAGahdfimklPNGYDTVLGenggNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495051738 425 PEILMLDEPTRGIDVGAKFEIYQLIAELaKKGKGIIIISSEMPELLGiTDRILVMSNG 482
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKN-ADKILVLDDG 213
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
41-229 |
8.59e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.18 E-value: 8.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 41 IHaLMGENGAGKSTLLKCLFGIYQKdSGSILFQGKEIDFHSAKEalengisMVHQELNLVLQRSVMDNM----WLGRYPT 116
Cdd:PRK03695 25 LH-LVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAE-------LARHRAYLSQQQTPPFAMpvfqYLTLHQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 117 KGVFVDQEKMYLDTKAIFDELDidiDPKAR-VGTLSVSQMQMIEIAKAF-------SYDAKIVIMDEPTSSLTEKEVNHL 188
Cdd:PRK03695 96 DKTRTEAVASALNEVAEALGLD---DKLGRsVNQLSGGEWQRVRLAAVVlqvwpdiNPAGQLLLLDEPMNSLDVAQQAAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 495051738 189 FKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIA 229
Cdd:PRK03695 173 DRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLA 213
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
13-95 |
8.99e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 59.03 E-value: 8.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGI--YQKDSGSILFQGKEIDFHSAKEALENGI 90
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
....*
gi 495051738 91 SMVHQ 95
Cdd:PRK09580 81 FMAFQ 85
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
258-479 |
1.05e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 60.11 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 258 ENKpgEVILEVRNLT---SLR-------QPS-----IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISL 322
Cdd:PRK15079 3 EGK--KVLLEVADLKvhfDIKdgkqwfwQPPktlkaVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 323 HGKKINNHSANE--AINNGFALVTEE-------RRSTG-IYA------YLDIGFNSLISNIRNYKSKIGLLDNsrmksdt 386
Cdd:PRK15079 81 LGKDLLGMKDDEwrAVRSDIQMIFQDplaslnpRMTIGeIIAeplrtyHPKLSRQEVKDRVKAMMLKVGLLPN------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 387 qwVIDsmrvKTPgHRtqigsLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-GKGIIIISSE 465
Cdd:PRK15079 154 --LIN----RYP-HE-----FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHD 221
|
250
....*....|....
gi 495051738 466 MPELLGITDRILVM 479
Cdd:PRK15079 222 LAVVKHISDRVLVM 235
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-229 |
1.18e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 59.26 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 11 EYLLEMTNINKSFPGVK--ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfhsakealEN 88
Cdd:PRK13635 3 EEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLS--------EE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 89 GISMVHQELNLVLQRSvmDNMWLGRYPTKGV-F------VDQEKMYLDTKAIFDELDI----DIDPkARvgtLSVSQMQM 157
Cdd:PRK13635 75 TVWDVRRQVGMVFQNP--DNQFVGATVQDDVaFglenigVPREEMVERVDQALRQVGMedflNREP-HR---LSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495051738 158 IEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLK-ERGCGIVYISHKMEEIFQlCDEITILRDGQWIA 229
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKeQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILE 220
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
5-226 |
1.19e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 60.64 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 5 NTQSSGEYLLEMTNINKSFP-----------GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQ 73
Cdd:PRK10261 305 DTVVDGEPILQVRNLVTRFPlrsgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFN 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 74 GKEIDFHSAK--EALENGISMVHQELNLVLQ------RSVMDNMWLGRyptkgvfvdqekmYLDTKAIFDELDIDIDpka 145
Cdd:PRK10261 385 GQRIDTLSPGklQALRRDIQFIFQDPYASLDprqtvgDSIMEPLRVHG-------------LLPGKAAAARVAWLLE--- 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 146 RVGTL-----------SVSQMQMIEIAKAFSYDAKIVIMDEPTSSLtekEVNHLFKIIRKL----KERGCGIVYISHKME 210
Cdd:PRK10261 449 RVGLLpehawryphefSGGQRQRICIARALALNPKVIIADEAVSAL---DVSIRGQIINLLldlqRDFGIAYLFISHDMA 525
|
250
....*....|....*.
gi 495051738 211 EIFQLCDEITILRDGQ 226
Cdd:PRK10261 526 VVERISHRVAVMYLGQ 541
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
265-484 |
1.20e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 59.48 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 265 ILEVRNLtSLRQP----SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINnHSAN------E 334
Cdd:PRK13636 5 ILKVEEL-NYNYSdgthALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKglmklrE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 335 AINNGFALVTEERRSTGIYAylDIGFNSLisNIRNYKSKI-GLLDNSRMKSDtqwvIDSMRVKtPGHrtqigSLSGGNQQ 413
Cdd:PRK13636 83 SVGMVFQDPDNQLFSASVYQ--DVSFGAV--NLKLPEDEVrKRVDNALKRTG----IEHLKDK-PTH-----CLSFGQKK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495051738 414 KVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-GKGIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:PRK13636 149 RVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRV 220
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
279-482 |
1.28e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 58.67 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 279 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHS--ANEAINNgfalvteeRRSTGIYAY- 355
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaAKAELRN--------QKLGFIYQFh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 356 -LDIGFNSLisniRNYKSKIgLLDNSRMKSDTQWVIDSMRVKTPGHRTQ--IGSLSGGNQQKVIIGRWLLTQPEILMLDE 432
Cdd:PRK11629 97 hLLPDFTAL----ENVAMPL-LIGKKKPAEINSRALEMLAAVGLEHRANhrPSELSGGERQRVAIARALVNNPRLVLADE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495051738 433 PTRGIDVGAKFEIYQLIAEL-AKKGKGIIIISSEMpELLGITDRILVMSNG 482
Cdd:PRK11629 172 PTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDL-QLAKRMSRQLEMRDG 221
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
250-482 |
1.29e-09 |
|
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: 61.18 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 250 LNQRFPDRENkPGEVI-LEVRNLTSLRQPSIRD----VSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHG 324
Cdd:TIGR01257 913 INDSFFEREL-PGLVPgVCVKNLVKIFEPSGRPavdrLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG 991
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 325 KKInnHSANEAInngfalvteeRRSTGIYAYLDIGFNSLI--SNIRNYKSKIGlldnsRMKSDTQWVIDSMRVKTPGHRT 402
Cdd:TIGR01257 992 KDI--ETNLDAV----------RQSLGMCPQHNILFHHLTvaEHILFYAQLKG-----RSWEEAQLEMEAMLEDTGLHHK 1054
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 403 ---QIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKGKGIIIISSEMPELLGITDRILVM 479
Cdd:TIGR01257 1055 rneEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAII 1133
|
...
gi 495051738 480 SNG 482
Cdd:TIGR01257 1134 SQG 1136
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
405-484 |
1.55e-09 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 58.47 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 405 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID---VGakfEIYQLIAELAKKGKGIIIISSEMpellG----ITDRIL 477
Cdd:COG1126 135 AQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDpelVG---EVLDVMRDLAKEGMTMVVVTHEM----GfareVADRVV 207
|
....*..
gi 495051738 478 VMSNGLV 484
Cdd:COG1126 208 FMDGGRI 214
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
264-482 |
1.57e-09 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 58.63 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 264 VILEVRNLT-SL-RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANE------- 334
Cdd:PRK13548 1 AMLEARNLSvRLgGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElarrrav 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 335 ---AINNGFALVTEErrstgIYAyldigfnslisnirnykskIGLLDNSRMKSDTQWVIDSMRVKTP----GHRtQIGSL 407
Cdd:PRK13548 81 lpqHSSLSFPFTVEE-----VVA-------------------MGRAPHGLSRAEDDALVAAALAQVDlahlAGR-DYPQL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 408 SGGNQQKVIIGRwLLTQ-------PEILMLDEPTRGIDVGAKFEIYQLIAELAKK-GKGIIIIssempeL--LGIT---- 473
Cdd:PRK13548 136 SGGEQQRVQLAR-VLAQlwepdgpPRWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIVV------LhdLNLAarya 208
|
....*....
gi 495051738 474 DRILVMSNG 482
Cdd:PRK13548 209 DRIVLLHQG 217
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
13-222 |
1.69e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.59 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEidfhsakealenGISM 92
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKL------------RIGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 93 VHQELNL--VLQRSVMDNMWLgRYPTKgvfvdqekmyldtkaifdelDIDIDPK-ARVGT----------LSVSQMQMIE 159
Cdd:PRK09544 72 VPQKLYLdtTLPLTVNRFLRL-RPGTK--------------------KEDILPAlKRVQAghlidapmqkLSGGETQRVL 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495051738 160 IAKAFSYDAKIVIMDEPTSSLtekEVN---HLFKIIRKLK-ERGCGIVYISHKMEEIFQLCDEITIL 222
Cdd:PRK09544 131 LARALLNRPQLLVLDEPTQGV---DVNgqvALYDLIDQLRrELDCAVLMVSHDLHLVMAKTDEVLCL 194
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
279-484 |
1.78e-09 |
|
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: 58.27 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 279 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGkkinnhsaneainNGFALVTEE--RRSTGIYAYL 356
Cdd:cd03252 18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDG-------------HDLALADPAwlRRQVGVVLQE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 357 DIGFN-SLISNI---RNYKSKIGLLDNSRMkSDTQWVIDSMRVktpGHRTQIG----SLSGGNQQKVIIGRWLLTQPEIL 428
Cdd:cd03252 85 NVLFNrSIRDNIalaDPGMSMERVIEAAKL-AGAHDFISELPE---GYDTIVGeqgaGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495051738 429 MLDEPTRGIDVGAKFEIYQLIAELAkKGKGIIIISSEMPELLGiTDRILVMSNGLV 484
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKN-ADRIIVMEKGRI 214
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
407-484 |
1.88e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 58.22 E-value: 1.88e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495051738 407 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
276-484 |
2.02e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 58.48 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 276 QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKIN-NHSANEAINNGFALVTEERRSTGIYA 354
Cdd:PRK13638 14 EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDySKRGLLALRQQVATVFQDPEQQIFYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 355 YLD--IGFNslisnIRNykskIGLLDN--SRMKSDTQWVIDSMRVKtpghRTQIGSLSGGNQQKVIIGRWLLTQPEILML 430
Cdd:PRK13638 94 DIDsdIAFS-----LRN----LGVPEAeiTRRVDEALTLVDAQHFR----HQPIQCLSHGQKKRVAIAGALVLQARYLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495051738 431 DEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:PRK13638 161 DEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQI 214
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
44-207 |
2.50e-09 |
|
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: 57.12 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 44 LMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSakealengiSMVHQELnlvlqrsvmdnMWLGRYP-TKGVFVD 122
Cdd:cd03231 31 VTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQR---------DSIARGL-----------LYLGHAPgIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 123 QEKMYL-----DTKAIFDELDiDID----PKARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFKIIR 193
Cdd:cd03231 91 LENLRFwhadhSDEQVEEALA-RVGlngfEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMA 169
|
170
....*....|....
gi 495051738 194 KLKERGCGIVYISH 207
Cdd:cd03231 170 GHCARGGMVVLTTH 183
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
265-482 |
2.56e-09 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 58.96 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 265 ILEVRNLTsLR---QPSIRDVSFDLHKGEI---LG------------IAGLvgakrtdivETLfgirekSGGTISLHGKK 326
Cdd:COG3842 5 ALELENVS-KRygdVTALDDVSLSIEPGEFvalLGpsgcgkttllrmIAGF---------ETP------DSGRILLDGRD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 327 INNhsaneainngfalVTEERRSTGI----YA---YLD----IGFnslisnirnykskiGL----LDNSRMKSDTQWVID 391
Cdd:COG3842 69 VTG-------------LPPEKRNVGMvfqdYAlfpHLTvaenVAF--------------GLrmrgVPKAEIRARVAELLE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 392 SMRVKTPGHRtQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKgkgiiiissempelLG 471
Cdd:COG3842 122 LVGLEGLADR-YPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRE--------------LG 186
|
250 260
....*....|....*....|....*.
gi 495051738 472 IT---------------DRILVMSNG 482
Cdd:COG3842 187 ITfiyvthdqeealalaDRIAVMNDG 212
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
263-482 |
2.92e-09 |
|
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: 57.44 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 263 EVILEVRNLT---------SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLH--GKKINNHS 331
Cdd:COG4778 2 TTLLEVENLSktftlhlqgGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdGGWVDLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 332 ANEAInngfalVTEERRSTgiyayldIGFNSLISNIRNYKSKI-----GLLDNSRMKSDTQwvidsMRVKTPGHRTQI-- 404
Cdd:COG4778 82 ASPRE------ILALRRRT-------IGYVSQFLRVIPRVSALdvvaePLLERGVDREEAR-----ARARELLARLNLpe 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 405 -------GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRIL 477
Cdd:COG4778 144 rlwdlppATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVV 223
|
....*
gi 495051738 478 VMSNG 482
Cdd:COG4778 224 DVTPF 228
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
407-484 |
3.15e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 58.11 E-value: 3.15e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495051738 407 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAK-KGKGIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:PRK13634 146 LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTHSMEDAARYADQIVVMHKGTV 224
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
407-482 |
3.23e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 57.87 E-value: 3.23e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495051738 407 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELA-KKGKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK13646 146 MSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEG 222
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
13-236 |
3.26e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 58.28 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFPG----VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIyQKDSGSIL---FQGKEIDF-----H 80
Cdd:PRK15093 3 LLDIRNLTIEFKTsdgwVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTadrMRFDDIDLlrlspR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 81 SAKEALENGISMVHQELNLVLQ------RSVMDNM----WLGRYPtkgvfvdQEKMYLDTKAIfdEL--DIDI-DPKARV 147
Cdd:PRK15093 82 ERRKLVGHNVSMIFQEPQSCLDpservgRQLMQNIpgwtYKGRWW-------QRFGWRKRRAI--ELlhRVGIkDHKDAM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 148 GT----LSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKL-KERGCGIVYISHKMEEIFQLCDEITIL 222
Cdd:PRK15093 153 RSfpyeLTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVL 232
|
250
....*....|....
