|
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: 1025.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 16 MTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENGISMVHQ 95
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 96 ELNLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYDAKIVIMDE 175
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 176 PTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIATQPLEGLDMDKIISMMVGRSLNQRFP 255
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVGRSLTQRFP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 256 DKENKPGEVILQVRNLTSLRQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEA 335
Cdd:PRK10982 241 DKENKPGEVILEVRNLTSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 336 INHGFALVTEERRSTGIYAYLDIGFNSLISNIQNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGNQQKV 415
Cdd:PRK10982 321 INHGFALVTEERRSTGIYAYLDIGFNSLISNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGNQQKV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 416 VIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTKTTTQ 495
Cdd:PRK10982 401 IIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTKTTTQ 480
|
490
....*....|.
gi 507082969 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: 796.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 11 EYLLEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENGI 90
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 91 SMVHQELNLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYDAKI 170
Cdd:COG1129 82 AIIHQELNLVPNLSVAENIFLGREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 171 VIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIATQPLEGLDMDKIISMMVGRSL 250
Cdd:COG1129 162 LILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMVGREL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 251 NQRFPDKENKPGEVILQVRNLTslRQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNH 330
Cdd:COG1129 242 EDLFPKRAAAPGEVVLEVEGLS--VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 331 SANEAINHGFALVTEERRSTGIYAYLDIGFNSLISNIQNYKNKvGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGG 410
Cdd:COG1129 320 SPRDAIRAGIAYVPEDRKGEGLVLDLSIRENITLASLDRLSRG-GLLDRRRERALAEEYIKRLRIKTPSPEQPVGNLSGG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 411 NQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDT 490
Cdd:COG1129 399 NQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDR 478
|
490
....*....|...
gi 507082969 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: 586.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 11 EYLLEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDS--GSILFQGKEIDFHSAKEALEN 88
Cdd:PRK13549 3 EYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNIRDTERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 89 GISMVHQELNLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYDA 168
Cdd:PRK13549 83 GIAIIHQELALVKELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 169 KIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIATQPLEGLDMDKIISMMVGR 248
Cdd:PRK13549 163 RLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITMMVGR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 249 SLNQRFPDKENKPGEVILQVRNLTSLR--QPSIR---DISFDLHKGEILGIAGLVGAKRTDIVETLFGIRE-KSSGTITL 322
Cdd:PRK13549 243 ELTALYPREPHTIGEVILEVRNLTAWDpvNPHIKrvdDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 323 HGKKINNHSANEAINHGFALVTEERRSTGIYAYLDIGFNSLISNIQNYkNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRT 402
Cdd:PRK13549 323 DGKPVKIRNPQQAIAQGIAMVPEDRKRDGIVPVMGVGKNITLAALDRF-TGGSRIDDAAELKTILESIQRLKVKTASPEL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 403 QIGSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK13549 402 AIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEG 481
|
490 500
....*....|....*....|
gi 507082969 483 LVAGIVDTKTTTQNEILRLA 502
Cdd:PRK13549 482 KLKGDLINHNLTQEQVMEAA 501
|
|
| 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: 552.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENGISM 92
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 93 VHQELNLVLQRSVMDNMWLGRYPTKGM-FVDQDKMYRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYDAKIV 171
Cdd:PRK10762 84 IHQELNLIPQLTIAENIFLGREFVNRFgRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 172 IMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIATQPLEGLDMDKIISMMVGRSLN 251
Cdd:PRK10762 164 IMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMMVGRKLE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 252 QRFPDKENKPGEVILQVRNLTSlrqPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHS 331
Cdd:PRK10762 244 DQYPRLDKAPGEVRLKVDNLSG---PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 332 ANEAINHGFALVTEERRSTGIYAYLDIGFNSLISNIQNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGN 411
Cdd:PRK10762 321 PQDGLANGIVYISEDRKRDGLVLGMSVKENMSLTALRYFSRAGGSLKHADEQQAVSDFIRLFNIKTPSMEQAIGLLSGGN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 412 QQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTK 491
Cdd:PRK10762 401 QQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTRE 480
|
490
....*....|.
gi 507082969 492 TTTQNEILRLA 502
Cdd:PRK10762 481 QATQEKLMAAA 491
|
|
| 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: 550.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENGISMV 93
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 94 HQELNLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYDAKIVIM 173
Cdd:PRK11288 85 YQELHLVPEMTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 174 DEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIATQP-LEGLDMDKIISMMVGRSLNQ 252
Cdd:PRK11288 165 DEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDdMAQVDRDQLVQAMVGREIGD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 253 RFPDKENKPGEVILQVRNLTS--LRQPsirdISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNH 330
Cdd:PRK11288 245 IYGYRPRPLGEVRLRLDGLKGpgLREP----ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 331 SANEAINHGFALVTEERRSTGIYAYLDIGFNSLISNIQNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGG 410
Cdd:PRK11288 321 SPRDAIRAGIMLCPEDRKAEGIIPVHSVADNINISARRHHLRAGCLINNRWEAENADRFIRSLNIKTPSREQLIMNLSGG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 411 NQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDT 490
Cdd:PRK11288 401 NQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELAR 480
|
490
....*....|..
gi 507082969 491 KTTTQNEILRLA 502
Cdd:PRK11288 481 EQATERQALSLA 492
|
|
| 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: 542.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 9 SGEYLLEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALEN 88
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 89 GISMVHQELNLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYDA 168
Cdd:COG3845 81 GIGMVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 169 KIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIATQPLEGLDMDKIISMMVGR 248
Cdd:COG3845 161 RILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAELMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 249 SLNQRFPDKENKPGEVILQVRNLTSLR---QPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGK 325
Cdd:COG3845 241 EVLLRVEKAPAEPGEVVLEVENLSVRDdrgVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 326 KINNHSANEAINHGFALVTEERRSTGIYAYLDIGFNSLISNIQNYK-NKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQI 404
Cdd:COG3845 321 DITGLSPRERRRLGVAYIPEDRLGRGLVPDMSVAENLILGRYRRPPfSRGGFLDRKAIRAFAEELIEEFDVRTPGPDTPA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 405 GSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:COG3845 401 RSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
490
....*....|....
gi 507082969 485 AGIVDTKTTTQNEI 498
Cdd:COG3845 481 VGEVPAAEATREEI 494
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
13-501 |
1.95e-178 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 510.49 E-value: 1.95e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDS--GSILFQGKEIDFHSAKEALENGI 90
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRFKDIRDSEALGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 91 SMVHQELNLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYDAKI 170
Cdd:NF040905 81 VIIHQELALIPYLSIAENIFLGNERAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 171 VIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIATqplegLDM-------DKIIS 243
Cdd:NF040905 161 LILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIET-----LDCradevteDRIIR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 244 MMVGRSLNQRFPDKENKPGEVILQVRNLT------SLRQpSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGireKS- 316
Cdd:NF040905 236 GMVGRDLEDRYPERTPKIGEVVFEVKNWTvyhplhPERK-VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFG---RSy 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 317 ----SGTITLHGKKINNHSANEAINHGFALVTEERRSTGIYAYLDIGFNSLISNIQNYKNKvGLLDNSRMKSDTQWVIDS 392
Cdd:NF040905 312 grniSGTVFKDGKEVDVSTVSDAIDAGLAYVTEDRKGYGLNLIDDIKRNITLANLGKVSRR-GVIDENEEIKVAEEYRKK 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 393 MRVKTPGHRTQIGSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGI 472
Cdd:NF040905 391 MNIKTPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGM 470
|
490 500
....*....|....*....|....*....
gi 507082969 473 TDRILVMSNGLVAGIVDTKTTTQNEILRL 501
Cdd:NF040905 471 CDRIYVMNEGRITGELPREEASQERIMRL 499
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
13-505 |
2.31e-169 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 487.75 E-value: 2.31e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENGISM 92
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 93 VHQELNLVLQRSVMDNMWLGRYPTKGMF----VDQDKMYRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYDA 168
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGRHLTKKVCgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 169 KIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIATQPLEGLDMDKIISMMVGR 248
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLMVGR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 249 SLNQRFPDKE----NKPGEVILQVRNLTSLRQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHG 324
Cdd:PRK09700 245 ELQNRFNAMKenvsNLAHETVFEVRNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 325 KKINNHSANEAINHGFALVTEERRSTGIYAYLDIGFNSLISN---IQNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHR 401
Cdd:PRK09700 325 KDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISRslkDGGYKGAMGLFHEVDEQRTAENQRELLALKCHSVN 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 402 TQIGSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSN 481
Cdd:PRK09700 405 QNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCE 484
|
490 500
....*....|....*....|....*
gi 507082969 482 GLVAGIVD-TKTTTQNEILRLASLH 505
Cdd:PRK09700 485 GRLTQILTnRDDMSEEEIMAWALPQ 509
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
13-502 |
1.83e-155 |
|
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: 451.97 E-value: 1.83e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDS--GSILFQGKEIDFHSAKEALENGI 90
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 91 SMVHQELNLVLQRSVMDNMWLGRYPT-KGMFVDQDKMYRDTKAIFDELDIDIDPRAR-VGTLSVSQMQMIEIAKAFSYDA 168
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEITlPGGRMAYNAMYLRAKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 169 KIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIATQPLEGLDMDKIISMMVGR 248
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 249 SLNQRFPDKENKPGEVILQVRNLTSL-----RQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIRE-KSSGTITL 322
Cdd:TIGR02633 241 EITSLYPHEPHEIGDVILEARNLTCWdvinpHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 323 HGKKINNHSANEAINHGFALVTEERRSTGIYAYLDIGFNSLISNIQNYkNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRT 402
Cdd:TIGR02633 321 NGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGKNITLSVLKSF-CFKMRIDAAAELQIIGSAIQRLKVKTASPFL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 403 QIGSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:TIGR02633 400 PIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
490 500
....*....|....*....|
gi 507082969 483 LVAGIVDTKTTTQNEILRLA 502
Cdd:TIGR02633 480 KLKGDFVNHALTQEQVLAAA 499
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-502 |
1.24e-119 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 360.91 E-value: 1.24e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 5 HTQSSGEYLLEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKE 84
Cdd:PRK15439 3 TSDTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 85 ALENGISMVHQELNLVLQRSVMDNMWLGRYPTKGmfvDQDKMyrdtKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAF 164
Cdd:PRK15439 83 AHQLGIYLVPQEPLLFPNLSVKENILFGLPKRQA---SMQKM----KQLLAALGCQLDLDSSAGSLEVADRQIVEILRGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 165 SYDAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIATQPLEGLDMDKIISM 244
Cdd:PRK15439 156 MRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 245 MVGRSLNQRFPDKE------------NKPGEVILQVRNLTSlrqPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGI 312
Cdd:PRK15439 236 ITPAAREKSLSASQklwlelpgnrrqQAAGAPVLTVEDLTG---EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 313 REKSSGTITLHGKKINNHSANEAINHGFALVTEERRSTGIYAYLDIGFN--SLISNIQNYknkvgLLDNSRMKSDTQWVI 390
Cdd:PRK15439 313 RPARGGRIMLNGKEINALSTAQRLARGLVYLPEDRQSSGLYLDAPLAWNvcALTHNRRGF-----WIKPARENAVLERYR 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 391 DSMRVKTPGHRTQIGSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELL 470
Cdd:PRK15439 388 RALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIE 467
|
490 500 510
....*....|....*....|....*....|..