gi 495051738 223 RDGQWIATQSLEGL 236
Cdd:PRK15093 233 YCGQTVETAPSKEL 246
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
407-482 |
3.64e-09 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 57.33 E-value: 3.64e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495051738 407 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:COG4161 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKG 217
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
266-480 |
3.68e-09 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 57.56 E-value: 3.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 266 LEVRNLtSLR-------QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANEAI-- 336
Cdd:COG4525 4 LTVRHV-SVRypgggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGVvf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 337 -------------NNGFAL----VTEERRSTGIYAYLdigfnslisnirnykSKIGLLDNsrmksdtqwvidsmrvktpg 399
Cdd:COG4525 83 qkdallpwlnvldNVAFGLrlrgVPKAERRARAEELL---------------ALVGLADF-------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 400 HRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKGKGIIIISSEMPELLGITDRILV 478
Cdd:COG4525 128 ARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEALFLATRLVV 207
|
..
gi 495051738 479 MS 480
Cdd:COG4525 208 MS 209
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
407-481 |
3.84e-09 |
|
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: 55.62 E-value: 3.84e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495051738 407 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIaelakKGKGIIIIS-SEMPELLGITDRILVMSN 481
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL-----KELGITVISvGHRPSLWKFHDRVLDLDG 162
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
263-499 |
4.25e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 58.51 E-value: 4.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 263 EVILEVRNLTSlrqpSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHG---KKINNHSANEAINNG 339
Cdd:PRK10070 32 EQILEKTGLSL----GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELREVRRKK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 340 FALVTEERRSTGIYAYLD-IGFNSLISNIRNYKSKIGLLDNSRmksdtQWVIDSMRVKTPGHrtqigsLSGGNQQKVIIG 418
Cdd:PRK10070 108 IAMVFQSFALMPHMTVLDnTAFGMELAGINAEERREKALDALR-----QVGLENYAHSYPDE------LSGGMRQRVGLA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 419 RWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKGKGIIIISSEMPELLGITDRILVMSNGLVsgivdTKTTTQNE 497
Cdd:PRK10070 177 RALAINPDILLMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV-----VQVGTPDE 251
|
..
gi 495051738 498 IL 499
Cdd:PRK10070 252 IL 253
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
405-482 |
4.49e-09 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 56.69 E-value: 4.49e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495051738 405 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-GKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:COG3840 128 GQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADG 206
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
8-236 |
4.53e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 57.47 E-value: 4.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 8 SSGEYLLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALE 87
Cdd:PRK11831 2 QSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 88 --NGISMVHQELNLVLQRSVMDNM-WLGRYPTK--------GVFVDQEKMYLDTKAifdeldididpKARVGTLSVSQMQ 156
Cdd:PRK11831 82 vrKRMSMLFQSGALFTDMNVFDNVaYPLREHTQlpapllhsTVMMKLEAVGLRGAA-----------KLMPSELSGGMAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 157 MIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWIATQSLEG 235
Cdd:PRK11831 151 RAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQA 230
|
.
gi 495051738 236 L 236
Cdd:PRK11831 231 L 231
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
275-484 |
4.92e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 58.82 E-value: 4.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 275 RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNhsaneainngfalVTEE--RRSTGI 352
Cdd:PRK13657 347 SRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRT-------------VTRAslRRNIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 353 yAYLDIG-FNSLIS-NIRnykskIGLLDNS----RMKSDTQWVIDSMRVKTPGHRTQIG----SLSGGNQQKVIIGRWLL 422
Cdd:PRK13657 414 -VFQDAGlFNRSIEdNIR-----VGRPDATdeemRAAAERAQAHDFIERKPDGYDTVVGergrQLSGGERQRLAIARALL 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495051738 423 TQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKGKGIIIISSempELLGI--TDRILVMSNGLV 484
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDEL-MKGRTTFIIAH---RLSTVrnADRILVFDNGRV 547
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
277-484 |
5.27e-09 |
|
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: 56.26 E-value: 5.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 277 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANEainngfalVTEERRSTGIyAYL 356
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRA--------IPYLRRKIGV-VFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 357 DigfNSLISNIRNYKS---------KIGLLDNSRMKSDTQWVIDSMRvktpgHRTQIGSLSGGNQQKVIIGRWLLTQPEI 427
Cdd:cd03292 86 D---FRLLPDRNVYENvafalevtgVPPREIRKRVPAALELVGLSHK-----HRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495051738 428 LMLDEPTRGIDVGAKFEIYQLIAELAKKGKgIIIISSEMPELLGITD-RILVMSNGLV 484
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKINKAGT-TVVVATHAKELVDTTRhRVIALERGKL 214
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
281-482 |
5.43e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 57.79 E-value: 5.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 281 DVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANE------------------AINNGFAL 342
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDrkvgfvfqhyalfrhmtvFDNIAFGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 343 VTEERRSTGIYAYLDIGFNSLISNIrnyksKIGLLDNsRMKSdtqwvidsmrvktpghrtqigSLSGGNQQKVIIGRWLL 422
Cdd:PRK10851 100 TVLPRRERPNAAAIKAKVTQLLEMV-----QLAHLAD-RYPA---------------------QLSGGQKQRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495051738 423 TQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGI-IIISSEMPELLGITDRILVMSNG 482
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTsVFVTHDQEEAMEVADRVVVMSQG 213
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
29-207 |
5.58e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.51 E-value: 5.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSakealengismvhqelnlvlQRSVMDN 108
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGR--------------------EASLIDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 109 MWLgryptKGVFVDqeKMY------LDTKAIFdeldididpKARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSL-- 180
Cdd:COG2401 106 IGR-----KGDFKD--AVEllnavgLSDAVLW---------LRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLdr 169
|
170 180
....*....|....*....|....*....
gi 495051738 181 -TEKEVNhlfKIIRKL-KERGCGIVYISH 207
Cdd:COG2401 170 qTAKRVA---RNLQKLaRRAGITLVVATH 195
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
29-229 |
5.84e-09 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 56.77 E-value: 5.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKdSGSILFQGKEIDFHSAKEalengismvhqelnLVLQRSvmdn 108
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAE--------------LARHRA---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 109 mWLGR--YPTKGVFVDQekmYLD-----------TKAIFDEL--DIDIDPK-AR-VGTLSVSQMQMIEIAKAF------- 164
Cdd:COG4138 73 -YLSQqqSPPFAMPVFQ---YLAlhqpagasseaVEQLLAQLaeALGLEDKlSRpLTQLSGGEWQRVRLAAVLlqvwpti 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495051738 165 SYDAKIVIMDEPTSSLtekEVNH---LFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIA 229
Cdd:COG4138 149 NPEGQLLLLDEPMNSL---DVAQqaaLDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVA 213
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
9-207 |
5.87e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 57.67 E-value: 5.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 9 SGEYLLEMTNINKSFP---G-------VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEID 78
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPvkrGlfkperlVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 79 FHS--AKEALENGISMVHQ----ELNlvlqrsvmdnmwlgryPTKGVfvdqekmyldtKAIFDE-LDI--DIDPK----- 144
Cdd:PRK11308 81 KADpeAQKLLRQKIQIVFQnpygSLN----------------PRKKV-----------GQILEEpLLIntSLSAAerrek 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 145 -----ARVG-----------TLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSL---TEKEVNHLFKIIRklKERGCGIVYI 205
Cdd:PRK11308 134 alammAKVGlrpehydryphMFSGGQRQRIAIARALMLDPDVVVADEPVSALdvsVQAQVLNLMMDLQ--QELGLSYVFI 211
|
..
gi 495051738 206 SH 207
Cdd:PRK11308 212 SH 213
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
27-207 |
6.17e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 57.41 E-value: 6.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 27 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKE--ALENGISMVHQE----LNlv 100
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEwrAVRSDIQMIFQDplasLN-- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 101 lqrsvmDNMWLGRYPTKGVFVDQEKMylDTKAIFDELdididpKA---RVGTL-----------SVSQMQMIEIAKAFSY 166
Cdd:PRK15079 113 ------PRMTIGEIIAEPLRTYHPKL--SRQEVKDRV------KAmmlKVGLLpnlinryphefSGGQCQRIGIARALIL 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495051738 167 DAKIVIMDEPTSSL---TEKEVNHLFKIIRklKERGCGIVYISH 207
Cdd:PRK15079 179 EPKLIICDEPVSALdvsIQAQVVNLLQQLQ--REMGLSLIFIAH 220
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
407-482 |
6.63e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 56.64 E-value: 6.63e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495051738 407 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK09493 137 LSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKG 212
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
315-499 |
7.31e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.50 E-value: 7.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 315 KSGGTISLHGKKINNHSANEaINNGFALVTEERRSTGIYAYLDIGFNSLISNIRNYK--SKIGLLDNsrmksdtqwVIDS 392
Cdd:PTZ00265 1274 KNSGKILLDGVDICDYNLKD-LRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKraCKFAAIDE---------FIES 1343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 393 MRVKtpgHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPE 468
Cdd:PTZ00265 1344 LPNK---YDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIA 1420
|
170 180 190
....*....|....*....|....*....|.
gi 495051738 469 LLGITDRILVMSNGLVSGIVDTKTTTQNEIL 499
Cdd:PTZ00265 1421 SIKRSDKIVVFNNPDRTGSFVQAHGTHEELL 1451
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
13-229 |
7.77e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 58.20 E-value: 7.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFPG----VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfhsakeALEN 88
Cdd:PRK10535 4 LLELKDIRRSYPSgeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVA------TLDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 89 G---------ISMVHQELNLVLQRSVMDNMwlgRYPTKGVFVDQEKMYLDTKAIFDELDIDIDPKARVGTLSVSQMQMIE 159
Cdd:PRK10535 78 DalaqlrrehFGFIFQRYHLLSHLTAAQNV---EVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 160 IAKAFSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKmEEIFQLCDEITILRDGQWIA 229
Cdd:PRK10535 155 IARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIVR 223
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
272-482 |
8.44e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 56.68 E-value: 8.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 272 TSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANEAINN-----GFALVTEE 346
Cdd:PRK13649 16 TPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQirkkvGLVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 347 RRSTGIYAYLDIGFNSlisniRNYK-SKIGLLDNSRMKSDTQWVIDSMRVKTPGhrtqigSLSGGNQQKVIIGRWLLTQP 425
Cdd:PRK13649 96 SQLFEETVLKDVAFGP-----QNFGvSQEEAEALAREKLALVGISESLFEKNPF------ELSGGQMRRVAIAGILAMEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495051738 426 EILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK13649 165 KILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKG 221
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
407-492 |
8.71e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 57.02 E-value: 8.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 407 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNGLVsg 486
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKI-- 243
|
....*.
gi 495051738 487 IVDTKT 492
Cdd:PRK13651 244 IKDGDT 249
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
404-487 |
8.72e-09 |
|
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: 55.93 E-value: 8.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 404 IGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-GKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:TIGR01184 112 PGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQIWEEhRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
....*
gi 495051738 483 LVSGI 487
Cdd:TIGR01184 192 PAANI 196
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
281-482 |
9.79e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 56.67 E-value: 9.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 281 DVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANEAINngfalvtEERRSTGI---YAYLD 357
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIK-------PVRKKVGVvfqFPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 358 IGFNSLISNIRNYKSKIGLLDNSRMKsdtqwvIDSMRVKTPGHRTQIGS-----LSGGNQQKVIIGRWLLTQPEILMLDE 432
Cdd:PRK13643 97 LFEETVLKDVAFGPQNFGIPKEKAEK------IAAEKLEMVGLADEFWEkspfeLSGGQMRRVAIAGILAMEPEVLVLDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495051738 433 PTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK13643 171 PTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKG 220
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
28-228 |
1.13e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 56.25 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 28 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfhsakeALENGISMVHQELNLVLQRSvmD 107
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDT-------SDEENLWDIRNKAGMVFQNP--D 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 108 NMWLGRYPTKGVFVDQEKMYLDTKAIFDELDidiDPKARVGT----------LSVSQMQMIEIAKAFSYDAKIVIMDEPT 177
Cdd:PRK13633 96 NQIVATIVEEDVAFGPENLGIPPEEIRERVD---ESLKKVGMyeyrrhaphlLSGGQKQRVAIAGILAMRPECIIFDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495051738 178 SSLTEKEVNHLFKIIRKL-KERGCGIVYISHKMEEIFQlCDEITILRDGQWI 228
Cdd:PRK13633 173 AMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVV 223
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
263-484 |
1.15e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 55.95 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 263 EVILEVRNLTSL---------RQ--PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISlhgkkINNHs 331
Cdd:PRK15112 2 ETLLEVRNLSKTfryrtgwfrRQtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELL-----IDDH- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 332 aneainngfalvteeRRSTGIYAYLDIGFNSLI---SNIRNYKSKIG-LLD-----NSRMKSDT--QWVIDSMRvktpgh 400
Cdd:PRK15112 76 ---------------PLHFGDYSYRSQRIRMIFqdpSTSLNPRQRISqILDfplrlNTDLEPEQreKQIIETLR------ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 401 rtQIG-----------SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKGKGIIIISSEMPE 468
Cdd:PRK15112 135 --QVGllpdhasyyphMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELqEKQGISYIYVTQHLGM 212
|
250
....*....|....*.
gi 495051738 469 LLGITDRILVMSNGLV 484
Cdd:PRK15112 213 MKHISDQVLVMHQGEV 228
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
395-496 |
1.15e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 55.94 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 395 VKTPGHRTQIGsLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKGKGIIIISSEMPELLGITD 474
Cdd:PRK14239 138 VKDRLHDSALG-LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISD 215
|
90 100
....*....|....*....|..
gi 495051738 475 RILVMSNGLVSGIVDTKTTTQN 496
Cdd:PRK14239 216 RTGFFLDGDLIEYNDTKQMFMN 237
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
407-482 |
1.29e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 57.14 E-value: 1.29e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495051738 407 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKGKGIIIISSempELLGIT--DRILVMSNG 482
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITH---RLTGLEqfDRICVMDNG 549
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
407-482 |
1.62e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 57.12 E-value: 1.62e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495051738 407 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAElakKGKGIIIIS-SEMPELLGITDRILVMSNG 482
Cdd:COG4178 486 LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE---ELPGTTVISvGHRSTLAAFHDRVLELTGD 559
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
13-226 |
1.62e-08 |
|
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: 55.13 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFPG----VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfhsakeAL-E 87
Cdd:COG4181 8 IIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLF------ALdE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 88 NGismvhqeLNLVLQRSVmdnmwlGryptkgvFVDQEKMYLDTKAIFD------ELDIDIDPKAR-------VG------ 148
Cdd:COG4181 82 DA-------RARLRARHV------G-------FVFQSFQLLPTLTALEnvmlplELAGRRDARARarallerVGlghrld 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 149 ----TLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKL-KERGCGIVYISHKmEEIFQLCDEITILR 223
Cdd:COG4181 142 hypaQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHD-PALAARCDRVLRLR 220
|
...
gi 495051738 224 DGQ 226
Cdd:COG4181 221 AGR 223
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
266-482 |
1.66e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 56.95 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 266 LEVRNLT----SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSAnEAINNGFA 341
Cdd:PRK11176 342 IEFRNVTftypGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTL-ASLRNQVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 342 LVTEErrstgiyAYLdigFNSLISNIRNYK-----SKIGLLDNSRMKSDTQWvIDSMRvktPGHRTQIG----SLSGGNQ 412
Cdd:PRK11176 421 LVSQN-------VHL---FNDTIANNIAYArteqySREQIEEAARMAYAMDF-INKMD---NGLDTVIGengvLLSGGQR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 413 QKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKGKGIIIISSEMPELLGiTDRILVMSNG 482
Cdd:PRK11176 487 QRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEK-ADEILVVEDG 554
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
406-485 |
1.66e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 56.58 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 406 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-GKGIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:PRK11000 133 ALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
.
gi 495051738 485 S 485
Cdd:PRK11000 213 A 213
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
11-226 |
1.70e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 55.17 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 11 EYLLEMTNINKSF----PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGK---EIDFHSAK 83
Cdd:PRK10584 4 ENIVEVHHLKKSVgqgeHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQplhQMDEEARA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 84 EALENGISMVHQELNLVLQRSVMDNMWLgryPT--KGVFVDQEKMylDTKAIFDELDIDIDPKARVGTLSVSQMQMIEIA 161
Cdd:PRK10584 84 KLRAKHVGFVFQSFMLIPTLNALENVEL---PAllRGESSRQSRN--GAKALLEQLGLGKRLDHLPAQLSGGEQQRVALA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495051738 162 KAFSYDAKIVIMDEPTSSLT----EKEVNHLFKIIRklkERGCGIVYISHKmEEIFQLCDEITILRDGQ 226
Cdd:PRK10584 159 RAFNGRPDVLFADEPTGNLDrqtgDKIADLLFSLNR---EHGTTLILVTHD-LQLAARCDRRLRLVNGQ 223
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
276-482 |
1.84e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 55.48 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 276 QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSA-------NEAI--------NNGF 340
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAergvvfqNEGLlpwrnvqdNVAF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 341 AL-----VTEERRSTGiyayldigfnslisniRNYKSKIGLldnsrmksdtqwvidsmrvKTPGHRtQIGSLSGGNQQKV 415
Cdd:PRK11248 94 GLqlagvEKMQRLEIA----------------HQMLKKVGL-------------------EGAEKR-YIWQLSGGQRQRV 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495051738 416 IIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKGKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK11248 138 GIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
33-226 |
1.88e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 54.97 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 33 NLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEidfHSAKEALENGISMVHQELNLVLQRSVMDNMWLG 112
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD---HTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 113 RYPTKGVFVDQEKMyldTKAIFDELDIDiDPKARV-GTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFKI 191
Cdd:PRK10771 96 LNPGLKLNAAQREK---LHAIARQMGIE-DLLARLpGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTL 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 495051738 192 IRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQ 226
Cdd:PRK10771 172 VSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGR 207
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
289-482 |
1.92e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 56.81 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 289 GEILGIAGLVGAKRTDIVETLFGireksggtiSLHGkkiNNHSANEAINNGfALVTEERRSTGIYAYLDIGFNSLisNIR 368
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAG---------RIQG---NNFTGTILANNR-KPTKQILKRTGFVTQDDILYPHL--TVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 369 NYKSKIGLL--DNSRMKSDTQWVIDSMRVK---TPGHRTQIGS-----LSGGNQQKVIIGRWLLTQPEILMLDEPTRGID 438
Cdd:PLN03211 159 ETLVFCSLLrlPKSLTKQEKILVAESVISElglTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495051738 439 VGAKFEIYQLIAELAKKGKgIIIISSEMP--ELLGITDRILVMSNG 482
Cdd:PLN03211 239 ATAAYRLVLTLGSLAQKGK-TIVTSMHQPssRVYQMFDSVLVLSEG 283
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
29-227 |
1.93e-08 |
|
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: 53.70 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQkdsgsiLFQGKeIDFHSAKEALengismvhqelnLVLQRSvmdn 108
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWP------WGSGR-IGMPEGEDLL------------FLPQRP---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 109 mwlgrYPTKGVFVDQEkmyldtkaifdeldidIDPKARVgtLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEvnhL 188
Cdd:cd03223 74 -----YLPLGTLREQL----------------IYPWDDV--LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEES---E 127
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495051738 189 FKIIRKLKERGCGIVYISHKmEEIFQLCD-EITILRDGQW 227
Cdd:cd03223 128 DRLYQLLKELGITVISVGHR-PSLWKFHDrVLDLDGEGGW 166
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
275-486 |
2.21e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 54.50 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 275 RQpSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANEainngfalVTEERRSTGIY- 353
Cdd:PRK10908 15 RQ-ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRE--------VPFLRRQIGMIf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 354 ----------AYLDIGFNSLIS-----NIRNYKS----KIGLLDNSRmksdtqwvidSMRVKtpghrtqigsLSGGNQQK 414
Cdd:PRK10908 86 qdhhllmdrtVYDNVAIPLIIAgasgdDIRRRVSaaldKVGLLDKAK----------NFPIQ----------LSGGEQQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495051738 415 VIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNGLVSG 486
Cdd:PRK10908 146 VGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHG 217
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
14-70 |
2.22e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.44 E-value: 2.22e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 495051738 14 LEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSI 70
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
407-495 |
2.40e-08 |
|
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: 56.23 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 407 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-GKGIIIISSEmpelLGI----TDRILVMSN 481
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHD----LGVvrrfADRVAVMRQ 232
|
90
....*....|....
gi 495051738 482 GLvsgIVDTKTTTQ 495
Cdd:COG4172 233 GE---IVEQGPTAE 243
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
265-506 |
2.51e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 55.13 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 265 ILEVRNLTsLRQP----SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANEaINNGF 340
Cdd:PRK13647 4 IIEVEDLH-FRYKdgtkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKW-VRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 341 ALVTEER-----RSTgiyAYLDIGFNSLisNIRNYKSKIGLLDNSRMKSDTQWvidSMRVKTPGHrtqigsLSGGNQQKV 415
Cdd:PRK13647 82 GLVFQDPddqvfSST---VWDDVAFGPV--NMGLDKDEVERRVEEALKAVRMW---DFRDKPPYH------LSYGQKKRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 416 IIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNGLVSGIVDTKTTTQ 495
Cdd:PRK13647 148 AIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTD 227
|
250
....*....|.
gi 495051738 496 NEILRLASLHL 506
Cdd:PRK13647 228 EDIVEQAGLRL 238
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
279-482 |
2.83e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 54.67 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 279 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIRE------KSGGTISLHGKKINNHSANEAINNGFALVTEERRSTGI 352
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 353 YAYLDIGFNSLISNIRNyKSKIGLLDNSRMKSDTQWVIDSMRVKTPGHRtqigsLSGGNQQKVIIGRWLLTQPEILMLDE 432
Cdd:PRK14246 106 SIYDNIAYPLKSHGIKE-KREIKKIVEECLRKVGLWKEVYDRLNSPASQ-----LSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495051738 433 PTRGIDVGAKFEIYQLIAELaKKGKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITEL-KNEIAIVIVSHNPQQVARVADYVAFLYNG 228
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
266-484 |
3.36e-08 |
|
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: 54.04 E-value: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 266 LEVRNLtSLR-----QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINnHSANEAINNGF 340
Cdd:cd03244 3 IEFKNV-SLRyrpnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDIS-KIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 341 ALVTEErrstgiyAYLDIGfnSLISNI--RNYKSK---IGLLDNSRMKSdtqwVIDSMRVKTPGHRTQIGS-LSGGNQQK 414
Cdd:cd03244 81 SIIPQD-------PVLFSG--TIRSNLdpFGEYSDeelWQALERVGLKE----FVESLPGGLDTVVEEGGEnLSVGQRQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 415 VIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAElAKKGKGIIIISSEMPELLGiTDRILVMSNGLV 484
Cdd:cd03244 148 LCLARALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLDTIID-SDRILVLDKGRV 215
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
407-482 |
3.55e-08 |
|
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: 53.81 E-value: 3.55e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495051738 407 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKG--IIIISSEMPELLGITDRILVMSNG 482
Cdd:cd03233 119 ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTttFVSLYQASDEIYDLFDKVLVLYEG 196
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
29-212 |
3.89e-08 |
|
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: 56.11 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG---KEIDFHSakeaLENGISMVHQELNLVLQRSV 105
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGlniAKIGLHD----LRFKITIIPQDPVLFSGSLR 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 106 MDNMWLGRYPTKGVFVDQEKMYLDT--KAIFDELDIDIDPKARvgTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLtEK 183
Cdd:TIGR00957 1378 MNLDPFSQYSDEEVWWALELAHLKTfvSALPDKLDHECAEGGE--NLSVGQRQLVCLARALLRKTKILVLDEATAAV-DL 1454
|
170 180
....*....|....*....|....*....
gi 495051738 184 EVNHLFKIIRKLKERGCGIVYISHKMEEI 212
Cdd:TIGR00957 1455 ETDNLIQSTIRTQFEDCTVLTIAHRLNTI 1483
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
277-482 |
4.13e-08 |
|
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: 53.63 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 277 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGkkinnhsaneainnGFALVTEErrstgiyAYL 356
Cdd:cd03250 19 FTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------------SIAYVSQE-------PWI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 357 digFN-SLISNIRNYKSkiglLDNSRMKSdtqwVIDS------MRVKTPGHRTQIG----SLSGGNQQKVIIGRWLLTQP 425
Cdd:cd03250 78 ---QNgTIRENILFGKP----FDEERYEK----VIKAcalepdLEILPDGDLTEIGekgiNLSGGQKQRISLARAVYSDA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 426 EILMLDEPTRGID--VGAK-FEiyQLIAELAKKGKGIIIISSEMpELLGITDRILVMSNG 482
Cdd:cd03250 147 DIYLLDDPLSAVDahVGRHiFE--NCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNG 203
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
356-482 |
4.43e-08 |
|
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: 52.07 E-value: 4.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 356 LDIGFNSLISNIR---NYKSKIGLL-DNSRMKS-----------DTQWVIDSMRVKTPGHRTQigsLSGGNQQKVIIGRW 420
Cdd:cd03221 8 KTYGGKLLLKDISltiNPGDRIGLVgRNGAGKStllkliagelePDEGIVTWGSTVKIGYFEQ---LSGGEKMRLALAKL 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495051738 421 LLTQPEILMLDEPTRGIDVGAkfeIYQLIAELAKKGKGIIIISSEmPELL-GITDRILVMSNG 482
Cdd:cd03221 85 LLENPNLLLLDEPTNHLDLES---IEALEEALKEYPGTVILVSHD-RYFLdQVATKIIELEDG 143
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
11-226 |
4.52e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 54.41 E-value: 4.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 11 EYLLEMTNINKSF---------PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHS 81
Cdd:PRK15112 2 ETLLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 82 AKEALENgISMVHQELNLVL---QR--SVMDnmwlgrYPTKgvfvdqekmyldtkaifdeLDIDIDPKAR---------- 146
Cdd:PRK15112 82 YSYRSQR-IRMIFQDPSTSLnprQRisQILD------FPLR-------------------LNTDLEPEQRekqiietlrq 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 147 VG-----------TLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLKER-GCGIVYISHKMEEIFQ 214
Cdd:PRK15112 136 VGllpdhasyyphMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKH 215
|
250
....*....|..