gi 507082969 471 GITDRILVMSNGLVAGIVDTKTTTQNEILRLA 502
Cdd:PRK15439 468 QMADRVLVMHQGEISGALTGAAINVDTIMRLA 499
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-230 |
4.68e-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: 259.28 E-value: 4.68e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENGISMV 93
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 94 HQelnlvlqrsvmdnmwlgryptkgmfvdqdkmyrdtkaifdeldididprarvgtLSVSQMQMIEIAKAFSYDAKIVIM 173
Cdd:cd03216 81 YQ------------------------------------------------------LSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 507082969 174 DEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIAT 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 |
1.92e-80 |
|
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: 248.50 E-value: 1.92e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 262 GEVILQVRNLTslRQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEAINHGFA 341
Cdd:cd03215 1 GEPVLEVRGLS--VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 342 LVTEERRSTGIYAYLDIGFNSLISNIqnyknkvglldnsrmksdtqwvidsmrvktpghrtqigsLSGGNQQKVVIGRWL 421
Cdd:cd03215 79 YVPEDRKREGLVLDLSVAENIALSSL---------------------------------------LSGGNQQKVVLARWL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 507082969 422 LTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:cd03215 120 ARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
13-482 |
5.22e-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: 208.60 E-value: 5.22e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSFPG--VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKD---SGSILFQGKEIDFHSAKEaLE 87
Cdd:COG1123 4 LLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL-RG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 88 NGISMVHQE----LNLVlqrSVMDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKA 163
Cdd:COG1123 83 RRIGMVFQDpmtqLNPV---TVGDQI---AEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 164 FSYDAKIVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITVLRDGQWIATQP-LEGLDMDKI 241
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPpEEILAAPQA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 242 ISMMVGRSLNQRFPDKENKPGEVILQVRNLT-------SLRQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIRE 314
Cdd:COG1123 237 LAAVPRLGAARGRAAPAAAAAEPLLEVRNLSkrypvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 315 KSSGTITLHGKKINNHSANEainhgfalVTEERRSTGI-----YAYLD----IGfNSLISNIQNYknkvGLLDNSRMKSD 385
Cdd:COG1123 317 PTSGSILFDGKDLTKLSRRS--------LRELRRRVQMvfqdpYSSLNprmtVG-DIIAEPLRLH----GLLSRAERRER 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 386 TQWVIDsmRVK-TPGHRTQ-IGSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIII 462
Cdd:COG1123 384 VAELLE--RVGlPPDLADRyPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFI 461
|
490 500
....*....|....*....|
gi 507082969 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 |
3.85e-52 |
|
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: 176.86 E-value: 3.85e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENGISMV 93
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 94 HQELNLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELD-----IDIDPRA--RVGTLSVSQMQMIEIAKAFSY 166
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTGSGLLLARARREEREARERAEellerVGLADLAdrPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507082969 167 DAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIAT 230
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAE 224
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
10-230 |
4.33e-49 |
|
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: 169.45 E-value: 4.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 10 GEYLLEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENG 89
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 90 ISMVHQELNLVLQRSVMDNMWLG-----RYPTKGMFVDQDKMYRDTKAIFDE----LD-IDIDPRA--RVGTLSVSQMQM 157
Cdd:COG0411 81 IARTFQNPRLFPELTVLENVLVAaharlGRGLLAALLRLPRARREEREARERaeelLErVGLADRAdePAGNLSYGQQRR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507082969 158 IEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFTIIRKLK-ERGCGIVYISHKMEEIFQLCDEITVLRDGQWIAT 230
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRdERGITILLIEHDMDLVMGLADRIVVLDFGRVIAE 234
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
14-236 |
2.66e-44 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 155.99 E-value: 2.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAkEALENgISMV 93
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPA-EVRRR-IGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 94 HQELNLVLQRSVMDNM-WLGRYptKGMfvDQDKMYRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYDAKIVI 172
Cdd:COG1131 79 PQEPALYPDLTVRENLrFFARL--YGL--PRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507082969 173 MDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIATQPLEGL 236
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
13-236 |
4.21e-44 |
|
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: 155.79 E-value: 4.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeIDFHSAKEALENGISM 92
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDG--EDVRKEPREARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 93 VHQELNLVLQRSVMDNMwlgRY--PTKGMFVDQDKmyRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYDAKI 170
Cdd:COG4555 79 LPDERGLYDRLTVRENI---RYfaELYGLFDEELK--KRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507082969 171 VIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIATQPLEGL 236
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
14-226 |
1.20e-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: 146.77 E-value: 1.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeiDFHSAKEALENGISMV 93
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGK--DIKKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 94 HQELNLVLQRSVMDNMWLgrypTKGMfvdqdkmyrdtkaifdeldididpRARVGtlsvsqmqmieIAKAFSYDAKIVIM 173
Cdd:cd03230 79 PEEPSLYENLTVRENLKL----SGGM------------------------KQRLA-----------LAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 507082969 174 DEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQ 226
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
5-249 |
5.40e-37 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 142.46 E-value: 5.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 5 HTQSSGEYLLEMTGINksfpGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKE 84
Cdd:COG1129 248 RAAAPGEVVLEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 85 ALENGISMV---HQELNLVLQRSVMDNM---WLGRYpTKGMFVDQDKMYRDTKAIFDELDIDI-DPRARVGTLSVSQMQM 157
Cdd:COG1129 324 AIRAGIAYVpedRKGEGLVLDLSIRENItlaSLDRL-SRGGLLDRRRERALAEEYIKRLRIKTpSPEQPVGNLSGGNQQK 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 158 IEIAKAFSYDAKIVIMDEPT-----SSLTEkevnhLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIATQP 232
Cdd:COG1129 403 VVLAKWLATDPKVLILDEPTrgidvGAKAE-----IYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELD 477
|
250
....*....|....*..
gi 507082969 233 LEGLDMDKIISMMVGRS 249
Cdd:COG1129 478 REEATEEAIMAAATGGA 494
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
14-241 |
2.62e-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: 134.62 E-value: 2.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFP-GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDF--HSAKEALENGI 90
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlkGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 91 SMVHQELNLVLQRSVMDNMWLGRYPTK-------GMFVDQDKmyRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKA 163
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRRstwrslfGLFPKEEK--QRALAALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 164 FSYDAKIVIMDEPTSSL---TEKEVNHLFTIIRklKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIATQPLEGLDMDK 240
Cdd:cd03256 159 LMQQPKLILADEPVASLdpaSSRQVMDLLKRIN--REEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEV 236
|
.
gi 507082969 241 I 241
Cdd:cd03256 237 L 237
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
15-226 |
7.79e-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: 132.21 E-value: 7.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 15 EMTGINKSFPG--VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENgISM 92
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK-VGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 93 V-----HQELNLVLQRSVMDNMwlgryptKGMFVDQDKMYRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYD 167
Cdd:cd03225 80 VfqnpdDQFFGPTVEEEVAFGL-------ENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 507082969 168 AKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQ 226
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
13-229 |
1.90e-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: 132.47 E-value: 1.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKE-ALEngIS 91
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElARR--IA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 92 MVHQELNLVLQRSVMDNMWLGRYPTKGMFVDQDKmyRDTKAIFDELDI-DIDPRA--RVGTLSVSQMQMIEIAKAFSYDA 168
Cdd:COG1120 79 YVPQEPPAPFGLTVRELVALGRYPHLGLFGRPSA--EDREAVEEALERtGLEHLAdrPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507082969 169 KIVIMDEPTSSLtekEVNH---LFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITVLRDGQWIA 229
Cdd:COG1120 157 PLLLLDEPTSHL---DLAHqleVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVA 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
14-226 |
3.35e-35 |
|
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: 130.72 E-value: 3.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfhSAKEALENGISMV 93
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV---TGVPPERRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 94 HQELNLVLQRSVMDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYDAKIVIM 173
Cdd:cd03259 78 FQDYALFPHLTVAENI---AFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 507082969 174 DEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITVLRDGQ 226
Cdd:cd03259 155 DEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGR 208
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
14-226 |
3.81e-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: 131.02 E-value: 3.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENGISMV 93
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 94 HQELNLVLQRSVMDNMWLGRYPTKGmfvdqdkmyRDTKAIFDELdIDIDPR------ARVGTLSVSQMQMIEIAKAFSYD 167
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRR---------AKRKARLERV-YELFPRlkerrkQLAGTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 507082969 168 AKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQ 226
Cdd:cd03224 151 PKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
15-226 |
7.33e-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: 7.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 15 EMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEaLENGISMVH 94
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE-LRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 95 QelnlvlqrsvmdnmwlgryptkgmfvdqdkmyrdtkaifdeldididprarvgtLSVSQMQMIEIAKAFSYDAKIVIMD 174
Cdd:cd00267 80 Q------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 507082969 175 EPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQ 226
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
13-234 |
9.69e-34 |
|
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: 127.31 E-value: 9.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSFPG----VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKE--AL 86
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 87 ENGISMVHQELNLVLQRSVMDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSY 166
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENV---ALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507082969 167 DAKIVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITVLRDGQWIATQPLE 234
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVE 226
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
24-226 |
2.32e-33 |
|
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: 126.29 E-value: 2.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 24 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENgISMVHQ--ELNLVL 101
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK-VGLVFQnpDDQLFA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 102 qRSVMDNMwlgryptkgMF------VDQDKMYRDTKAIFDELDIDiDPRAR-VGTLSVSQMQMIEIAKAFSYDAKIVIMD 174
Cdd:COG1122 91 -PTVEEDV---------AFgpenlgLPREEIRERVEEALELVGLE-HLADRpPHELSGGQKQRVAIAGVLAMEPEVLVLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 507082969 175 EPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQ 226
Cdd:COG1122 160 EPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGR 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
14-226 |
7.36e-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: 123.07 E-value: 7.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAK-EALENGISM 92
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 93 VHQELNLVLQRSVMDNMWLGryptkgmfvdqdkmyrdtkaifdeldididprarvgtLSVSQMQMIEIAKAFSYDAKIVI 172
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG-------------------------------------LSGGQQQRVALARALAMDPDVLL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 507082969 173 MDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITVLRDGQ 226
Cdd:cd03229 124 LDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
29-178 |
8.99e-33 |
|
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: 121.99 E-value: 8.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKeALENGISMVHQELNLVLQRSVMDN 108
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERK-SLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507082969 109 MWLGRYptkGMFVDQDKMYRDTKAIFDELDIDID----PRARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTS 178
Cdd:pfam00005 80 LRLGLL---LKGLSKREKDARAEEALEKLGLGDLadrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
14-229 |
9.23e-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: 123.93 E-value: 9.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFhsakeALENGISMV 93
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI-----AARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 94 HQELNLVLQRSVMDNM-WLGRYptKGMFVDQDKmyRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYDAKIVI 172
Cdd:cd03269 76 PEERGLYPKMKVIDQLvYLAQL--KGLKKEEAR--RRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 507082969 173 MDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIA 229
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVL 208
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
13-226 |
1.20e-32 |
|
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: 124.16 E-value: 1.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSFPG----VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALEN 88
Cdd:cd03257 1 LLEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 89 G--ISMVHQE----LNLVL--QRSVMDNMWLGRYPTKgmfvdqdkmYRDTKAIFDELDIDIDPRARVGT-----LSVSQM 155
Cdd:cd03257 81 RkeIQMVFQDpmssLNPRMtiGEQIAEPLRIHGKLSK---------KEARKEAVLLLLVGVGLPEEVLNrypheLSGGQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507082969 156 QMIEIAKAFSYDAKIVIMDEPTSSL---TEKEVNHLFtiiRKLK-ERGCGIVYISHKMEEIFQLCDEITVLRDGQ 226
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALdvsVQAQILDLL---KKLQeELGLTLLFITHDLGVVAKIADRVAVMYAGK 223
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
11-226 |
6.65e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 122.51 E-value: 6.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 11 EYLLEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKealengI 90
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR------I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 91 SMVHQ--ELNLVLQRSVMDNMWLGRYPTKGMFvdqdKMYR--DTKAIFDELD-IDIDPRA--RVGTLSVSQMQMIEIAKA 163
Cdd:COG1121 78 GYVPQraEVDWDFPITVRDVVLMGRYGRRGLF----RRPSraDREAVDEALErVGLEDLAdrPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507082969 164 FSYDAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQ 226
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGL 216
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
13-226 |
7.00e-32 |
|
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: 122.40 E-value: 7.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENGISM 92
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 93 VHQELNLVLQRSVMDNMWLGRYPTKGMfvdqdkmyRDTKAIFDELdIDIDPR------ARVGTLSVSQMQMIEIAKAFSY 166
Cdd:COG0410 83 VPEGRRIFPSLTVEENLLLGAYARRDR--------AEVRADLERV-YELFPRlkerrrQRAGTLSGGEQQMLAIGRALMS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 167 DAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQ 226
Cdd:COG0410 154 RPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGR 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-226 |
7.40e-32 |
|
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: 128.10 E-value: 7.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 8 SSGEYLLEMTGINKSFP-----GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSA 82
Cdd:COG1123 255 AAAEPLLEVRNLSKRYPvrgkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 83 KEALENG--ISMVHQE----LN--LVLQRSVMDNMWLGRYPTKgmfvdqdkmyRDTKAIFDEL--DIDIDPRA---RVGT 149
Cdd:COG1123 335 RSLRELRrrVQMVFQDpyssLNprMTVGDIIAEPLRLHGLLSR----------AERRERVAELleRVGLPPDLadrYPHE 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507082969 150 LSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITVLRDGQ 226
Cdd:COG1123 405 LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLqRELGLTYLFISHDLAVVRYIADRVAVMYDGR 482
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
15-222 |
1.09e-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: 121.10 E-value: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 15 EMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKealengISMVH 94
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR------IGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 95 QELNLVLQR--SVMDNMWLGRYPTKGMFvdqDKMYRDTKAIFDE-LDI----DIDPRaRVGTLSVSQMQMIEIAKAFSYD 167
Cdd:cd03235 75 QRRSIDRDFpiSVRDVVLMGLYGHKGLF---RRLSKADKAKVDEaLERvglsELADR-QIGELSGGQQQRVLLARALVQD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 507082969 168 AKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVL 222
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
14-226 |
2.03e-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: 119.02 E-value: 2.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPG--VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfHSAKEALENGIS 91
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLR-DLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 92 MVHQELNLvLQRSVMDNMwlgryptkgmfvdqdkmyrdtkaifdeldididprarvgtLSVSQMQMIEIAKAFSYDAKIV 171
Cdd:cd03228 80 YVPQDPFL-FSGTIRENI----------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 507082969 172 IMDEPTSSL---TEKEVnhlFTIIRKLKeRGCGIVYISHKMEEIfQLCDEITVLRDGQ 226
Cdd:cd03228 119 ILDEATSALdpeTEALI---LEALRALA-KGKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
14-230 |
4.25e-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: 116.55 E-value: 4.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfhSAKEALENGISMV 93
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ--KNIEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 94 hQELNLVLQRSVMDNMwlgRYPTKGMFVDqdkmYRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYDAKIVIM 173
Cdd:cd03268 79 -EAPGFYPNLTARENL---RLLARLLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 507082969 174 DEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIAT 230
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
10-247 |
4.33e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 122.83 E-value: 4.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 10 GEYLLEMTGIN-KSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALEN 88
Cdd:COG3845 254 GEVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 89 GISMVHQELN---LVLQRSVMDNMWLGRYPT----KGMFVDQDKMYRDTKAIFDELDIDI-DPRARVGTLSVSQMQMIEI 160
Cdd:COG3845 334 GVAYIPEDRLgrgLVPDMSVAENLILGRYRRppfsRGGFLDRKAIRAFAEELIEEFDVRTpGPDTPARSLSGGNQQKVIL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 161 AKAFSYDAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIATQPLEGLDMDK 240
Cdd:COG3845 414 ARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEATREE 493
|
....*..