gi 495051738 215 LCDEITILRDGQ 226
Cdd:PRK15112 216 ISDQVLVMHQGE 227
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
172-438 |
4.73e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.41 E-value: 4.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 172 IMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQSLEGLDMDKIIAMMV--GRS 249
Cdd:PRK10938 158 ILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQALVAQLAhsEQL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 250 LNQRFPDRENKPGEVIL-EVRNLTSLR--------QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVE------------- 307
Cdd:PRK10938 238 EGVQLPEPDEPSARHALpANEPRIVLNngvvsyndRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSlitgdhpqgysnd 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 308 -TLFGIREKSGGTISLHGKKINNHSAneainngfALVTEERRSTGIYayldigfNSLISNirnYKSKIGLL----DNSRM 382
Cdd:PRK10938 318 lTLFGRRRGSGETIWDIKKHIGYVSS--------SLHLDYRVSTSVR-------NVILSG---FFDSIGIYqavsDRQQK 379
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 383 KSDtQWV----IDSMRVKTPGHrtqigSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID 438
Cdd:PRK10938 380 LAQ-QWLdilgIDKRTADAPFH-----SLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
407-461 |
4.95e-08 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 53.52 E-value: 4.95e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 495051738 407 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIII 461
Cdd:COG2884 138 LSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLI 192
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
263-474 |
5.57e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 54.02 E-value: 5.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 263 EVILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVG-AKRT---------DIVETLfgireKSGGTISLHGKKINNH 330
Cdd:PRK14243 8 ETVLRTENLNVYygSFLAVKNVWLDIPKNQITAFIGPSGcGKSTilrcfnrlnDLIPGF-----RVEGKVTFHGKNLYAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 331 SANEAinngfalvtEERRSTGIY----------AYLDIGFNSlisNIRNYKSKIGLLDNSRMKSDTQW--VIDSMRvktp 398
Cdd:PRK14243 83 DVDPV---------EVRRRIGMVfqkpnpfpksIYDNIAYGA---RINGYKGDMDELVERSLRQAALWdeVKDKLK---- 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495051738 399 ghrtQIG-SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKGKGIIIISSEMPELLGITD 474
Cdd:PRK14243 147 ----QSGlSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL-KEQYTIIIVTHNMQQAARVSD 218
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-180 |
5.74e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.34 E-value: 5.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 5 NTQSSGEYLLEMTNINKSFPGVKALDNVNLKV-RPHSIhALMGENGAGKSTLLKCLFGIYQKDSGSILFQGK-EID-FHS 81
Cdd:PRK11147 311 EASRSGKIVFEMENVNYQIDGKQLVKDFSAQVqRGDKI-ALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlEVAyFDQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 82 AKEALEngismvhqelnlvLQRSVMDNMWLGRyptkgvfvdQEKM----------YLDtkaifdelDIDIDPK-AR--VG 148
Cdd:PRK11147 390 HRAELD-------------PEKTVMDNLAEGK---------QEVMvngrprhvlgYLQ--------DFLFHPKrAMtpVK 439
|
170 180 190
....*....|....*....|....*....|..
gi 495051738 149 TLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSL 180
Cdd:PRK11147 440 ALSGGERNRLLLARLFLKPSNLLILDEPTNDL 471
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
29-229 |
6.04e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.06 E-value: 6.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYqkdSGSILFQGKEI--DFHSAKEALENGISMVHQELNLVLQR--- 103
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDL---TGGGAPRGARVtgDVTLNGEPLAAIDAPRLARLRAVLPQaaq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 104 -----SVMDNMWLGRYPTkgVFVDQEKMYLDTKAIFDELDI-DIDPKAR--VGTLSVSQMQMIEIAKAFSY--------- 166
Cdd:PRK13547 94 pafafSAREIVLLGRYPH--ARRAGALTHRDGEIAWQALALaGATALVGrdVTTLSGGELARVQFARVLAQlwpphdaaq 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495051738 167 DAKIVIMDEPTSSLTEKEVNHLFKIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWIA 229
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDPNLAARHADRIAMLADGAIVA 235
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
277-485 |
6.58e-08 |
|
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: 55.34 E-value: 6.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 277 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKK--------INNHSANEAINNGFALvtEERR 348
Cdd:TIGR00957 652 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVayvpqqawIQNDSLRENILFGKAL--NEKY 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 349 stgiyayldigfnslisnirnYKSKIglldnsrmksDTQWVIDSMRVKTPGHRTQIG----SLSGGNQQKVIIGRWLLTQ 424
Cdd:TIGR00957 730 ---------------------YQQVL----------EACALLPDLEILPSGDRTEIGekgvNLSGGQKQRVSLARAVYSN 778
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495051738 425 PEILMLDEPTRGIDVGAKFEIYQLI--AELAKKGKGIIIISSEMpELLGITDRILVMSNGLVS 485
Cdd:TIGR00957 779 ADIYLFDDPLSAVDAHVGKHIFEHVigPEGVLKNKTRILVTHGI-SYLPQVDVIIVMSGGKIS 840
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
405-482 |
7.17e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 53.38 E-value: 7.17e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495051738 405 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKGKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK14247 145 GKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLEL-KKDMTIVLVTHFPQQAARISDYVAFLYKG 221
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
265-484 |
8.09e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 53.58 E-value: 8.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 265 ILEVRNLT-----SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSaneainng 339
Cdd:PRK13650 4 IIEVKNLTfkykeDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEN-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 340 falVTEERRSTG-IYAYLDigfNSLISNIRNYKSKIGL----LDNSRMKSDTQWVIDSMRVKTPGHRtQIGSLSGGNQQK 414
Cdd:PRK13650 76 ---VWDIRHKIGmVFQNPD---NQFVGATVEDDVAFGLenkgIPHEEMKERVNEALELVGMQDFKER-EPARLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495051738 415 VIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-GKGIIIISSEMPElLGITDRILVMSNGLV 484
Cdd:PRK13650 149 VAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDE-VALSDRVLVMKNGQV 218
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
265-482 |
8.22e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 53.56 E-value: 8.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 265 ILEVRNLTSLRQP-----SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSA-NEAINN 338
Cdd:PRK13642 4 ILEVENLVFKYEKesdvnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 339 GFALVTEERRSTGIYAYLDIGFNSLISNIRNyKSKIGLLDNSRMksdtqwVIDSMRVKTpghrTQIGSLSGGNQQKVIIG 418
Cdd:PRK13642 84 GMVFQNPDNQFVGATVEDDVAFGMENQGIPR-EEMIKRVDEALL------AVNMLDFKT----REPARLSGGQKQRVAVA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495051738 419 RWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK13642 153 GIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAG 216
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
11-439 |
9.13e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 54.56 E-value: 9.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 11 EYLLEMTNINKSFPGVKA-LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIyQKDsgsilFQGKeidfhsAKEALENG 89
Cdd:TIGR03719 2 QYIYTMNRVSKVVPPKKEiLKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-DKD-----FNGE------ARPQPGIK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 90 ISMVHQELNLVLQRSVMDNMWLGRYPTKGVFVDQEKMYL---DTKAIFDEL--------DI-------DIDPK------- 144
Cdd:TIGR03719 70 VGYLPQEPQLDPTKTVRENVEEGVAEIKDALDRFNEISAkyaEPDADFDKLaaeqaelqEIidaadawDLDSQleiamda 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 145 -------ARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLK--------------------- 196
Cdd:TIGR03719 150 lrcppwdADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPgtvvavthdryfldnvagwil 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 197 --ERGCGIVYISH------------KMEEIFQLCDEITILRDGQWI-----ATQSLEGLDMDKIIAMmvgrsLNQRFPDR 257
Cdd:TIGR03719 230 elDRGRGIPWEGNysswleqkqkrlEQEEKEESARQKTLKRELEWVrqspkGRQAKSKARLARYEEL-----LSQEFQKR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 258 ENK------PGE----VILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTdiveTLF----GIREKSGGTIS 321
Cdd:TIGR03719 305 NETaeiyipPGPrlgdKVIEAENLTKAfgDKLLIDDLSFKLPPGGIVGVIGPNGAGKS----TLFrmitGQEQPDSGTIE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 322 LhGKKI-------------NNHSANEAINNGFALVTEERRSTGIYAYLDiGFnslisnirNYKSkiglldnsrmkSDTQw 388
Cdd:TIGR03719 381 I-GETVklayvdqsrdaldPNKTVWEEISGGLDIIKLGKREIPSRAYVG-RF--------NFKG-----------SDQQ- 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 495051738 389 vidsmrvktpghrTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDV 439
Cdd:TIGR03719 439 -------------KKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV 476
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
252-482 |
9.81e-08 |
|
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: 54.92 E-value: 9.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 252 QRFPDRENKPGEVILEVRNLTSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISlHGKKINNHS 331
Cdd:TIGR01271 415 QNNKARKQPNGDDGLFFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK-HSGRISFSP 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 332 ANEAINNG-------FALVTEERRSTGIyayldIGFNSLISNIRNY--KSKIGLLDNSRmksdtqwvidsmrvktpghrt 402
Cdd:TIGR01271 494 QTSWIMPGtikdniiFGLSYDEYRYTSV-----IKACQLEEDIALFpeKDKTVLGEGGI--------------------- 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 403 qigSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQ--LIAELAKKGKgiIIISSEMpELLGITDRILVMS 480
Cdd:TIGR01271 548 ---TLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFEscLCKLMSNKTR--ILVTSKL-EHLKKADKILLLH 621
|
..
gi 495051738 481 NG 482
Cdd:TIGR01271 622 EG 623
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
407-484 |
9.97e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 53.55 E-value: 9.97e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495051738 407 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-GKGIIIISSEMPELLGiTDRILVMSNGLV 484
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKV 222
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
404-496 |
1.02e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 53.01 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 404 IGSLSGGNQQKV-----IIGRWLLTQPE--ILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRI 476
Cdd:PRK03695 124 VNQLSGGEWQRVrlaavVLQVWPDINPAgqLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRV 203
|
90 100
....*....|....*....|..
gi 495051738 477 LVMSNG--LVSGIVDTKTTTQN 496
Cdd:PRK03695 204 WLLKQGklLASGRRDEVLTPEN 225
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
266-482 |
1.03e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 53.16 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 266 LEVRNLT-SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIR----EKSGGTISLHGKKInnhSANEAINNGF 340
Cdd:PRK10418 5 IELRNIAlQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGRVLLDGKPV---APCALRGRKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 341 ALVTEERRStgiyayldiGFNSLiSNIRNYKSKIgLLDNSRMKSDTQwVIDSMRVKTPGHRTQIGSL-----SGGNQQKV 415
Cdd:PRK10418 82 ATIMQNPRS---------AFNPL-HTMHTHARET-CLALGKPADDAT-LTAALEAVGLENAARVLKLypfemSGGMLQRM 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495051738 416 IIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKGKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHG 217
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
406-484 |
1.45e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 52.76 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 406 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKGKGIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:PRK11247 133 ALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
272-503 |
1.46e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 52.77 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 272 TSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKIN--NHSANEAINNGFALVTEE--- 346
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAklNRAQRKAFRRDIQMVFQDsis 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 347 ----RRSTGiyayldigfNSLISNIRNYKSkiglLDNSRMKSDTQWVIDSMRVkTPGHRTQI-GSLSGGNQQKVIIGRWL 421
Cdd:PRK10419 101 avnpRKTVR---------EIIREPLRHLLS----LDKAERLARASEMLRAVDL-DDSVLDKRpPQLSGGQLQRVCLARAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 422 LTQPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKGKGIIIISSEMPELLGITDRILVMSNGlvsGIVDTKTTTqnEILR 500
Cdd:PRK10419 167 AVEPKLLILDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITHDLRLVERFCQRVMVMDNG---QIVETQPVG--DKLT 241
|
...
gi 495051738 501 LAS 503
Cdd:PRK10419 242 FSS 244
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
263-455 |
1.53e-07 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 52.73 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 263 EVILEVRNLtSLR---QPSIRDVSFDLHKGEILGIAGLVGA-KRT---------DIVEtlfGIREKsgGTISLHGKKINN 329
Cdd:COG1117 9 EPKIEVRNL-NVYygdKQALKDINLDIPENKVTALIGPSGCgKSTllrclnrmnDLIP---GARVE--GEILLDGEDIYD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 330 HSANeainngfalVTEERRSTG------------IY---AYldiGFNslisnIRNYKSKiGLLDNSRMKSDTQ---W--V 389
Cdd:COG1117 83 PDVD---------VVELRRRVGmvfqkpnpfpksIYdnvAY---GLR-----LHGIKSK-SELDEIVEESLRKaalWdeV 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495051738 390 IDsmRVKTPGhrtqiGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK 455
Cdd:COG1117 145 KD--RLKKSA-----LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD 203
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
266-474 |
2.13e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 51.41 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 266 LEVRNLTSLRQPSI--RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANEAInngfalv 343
Cdd:PRK13539 3 LEGEDLACVRGGRVlfSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAC------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 344 teerrstgiyAYLdiG-------FNSLISNIRNYKskiGLLDNSRmkSDTQWVIDSMRVKTPGHRtQIGSLSGGNQQKVI 416
Cdd:PRK13539 76 ----------HYL--GhrnamkpALTVAENLEFWA---AFLGGEE--LDIAAALEAVGLAPLAHL-PFGYLSAGQKRRVA 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495051738 417 IGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGkGIIIISSEMPelLGITD 474
Cdd:PRK13539 138 LARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQG-GIVIAATHIP--LGLPG 192
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
407-482 |
2.52e-07 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 52.46 E-value: 2.52e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495051738 407 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISS---EmpELLGITDRILVMSNG 482
Cdd:COG1118 134 LSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVThdqE--EALELADRVVVMNQG 210
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
26-228 |
2.75e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 52.02 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 26 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEaLENGISMVHQEL-NLVLQRS 104
Cdd:PRK13642 20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWN-LRRKIGMVFQNPdNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 105 VMDNMWLGrYPTKGVFVDQEKMYLDTKAI-FDELDIDIDPKARvgtLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEK 183
Cdd:PRK13642 99 VEDDVAFG-MENQGIPREEMIKRVDEALLaVNMLDFKTREPAR---LSGGQKQRVAVAGIIALRPEIIILDESTSMLDPT 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495051738 184 EVNHLFKIIRKLKER-GCGIVYISHKMEEIFQlCDEITILRDGQWI 228
Cdd:PRK13642 175 GRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEII 219
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
261-482 |
3.33e-07 |
|
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: 51.28 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 261 PGEVILEVRNLT-SLRQPS-----IRDVSFDLHKGEILGIAGLVGAKRTdiveTLFGI----REKSGGTISLHGKKInnh 330
Cdd:COG4181 4 SSAPIIELRGLTkTVGTGAgeltiLKGISLEVEAGESVAIVGASGSGKS----TLLGLlaglDRPTSGTVRLAGQDL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 331 saneainngFALvTEERRSTGIYAYLDIGFNS--LISNirnykskigL--LDNsrmksdtqwvidsmrVKTP-------- 398
Cdd:COG4181 77 ---------FAL-DEDARARLRARHVGFVFQSfqLLPT---------LtaLEN---------------VMLPlelagrrd 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 399 --------------GHRTQ--IGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID--VGAKfeIYQLIAEL-AKKGKGI 459
Cdd:COG4181 123 arararallervglGHRLDhyPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDaaTGEQ--IIDLLFELnRERGTTL 200
|
250 260
....*....|....*....|...
gi 495051738 460 IIISSEmPELLGITDRILVMSNG 482
Cdd:COG4181 201 VLVTHD-PALAARCDRVLRLRAG 222
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
277-484 |
3.38e-07 |
|
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: 52.82 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 277 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINN---HSANEAINngfALVTEERRSTGiy 353
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDidrHTLRQFIN---YLPQEPYIFSG-- 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 354 AYLDigfNSLISNIRNYKSK--IGLLDNSRMKSDtqwvIDSMRVktpGHRTQI----GSLSGGNQQKVIIGRWLLTQPEI 427
Cdd:TIGR01193 563 SILE---NLLLGAKENVSQDeiWAACEIAEIKDD----IENMPL---GYQTELseegSSISGGQKQRIALARALLTDSKV 632
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495051738 428 LMLDEPTRGIDVGAKFEIYQLIAELakKGKGIIIISSEMpELLGITDRILVMSNGLV 484
Cdd:TIGR01193 633 LILDESTSNLDTITEKKIVNNLLNL--QDKTIIFVAHRL-SVAKQSDKIIVLDHGKI 686
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
390-506 |
4.03e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 51.73 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 390 IDSMRVKTPGHrtqigsLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPEL 469
Cdd:PRK13652 127 LEELRDRVPHH------LSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDL 200
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 495051738 470 LG-ITDRILVMSNGLV--SGIVDtKTTTQNEILRLASLHL 506
Cdd:PRK13652 201 VPeMADYIYVMDKGRIvaYGTVE-EIFLQPDLLARVHLDL 239
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
280-455 |
5.00e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 51.14 E-value: 5.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 280 RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANEaINNGFALVTEERRSTGiyaylDIG 359
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE-VARRIGLLAQNATTPG-----DIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 360 FNSLISNIRnYKSKiGLLDNSRmKSDTQWVIDSMRVKTPGH--RTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGI 437
Cdd:PRK10253 98 VQELVARGR-YPHQ-PLFTRWR-KEDEEAVTKAMQATGITHlaDQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170
....*....|....*...
gi 495051738 438 DVGAKFEIYQLIAELAKK 455
Cdd:PRK10253 175 DISHQIDLLELLSELNRE 192
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
3-225 |
5.56e-07 |
|
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: 52.61 E-value: 5.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 3 SNNTQSSGEYLLEMTNInkSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeIDFHSa 82
Cdd:TIGR01271 418 KARKQPNGDDGLFFSNF--SLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-ISFSP- 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 83 kealengismvhqELNLVLQRSVMDNMWLgryptkGVFVDQEKMYLDTKAIFDELDIDIDP---KARVG----TLSVSQM 155
Cdd:TIGR01271 494 -------------QTSWIMPGTIKDNIIF------GLSYDEYRYTSVIKACQLEEDIALFPekdKTVLGeggiTLSGGQR 554
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495051738 156 QMIEIAKAFSYDAKIVIMDEPTSSL---TEKEVnhLFKIIRKLKERGCGIVYIShKMEEIfQLCDEITILRDG 225
Cdd:TIGR01271 555 ARISLARAVYKDADLYLLDSPFTHLdvvTEKEI--FESCLCKLMSNKTRILVTS-KLEHL-KKADKILLLHEG 623
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
276-484 |
5.66e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 52.42 E-value: 5.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 276 QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGK---KINNHSANEAInngfALVTEErrstgi 352
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVplvQYDHHYLHRQV----ALVGQE------ 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 353 yaylDIGFN-SLISNIR---NYKSKIGLLdNSRMKSDTQWVIDSMrvkTPGHRTQIGS----LSGGNQQKVIIGRWLLTQ 424
Cdd:TIGR00958 564 ----PVLFSgSVRENIAyglTDTPDEEIM-AAAKAANAHDFIMEF---PNGYDTEVGEkgsqLSGGQKQRIAIARALVRK 635
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495051738 425 PEILMLDEPTRGIDVgakfEIYQLIAELAK-KGKGIIIISSEMPeLLGITDRILVMSNGLV 484
Cdd:TIGR00958 636 PRVLILDEATSALDA----ECEQLLQESRSrASRTVLLIAHRLS-TVERADQILVLKKGSV 691
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
407-484 |
6.86e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 50.78 E-value: 6.86e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495051738 407 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-GKGIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:PRK13645 151 LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
29-221 |
7.38e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 49.87 E-value: 7.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEAL-----ENGismVHQELnlvlqr 103
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAChylghRNA---MKPAL------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 104 SVMDNM--WLGryptkgvFVDQEKMYLDTKAIFDELDIDIDPKArvGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLT 181
Cdd:PRK13539 89 TVAENLefWAA-------FLGGEELDIAAALEAVGLAPLAHLPF--GYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 495051738 182 EKEVNHLFKIIRKLKERGcGIVYIS-HKMEEIFQlCDEITI 221
Cdd:PRK13539 160 AAAVALFAELIRAHLAQG-GIVIAAtHIPLGLPG-ARELDL 198
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
65-231 |
8.19e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.95 E-value: 8.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 65 KDSGSILFQGKEIDFHSAKEaLENGISMVHQElNLVLQRSVMDNMWLGRYPTKGVFVDQEKMYLDTKAIFDEL----DID 140
Cdd:PTZ00265 1274 KNSGKILLDGVDICDYNLKD-LRNLFSIVSQE-PMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLpnkyDTN 1351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 141 IDPKARvgTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLKERG-CGIVYISHKMEEIfQLCDEI 219
Cdd:PTZ00265 1352 VGPYGK--SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASI-KRSDKI 1428
|
170
....*....|....*.
gi 495051738 220 TIL----RDGQWIATQ 231
Cdd:PTZ00265 1429 VVFnnpdRTGSFVQAH 1444
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
407-482 |
8.24e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 50.48 E-value: 8.24e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495051738 407 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKgKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDG 238
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
29-226 |
9.11e-07 |
|
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: 51.36 E-value: 9.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfHSAKEALENGISMVHQElnLVL-QRSVMD 107
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIR-DVTQASLRAAIGIVPQD--TVLfNDTIAY 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 108 NMWLGRyPTkgvfVDQEKMYLDTKAIfdELD--IDIDPK---ARVG----TLSVSQMQMIEIAKAFSYDAKIVIMDEPTS 178
Cdd:COG5265 451 NIAYGR-PD----ASEEEVEAAARAA--QIHdfIESLPDgydTRVGerglKLSGGEKQRVAIARTLLKNPPILIFDEATS 523
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495051738 179 SL---TEKEvnhlfkIIRKLKE--RGCGIVYISHKMEEIfQLCDEITILRDGQ 226
Cdd:COG5265 524 ALdsrTERA------IQAALREvaRGRTTLVIAHRLSTI-VDADEILVLEAGR 569
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
257-482 |
9.13e-07 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 51.10 E-value: 9.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 257 RENKPgevILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSA-N 333
Cdd:PRK09452 9 SSLSP---LVELRGISKSfdGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAeN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 334 EAINNGFalvteerRSTGIYAYLdigfnSLISNIrnyksKIGLldnsRMKSD-----TQWVIDSMR-VKTPGHRTQ-IGS 406
Cdd:PRK09452 86 RHVNTVF-------QSYALFPHM-----TVFENV-----AFGL----RMQKTpaaeiTPRVMEALRmVQLEEFAQRkPHQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 407 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGID----VGAKFEIYQLIAELakkgkGI--IIISSEMPELLGITDRILVMS 480
Cdd:PRK09452 145 LSGGQQQRVAIARAVVNKPKVLLLDESLSALDyklrKQMQNELKALQRKL-----GItfVFVTHDQEEALTMSDRIVVMR 219
|
..
gi 495051738 481 NG 482
Cdd:PRK09452 220 DG 221
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
399-484 |
1.08e-06 |
|
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: 49.85 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 399 GHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIaELAKKGKGIIIISSempELLGI-- 472
Cdd:cd03249 128 GYDTLVGergsQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEAL-DRAMKGRTTIVIAH---RLSTIrn 203
|
90
....*....|..