gi 507082969 241 IISMMVG 247
Cdd:COG3845 494 IGLLMAG 500
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
13-236 |
5.79e-30 |
|
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: 117.60 E-value: 5.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSFP----GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdFHSAKEALEN 88
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV-TRRRRKAFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 89 GISMVHQE----LN--LVLQRSVMDnmwlgryPTKGMFVDQDKmyRDTKAIFDELDIDIDPRAR-VGTLSVSQMQMIEIA 161
Cdd:COG1124 80 RVQMVFQDpyasLHprHTVDRILAE-------PLRIHGLPDRE--ERIAELLEQVGLPPSFLDRyPHQLSGGQRQRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507082969 162 KAFSYDAKIVIMDEPTSSL---TEKEVNHLFTIIRKlkERGCGIVYISHKMEEIFQLCDEITVLRDGQWIATQPLEGL 236
Cdd:COG1124 151 RALILEPELLLLDEPTSALdvsVQAEILNLLKDLRE--ERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
10-226 |
5.96e-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: 115.22 E-value: 5.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 10 GEYLLEMTGInkSFPGvkALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENG 89
Cdd:cd03215 1 GEPVLEVRGL--SVKG--AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 90 ISMV----HQELnLVLQRSVMDNMWLGRYptkgmfvdqdkmyrdtkaifdeldididprarvgtLSVSQMQMIEIAKAFS 165
Cdd:cd03215 77 IAYVpedrKREG-LVLDLSVAENIALSSL-----------------------------------LSGGNQQKVVLARWLA 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 507082969 166 YDAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQ 226
Cdd:cd03215 121 RDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
14-226 |
1.51e-29 |
|
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: 115.28 E-value: 1.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPG----VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALE-- 87
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 88 -NGISMVHQELNLVLQRSVMDNMWLGRYPTKgmfVDQDKMYRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSY 166
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVELPLLLAG---VPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507082969 167 DAKIVIMDEPTSSL---TEKEVnhlFTIIRKL-KERGCGIVYISHKMeEIFQLCDEITVLRDGQ 226
Cdd:cd03255 158 DPKIILADEPTGNLdseTGKEV---MELLRELnKEAGTTIVVVTHDP-ELAEYADRIIELRDGK 217
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
14-226 |
1.73e-29 |
|
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: 122.64 E-value: 1.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPG--VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG---KEIDfhsaKEALEN 88
Cdd:COG2274 474 IELENVSFRYPGdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlRQID----PASLRR 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 89 GISMVHQELNLvLQRSVMDNMWLGRyPTkgmfVDQDKMYRDTK--AIFDelDIDIDPR---ARVG----TLSVSQMQMIE 159
Cdd:COG2274 550 QIGVVLQDVFL-FSGTIRENITLGD-PD----ATDEEIIEAARlaGLHD--FIEALPMgydTVVGeggsNLSGGQRQRLA 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 160 IAKAFSYDAKIVIMDEPTSSL---TEKEVNHLftiIRKLKeRGCGIVYISHKMEEIfQLCDEITVLRDGQ 226
Cdd:COG2274 622 IARALLRNPRILILDEATSALdaeTEAIILEN---LRRLL-KGRTVIIIAHRLSTI-RLADRIIVLDKGR 686
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
14-229 |
1.98e-29 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 115.29 E-value: 1.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPG--VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfHSAKEALENGIS 91
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI--RTDRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 92 MVHQELNLVLQRSVMDNMWL-GR---YPTKGMFVDQDKMYRDTKaIFDELDididprARVGTLSVSQMQMIEIAKAFSYD 167
Cdd:cd03263 79 YCPQFDALFDELTVREHLRFyARlkgLPKSEIKEEVELLLRVLG-LTDKAN------KRARTLSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507082969 168 AKIVIMDEPTSSLTEKEVNHLFTIIRKLKeRGCGIVYISHKMEEIFQLCDEITVLRDGQWIA 229
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRC 212
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-226 |
2.18e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 117.13 E-value: 2.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAK------EalE 87
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRrigylpE--E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 88 NGI--SMvhqelnlvlqrSVMDN-MWLGRYptKGMFVDQDKmyRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAF 164
Cdd:COG4152 80 RGLypKM-----------KVGEQlVYLARL--KGLSKAEAK--RRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAAL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507082969 165 SYDAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQ 226
Cdd:COG4152 145 LHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGR 206
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
13-229 |
3.22e-29 |
|
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: 114.39 E-value: 3.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSF----PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeIDFHSAKEALEN 88
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPAEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 89 GISMVHQELNLVLQRSVMDNM-WLGR-YPTKGmfvdqDKMYRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSY 166
Cdd:cd03266 79 RLGFVSDSTGLYDRLTARENLeYFAGlYGLKG-----DELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507082969 167 DAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIA 229
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVY 216
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
15-229 |
3.61e-29 |
|
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: 113.30 E-value: 3.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 15 EMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENgISMVH 94
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK-IAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 95 QELNLVlqrsvmdnmwlgryptkGM--FVDQDkmyrdtkaifdeldididprarVGTLSVSQMQMIEIAKAFSYDAKIVI 172
Cdd:cd03214 80 QALELL-----------------GLahLADRP----------------------FNELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 507082969 173 MDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITVLRDGQWIA 229
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVA 178
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
13-226 |
5.48e-29 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 113.98 E-value: 5.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSFP----GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfHSAKEA--- 85
Cdd:COG1136 4 LLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDI--SSLSERela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 86 ---LENgISMVHQELNLVLQRSVMDNMWLGRYPTKgmfVDQDKMYRDTKAIFDELdiDIDPRA--RVGTLSVSQMQMIEI 160
Cdd:COG1136 82 rlrRRH-IGFVFQFFNLLPELTALENVALPLLLAG---VSRKERRERARELLERV--GLGDRLdhRPSQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 161 AKAFSYDAKIVIMDEPTSSL---TEKEVnhlFTIIRKL-KERGCGIVYISHKmEEIFQLCDEITVLRDGQ 226
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLdskTGEEV---LELLRELnRELGTTIVMVTHD-PELAARADRVIRLRDGR 221
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
266-485 |
1.04e-28 |
|
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: 113.30 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 266 LQVRNLTSL--RQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEAINHGFALV 343
Cdd:cd03224 1 LEVENLNAGygKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 344 TEERRstgIYAYLdigfnSLISNIQnyknkVGLLDnsRMKSDTQWVIDSM---------RVKTPGhrtqiGSLSGGNQQK 414
Cdd:cd03224 81 PEGRR---IFPEL-----TVEENLL-----LGAYA--RRRAKRKARLERVyelfprlkeRRKQLA-----GTLSGGEQQM 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507082969 415 VVIGRWLLTQPEILMLDEPTRG-----IDvgakfEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVA 485
Cdd:cd03224 141 LAIARALMSRPKLLLLDEPSEGlapkiVE-----EIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVV 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
261-485 |
2.60e-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: 2.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 261 PGEVILQVRNLT-SL-RQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSA------ 332
Cdd:COG1121 2 MMMPAIELENLTvSYgGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRrigyvp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 333 -NEAINHGFALVTEERRSTGIYAyldigfnslisniqnyknKVGLLDNSRmKSDTQWVIDSM-RVKTPGHR-TQIGSLSG 409
Cdd:COG1121 82 qRAEVDWDFPITVRDVVLMGRYG------------------RRGLFRRPS-RADREAVDEALeRVGLEDLAdRPIGELSG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507082969 410 GNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVA 485
Cdd:COG1121 143 GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVA 218
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
275-485 |
3.59e-28 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 111.47 E-value: 3.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 275 RQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSA-------NEAINHGFALVTEER 347
Cdd:cd03235 11 GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKrigyvpqRRSIDRDFPISVRDV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 348 RSTGIYAYldIGFNSLISNIQNYK-----NKVGLLDNSrmksdtqwvidsmrvktpgHRtQIGSLSGGNQQKVVIGRWLL 422
Cdd:cd03235 91 VLMGLYGH--KGLFRRLSKADKAKvdealERVGLSELA-------------------DR-QIGELSGGQQQRVLLARALV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507082969 423 TQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVA 485
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVVA 211
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
14-226 |
2.27e-27 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 109.16 E-value: 2.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAK-EALENGISM 92
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNiNELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 93 VHQELNLVLQRSVMDNMWLGRYPTKGMfvDQDKMYRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYDAKIVI 172
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKGM--SKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 507082969 173 MDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQ 226
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
266-485 |
5.64e-27 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 108.61 E-value: 5.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 266 LQVRNLTSL--RQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSAneAINHGFALV 343
Cdd:COG1131 1 IEVRGLTKRygDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPA--EVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 344 TEErrsTGIYAYLdigfnSLISNIQNYKNKVGLlDNSRMKSDTQWVIDSMRVKTPGHRtQIGSLSGGNQQKVVIGRWLLT 423
Cdd:COG1131 79 PQE---PALYPDL-----TVRENLRFFARLYGL-PRKEARERIDELLELFGLTDAADR-KVGTLSGGMKQRLGLALALLH 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507082969 424 QPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG-LVA 485
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGrIVA 211
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
266-482 |
5.67e-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: 106.71 E-value: 5.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 266 LQVRNLTSL--RQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSanEAINHGFALV 343
Cdd:cd03230 1 IEVRNLSKRygKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP--EEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 344 TEErrsTGIYAYLdigfnsliSNIQNYKnkvglldnsrmksdtqwvidsmrvktpghrtqigsLSGGNQQKVVIGRWLLT 423
Cdd:cd03230 79 PEE---PSLYENL--------TVRENLK-----------------------------------LSGGMKQRLALAQALLH 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 507082969 424 QPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:cd03230 113 DPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
14-226 |
8.02e-27 |
|
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: 107.73 E-value: 8.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKealENGISMV 93
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK---DRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 94 HQELNLVLQRSVMDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYDAKIVIM 173
Cdd:cd03301 78 FQNYALYPHMTVYDNI---AFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 507082969 174 DEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITVLRDGQ 226
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQ 208
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
263-485 |
3.20e-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: 3.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 263 EVILQVRNLTSLRQPS--IRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEAINHGF 340
Cdd:COG0410 1 MPMLEVENLHAGYGGIhvLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 341 ALVTEERRstgIYAYLdigfnSLISNIQnyknkVGLLdNSRMKSDTQWVIDSM-----RVKTpgHRTQI-GSLSGGNQQK 414
Cdd:COG0410 81 GYVPEGRR---IFPSL-----TVEENLL-----LGAY-ARRDRAEVRADLERVyelfpRLKE--RRRQRaGTLSGGEQQM 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507082969 415 VVIGRWLLTQPEILMLDEPTRG-----IDvgakfEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVA 485