gi 495051738 473 TDRILVMSNGLV 484
Cdd:cd03249 204 ADLIAVLQNGQV 215
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
256-482 |
1.11e-06 |
|
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: 50.24 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 256 DRENKPGEVILEVRNLTSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISlHGKKINNHSANEA 335
Cdd:cd03291 30 DRKHSSDDNNLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK-HSGRISFSSQFSW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 336 INNG-------FALVTEERRstgiyayldigfnslisnirnYKSKIgllDNSRMKSDTQWVIDsmRVKTPGHRTQIgSLS 408
Cdd:cd03291 109 IMPGtikeniiFGVSYDEYR---------------------YKSVV---KACQLEEDITKFPE--KDNTVLGEGGI-TLS 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495051738 409 GGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMpELLGITDRILVMSNG 482
Cdd:cd03291 162 GGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKTRILVTSKM-EHLKKADKILILHEG 234
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
405-463 |
1.11e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 49.84 E-value: 1.11e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 405 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID-VGAKfEIYQLIAELaKKGKGIIIIS 463
Cdd:PRK14267 148 SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDpVGTA-KIEELLFEL-KKEYTIVLVT 205
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
30-203 |
1.18e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 49.03 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 30 DNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfHSAKEALengismvHQELnlvlqrsvmdnM 109
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI--RRQRDEY-------HQDL-----------L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 110 WLGRYPtkGV-----------FVDQEKMYLDTKAIFDELdididpkARVG----------TLSVSQMQMIEIAKAFSYDA 168
Cdd:PRK13538 78 YLGHQP--GIkteltalenlrFYQRLHGPGDDEALWEAL-------AQVGlagfedvpvrQLSAGQQRRVALARLWLTRA 148
|
170 180 190
....*....|....*....|....*....|....*
gi 495051738 169 KIVIMDEPTSSLTEKEVNHLFKIIRKLKERGcGIV 203
Cdd:PRK13538 149 PLWILDEPFTAIDKQGVARLEALLAQHAEQG-GMV 182
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
29-271 |
1.19e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.39 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGiyQKDSGSILFQGKEIDFHSAKEALENgISMVHQELNL-----VLQR 103
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGDIRISGFPKKQETFAR-ISGYCEQNDIhspqvTVRE 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 104 SVMDNMWLgRYPtKGVFVDQEKMYLDTKAIFDELDIDIDpkARVGT-----LSVSQMQMIEIAKAFSYDAKIVIMDEPTS 178
Cdd:PLN03140 973 SLIYSAFL-RLP-KEVSKEEKMMFVDEVMELVELDNLKD--AIVGLpgvtgLSTEQRKRLTIAVELVANPSIIFMDEPTS 1048
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 179 SLTEKEVNHLFKIIRKLKERGCGIVYISHKME-EIFQLCDEITIL-RDGQWIATQSLeGLDMDKIIAMMVGRSLNQRFPD 256
Cdd:PLN03140 1049 GLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLMkRGGQVIYSGPL-GRNSHKIIEYFEAIPGVPKIKE 1127
|
250
....*....|....*
gi 495051738 257 RENkPGEVILEVRNL 271
Cdd:PLN03140 1128 KYN-PATWMLEVSSL 1141
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
275-484 |
1.30e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 50.87 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 275 RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINnHSANEAINNGFALVteerrSTGIYA 354
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLT-KLQLDSWRSRLAVV-----SQTPFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 355 YLDigfnSLISNI---RNYKSKIGLLDNSRMKSdtqwVIDSMRVKTPGHRTQIGS----LSGGNQQKVIIGRWLLTQPEI 427
Cdd:PRK10789 401 FSD----TVANNIalgRPDATQQEIEHVARLAS----VHDDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLLNAEI 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495051738 428 LMLDEPTRGIDvgAKFEiYQLIAELAKKGKG-IIIISSEMPELLGITDRILVMSNGLV 484
Cdd:PRK10789 473 LILDDALSAVD--GRTE-HQILHNLRQWGEGrTVIISAHRLSALTEASEILVMQHGHI 527
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
407-484 |
1.38e-06 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 50.46 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 407 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDvgAKF------EIYQLIAELakkGKGIIIISSEMPELLGITDRILVMS 480
Cdd:COG3839 134 LSGGQRQRVALGRALVREPKVFLLDEPLSNLD--AKLrvemraEIKRLHRRL---GTTTIYVTHDQVEAMTLADRIAVMN 208
|
....
gi 495051738 481 NGLV 484
Cdd:COG3839 209 DGRI 212
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
407-484 |
1.59e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 50.13 E-value: 1.59e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495051738 407 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-GKGIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
43-207 |
1.86e-06 |
|
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: 48.51 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 43 ALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEidfhsakealengismvHQELNLVLQRSVmdnMWLGRYP-TKGVFV 121
Cdd:TIGR01189 30 QVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTP-----------------LAEQRDEPHENI---LYLGHLPgLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 122 DQEKMYLdTKAIFDELDIDI-DPKARVG----------TLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFK 190
Cdd:TIGR01189 90 ALENLHF-WAAIHGGAQRTIeDALAAVGltgfedlpaaQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAG 168
|
170
....*....|....*..
gi 495051738 191 IIRKLKERGCGIVYISH 207
Cdd:TIGR01189 169 LLRAHLARGGIVLLTTH 185
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
421-482 |
2.01e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 49.70 E-value: 2.01e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495051738 421 LLTQPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKGKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:COG4586 169 LLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHG 231
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
280-482 |
2.05e-06 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 49.80 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 280 RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANEainngfalVTEERRSTG-IYAYldi 358
Cdd:PRK11153 22 NNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKE--------LRKARRQIGmIFQH--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 359 gFNSLIS-----NI-------RNYKSKIG-----LLDnsrmksdtqwvidsmRVKTPGHRTQIGS-LSGGNQQKVIIGRW 420
Cdd:PRK11153 91 -FNLLSSrtvfdNValplelaGTPKAEIKarvteLLE---------------LVGLSDKADRYPAqLSGGQKQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495051738 421 LLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-GKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK11153 155 LASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAG 217
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
407-484 |
2.40e-06 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 49.69 E-value: 2.40e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495051738 407 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-GKGIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
2-226 |
2.40e-06 |
|
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: 49.08 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 2 VSNNTQSSGEYLLEMTNInkSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeIDFHS 81
Cdd:cd03291 28 NNDRKHSSDDNNLFFSNL--CLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-ISFSS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 82 akealengismvhqELNLVLQRSVMDNMWLgryptkGVFVDQEKMYLDTKAIFDELDI------DIDPKARVG-TLSVSQ 154
Cdd:cd03291 105 --------------QFSWIMPGTIKENIIF------GVSYDEYRYKSVVKACQLEEDItkfpekDNTVLGEGGiTLSGGQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495051738 155 MQMIEIAKAFSYDAKIVIMDEPTSSL---TEKEVnhLFKIIRKLKERGCGIVyISHKMEEIfQLCDEITILRDGQ 226
Cdd:cd03291 165 RARISLARAVYKDADLYLLDSPFGYLdvfTEKEI--FESCVCKLMANKTRIL-VTSKMEHL-KKADKILILHEGS 235
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
275-484 |
2.89e-06 |
|
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: 49.82 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 275 RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNhsaneainngfalVTEE--RRSTGI 352
Cdd:COG5265 370 ERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRD-------------VTQAslRAAIGI 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 353 YAYLDIGFN-SLISNIRnYkskiGLLDNS--------RMKSdtqwvIDSMRVKTP-GHRTQIGS----LSGGNQQKVIIG 418
Cdd:COG5265 437 VPQDTVLFNdTIAYNIA-Y----GRPDASeeeveaaaRAAQ-----IHDFIESLPdGYDTRVGErglkLSGGEKQRVAIA 506
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495051738 419 RWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKGKGIIII----SSempellgIT--DRILVMSNGLV 484
Cdd:COG5265 507 RTLLKNPPILIFDEATSALDSRTERAIQAALREVA-RGRTTLVIahrlST-------IVdaDEILVLEAGRI 570
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
10-70 |
3.07e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.73 E-value: 3.07e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495051738 10 GEYLLEMTNINKSFpGVKAL-DNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSI 70
Cdd:PRK11819 321 GDKVIEAENLSKSF-GDRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
279-484 |
3.29e-06 |
|
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: 48.30 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 279 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKkinnhsaneainngfalvteerrstgIYAYLDI 358
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR--------------------------VSSLLGL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 359 --GFNSLIS---NIRNYKSKIGlLDNSRMKSDTQWVID--------SMRVKTpghrtqigsLSGGNQQKVIIGRWLLTQP 425
Cdd:cd03220 92 ggGFNPELTgreNIYLNGRLLG-LSRKEIDEKIDEIIEfselgdfiDLPVKT---------YSSGMKARLAFAIATALEP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495051738 426 EILMLDEptrGIDVG-AKFEI--YQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:cd03220 162 DILLIDE---VLAVGdAAFQEkcQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
13-207 |
3.40e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.56 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 13 LLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILF-----------------QGK 75
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYeqdlivarlqqdpprnvEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 76 EIDFHSA-----KEALENgismVHQELNLVLQRSvMDNMW--LGRYptkgvfvdQEKM------YLDTKaIFDELD-IDI 141
Cdd:PRK11147 83 VYDFVAEgieeqAEYLKR----YHDISHLVETDP-SEKNLneLAKL--------QEQLdhhnlwQLENR-INEVLAqLGL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495051738 142 DPKARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTssltekevNHL----------FkiirkLKERGCGIVYISH 207
Cdd:PRK11147 149 DPDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPT--------NHLdietiewlegF-----LKTFQGSIIFISH 211
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
407-482 |
3.41e-06 |
|
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: 47.91 E-value: 3.41e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495051738 407 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIIsSEMPELLG--ITDRILVMSNG 482
Cdd:cd03217 105 FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLII-THYQRLLDyiKPDRVHVLYDG 181
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
28-226 |
3.48e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 49.71 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 28 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfHSAKEALENGISMVHQELNLvLQRSVMD 107
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLT-KLQLDSWRSRLAVVSQTPFL-FSDTVAN 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 108 NMWLGRyPTkgvfVDQEKMYLDTKAIFDELDIDIDPKA---RVG----TLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSL 180
Cdd:PRK10789 408 NIALGR-PD----ATQQEIEHVARLASVHDDILRLPQGydtEVGergvMLSGGQKQRISIARALLLNAEILILDDALSAV 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495051738 181 ---TEKEvnhlfkIIRKLKERGCG-IVYIS-HKMEEIFQlCDEITILRDGQ 226
Cdd:PRK10789 483 dgrTEHQ------ILHNLRQWGEGrTVIISaHRLSALTE-ASEILVMQHGH 526
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
407-479 |
3.64e-06 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 48.75 E-value: 3.64e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495051738 407 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAK-KGKGIIIISSEMPELLGITDRILVM 479
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVL 232
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
407-481 |
4.26e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.24 E-value: 4.26e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495051738 407 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSN 481
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLAD 210
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
404-479 |
4.55e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 48.13 E-value: 4.55e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495051738 404 IGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVM 479
Cdd:cd03236 137 IDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
261-479 |
5.33e-06 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 48.57 E-value: 5.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 261 PGEVILEVRNLT--------SLRQPS-----IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKI 327
Cdd:COG4608 3 MAEPLLEVRDLKkhfpvrggLFGRTVgvvkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 328 NNHSANEainngfalVTEERRSTGI-----YAyldigfnSLisnirnykskiglldNSRMKsdtqwVIDS----MRVKTP 398
Cdd:COG4608 83 TGLSGRE--------LRPLRRRMQMvfqdpYA-------SL---------------NPRMT-----VGDIiaepLRIHGL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 399 GHRTQIGS----------------------LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK- 455
Cdd:COG4608 128 ASKAERRErvaellelvglrpehadrypheFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDEl 207
|
250 260
....*....|....*....|....*...
gi 495051738 456 GKGIIIISSEmpelLG----ITDRILVM 479
Cdd:COG4608 208 GLTYLFISHD----LSvvrhISDRVAVM 231
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
407-482 |
6.32e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 47.87 E-value: 6.32e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495051738 407 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAK-KGKGIIIISSEMPELLGiTDRILVMSNG 482
Cdd:PRK13640 144 LSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKkNNLTVISITHDIDEANM-ADQVLVLDDG 219
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
402-500 |
7.74e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.41 E-value: 7.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 402 TQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVgakfEIYQLIAELAKKGKG-IIIISSEMPELLGITDRILVMS 480
Cdd:PRK11147 152 AALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI----ETIEWLEGFLKTFQGsIIFISHDRSFIRNMATRIVDLD 227
|
90 100
....*....|....*....|...
gi 495051738 481 NG-LVS--GIVDTKTTTQNEILR 500
Cdd:PRK11147 228 RGkLVSypGNYDQYLLEKEEALR 250
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
43-478 |
8.50e-06 |
|
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: 48.24 E-value: 8.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 43 ALMGENGAGKSTLLKCL-------FGIYQKDSG--SIL--FQGKEIDFHSAKEAlENGISMVH--QELNL---VLQRSVM 106
Cdd:COG1245 103 GILGPNGIGKSTALKILsgelkpnLGDYDEEPSwdEVLkrFRGTELQDYFKKLA-NGEIKVAHkpQYVDLipkVFKGTVR 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 107 DnmWLGRYPTKGVFVDqekmyldtkaIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVN 186
Cdd:COG1245 182 E--LLEKVDERGKLDE----------LAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 187 HLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITIL----------------RDGqwIaTQSLEG-LdmdkiiammvgRS 249
Cdd:COG1245 250 NVARLIRELAEEGKYVLVVEHDLAILDYLADYVHILygepgvygvvskpksvRVG--I-NQYLDGyL-----------PE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 250 LNQRF----------PDRENKPGEVILEVRNLT-SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGG 318
Cdd:COG1245 316 ENVRIrdepiefevhAPRREKEEETLVEYPDLTkSYGGFSLEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEG 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 319 TISLhGKKINnhsaneainngfalvteerrstgiYA--YLDIGFN-SLISNIRNYKSKIglLDNSRMKSDtqwVIDSMRV 395
Cdd:COG1245 396 EVDE-DLKIS------------------------YKpqYISPDYDgTVEEFLRSANTDD--FGSSYYKTE---IIKPLGL 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 396 KtPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELA-KKGKGIIIISSEMPELLGITD 474
Cdd:COG1245 446 E-KLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAeNRGKTAMVVDHDIYLIDYISD 524
|
....
gi 495051738 475 RILV 478
Cdd:COG1245 525 RLMV 528
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
394-482 |
1.01e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.49 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 394 RVKTPGHRTQIGS----LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAK-KGKGIIIISSEMPE 468
Cdd:PRK15093 142 RVGIKDHKDAMRSfpyeLTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQM 221
|
90
....*....|....
gi 495051738 469 LLGITDRILVMSNG 482
Cdd:PRK15093 222 LSQWADKINVLYCG 235
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
260-484 |
1.06e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.43 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 260 KPGEVILEVRN-----LTSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGireksggtislhgkkinnhsane 334
Cdd:PLN03232 609 QPGAPAISIKNgyfswDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG----------------------- 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 335 ainngfALVTEERRSTGIYAylDIGFNSLISNIRNYKSKIGLLDNSRMKSDTQW-VIDSMRVKT-----PGH-RTQIG-- 405
Cdd:PLN03232 666 ------ELSHAETSSVVIRG--SVAYVPQVSWIFNATVRENILFGSDFESERYWrAIDVTALQHdldllPGRdLTEIGer 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 406 --SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMpELLGITDRILVMSNGL 483
Cdd:PLN03232 738 gvNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQL-HFLPLMDRIILVSEGM 816
|
.
gi 495051738 484 V 484
Cdd:PLN03232 817 I 817
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
403-482 |
1.09e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 48.18 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 403 QIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEmPELLGITDRILVMSNG 482
Cdd:PRK10535 141 QPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDG 219
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
29-236 |
1.12e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.20 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfhsakeaLENGISMVHQELNLVLQRSVM-- 106
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDI--------SKFGLMDLRKVLGIIPQAPVLfs 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 107 ---------------DNMW--LGRYPTKGVfVDQEKMYLDTKAifdeldididpkARVG-TLSVSQMQMIEIAKAFSYDA 168
Cdd:PLN03130 1327 gtvrfnldpfnehndADLWesLERAHLKDV-IRRNSLGLDAEV------------SEAGeNFSVGQRQLLSLARALLRRS 1393
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495051738 169 KIVIMDEPTSSLTEKEVNHLFKIIRKlKERGCGIVYISHKMEEIFQlCDEITILRDGQWIATQSLEGL 236
Cdd:PLN03130 1394 KILVLDEATAAVDVRTDALIQKTIRE-EFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENL 1459
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
277-484 |
1.24e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.05 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 277 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNhsaneainngFALvTEERRSTGIYAYL 356
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAK----------FGL-TDLRRVLSIIPQS 1318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 357 DIGFNSLIS-NIRNYK--SKIGL---LDNSRMKsdtqwviDSMRVKTPGHRTQIG----SLSGGNQQKVIIGRWLLTQPE 426
Cdd:PLN03232 1319 PVLFSGTVRfNIDPFSehNDADLweaLERAHIK-------DVIDRNPFGLDAEVSeggeNFSVGQRQLLSLARALLRRSK 1391
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495051738 427 ILMLDEPTRGIDVGAKFEIYQLIAELAKKGKgIIIISSEMPELLGiTDRILVMSNGLV 484
Cdd:PLN03232 1392 ILVLDEATASVDVRTDSLIQRTIREEFKSCT-MLVIAHRLNTIID-CDKILVLSSGQV 1447
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
361-481 |
1.74e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.72 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 361 NSLISNIRNYKSkiglLDNSRMKSDTQWVI--DSMRVKTPGHRTQIGS----LSGGNQQKVIIGRWLLTQPEILMLDEPT 434
Cdd:PTZ00265 532 NELIEMRKNYQT----IKDSEVVDVSKKVLihDFVSALPDKYETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEAT 607
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 495051738 435 RGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSN 481
Cdd:PTZ00265 608 SSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYANTIFVLSN 654
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
26-212 |
1.89e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.72 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 26 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQgkeiDFHSAKEA----LENGISMVHQElNLVL 101
Cdd:PTZ00265 398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN----DSHNLKDInlkwWRSKIGVVSQD-PLLF 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 102 QRSVMDNMWLGRYPTKGVFVDQEKMYLDTKAIFDELDIDIDPKAR----------------------------------- 146
Cdd:PTZ00265 473 SNSIKNNIKYSLYSLKDLEALSNYYNEDGNDSQENKNKRNSCRAKcagdlndmsnttdsneliemrknyqtikdsevvdv 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 147 --------------------VGT----LSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGI 202
Cdd:PTZ00265 553 skkvlihdfvsalpdkyetlVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRI 632
|
250
....*....|.
gi 495051738 203 -VYISHKMEEI 212
Cdd:PTZ00265 633 tIIIAHRLSTI 643
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
266-464 |
1.90e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 45.57 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 266 LEVRNLTSLRQPSI--RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNhsaneainngfalV 343
Cdd:PRK13538 2 LEARNLACERDERIlfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR-------------Q 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 344 TEERRS--------TGIYAYL----DIGFNSLISN------IRNYKSKIGLLDnsrmksdtqwvidsmRVKTPghrtqIG 405
Cdd:PRK13538 69 RDEYHQdllylghqPGIKTELtaleNLRFYQRLHGpgddeaLWEALAQVGLAG---------------FEDVP-----VR 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495051738 406 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGkGIIIISS 464
Cdd:PRK13538 129 QLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQG-GMVILTT 186
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
277-482 |
2.44e-05 |
|
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: 45.40 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 277 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANEA-INNGFALVTEERRSTGIYAY 355
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrSRNRYSVAYAAQKPWLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 356 LD--IGFNSLIsNIRNYKSkigLLDNSRMKSDtqwvIDSMRVktpGHRTQIG----SLSGGNQQKVIIGRWLLTQPEILM 429
Cdd:cd03290 95 VEenITFGSPF-NKQRYKA---VTDACSLQPD----IDLLPF---GDQTEIGergiNLSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495051738 430 LDEPTRGIDVGAKFEIYQL-IAELAKKGKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:cd03290 164 LDDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
407-482 |
2.69e-05 |
|
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: 44.93 E-value: 2.69e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495051738 407 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIII-ISSEMPELLGITDRILVMSNG 482
Cdd:cd03232 109 LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCtIHQPSASIFEKFDRLLLLKRG 185
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
27-210 |
3.18e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.86 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 27 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfHSAKEALengiSMVHQELNLVLQRSVM 106
Cdd:PRK13541 14 KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNIN-NIAKPYC----TYIGHNLGLKLEMTVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 107 DN--MWLGRYPTKGVfVDQEKMYLDTKAIFDEldididpkaRVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKE 184
Cdd:PRK13541 89 ENlkFWSEIYNSAET-LYAAIHYFKLHDLLDE---------KCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKEN 158
|
170 180
....*....|....*....|....*.
gi 495051738 185 VNHLFKIIrKLKERGCGIVYISHKME 210
Cdd:PRK13541 159 RDLLNNLI-VMKANSGGIVLLSSHLE 183
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
281-484 |
3.20e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 46.11 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 281 DVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSGGTISLHGKKINNHSANEainngfalVTEERRSTGI-----YAY 355
Cdd:PRK11308 33 GVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEA--------QKLLRQKIQIvfqnpYGS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 356 LdigfnslisnirNYKSKIG------LLDNSRM--KSDTQWVIDSMRvkTPGHRTQIGS-----LSGGNQQKVIIGRWLL 422
Cdd:PRK11308 105 L------------NPRKKVGqileepLLINTSLsaAERREKALAMMA--KVGLRPEHYDryphmFSGGQRQRIAIARALM 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495051738 423 TQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-GKGIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:PRK11308 171 LDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRC 233
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
29-78 |
3.77e-05 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 44.78 E-value: 3.77e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 495051738 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKD---SGSILFQGKEID 78
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLT 69
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
29-226 |
4.68e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 46.03 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDS--GSILFQGKEIdfhsAKEALENgISMVHQELNLVLQRSVM 106
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKP----TKQILKR-TGFVTQDDILYPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 107 DNM---WLGRYPTKgvFVDQEKMYLdTKAIFDELDIDIDPKARVGT-----LSVSQMQMIEIAKAFSYDAKIVIMDEPTS 178
Cdd:PLN03211 159 ETLvfcSLLRLPKS--LTKQEKILV-AESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495051738 179 SLTEKEVNHLFKIIRKLKERGCGIVYISHK-MEEIFQLCDEITILRDGQ 226
Cdd:PLN03211 236 GLDATAAYRLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
403-484 |
4.84e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 45.99 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 403 QIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAElAKKGKGIIIISSEMPELLGItDRILVMSNG 482
Cdd:PRK11174 482 QAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNA-ASRRQTTLMVTHQLEDLAQW-DQIWVMQDG 559
|
..
gi 495051738 483 LV 484
Cdd:PRK11174 560 QI 561
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
6-207 |
4.84e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.96 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 6 TQSSGEYLLEMTNINKSFPGVKaldnvnLKVRPHSIHA-----LMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeidfh 80
Cdd:PRK13409 333 DESERETLVEYPDLTKKLGDFS------LEVEGGEIYEgevigIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK----- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 81 sakealengISMVHQELNLVLQRSVMDnmWLGRYPTK--GVFVDQEkmyldtkaIFDELDIDIDPKARVGTLSVSQMQMI 158
Cdd:PRK13409 402 ---------ISYKPQYIKPDYDGTVED--LLRSITDDlgSSYYKSE--------IIKPLQLERLLDKNVKDLSGGELQRV 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495051738 159 EIAKAFSYDAKIVIMDEPTSSL-TEKEVNhLFKIIRKL-KERGCGIVYISH 207
Cdd:PRK13409 463 AIAACLSRDADLYLLDEPSAHLdVEQRLA-VAKAIRRIaEEREATALVVDH 512
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
14-236 |
5.59e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 44.69 E-value: 5.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPGVkALDNVNLKVRPHSIHALMGENGAGKStlLKC--LFGIY----QKDSGSILFQGKEIdfhsAKEALE 87
Cdd:PRK10418 5 IELRNIALQAAQP-LVHGVSLTLQRGRVLALVGGSGSGKS--LTCaaALGILpagvRQTAGRVLLDGKPV----APCALR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 88 nGISMVhqelnLVLQ--RSVMD---NM---------WLGRYPTKGVFVdqekmyldtkAIFDELDIDiDPkARVGTLSVS 153
Cdd:PRK10418 78 -GRKIA-----TIMQnpRSAFNplhTMhtharetclALGKPADDATLT----------AALEAVGLE-NA-ARVLKLYPF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 154 QM-----QMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQW 227
Cdd:PRK10418 140 EMsggmlQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
....*....
gi 495051738 228 IATQSLEGL 236
Cdd:PRK10418 220 VEQGDVETL 228
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
408-505 |
7.96e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 44.73 E-value: 7.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 408 SGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNGLV--S 485
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRViaD 225
|
90 100
....*....|....*....|.
gi 495051738 486 GIVDT-KTTTQNEILRLASLH 505
Cdd:NF000106 226 GKVDElKTKVGGRTLQIRPAH 246
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
407-482 |
8.10e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 44.00 E-value: 8.10e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495051738 407 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK10584 147 LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNG 222
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
26-219 |
8.51e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 43.47 E-value: 8.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 26 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKclfgiyqkdsgsilfqgkEIDFHSAKEALENGISMVhqelnlvlqrsv 105
Cdd:cd03238 8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN------------------EGLYASGKARLISFLPKF------------ 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 106 mdnmwlgrYPTKGVFVDQEKMYLDTKAIFDELDididpkARVGTLSVSQMQMIEIAK--AFSYDAKIVIMDEPTSSLTEK 183
Cdd:cd03238 58 --------SRNKLIFIDQLQFLIDVGLGYLTLG------QKLSTLSGGELQRVKLASelFSEPPGTLFILDEPSTGLHQQ 123
|
170 180 190
....*....|....*....|....*....|....*.
gi 495051738 184 EVNHLFKIIRKLKERGCGIVYISHKmEEIFQLCDEI 219
Cdd:cd03238 124 DINQLLEVIKGLIDLGNTVILIEHN-LDVLSSADWI 158
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
36-478 |
8.72e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.18 E-value: 8.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 36 VRPHSIHALMGENGAGKSTLLKCL-------FGIYQKDSG--SIL--FQGKEIdFHSAKEALENGISMVH--QELNL--- 99
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILsgelipnLGDYEEEPSwdEVLkrFRGTEL-QNYFKKLYNGEIKVVHkpQYVDLipk 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 100 VLQRSVMDnmWLGRYPTKGVFvDQEKMYLDTKAIfdeLDIDIDpkarvgTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSS 179
Cdd:PRK13409 175 VFKGKVRE--LLKKVDERGKL-DEVVERLGLENI---LDRDIS------ELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 180 LTEKEVNHLFKIIRKLKErGCGIVYISHKMEEIFQLCDEITIL----------------RDGqwIaTQSLEG-Ldmdkii 242
Cdd:PRK13409 243 LDIRQRLNVARLIRELAE-GKYVLVVEHDLAVLDYLADNVHIAygepgaygvvskpkgvRVG--I-NEYLKGyL------ 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 243 ammvgRSLNQRF----------PDRENKPGEVILEVRNLT-SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFG 311
Cdd:PRK13409 313 -----PEENMRIrpepiefeerPPRDESERETLVEYPDLTkKLGDFSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAG 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 312 IREKSGGTISlhgkkinnhsaneainngfalvTEERRStgiYA--YLDIGFN----SLISNIRnykskiGLLDNSRMKSD 385
Cdd:PRK13409 388 VLKPDEGEVD----------------------PELKIS---YKpqYIKPDYDgtveDLLRSIT------DDLGSSYYKSE 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 386 tqwVIDSMRVKtPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELA-KKGKGIIIISS 464
Cdd:PRK13409 437 ---IIKPLQLE-RLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAeEREATALVVDH 512
|
490
....*....|....