Cdd:COG0410 145 LAIGRALMSRPKLLLLDEPSLGlapliVE-----EIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIV 215
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
25-236 |
1.46e-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: 110.23 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 25 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfHSAKEALENGISMVHQElNLVLQRS 104
Cdd:COG4988 349 GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLS-DLDPASWRRQIAWVPQN-PYLFAGT 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 105 VMDNMWLGRyPTkgmfVDQDKMYR---------DTKAIFDELDIDIDPRARvgTLSVSQMQMIEIAKAFSYDAKIVIMDE 175
Cdd:COG4988 427 IRENLRLGR-PD----ASDEELEAaleaagldeFVAALPDGLDTPLGEGGR--GLSGGQAQRLALARALLRDAPLLLLDE 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507082969 176 PTSSL---TEKEVnhlFTIIRKLKeRGCGIVYISHKMEEIfQLCDEITVLRDGQWIATQPLEGL 236
Cdd:COG4988 500 PTAHLdaeTEAEI---LQALRRLA-KGRTVILITHRLALL-AQADRILVLDDGRIVEQGTHEEL 558
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
14-234 |
1.51e-25 |
|
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: 104.89 E-value: 1.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKE--ALENGIS 91
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 92 MVHQELNLVLQRSVMDNMwlgRYPTKGMFVDQDKMYRD-TKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYDAKI 170
Cdd:cd03261 81 MLFQSGALFDSLTVFENV---AFPLREHTRLSEEEIREiVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507082969 171 VIMDEPTSSL---TEKEVNHLftiIRKLKER-GCGIVYISHKMEEIFQLCDEITVLRDGQWIATQPLE 234
Cdd:cd03261 158 LLYDEPTAGLdpiASGVIDDL---IRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPE 222
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
8-225 |
4.47e-25 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 104.02 E-value: 4.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 8 SSGEYLLEMTGINKSFP----GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAK 83
Cdd:COG1116 2 SAAAPALELRGVSKRFPtgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 84 ealengISMVHQELNLVLQRSVMDNMWLGRyptkgMFVDQDKMYRDTKAifDELdIDidpraRVG----------TLSVS 153
Cdd:COG1116 82 ------RGVVFQEPALLPWLTVLDNVALGL-----ELRGVPKAERRERA--REL-LE-----LVGlagfedayphQLSGG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507082969 154 QMQMIEIAKAFSYDAKIVIMDEPTSSL---TEKEVNHLftIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDG 225
Cdd:COG1116 143 MRQRVAIARALANDPEVLLMDEPFGALdalTRERLQDE--LLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
14-226 |
5.65e-25 |
|
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: 103.03 E-value: 5.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIY-----QKDSGSILFQGKEI-DFHSAKEALE 87
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIyDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 88 NGISMVHQELNLvLQRSVMDNMwlgRYPTK--GMFVDQDKMYRDTKAI-FDELDIDIDPRARVGTLSVSQMQMIEIAKAF 164
Cdd:cd03260 81 RRVGMVFQKPNP-FPGSIYDNV---AYGLRlhGIKLKEELDERVEEALrKAALWDEVKDRLHALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507082969 165 SYDAKIVIMDEPTSSL----TEK-EvnhlfTIIRKLKERgCGIVYISHKMEEIFQLCDEITVLRDGQ 226
Cdd:cd03260 157 ANEPEVLLLDEPTSALdpisTAKiE-----ELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGR 217
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-229 |
2.27e-24 |
|
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: 101.13 E-value: 2.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPG--VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEaLENGIS 91
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD-LRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 92 MVHQELNLVLQrSVMDNMWLGRYPTKgmfvDQDKMYRDTKAIFDELdIDIDPRA---RVG----TLSVSQMQMIEIAKAF 164
Cdd:cd03245 82 YVPQDVTLFYG-TLRDNITLGAPLAD----DERILRAAELAGVTDF-VNKHPNGldlQIGergrGLSGGQRQAVALARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 165 SYDAKIVIMDEPTSSL---TEKEVnhlftiIRKLKERGCG--IVYISHKMeEIFQLCDEITVLRDGQWIA 229
Cdd:cd03245 156 LNDPPILLLDEPTSAMdmnSEERL------KERLRQLLGDktLIIITHRP-SLLDLVDRIIVMDSGRIVA 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
9-226 |
2.55e-24 |
|
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: 102.34 E-value: 2.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 9 SGEYLLEMTGinkSFPGVKaldNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALE- 87
Cdd:cd03294 26 SKEEILKKTG---QTVGVN---DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELREl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 88 --NGISMVHQELNLVLQRSVMDNMWLGrYPTKGMfvdqDKMYRDTKAI--FDELDIDIDPRARVGTLSVSQMQMIEIAKA 163
Cdd:cd03294 100 rrKKISMVFQSFALLPHRTVLENVAFG-LEVQGV----PRAEREERAAeaLELVGLEGWEHKYPDELSGGMQQRVGLARA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507082969 164 FSYDAKIVIMDEPTSSL---TEKEV-NHLFTIIRKLKERgcgIVYISHKMEEIFQLCDEITVLRDGQ 226
Cdd:cd03294 175 LAVDPDILLMDEAFSALdplIRREMqDELLRLQAELQKT---IVFITHDLDEALRLGDRIAIMKDGR 238
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
14-226 |
3.21e-24 |
|
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: 101.26 E-value: 3.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfhSAKEALENGISMV 93
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA---TDVPVQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 94 HQELNLVLQRSVMDNMWLG-RYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYDAKIVI 172
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGlRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 507082969 173 MDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITVLRDGQ 226
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGR 214
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
24-226 |
3.68e-24 |
|
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: 100.02 E-value: 3.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 24 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfhSAKEALENgISMVHQELNLVLQR 103
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKS-IGYVMQDVDYQLFT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 104 -SVMDNMWLGRYPTkgmfvdqDKMYRDTKAIFDELDI----DIDPRarvgTLSVSQMQMIEIAKAFSYDAKIVIMDEPTS 178
Cdd:cd03226 87 dSVREELLLGLKEL-------DAGNEQAETVLKDLDLyalkERHPL----SLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 507082969 179 SLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQ 226
Cdd:cd03226 156 GLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGA 203
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
267-482 |
5.04e-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: 99.85 E-value: 5.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 267 QVRNLT----SLRQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEAINH-GFA 341
Cdd:cd03225 1 ELKNLSfsypDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKvGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 342 L-----------VTEErrstgiyayldigfnsLISNIQNYKnkvglLDNSRMKSDTQWVIDSMRVKTPGHRtQIGSLSGG 410
Cdd:cd03225 81 FqnpddqffgptVEEE----------------VAFGLENLG-----LPEEEIEERVEEALELVGLEGLRDR-SPFTLSGG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507082969 411 NQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:cd03225 139 QKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
13-487 |
6.42e-24 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 105.32 E-value: 6.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSF----PGVKALDNVNLKVRPHSIHALMGENGAGKS-TLLKCLFGIYQK----DSGSILFQGKE---IDFH 80
Cdd:PRK10261 12 VLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAgglvQCDKMLLRRRSrqvIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 81 SAKEALENG-----ISMVHQE----LNLV------LQRSVMDNMWLGRyptkgmfvdqDKMYRDTKAIFDELDIdidPRA 145
Cdd:PRK10261 92 EQSAAQMRHvrgadMAMIFQEpmtsLNPVftvgeqIAESIRLHQGASR----------EEAMVEAKRMLDQVRI---PEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 146 RV------GTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDE 218
Cdd:PRK10261 159 QTilsrypHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAEIADR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 219 ITVLRDGQWIATQPLEG-------------LDMDKIISMMVGRSLNQRFP------------DKENK---PGEVILQVRN 270
Cdd:PRK10261 239 VLVMYQGEAVETGSVEQifhapqhpytralLAAVPQLGAMKGLDYPRRFPlislehpakqepPIEQDtvvDGEPILQVRN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 271 LTSlRQP--------------SIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSAN--E 334
Cdd:PRK10261 319 LVT-RFPlrsgllnrvtrevhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 335 AINHGFALVTEERrstgiYAYLD----IGFnSLISNIQNYknkvGLLDNSRMKSDTQWVIDSMRVKtPGHRTQI-GSLSG 409
Cdd:PRK10261 398 ALRRDIQFIFQDP-----YASLDprqtVGD-SIMEPLRVH----GLLPGKAAAARVAWLLERVGLL-PEHAWRYpHEFSG 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 410 GNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGI--IIISSEMPELLGITDRILVMSNGLVAGI 487
Cdd:PRK10261 467 GQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDL-QRDFGIayLFISHDMAVVERISHRVAVMYLGQIVEI 545
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
14-226 |
8.27e-24 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 102.08 E-value: 8.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPG----VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKE--ALE 87
Cdd:COG1135 2 IELENLSKTFPTkggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElrAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 88 NGISMVHQELNLVLQRSVMDNMwlgRYPTK--GMfvdqDKMYRDTKAifDELdIDidpraRVG----------TLSVSQM 155
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENV---ALPLEiaGV----PKAEIRKRV--AEL-LE-----LVGlsdkadaypsQLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 156 QMIEIAKAFSYDAKIVIMDEPTSSL----TE------KEVNhlftiirklKERGCGIVYISHKMEEIFQLCDEITVLRDG 225
Cdd:COG1135 147 QRVGIARALANNPKVLLCDEATSALdpetTRsildllKDIN---------RELGLTIVLITHEMDVVRRICDRVAVLENG 217
|
.
gi 507082969 226 Q 226
Cdd:COG1135 218 R 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
266-482 |
9.91e-24 |
|
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: 9.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 266 LQVRNLTSLR--QPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANeainhgfalV 343
Cdd:cd03229 1 LELKNVSKRYgqKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDE---------L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 344 TEERRSTGiYAYLDIGFNSLISNIQNyknkVGLLdnsrmksdtqwvidsmrvktpghrtqigsLSGGNQQKVVIGRWLLT 423
Cdd:cd03229 72 PPLRRRIG-MVFQDFALFPHLTVLEN----IALG-----------------------------LSGGQQQRVALARALAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 424 QPEILMLDEPTRGIDVGAKFEIYQLIAELAKKD-KGIIIISSEMPELLGITDRILVMSNG 482
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLQAQLgITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
265-482 |
1.08e-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: 99.12 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 265 ILQVRNLT------SLRQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEAinh 338
Cdd:cd03257 1 LLEVKNLSvsfptgGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 339 gfalvtEERRStgiyaylDIG------FNSLisniqnyknkvglldNSRMKSDTQwVIDSMRVKTPGHRTQI-------- 404
Cdd:cd03257 78 ------KIRRK-------EIQmvfqdpMSSL---------------NPRMTIGEQ-IAEPLRIHGKLSKKEArkeavlll 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 405 ---------------GSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPE 468
Cdd:cd03257 129 lvgvglpeevlnrypHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGV 208
|
250
....*....|....
gi 507082969 469 LLGITDRILVMSNG 482
Cdd:cd03257 209 VAKIADRVAVMYAG 222
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
13-207 |
2.69e-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: 97.55 E-value: 2.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfHSAKEALENGISM 92
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI--RDAREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 93 VHQELNLVLQRSVMDN--MWLGRYPTKGmfvdqdkmyrDTKAIFDELD-IDIDPRA--RVGTLSVSQMQMIEIAKAFSYD 167
Cdd:COG4133 80 LGHADGLKPELTVRENlrFWAALYGLRA----------DREAIDEALEaVGLAGLAdlPVRQLSAGQKRRVALARLLLSP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 507082969 168 AKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISH 207
Cdd:COG4133 150 APLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
9-230 |
3.13e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 98.52 E-value: 3.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 9 SGEYLLEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALEN 88
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 89 GISMVHQELNLVLQRSVMDNMWLG--RYPTKGMFVDQDKM--YRdtKAIFDELDididpRA-----RV----------GT 149
Cdd:PRK11300 81 GVVRTFQHVRLFREMTVIENLLVAqhQQLKTGLFSGLLKTpaFR--RAESEALD-----RAatwleRVgllehanrqaGN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 150 LSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFTIIRKLK-ERGCGIVYISHKMEEIFQLCDEITVLRDGQWI 228
Cdd:PRK11300 154 LAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRnEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPL 233
|
..