gi 495051738 465 EMPELLGITDRILV 478
Cdd:PRK13409 513 DIYMIDYISDRLMV 526
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
407-482 |
8.97e-05 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 44.71 E-value: 8.97e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495051738 407 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKgKGI--IIISSEMPELLGITDRILVMSNG 482
Cdd:PRK11432 137 ISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQ-FNItsLYVTHDQSEAFAVSDTVIVMNKG 213
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-253 |
1.28e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 44.34 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 2 VSNNTQSSgeylLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAG--KSTLLKCLFGiyqKDSGSILFqgKEIDF 79
Cdd:NF000106 6 ISNGARNA----VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPW--RF*TW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 80 HSAKEALENGISMvhqelnlvlQRSVmdnmwlgRYPTKGVFVDQEKMYL----------DTKAIFDELDIDIDPKARVG- 148
Cdd:NF000106 77 CANRRALRRTIG*---------HRPV-------R*GRRESFSGRENLYMigr*ldlsrkDARARADELLERFSLTEAAGr 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 149 ---TLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDG 225
Cdd:NF000106 141 aaaKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRG 220
|
250 260
....*....|....*....|....*...
gi 495051738 226 QWIATQSLegldmDKIIAMMVGRSLNQR 253
Cdd:NF000106 221 RVIADGKV-----DELKTKVGGRTLQIR 243
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
7-207 |
1.36e-04 |
|
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: 44.39 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 7 QSSGEYLLEMTNINKSFPGVKaldnvnLKVRPHSIH-----ALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeidfhs 81
Cdd:COG1245 335 EKEEETLVEYPDLTKSYGGFS------LEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK------ 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 82 akealengISMVHQELNLVLQRSVMDNMwlgryptKGVFVDQekmyLDTKAIFDELdidIDP-------KARVGTLSVSQ 154
Cdd:COG1245 403 --------ISYKPQYISPDYDGTVEEFL-------RSANTDD----FGSSYYKTEI---IKPlglekllDKNVKDLSGGE 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495051738 155 MQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKL-KERGCGIVYISH 207
Cdd:COG1245 461 LQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFaENRGKTAMVVDH 514
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
14-78 |
1.63e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 44.19 E-value: 1.63e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495051738 14 LEMTNINKSFPGVK-ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEID 78
Cdd:PRK10522 323 LELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT 388
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
407-474 |
2.54e-04 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 42.83 E-value: 2.54e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495051738 407 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-GKGIIIISSEMPELLGITD 474
Cdd:PRK11831 144 LSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIAD 212
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
13-70 |
2.62e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.62 E-value: 2.62e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 495051738 13 LLEMTNINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSI 70
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI 369
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
405-482 |
3.53e-04 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 42.26 E-value: 3.53e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495051738 405 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKGKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK10771 128 GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADG 206
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
402-434 |
4.52e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.80 E-value: 4.52e-04
10 20 30
....*....|....*....|....*....|...
gi 495051738 402 TQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPT 434
Cdd:PRK11819 159 AKVTKLSGGERRRVALCRLLLEKPDMLLLDEPT 191
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
406-485 |
5.45e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.54 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 406 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAkfeIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNGLVS 485
Cdd:PLN03073 627 TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA---VEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVT 703
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
29-236 |
5.78e-04 |
|
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: 41.82 E-value: 5.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEID---FHSakeaLENGISMVHQE--------- 96
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISklpLHT----LRSRLSIILQDpilfsgsir 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 97 LNLVLQRSVMDN-MWlgryptKGVFVDQEKMYLdtKAIFDELDIDIDPKARvgTLSVSQMQMIEIAKAFSYDAKIVIMDE 175
Cdd:cd03288 113 FNLDPECKCTDDrLW------EALEIAQLKNMV--KSLPGGLDAVVTEGGE--NFSVGQRQLFCLARAFVRKSSILIMDE 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495051738 176 PTSSLTEKEVNHLFKII-RKLKERgcGIVYISHKMEEIFQlCDEITILRDGQWIATQSLEGL 236
Cdd:cd03288 183 ATASIDMATENILQKVVmTAFADR--TVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENL 241
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
391-478 |
6.94e-04 |
|
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: 40.63 E-value: 6.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 391 DSMRVKTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKG-KGIIIISSEMPEL 469
Cdd:cd03222 56 DEWDGITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGkKTALVVEHDLAVL 135
|
....*....
gi 495051738 470 LGITDRILV 478
Cdd:cd03222 136 DYLSDRIHV 144
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
280-482 |
7.62e-04 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 41.22 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 280 RDVSFDLHKGEILGIAGLVGAKRTdiveTLF----GIREKSGGTISLHGKkinnhsaneainngfalvteerrstgIYAY 355
Cdd:COG1134 43 KDVSFEVERGESVGIIGRNGAGKS----TLLkliaGILEPTSGRVEVNGR--------------------------VSAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 356 LDI--GFNSLIS---NIRNykskiglldNSRM----KSDTQWVIDS------------MRVKT--PGHRTQIG-SLSggn 411
Cdd:COG1134 93 LELgaGFHPELTgreNIYL---------NGRLlglsRKEIDEKFDEivefaelgdfidQPVKTysSGMRARLAfAVA--- 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495051738 412 qqkviigrwLLTQPEILMLDEptrGIDVG-AKFEI--YQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:COG1134 161 ---------TAVDPDILLVDE---VLAVGdAAFQKkcLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKG 222
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
424-486 |
7.64e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.42 E-value: 7.64e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495051738 424 QPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSE-MPELLGiTDRILVMSNG--LVSG 486
Cdd:NF033858 415 KPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHfMNEAER-CDRISLMHAGrvLASD 479
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
263-438 |
8.25e-04 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 41.15 E-value: 8.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 263 EVILEVRNL--TSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGI---REKSGGTISLHGKKINNHSAneain 337
Cdd:PRK09984 2 QTIIRVEKLakTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGR----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 338 ngfaLVTEERRSTGIYAYLDIGFN-----SLISNIRnykskIGLLDNSRM-KSDTQWVIDSMRVKTPGHRTQIG------ 405
Cdd:PRK09984 77 ----LARDIRKSRANTGYIFQQFNlvnrlSVLENVL-----IGALGSTPFwRTCFSWFTREQKQRALQALTRVGmvhfah 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 495051738 406 ----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID 438
Cdd:PRK09984 148 qrvsTLSGGQQQRVAIARALMQQAKVILADEPIASLD 184
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
14-109 |
8.51e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 41.75 E-value: 8.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 14 LEMTNINKSFPG-VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfhsAKEALENGISM 92
Cdd:PRK11650 4 LKLQAVRKSYDGkTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVN---ELEPADRDIAM 80
|
90
....*....|....*..
gi 495051738 93 VHQELNLVLQRSVMDNM 109
Cdd:PRK11650 81 VFQNYALYPHMSVRENM 97
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
149-230 |
8.96e-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: 41.06 E-value: 8.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 149 TLSVSQMQMIEIAKAFSYDAK---IVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIfQLCDEITIL--- 222
Cdd:cd03271 169 TLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVI-KCADWIIDLgpe 247
|
90
....*....|.
gi 495051738 223 ---RDGQWIAT 230
Cdd:cd03271 248 ggdGGGQVVAS 258
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
28-226 |
1.31e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.41 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 28 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeidfhSAKEALENGISMvhqelnlvlQRSVMD 107
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS-----AALIAISSGLNG---------QLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 108 NMWLgryptKGVF--VDQEKMYLDTKAIFDELDIDIDPKARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEV 185
Cdd:PRK13545 105 NIEL-----KGLMmgLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFT 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 495051738 186 NHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 226
Cdd:PRK13545 180 KKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQ 220
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
29-226 |
1.48e-03 |
|
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: 41.47 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGiyqkdsgsilfqgkEIDFHSAKEALENGISMVHQEL---NLVLQRSV 105
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLA--------------EMDKVEGHVHMKGSVAYVPQQAwiqNDSLRENI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 106 MDNMWLgryptkgvfvdQEKMY---LDTKAIFDELDI-------DIDPKARvgTLSVSQMQMIEIAKAFSYDAKIVIMDE 175
Cdd:TIGR00957 720 LFGKAL-----------NEKYYqqvLEACALLPDLEIlpsgdrtEIGEKGV--NLSGGQKQRVSLARAVYSNADIYLFDD 786
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495051738 176 PTSSLTEKEVNHLF------KIIRKLKERgcgiVYISHKMEEIFQLcDEITILRDGQ 226
Cdd:TIGR00957 787 PLSAVDAHVGKHIFehvigpEGVLKNKTR----ILVTHGISYLPQV-DVIIVMSGGK 838
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
149-212 |
1.48e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.15 E-value: 1.48e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495051738 149 TLSVSQMQMIEIAKAFSYDAK---IVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEI 212
Cdd:TIGR00630 829 TLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVI 895
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
11-62 |
1.64e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.87 E-value: 1.64e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 495051738 11 EYLLEMTNINKSFPGVKA-LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGI 62
Cdd:PRK11819 4 QYIYTMNRVSKVVPPKKQiLKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV 56
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
390-463 |
1.77e-03 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 40.16 E-value: 1.77e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495051738 390 IDSMRVKTPGHRTqIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKgKGIIIIS 463
Cdd:PRK10575 132 ISLVGLKPLAHRL-VDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQE-RGLTVIA 203
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
399-482 |
1.85e-03 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 40.86 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 399 GHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIIS--SEMPEllgi 472
Cdd:PRK10790 465 GLYTPLGeqgnNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHrlSTIVE---- 540
|
90
....*....|
gi 495051738 473 TDRILVMSNG 482
Cdd:PRK10790 541 ADTILVLHRG 550
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
408-482 |
2.01e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 40.01 E-value: 2.01e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495051738 408 SGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIIsSEMPELLG--ITDRILVMSNG 482
Cdd:CHL00131 153 SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILI-THYQRLLDyiKPDYVHVMQNG 228
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
29-74 |
2.04e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.92 E-value: 2.04e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 495051738 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG 74
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG 62
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
406-500 |
2.61e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 406 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAkfeIYQLIAELAKKGKGIIIISSEMpELLG--ITDRILVMSNGL 483
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA---VLWLETYLLKWPKTFIVVSHAR-EFLNtvVTDILHLHGQKL 419
|
90
....*....|....*....
gi 495051738 484 VS--GIVDTKTTTQNEILR 500
Cdd:PLN03073 420 VTykGDYDTFERTREEQLK 438
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
124-219 |
3.32e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.20 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 124 EKMYLDTKAIFDE------LDIDIDPKAR-VGTLSVSQMQMIEIAKAFSYDAK---IVIMDEPTSSLTEKEVNHLFKIIR 193
Cdd:PRK00635 777 EKFFLDEPSIHEKihalcsLGLDYLPLGRpLSSLSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHTHDIKALIYVLQ 856
|
90 100
....*....|....*....|....*.
gi 495051738 194 KLKERGCGIVYISHKMeEIFQLCDEI 219
Cdd:PRK00635 857 SLTHQGHTVVIIEHNM-HVVKVADYV 881
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
27-228 |
3.45e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 39.68 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 27 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeiDFHSAKEALENGISMVHQELNLVLQRSVm 106
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFK--DEKNKKKTKEKEKVLEKLVIQKTRFKKI- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 107 DNMWLGRYPTKGVF------------------------VDQEKMYLDTKAIFDELDIDID--PKARVGtLSVSQMQMIEI 160
Cdd:PRK13651 98 KKIKEIRRRVGVVFqfaeyqlfeqtiekdiifgpvsmgVSKEEAKKRAAKYIELVGLDESylQRSPFE-LSGGQKRRVAL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495051738 161 AKAFSYDAKIVIMDEPTSSLTEKEVNHLFKIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWI 228
Cdd:PRK13651 177 AGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKII 244
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
46-85 |
3.53e-03 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 39.06 E-value: 3.53e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 495051738 46 GENGAGKSTLLKCLFGIYQKDSGSIlfqgkEIDFHSAKEA 85
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQI-----QIDGKTATRG 78
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
43-212 |
3.86e-03 |
|
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: 38.12 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 43 ALMGENGAGKSTLLKCLFGIYQKDSGSIlfqgkeidfhsakealengismvhqelnlvlqrsvmdnmwlgryptkgVFVD 122
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELGPPGGGV------------------------------------------------IYID 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495051738 123 QEKMYLDTKAIFDELDIDIDPKArvgtLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFKIIR------KLK 196
Cdd:smart00382 38 GEDILEEVLDQLLLIIVGGKKAS----GSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrllllLKS 113
|
170
....*....|....*.
gi 495051738 197 ERGCGIVYISHKMEEI 212
Cdd:smart00382 114 EKNLTVILTTNDEKDL 129
|
|
| |