gi 507082969 229 AT 230
Cdd:PRK11300 234 AN 235
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
14-225 |
3.43e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 101.46 E-value: 3.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENgISMV 93
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR-VASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 94 HQELNLVLQRSVMDNMWLGRYPTKGMFVDQDKMyrDTKAIFDELD-IDIDPRA--RVGTLSVSQMQMIEIAKAFSYDAKI 170
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMGRTPHRSRFDTWTET--DRAAVERAMErTGVAQFAdrPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 507082969 171 VIMDEPTSSLtekEVNH---LFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDG 225
Cdd:PRK09536 161 LLLDEPTASL---DINHqvrTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADG 215
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
266-486 |
4.28e-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: 95.57 E-value: 4.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 266 LQVRNLTSlRQPSI---RDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEAINHGFAL 342
Cdd:cd03216 1 LELRGITK-RFGGVkalDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 343 VTEerrstgiyayldigfnslisniqnyknkvglldnsrmksdtqwvidsmrvktpghrtqigsLSGGNQQKVVIGRWLL 422
Cdd:cd03216 80 VYQ-------------------------------------------------------------LSVGERQMVEIARALA 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507082969 423 TQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAG 486
Cdd:cd03216 99 RNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVG 162
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
267-482 |
4.39e-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: 95.39 E-value: 4.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 267 QVRNLT--SLRQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSaneainhgfalvt 344
Cdd:cd00267 1 EIENLSfrYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 345 eerrstgiyayldigfnslisnIQNYKNKVGLldnsrmksdtqwvidsmrvktpghrtqIGSLSGGNQQKVVIGRWLLTQ 424
Cdd:cd00267 68 ----------------------LEELRRRIGY---------------------------VPQLSGGQRQRVALARALLLN 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 507082969 425 PEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:cd00267 99 PDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
9-237 |
5.19e-23 |
|
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: 97.74 E-value: 5.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 9 SGEYLLEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKE--AL 86
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 87 ENGISMVHQE------LnlvlqrSVMDNMwlgRYPtkgmfvdqdkMYRDTKaifdeLDID-IDPRAR-----VGtLSVSQ 154
Cdd:COG1127 81 RRRIGMLFQGgalfdsL------TVFENV---AFP----------LREHTD-----LSEAeIRELVLeklelVG-LPGAA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 155 MQM-----------IEIAKAFSYDAKIVIMDEPTSSL---TEKEVNHLftiIRKLKER-GCGIVYISHKMEEIFQLCDEI 219
Cdd:COG1127 136 DKMpselsggmrkrVALARALALDPEILLYDEPTAGLdpiTSAVIDEL---IRELRDElGLTSVVVTHDLDSAFAIADRV 212
|
250
....*....|....*...
gi 507082969 220 TVLRDGQWIATQPLEGLD 237
Cdd:COG1127 213 AVLADGKIIAEGTPEELL 230
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
14-229 |
5.42e-23 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 97.06 E-value: 5.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfhsAKEALE--NGIS 91
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV----VREPREvrRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 92 MVHQELNLVLQRSVMDNM-WLGR-YPTKGmfvdqDKMYRDTKAIFDELDIdIDPRAR-VGTLSVSQMQMIEIAKAFSYDA 168
Cdd:cd03265 77 IVFQDLSVDDELTGWENLyIHARlYGVPG-----AERRERIDELLDFVGL-LEAADRlVKTYSGGMRRRLEIARSLVHRP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507082969 169 KIVIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITVLRDGQWIA 229
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIA 212
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
13-226 |
5.88e-23 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 99.79 E-value: 5.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfhSAKEALENGISM 92
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV---TGLPPEKRNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 93 VHQELNLVLQRSVMDNMwlgRYPTKgmfvdQDKMYRDTKA--IFDELD-IDIDPRA--RVGTLSVSQMQMIEIAKAFSYD 167
Cdd:COG3842 82 VFQDYALFPHLTVAENV---AFGLR-----MRGVPKAEIRarVAELLElVGLEGLAdrYPHQLSGGQQQRVALARALAPE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 168 AKIVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITVLRDGQ 226
Cdd:COG3842 154 PRVLLLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHDQEEALALADRIAVMNDGR 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
14-222 |
7.35e-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: 7.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPG----VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKealeng 89
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 90 ISMVHQELNLVLQRSVMDNMWLGRyptKGMFVDQDKMYRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYDAK 169
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGL---ELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 507082969 170 IVIMDEPTSSLTE--KEV--NHLFTIIRklkERGCGIVYISHKMEEIFQLCDEITVL 222
Cdd:cd03293 152 VLLLDEPFSALDAltREQlqEELLDIWR---ETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
14-229 |
9.43e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 98.72 E-value: 9.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENGIsmV 93
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGV--V 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 94 HQELNLVLQRSVMDNMWL-GRYptKGMFVDQDKMYRDTKAIFDELDIDIDprARVGTLSVSQMQMIEIAKAFSYDAKIVI 172
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVfGRY--FGLSAAAARALVPPLLEFAKLENKAD--AKVGELSGGMKRRLTLARALVNDPDVLV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 507082969 173 MDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIA 229
Cdd:PRK13537 162 LDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIA 218
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
14-226 |
1.16e-22 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 98.99 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfhSAKEALENGISMV 93
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV---TDLPPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 94 HQelNLVL--QRSVMDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELDID--IDpRaRVGTLSVSQMQMIEIAKAFSYDAK 169
Cdd:COG3839 81 FQ--SYALypHMTVYENI---AFPLKLRKVPKAEIDRRVREAAELLGLEdlLD-R-KPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 507082969 170 IVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITVLRDGQ 226
Cdd:COG3839 154 VFLLDEPLSNLDAKLRVEMRAEIKRLhRRLGTTTIYVTHDQVEAMTLADRIAVMNDGR 211
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
24-226 |
1.73e-22 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 100.62 E-value: 1.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 24 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfHSAKEALENGISMVHQElNLVLQR 103
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIR-DLTLESLRRQIGVVPQD-TFLFSG 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 104 SVMDNMWLGRyPTkgmfVDQDKMYRDTKA-----IFDELDIDIDprARVG----TLSVSQMQMIEIAKAFSYDAKIVIMD 174
Cdd:COG1132 429 TIRENIRYGR-PD----ATDEEVEEAAKAaqaheFIEALPDGYD--TVVGergvNLSGGQRQRIAIARALLKDPPILILD 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 507082969 175 EPTSSL---TEKEvnhlftIIRKLKE--RGCGIVYISHKMEEIfQLCDEITVLRDGQ 226
Cdd:COG1132 502 EATSALdteTEAL------IQEALERlmKGRTTIVIAHRLSTI-RNADRILVLDDGR 551
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
13-226 |
1.95e-22 |
|
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: 95.58 E-value: 1.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSFP-----GVK--ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILF--QGKEIDFHSAK 83
Cdd:COG4778 4 LLEVENLSKTFTlhlqgGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 84 E----AL-ENGISMVHQELNlVLQRS-----VMDnmwlgryPTKGMFVDQDKMYRDTKAIFDELDI-----DIDPrarvG 148
Cdd:COG4778 84 PreilALrRRTIGYVSQFLR-VIPRVsaldvVAE-------PLLERGVDREEARARARELLARLNLperlwDLPP----A 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 149 TLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSL--TEKEVnhLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQ 226
Cdd:COG4778 152 TFSGGEQQRVNIARGFIADPPLLLLDEPTASLdaANRAV--VVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
266-482 |
1.99e-22 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 95.97 E-value: 1.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 266 LQVRNLT----SLRqpSIRDISFDLHKGEILGIAGLVGAKRTdiveTLF----GIREKSSGTITLHGKKINNHSANEAIN 337
Cdd:cd03219 1 LEVRGLTkrfgGLV--ALDDVSFSVRPGEIHGLIGPNGAGKT----TLFnlisGFLRPTSGSVLFDGEDITGLPPHEIAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 338 HGFAlvteerRS---TGIYAYLdigfnSLISNIQ---NYKNKVGLLDNSRMKSDTQ------WVIDsmRVKTPGHR-TQI 404
Cdd:cd03219 75 LGIG------RTfqiPRLFPEL-----TVLENVMvaaQARTGSGLLLARARREEREareraeELLE--RVGLADLAdRPA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507082969 405 GSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:cd03219 142 GELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQG 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
262-501 |
2.35e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 100.10 E-value: 2.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 262 GEVILQVRNLTSlRQPSIR---DISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEAINH 338
Cdd:COG3845 2 MPPALELRGITK-RFGGVVandDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 339 G-------FAL-----VTEerrstgiyayldigfnslisNIQ--NYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTqI 404
Cdd:COG3845 81 GigmvhqhFMLvpnltVAE--------------------NIVlgLEPTKGGRLDRKAARARIRELSERYGLDVDPDAK-V 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 405 GSLSGGNQQKVVIGRWLLTQPEILMLDEPT-----RGIDvgakfEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVM 479
Cdd:COG3845 140 EDLSVGEQQRVEILKALYRGARILILDEPTavltpQEAD-----ELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVL 214
|
250 260
....*....|....*....|..
gi 507082969 480 SNGLVAGIVDTKTTTQNEILRL 501
Cdd:COG3845 215 RRGKVVGTVDTAETSEEELAEL 236
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
14-229 |
3.10e-22 |
|
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: 95.48 E-value: 3.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPGVKaLDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFHSAKEalenGISM 92
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDItNLPPEKR----DISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 93 VHQELNLVLQRSVMDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYDAKIVI 172
Cdd:cd03299 76 VPQNYALFPHMTVYKNI---AYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 507082969 173 MDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITVLRDGQWIA 229
Cdd:cd03299 153 LDEPFSALDVRTKEKLREELKKIrKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQ 210
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
24-225 |
3.34e-22 |
|
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: 94.98 E-value: 3.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 24 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSaKEALENGISMVHQElNLVLQR 103
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS-RKSLRSMIGVVLQD-TFLFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 104 SVMDNMWLGRyPTkgmfVDQDKMYRDTKAI-FDEL------DIDIDPRARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEP 176
Cdd:cd03254 92 TIMENIRLGR-PN----ATDEEVIEAAKEAgAHDFimklpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 507082969 177 TSSL---TEKEVNhlfTIIRKLKERGCGIVyISHKMEEIfQLCDEITVLRDG 225
Cdd:cd03254 167 TSNIdteTEKLIQ---EALEKLMKGRTSII-IAHRLSTI-KNADKILVLDDG 213
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
267-482 |
3.38e-22 |
|
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: 93.65 E-value: 3.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 267 QVRNLT-SLRQ-PSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEAINHgFALVT 344
Cdd:cd03214 1 EVENLSvGYGGrTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK-IAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 345 EERRSTGIYAYLDIGFNSLisniqnyknkvglldnsrmksdtqwvidsmrvktpghrtqigslSGGNQQKVVIGRWLLTQ 424
Cdd:cd03214 80 QALELLGLAHLADRPFNEL--------------------------------------------SGGERQRVLLARALAQE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 507082969 425 PEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPEL-LGITDRILVMSNG 482
Cdd:cd03214 116 PPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLaARYADRVILLKDG 174
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
14-226 |
5.44e-22 |
|
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: 93.80 E-value: 5.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPGVKALDNVNLKVrPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeIDFHSAKEALENGISMV 93
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDG--QDVLKQPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 94 HQELNLVLQRSVMDNM----WLGRYPTKgmfvdqdkmyrDTKAIFDEL--DIDIDPRA--RVGTLSVSQMQMIEIAKAFS 165
Cdd:cd03264 78 PQEFGVYPNFTVREFLdyiaWLKGIPSK-----------EVKARVDEVleLVNLGDRAkkKIGSLSGGMRRRVGIAQALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507082969 166 YDAKIVIMDEPTSSLTEKEVNHLFTIIRKL-KERgcgIVYIS-HKMEEIFQLCDEITVLRDGQ 226
Cdd:cd03264 147 GDPSILIVDEPTAGLDPEERIRFRNLLSELgEDR---IVILStHIVEDVESLCNQVAVLNKGK 206
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
14-229 |
5.45e-22 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 94.53 E-value: 5.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFHSAKEAlENGISM 92
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDItKLPMHKRA-RLGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 93 VHQELNLVLQRSVMDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYDAKIVI 172
Cdd:cd03218 80 LPQEASIFRKLTVEENI---LAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 507082969 173 MDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIA 229
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLA 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
279-482 |
1.02e-21 |
|
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: 93.09 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 279 IRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNhsaneainhgfalvtEERRSTGIYAYLDI 358
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---------------KERRKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 359 GFnslisniQNYKNKV------GLLDNSRMKSDTQWVIDSMRVKTPGHRTQIgSLSGGNQQKVVIGRWLLTQPEILMLDE 432
Cdd:cd03226 81 DY-------QLFTDSVreelllGLKELDAGNEQAETVLKDLDLYALKERHPL-SLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 507082969 433 PTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:cd03226 153 PTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
14-222 |
1.73e-21 |
|
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: 97.36 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPGV-KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKeALENGISM 92
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAD-SWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 93 VHQeLNLVLQRSVMDNMWLGRYPTKGMFVDQ--DKMYRD--TKAIFDELDIDIDPRARvgTLSVSQMQMIEIAKAFSYDA 168
Cdd:TIGR02857 401 VPQ-HPFLFAGTIAENIRLARPDASDAEIREalERAGLDefVAALPQGLDTPIGEGGA--GLSGGQAQRLALARAFLRDA 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 507082969 169 KIVIMDEPTSSL---TEKEVNHlftIIRKLKERGCGIVyISHKmEEIFQLCDEITVL 222
Cdd:TIGR02857 478 PLLLLDEPTAHLdaeTEAEVLE---ALRALAQGRTVLL-VTHR-LALAALADRIVVL 529
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
13-226 |
2.00e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 93.02 E-value: 2.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENGISM 92
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 93 VHQELNLVLQRSVMDNMWLGryptkGMFVDQDKMYRDTKAIFDELDIDIDPRA-RVGTLSVSQMQMIEIAKAFSYDAKIV 171
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMG-----GFFAERDQFQERIKWVYELFPRLHERRIqRAGTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 507082969 172 IMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQ 226
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGH 214
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
15-226 |
2.93e-21 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 94.87 E-value: 2.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 15 EMTGINKSFPG----VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKE--ALEN 88
Cdd:PRK11153 3 ELKNISKVFPQggrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 89 GISMVHQELNLVLQRSVMDNMWLgryPTKGMFVDQDKMyrdtKAIFDELdididpRARVG----------TLSVSQMQMI 158
Cdd:PRK11153 83 QIGMIFQHFNLLSSRTVFDNVAL---PLELAGTPKAEI----KARVTEL------LELVGlsdkadrypaQLSGGQKQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507082969 159 EIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITVLRDGQ 226
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDInRELGLTIVLITHEMDVVKRICDRVAVIDAGR 218
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
14-225 |
3.65e-21 |
|
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: 92.30 E-value: 3.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfhSAKEALENGISMV 93
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI---TNLPPHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 94 HQELNLVLQRSVMDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYDAKIVIM 173
Cdd:cd03300 78 FQNYALFPHLTVFENI---AFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 507082969 174 DEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITVLRDG 225
Cdd:cd03300 155 DEPLGALDLKLRKDMQLELKRLqKELGITFVFVTHDQEEALTMSDRIAVMNKG 207
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
263-484 |
4.15e-21 |
|
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: 96.13 E-value: 4.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 263 EVILQVRNLT----SLRQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKS---SGTITLHGKKINNHSANEA 335
Cdd:COG1123 2 TPLLEVRDLSvrypGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 336 INHgFALVTEERRS--TGIYAYLDIGFNSLIsniqnyknkvGLLDNSRMKSDTQWVIDSMRVKTPGHRtQIGSLSGGNQQ 413
Cdd:COG1123 82 GRR-IGMVFQDPMTqlNPVTVGDQIAEALEN----------LGLSRAEARARVLELLEAVGLERRLDR-YPHQLSGGQRQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507082969 414 KVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:COG1123 150 RVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRI 221
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
265-482 |
4.24e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 92.75 E-value: 4.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 265 ILQVRNLtSLR---QPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEAINHG-- 339
Cdd:PRK11300 5 LLSVSGL-MMRfggLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGvv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 340 --FALVTEERRSTGIYayldigfNSLISNIQNYKNKV--GLL--------DNSRMKSDTQWvIDSMRVKTPGHRtQIGSL 407
Cdd:PRK11300 84 rtFQHVRLFREMTVIE-------NLLVAQHQQLKTGLfsGLLktpafrraESEALDRAATW-LERVGLLEHANR-QAGNL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507082969 408 SGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK11300 155 AYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
14-229 |
5.74e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 94.13 E-value: 5.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfhSAKEALENGISMV 93
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP--ARARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 94 HQELNLVLQRSVMDNMWL-GRYptKGMFVdqdkmyRDTKAI------FDELDIDIDprARVGTLSVSQMQMIEIAKAFSY 166
Cdd:PRK13536 120 PQFDNLDLEFTVRENLLVfGRY--FGMST------REIEAVipslleFARLESKAD--ARVSDLSGGMKRRLTLARALIN 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507082969 167 DAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIA 229
Cdd:PRK13536 190 DPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIA 252
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
266-482 |
6.67e-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: 91.24 E-value: 6.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 266 LQVRNLT---SLRQPSIRDISFDLHKGEILGIAGLVGAKRTdiveTLF----GIREKSSGTITLHGKKINNHSANEAinh 338
Cdd:COG1122 1 IELENLSfsyPGGTPALDDVSLSIEKGEFVAIIGPNGSGKS----TLLrllnGLLKPTSGEVLVDGKDITKKNLREL--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 339 gfalvteeRRSTGI---YA---------YLDIGFnslisniqnyknkvGL----LDNSRMKSDTQWVIDsmRVKTPGHRT 402
Cdd:COG1122 74 --------RRKVGLvfqNPddqlfaptvEEDVAF--------------GPenlgLPREEIRERVEEALE--LVGLEHLAD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 403 Q-IGSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSN 481
Cdd:COG1122 130 RpPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDD 209
|
.
gi 507082969 482 G 482
Cdd:COG1122 210 G 210
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-226 |
8.46e-21 |
|
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: 90.82 E-value: 8.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 27 KALDNVNLKVR---PHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG-------KEIDFHSAKEalenGISMVHQE 96
Cdd:cd03297 8 KRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKINLPPQQR----KIGLVFQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 97 LNLVLQRSVMDNMWLGrYPTKGMFVDQDKMyrdtKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEP 176
Cdd:cd03297 84 YALFPHLNVRENLAFG-LKRKRNREDRISV----DELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 507082969 177 TSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITVLRDGQ 226
Cdd:cd03297 159 FSALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
29-229 |
8.57e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 91.61 E-value: 8.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEaLENGISMVHQEL---------NL 99
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ-LARRLALLPQHHltpegitvrEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 100 V-LQRSVMDNMWlgryptkGMFVDQDKMyRDTKAIfDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTS 178
Cdd:PRK11231 97 VaYGRSPWLSLW-------GRLSAEDNA-RVNQAM-EQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 507082969 179 SLtekEVNH---LFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIA 229
Cdd:PRK11231 168 YL---DINHqveLMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMA 218
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
265-485 |
8.61e-21 |
|
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: 90.89 E-value: 8.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 265 ILQVRNLT------SLRQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGkkINNHSANEAINH 338
Cdd:cd03266 1 MITADALTkrfrdvKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPAEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 339 GFALVTEerrSTGIYAYLdigfnSLISNIQNYKNKVGLlDNSRMKSDTQWVIDSMRVKTPGHRtQIGSLSGGNQQKVVIG 418
Cdd:cd03266 79 RLGFVSD---STGLYDRL-----TARENLEYFAGLYGL-KGDELTARLEELADRLGMEELLDR-RVGGFSTGMRQKVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507082969 419 RWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVA 485
Cdd:cd03266 149 RALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
13-482 |
9.32e-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: 95.14 E-value: 9.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSFPG----VKALDNVNLKVRPHSIHALMGENGAGKS----TLLKCLFGIYQKDSGSILFQGKEIdFHSAKE 84
Cdd:COG4172 6 LLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDL-LGLSER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 85 ALE----NGISMVHQE----LNLV--LQRSVMDNMWLGRyptkGMfvdqdkmyRDTKA------IFDELDIDiDPRARVG 148
Cdd:COG4172 85 ELRrirgNRIAMIFQEpmtsLNPLhtIGKQIAEVLRLHR----GL--------SGAAAraraleLLERVGIP-DPERRLD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 149 T----LSVSQMQMIEIAKAFSYDAKIVIMDEPTSSL---TEKEVNHLftiIRKLK-ERGCGIVYISHKMEEIFQLCDEIT 220
Cdd:COG4172 152 AyphqLSGGQRQRVMIAMALANEPDLLIADEPTTALdvtVQAQILDL---LKDLQrELGMALLLITHDLGVVRRFADRVA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 221 VLRDGQWIATQPLEG-------------LDmdkiismmvgrSLNQRFPDKENKPGEVILQVRNLT--------SLRQPS- 278
Cdd:COG4172 229 VMRQGEIVEQGPTAElfaapqhpytrklLA-----------AEPRGDPRPVPPDAPPLLEARDLKvwfpikrgLFRRTVg 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 279 ----IRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIrEKSSGTITLHGKKINNHSANEainhgfalVTEERRstgiya 354
Cdd:COG4172 298 hvkaVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRA--------LRPLRR------ 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 355 ylDIG------FNSLisniqnyknkvglldNSRMkSDTQWVIDSMRVKTPG-----HRTQIGSL---------------- 407
Cdd:COG4172 363 --RMQvvfqdpFGSL---------------SPRM-TVGQIIAEGLRVHGPGlsaaeRRARVAEAleevgldpaarhryph 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 408 --SGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKdKGI--IIISSEmpelLG----ITDRILVM 479
Cdd:COG4172 425 efSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQRE-HGLayLFISHD----LAvvraLAHRVMVM 499
|
...
gi 507082969 480 SNG 482
Cdd:COG4172 500 KDG 502
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
16-484 |
9.63e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.13 E-value: 9.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 16 MTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfhsakealengISMVHQ 95
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLR------------IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 96 ELNLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTK-------------AIFDELDI-DIDPRAR--------------- 146
Cdd:COG0488 69 EPPLDDDLTVLDTVLDGDAELRALEAELEELEAKLAepdedlerlaelqEEFEALGGwEAEARAEeilsglgfpeedldr 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 147 -VGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTssltekevNHL--FTII---RKLKERGCGIVYISH------------- 207
Cdd:COG0488 149 pVSELSGGWRRRVALARALLSEPDLLLLDEPT--------NHLdlESIEwleEFLKNYPGTVLVVSHdryfldrvatril 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 208 -----------------------------KMEEIFQlcDEITVLRDgqWI---------ATQP------LEglDMDKIIS 243
Cdd:COG0488 221 eldrgkltlypgnysayleqraerleqeaAAYAKQQ--KKIAKEEE--FIrrfrakarkAKQAqsrikaLE--KLEREEP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 244 MMVGRSLNQRFPDKEnKPGEVILQVRNLtSLR---QPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTI 320
Cdd:COG0488 295 PRRDKTVEIRFPPPE-RLGKKVLELEGL-SKSygdKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 321 TLhGKKINnhsaneainhgFALVTEERrstgiyAYLDIGfNSLISNIQNYKNKV------GLLdnSRM--KSDTQWvids 392
Cdd:COG0488 373 KL-GETVK-----------IGYFDQHQ------EELDPD-KTVLDELRDGAPGGteqevrGYL--GRFlfSGDDAF---- 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 393 mrvktpghrTQIGSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKfeiyQLIAELAKKDKGIIIISSEMPELL-G 471
Cdd:COG0488 428 ---------KPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETL----EALEEALDDFPGTVLLVSHDRYFLdR 494
|
570
....*....|...
gi 507082969 472 ITDRILVMSNGLV 484
Cdd:COG0488 495 VATRILEFEDGGV 507
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
41-231 |
1.19e-20 |
|
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: 90.24 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 41 IHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEidfHSAKEALENGISMVHQELNLVLQRSVMDNMWLGRYPT-KGM 119
Cdd:cd03298 26 ITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVD---VTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGLSPGlKLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 120 FVDQDKMyrdtKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFTIIRKL-KER 198
Cdd:cd03298 103 AEDRQAI----EVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhAET 178
|
170 180 190
....*....|....*....|....*....|...
gi 507082969 199 GCGIVYISHKMEEIFQLCDEITVLRDGQWIATQ 231
Cdd:cd03298 179 KMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
14-501 |
1.32e-20 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 94.87 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGI--YQKDSGSIL-------------------- 71
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 72 --------FQGKEIDFHSAKEALENGIS-----MVHQELNLVLQRSVMDNMwLGRYPTKGmFVDQDKMYRDTKAI-FDEL 137
Cdd:TIGR03269 81 pcpvcggtLEPEEVDFWNLSDKLRRRIRkriaiMLQRTFALYGDDTVLDNV-LEALEEIG-YEGKEAVGRAVDLIeMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 138 DIDIDPRARvgTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLC 216
Cdd:TIGR03269 159 SHRITHIAR--DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEVIEDLS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 217 DEITVLRDGQWIAtqplEGLDMDKIISMMVGRSLNQRFpdKENKPGEVILQVRNLT----SLRQPSIR---DISFDLHKG 289
Cdd:TIGR03269 237 DKAIWLENGEIKE----EGTPDEVVAVFMEGVSEVEKE--CEVEVGEPIIKVRNVSkryiSVDRGVVKavdNVSLEVKEG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 290 EILGIAGLVGAKRTDIVETLFGIREKSSGtitlhgkKINNHSANEAIN---HGFALVTEERRSTGI-------YAYLDIg 359
Cdd:TIGR03269 311 EIFGIVGTSGAGKTTLSKIIAGVLEPTSG-------EVNVRVGDEWVDmtkPGPDGRGRAKRYIGIlhqeydlYPHRTV- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 360 fnslisnIQNYKNKVGL---LDNSRMKSdtqwVIdsmRVKTPGHRTQIG---------SLSGGNQQKVVIGRWLLTQPEI 427
Cdd:TIGR03269 383 -------LDNLTEAIGLelpDELARMKA----VI---TLKMVGFDEEKAeeildkypdELSEGERHRVALAQVLIKEPRI 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507082969 428 LMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTKtttqnEILRL 501
Cdd:TIGR03269 449 VILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPE-----EIVEE 518
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
7-252 |
1.38e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 94.69 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 7 QSSGEYLLEMTGInkSFPGVkalDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEAL 86
Cdd:PRK10762 251 KAPGEVRLKVDNL--SGPGV---NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 87 ENGISMVHQELN---LVLQRSVMDNMWLG--RYPTKGMFvdQDKMYRDTKAIFDELDI-DIDPRAR---VGTLSVSQMQM 157
Cdd:PRK10762 326 ANGIVYISEDRKrdgLVLGMSVKENMSLTalRYFSRAGG--SLKHADEQQAVSDFIRLfNIKTPSMeqaIGLLSGGNQQK 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 158 IEIAKAFSYDAKIVIMDEPTSSL---TEKEVNHLftiIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIATQPLE 234
Cdd:PRK10762 404 VAIARGLMTRPKVLILDEPTRGVdvgAKKEIYQL---INQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTRE 480
|
250
....*....|....*...
gi 507082969 235 GLDMDKIISMMVGRSLNQ 252
Cdd:PRK10762 481 QATQEKLMAAAVGKLNRV 498
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
266-500 |
2.11e-20 |
|
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: 90.25 E-value: 2.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 266 LQVRNLTSLR--QPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEAInhgfalv 343
Cdd:cd03261 1 IELRGLTKSFggRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELY------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 344 tEERRSTGI---YAYLdigFNSLiSNIQNyknkVG--LLDNSRMKSDTQWVIDSMRVKTPGHRTQI----GSLSGGNQQK 414
Cdd:cd03261 74 -RLRRRMGMlfqSGAL---FDSL-TVFEN----VAfpLREHTRLSEEEIREIVLEKLEAVGLRGAEdlypAELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 415 VVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAK-KDKGIIIISSEMPELLGITDRILVMSNGLV--AGIVDTK 491
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKeLGLTSIMVTHDLDTAFAIADRIAVLYDGKIvaEGTPEEL 224
|
....*....
gi 507082969 492 TTTQNEILR 500
Cdd:cd03261 225 RASDDPLVR 233
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
13-210 |
2.66e-20 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 89.77 E-value: 2.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEAL---ENG 89
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLirqEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 90 isMVHQELNLVLQRSVMDNMWLGRYPTKGMfvdqdkMYRDTKAIFDELDIDIDPRARVG----TLSVSQMQMIEIAKAFS 165
Cdd:PRK09493 81 --MVFQQFYLFPHLTALENVMFGPLRVRGA------SKEEAEKQARELLAKVGLAERAHhypsELSGGQQQRVAIARALA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 507082969 166 YDAKIVIMDEPTSSLtEKEVNH-LFTIIRKLKERGCGIVYISHKME 210
Cdd:PRK09493 153 VKPKLMLFDEPTSAL-DPELRHeVLKVMQDLAEEGMTMVIVTHEIG 197
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
21-229 |
6.87e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 88.80 E-value: 6.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 21 KSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENGISMVHQELNLV 100
Cdd:PRK10895 11 KAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 101 LQRSVMDNMWLGRYPTKGMFVDQDKmyRDTKAIFDELDIdIDPRARVG-TLSVSQMQMIEIAKAFSYDAKIVIMDEPTSS 179
Cdd:PRK10895 91 RRLSVYDNLMAVLQIRDDLSAEQRE--DRANELMEEFHI-EHLRDSMGqSLSGGERRRVEIARALAANPKFILLDEPFAG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 507082969 180 LTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIA 229
Cdd:PRK10895 168 VDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIA 217
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
24-226 |
7.74e-20 |
|
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: 88.44 E-value: 7.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 24 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG---KEIDFHSAKEAlengISMVHQELNLv 100
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdiREVTLDSLRRA----IGVVPQDTVL- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 101 LQRSVMDNMWLGRyPTkgmfVDQDKMYRDTKAifdeldIDIDPR---------ARVG----TLSVSQMQMIEIAKAFSYD 167
Cdd:cd03253 87 FNDTIGYNIRYGR-PD----ATDEEVIEAAKA------AQIHDKimrfpdgydTIVGerglKLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507082969 168 AKIVIMDEPTSSL---TEKEVnhLFTIIRKLKERgcGIVYISHKMEEIFQlCDEITVLRDGQ 226
Cdd:cd03253 156 PPILLLDEATSALdthTEREI--QAALRDVSKGR--TTIVIAHRLSTIVN-ADKIIVLKDGR 212
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
266-482 |
8.93e-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: 87.95 E-value: 8.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 266 LQVRNLT----SLRQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHsaneainhgfa 341
Cdd:cd03263 1 LQIRNLTktykKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTD----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 342 lVTEERRSTGIYAYLDIGFNSL--------ISNIQNYKNKvglldnsRMKSDTQWVIDSMRVkTPGHRTQIGSLSGGNQQ 413
Cdd:cd03263 70 -RKAARQSLGYCPQFDALFDELtvrehlrfYARLKGLPKS-------EIKEEVELLLRVLGL-TDKANKRARTLSGGMKR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507082969 414 KVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:cd03263 141 KLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDG 208
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
14-225 |
1.21e-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: 87.46 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFP-GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFH-SAKEALENGI 90
Cdd:cd03292 1 IEFINVTKTYPnGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsDLRgRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 91 SMVHQELNLVLQRSVMDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYDAKI 170
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENV---AFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 507082969 171 VIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDG 225
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERG 212
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
31-249 |
1.61e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 91.27 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 31 NVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENGIsmVH-----QELNLVLQRSV 105
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGL--VYlpedrQSSGLYLDAPL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 106 MDNMWLGRYPTKGMFVDQDKmyrdTKAIFDE----LDIDI-DPRARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSL 180
Cdd:PRK15439 359 AWNVCALTHNRRGFWIKPAR----ENAVLERyrraLNIKFnHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507082969 181 TEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIATQPLEGLDMDKIISMMVGRS 249
Cdd:PRK15439 435 DVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAINVDTIMRLAFGEH 503
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
14-226 |
1.84e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 87.03 E-value: 1.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFP-GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKE--ALENGI 90
Cdd:COG2884 2 IRFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 91 SMVHQELNLVLQRSVMDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYDAKI 170
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENV---ALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 507082969 171 VIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQ 226
Cdd:COG2884 159 LLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGR 214
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
11-255 |
1.92e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 88.37 E-value: 1.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 11 EYLLEMTGINKSFP-GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFhSAKEALE-- 87
Cdd:PRK13636 3 DYILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDY-SRKGLMKlr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 88 NGISMVHQEL-NLVLQRSVMDNMWLGrypTKGMFVDQDKMYRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSY 166
Cdd:PRK13636 82 ESVGMVFQDPdNQLFSASVYQDVSFG---AVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 167 DAKIVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITVLRDGQWIatqpLEGLDMDKIISMM 245
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMqKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI----LQGNPKEVFAEKE 234
|
250
....*....|
gi 507082969 246 VGRSLNQRFP 255
Cdd:PRK13636 235 MLRKVNLRLP 244
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-232 |
3.25e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 86.89 E-value: 3.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKC---LFGIYQKD--SGSILFQGKEIdFHSAKEALEN 88
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYPEArvSGEVYLDGQDI-FKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 89 GISMVHQELNLVLQRSVMDNMWLGR-----YPTKGMFVDQDKMYRDTKAIFDELDIDIDprARVGTLSVSQMQMIEIAKA 163
Cdd:PRK14247 83 RVQMVFQIPNPIPNLSIFENVALGLklnrlVKSKKELQERVRWALEKAQLWDEVKDRLD--APAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507082969 164 FSYDAKIVIMDEPTSSLTEKEVNHLFTIIRKLKeRGCGIVYISHKMEEIFQLCDEITVLRDGQWIATQP 232
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELK-KDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGP 228
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
24-226 |
3.28e-19 |
|
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: 86.82 E-value: 3.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 24 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEaLENGISMVHQELNLvLQR 103
Cdd:cd03249 14 PDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRW-LRSQIGLVSQEPVL-FDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 104 SVMDNMWLGRYP-TKGMFVDQDKMYRDTKAIF---DELDIDIDPRArvGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSS 179
Cdd:cd03249 92 TIAENIRYGKPDaTDEEVEEAAKKANIHDFIMslpDGYDTLVGERG--SQLSGGQKQRIAIARALLRNPKILLLDEATSA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 507082969 180 L---TEKEVNHlfTIIRKLKERGCgiVYISHKMEEIfQLCDEITVLRDGQ 226
Cdd:cd03249 170 LdaeSEKLVQE--ALDRAMKGRTT--IVIAHRLSTI-RNADLIAVLQNGQ 214
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-229 |
3.35e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 87.37 E-value: 3.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHS-AKEALENGIS 91
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKrGLLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 92 MVHQELNLVLQRSVMDNMWlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYDAKIV 171
Cdd:PRK13638 81 TVFQDPEQQIFYTDIDSDI--AFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 507082969 172 IMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIA 229
Cdd:PRK13638 159 LLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILT 216
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
266-482 |
3.82e-19 |
|
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: 86.62 E-value: 3.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 266 LQVRNLT-SLRQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSAneaINHGFALVT 344
Cdd:cd03299 1 LKVENLSkDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPP---EKRDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 345 EErrstgiYAyldigfnsLISNIQNYKN-KVGLLDNSRMKS-DTQWVIDSMRVKTPGH--RTQIGSLSGGNQQKVVIGRW 420
Cdd:cd03299 78 QN------YA--------LFPHMTVYKNiAYGLKKRKVDKKeIERKVLEIAEMLGIDHllNRKPETLSGGEQQRVAIARA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507082969 421 LLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIII-ISSEMPELLGITDRILVMSNG 482
Cdd:cd03299 144 LVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLhVTHDFEEAWALADKVAIMLNG 206
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
266-482 |
3.84e-19 |
|
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: 85.80 E-value: 3.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 266 LQVRNLTSL--RQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTItlhgkKINNHSANEAINHGFALV 343
Cdd:cd03269 1 LEVENVTKRfgRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEV-----LFDGKPLDIAARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 344 TEERrstGIYAYLDIGFNSL-ISNIQNYKnkvglldnsrmKSDTQWVIDSM--RVKTPGHRTQ-IGSLSGGNQQKVVIGR 419
Cdd:cd03269 76 PEER---GLYPKMKVIDQLVyLAQLKGLK-----------KEEARRRIDEWleRLELSEYANKrVEELSKGNQQKVQFIA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507082969 420 WLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:cd03269 142 AVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
265-485 |
3.90e-19 |
|
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: 87.02 E-value: 3.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 265 ILQVRNLT-SLRQPSI-RDISFDLHKGEILGIAGLVGA-KRTdIVETLFGIREKSSGTITLHGKKINNHSANE------- 334
Cdd:COG1120 1 MLEAENLSvGYGGRPVlDDVSLSLPPGEVTALLGPNGSgKST-LLRALAGLLKPSSGEVLLDGRDLASLSRRElarriay 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 335 ---AINHGFALVTEERRSTGIYAYLdigfnslisniqnyknkvGLLDNSRmKSDTQWVIDSM-RVKTPGHRTQ-IGSLSG 409
Cdd:COG1120 80 vpqEPPAPFGLTVRELVALGRYPHL------------------GLFGRPS-AEDREAVEEALeRTGLEHLADRpVDELSG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507082969 410 GNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPEL-LGITDRILVMSNG-LVA 485
Cdd:COG1120 141 GERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLaARYADRLVLLKDGrIVA 218
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
29-226 |
7.69e-19 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 89.78 E-value: 7.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSaKEALENGISMVHQElNLVLQRSVMDN 108
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS-HSVLRQGVAMVQQD-PVVLADTFLAN 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 109 MWLGRYptkgmfVDQDKMYRDTKAI-FDELDIDIDP--RARVG----TLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSL- 180
Cdd:PRK10790 435 VTLGRD------ISEEQVWQALETVqLAELARSLPDglYTPLGeqgnNLSVGQKQLLALARVLVQTPQILILDEATANId 508
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 507082969 181 --TEKEVNHLFTIIRKLKErgcgIVYISHKMEEIFQlCDEITVLRDGQ 226
Cdd:PRK10790 509 sgTEQAIQQALAAVREHTT----LVVIAHRLSTIVE-ADTILVLHRGQ 551
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
28-245 |
8.60e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 86.20 E-value: 8.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 28 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEaLENGISMVHQEL-NLVLQRSVM 106
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE-IRKKIGIIFQNPdNQFIGATVE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 107 DNMWLG----RYPTKGMfvdQDKMYRDTKAIFDELDIDIDPRarvgTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTE 182
Cdd:PRK13632 103 DDIAFGlenkKVPPKKM---KDIIDDLAKKVGMEDYLDKEPQ----NLSGGQKQRVAIASVLALNPEIIIFDESTSMLDP 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507082969 183 KEVNHLFTIIRKLKERGCG-IVYISHKMEEIFqLCDEITVLRDGQWIAT-QPLEGLDMDKIISMM 245
Cdd:PRK13632 176 KGKREIKKIMVDLRKTRKKtLISITHDMDEAI-LADKVIVFSEGKLIAQgKPKEILNNKEILEKA 239
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
14-226 |
2.58e-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: 82.26 E-value: 2.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPGVKA--LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfHSAKEALENGIS 91
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIS-QWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 92 MVHQELNLvLQRSVMDNMwlgryptkgmfvdqdkmyrdtkaifdeldididprarvgtLSVSQMQMIEIAKAFSYDAKIV 171
Cdd:cd03246 80 YLPQDDEL-FSGSIAENI----------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 507082969 172 IMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIfQLCDEITVLRDGQ 226
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETL-ASADRILVLEDGR 172
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
281-487 |
2.89e-18 |
|
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: 83.50 E-value: 2.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 281 DISFDLhKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINnhSANEAINhgfaLVTEERRstgiyayldIGF 360
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLF--DSRKKIN----LPPQQRK---------IGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 361 ----NSLISNIQNYKNKVGLLDNSRMKSDTQWV---IDSMRVKTPGHRtQIGSLSGGNQQKVVIGRWLLTQPEILMLDEP 433
Cdd:cd03297 80 vfqqYALFPHLNVRENLAFGLKRKRNREDRISVdelLDLLGLDHLLNR-YPAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 507082969 434 TRGIDVGAKFEIYQLIAELAKKDKG-IIIISSEMPELLGITDRILVMSNGLVAGI 487
Cdd:cd03297 159 FSALDRALRLQLLPELKQIKKNLNIpVIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
14-229 |
3.17e-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: 3.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPG--VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfHSAKEALENGIS 91
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV--SDLEKALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 92 MVHQELNLvLQRSVMDNmwLGRyptkgmfvdqdkmyrdtkaifdeldididprarvgTLSVSQMQMIEIAKAFSYDAKIV 171
Cdd:cd03247 79 VLNQRPYL-FDTTLRNN--LGR-----------------------------------RFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 507082969 172 IMDEPTSSL---TEKEVnhLFTIIRKLKERgcGIVYISHKMEEIFQLcDEITVLRDGQWIA 229
Cdd:cd03247 121 LLDEPTVGLdpiTERQL--LSLIFEVLKDK--TLIWITHHLTGIEHM-DKILFLENGKIIM 176
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
266-484 |
3.45e-18 |
|
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: 83.31 E-value: 3.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 266 LQVRNLT------SLRQPSIRDISFDLHKGEILGIAGLVGAKRTdiveTLF----GIREKSSGTITLHGKKINNHSANEa 335
Cdd:cd03255 1 IELKNLSktygggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKS----TLLnilgGLDRPTSGEVRVDGTDISKLSEKE- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 336 inhgfalVTEERRSTgiyayldIGF----NSLISNIQNYKN-KVGLLDNSRMKSDTQWVIDSM--RVKTPGHRTQ-IGSL 407
Cdd:cd03255 76 -------LAAFRRRH-------IGFvfqsFNLLPDLTALENvELPLLLAGVPKKERRERAEELleRVGLGDRLNHyPSEL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507082969 408 SGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:cd03255 142 SGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
13-234 |
3.45e-18 |
|
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: 83.98 E-value: 3.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSFPGVKALDNVNLKVRPHSiH-ALMGENGAGKSTLLKCLFG-IYQKDSGSILFQGKEIDFHSAKEaLENGI 90
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGE-HwAILGPNGAGKSTLLSLITGdLPPTYGNDVRLFGERRGGEDVWE-LRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 91 SMVHQELNLVLQR--SVMDnMWL-GRYPTKGMFVD-QDKMYRDTKAIFDELDIDidPRA--RVGTLSVSQMQMIEIAKAF 164
Cdd:COG1119 81 GLVSPALQLRFPRdeTVLD-VVLsGFFDSIGLYREpTDEQRERARELLELLGLA--HLAdrPFGTLSQGEQRRVLIARAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 507082969 165 SYDAKIVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITVLRDGQWIATQPLE 234
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGARELLLALLDKLaAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKE 228
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
24-226 |
4.50e-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: 4.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 24 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGK---EIDFHSakeaLENGISMVHQElNLV 100
Cdd:TIGR00958 492 PDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVplvQYDHHY----LHRQVALVGQE-PVL 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 101 LQRSVMDNMWLG--RYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTS 178
Cdd:TIGR00958 567 FSGSVRENIAYGltDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 507082969 179 SLtEKEVNHLFTIIRKLKERgcGIVYISHKMEEIfQLCDEITVLRDGQ 226
Cdd:TIGR00958 647 AL-DAECEQLLQESRSRASR--TVLLIAHRLSTV-ERADQILVLKKGS 690
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
14-210 |
6.72e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 83.48 E-value: 6.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEA-------- 85
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGqlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 86 ----LENGISMVHQELNLVLQRSVMDNMWLGRYPTKGMfvdqDKMYRDTKAIFDELDIDIDPRARVG---TLSVSQMQMI 158
Cdd:PRK10619 86 qlrlLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGL----SKQEARERAVKYLAKVGIDERAQGKypvHLSGGQQQRV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 507082969 159 EIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKME 210
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMG 213
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
278-504 |
7.05e-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: 7.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 278 SIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEAINHGFALVTEERRstgIYAYLD 357
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRR---VFSRMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 358 IGFN----SLISNIQNYKNKVglldnsrmksdtQWVIDsMRVKTPGHRTQ-IGSLSGGNQQKVVIGRWLLTQPEILMLDE 432
Cdd:PRK11614 97 VEENlamgGFFAERDQFQERI------------KWVYE-LFPRLHERRIQrAGTMSGGEQQMLAIGRALMSQPRLLLLDE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507082969 433 PTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAgIVDT-KTTTQNEILRLASL 504
Cdd:PRK11614 164 PSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVV-LEDTgDALLANEAVRSAYL 235
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
261-485 |
9.09e-18 |
|
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: 85.97 E-value: 9.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 261 PGEVILQVRNLT---SLRQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSAnEAIN 337
Cdd:COG4988 332 AGPPSIELEDVSfsyPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDP-ASWR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 338 HGFALVTEErrstgiyAYLdigFN-SLISNIQNYK------------NKVGLLDnsrmksdtqwVIDSMrvktP-GHRTQ 403
Cdd:COG4988 411 RQIAWVPQN-------PYL---FAgTIRENLRLGRpdasdeeleaalEAAGLDE----------FVAAL----PdGLDTP 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 404 IGS----LSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIIISSEmPELLGITDRILVM 479
Cdd:COG4988 467 LGEggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHR-LALLAQADRILVL 544
|
....*.
gi 507082969 480 SNGLVA 485
Cdd:COG4988 545 DDGRIV 550
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
259-504 |
9.73e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 83.12 E-value: 9.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 259 NKPGEVILQVRNL----TSLRQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANE 334
Cdd:PRK13632 1 IKNKSVMIKVENVsfsyPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 335 AINH-GFALVTEERRSTGIYAYLDIGF---NSLISN------IQNYKNKVGLLDnsRMKSDTQwvidsmrvktpghrtqi 404
Cdd:PRK13632 81 IRKKiGIIFQNPDNQFIGATVEDDIAFgleNKKVPPkkmkdiIDDLAKKVGMED--YLDKEPQ----------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 405 gSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLgITDRILVMSNGL 483
Cdd:PRK13632 142 -NLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTrKKTLISITHDMDEAI-LADKVIVFSEGK 219
|
250 260
....*....|....*....|..
gi 507082969 484 VAGIVDTKTTTQN-EILRLASL 504
Cdd:PRK13632 220 LIAQGKPKEILNNkEILEKAKI 241
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
266-492 |
1.37e-17 |
|
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: 81.84 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 266 LQVRNLTSLRQPS--IRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIRE-----KSSGTITLHGKKINNHSANeainh 338
Cdd:cd03260 1 IELRDLNVYYGDKhaLKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVD----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 339 gfalVTEERRSTG------------IYAYLDIGfnslisniqnyKNKVGLLDNSRMKSDTQWVIDSM----RVKTpghRT 402
Cdd:cd03260 76 ----VLELRRRVGmvfqkpnpfpgsIYDNVAYG-----------LRLHGIKLKEELDERVEEALRKAalwdEVKD---RL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 403 QIGSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:cd03260 138 HALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAEL-KKEYTIVIVTHNMQQAARVADRTAFLLNG 216
|
250
....*....|
gi 507082969 483 LVAGIVDTKT 492
Cdd:cd03260 217 RLVEFGPTEQ 226
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
266-482 |
1.50e-17 |
|
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: 82.16 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 266 LQVRNLT------SLRQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINN---------- 329
Cdd:COG1124 2 LEVRNLSvsygqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRrrrkafrrrv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 330 --------------HSANEAINHGFALVTEERRSTGIYAYLDigfnslisniqnyknKVGLldnsrmksdtqwvidsmrv 395
Cdd:COG1124 82 qmvfqdpyaslhprHTVDRILAEPLRIHGLPDREERIAELLE---------------QVGL------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 396 kTPGHRTQ-IGSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDK-GIIIISSEMPELLGIT 473
Cdd:COG1124 128 -PPSFLDRyPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGlTYLFVSHDLAVVAHLC 206
|
....*....
gi 507082969 474 DRILVMSNG 482
Cdd:COG1124 207 DRVAVMQNG 215
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
14-209 |
2.21e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 81.72 E-value: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDF-------HSAKEAL 86
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTarslsqqKGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 87 ENGISMVHQELNLVLQRSVMDNMWLGRYPTKGMFVDQdkmyrdTKAIFDELdididpRARVG----------TLSVSQMQ 156
Cdd:PRK11264 84 RQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEE------ATARAREL------LAKVGlagketsyprRLSGGQQQ 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 507082969 157 MIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKM 209
Cdd:PRK11264 152 RVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEM 204
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
266-484 |
2.50e-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: 79.57 E-value: 2.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 266 LQVRNLT----SLRQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEAinhgfa 341
Cdd:cd03246 1 LEVENVSfrypGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 342 lvteeRRSTGIYAYLDIGFN-SLISNIqnyknkvglldnsrmksdtqwvidsmrvktpghrtqigsLSGGNQQKVVIGRW 420
Cdd:cd03246 75 -----GDHVGYLPQDDELFSgSIAENI---------------------------------------LSGGQRQRLGLARA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507082969 421 LLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:cd03246 111 LYGNPRILVLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
261-482 |
2.66e-17 |
|
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: 84.82 E-value: 2.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 261 PGEVILQVRNLT----SLRQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSAnEAI 336
Cdd:COG4987 329 PGGPSLELEDVSfrypGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDE-DDL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 337 NHGFALVTEErrstgiyAYLdigFNSLISNiqnykN------------------KVGLLDnsrmksdtqWViDSMRvktP 398
Cdd:COG4987 408 RRRIAVVPQR-------PHL---FDTTLRE-----NlrlarpdatdeelwaaleRVGLGD---------WL-AALP---D 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 399 GHRTQIGS----LSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIIISSEmPELLGITD 474
Cdd:COG4987 460 GLDTWLGEggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHR-LAGLERMD 537
|
....*...
gi 507082969 475 RILVMSNG 482
Cdd:COG4987 538 RILVLEDG 545
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
266-482 |
2.70e-17 |
|
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: 79.35 E-value: 2.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 266 LQVRNLT----SLRQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEAINHgFA 341
Cdd:cd03228 1 IEFKNVSfsypGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 342 LVTEErrstgiyAYLdigFN-SLISNIqnyknkvglldnsrmksdtqwvidsmrvktpghrtqigsLSGGNQQKVVIGRW 420
Cdd:cd03228 80 YVPQD-------PFL---FSgTIRENI---------------------------------------LSGGQRQRIAIARA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507082969 421 LLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIIISSEMpELLGITDRILVMSNG 482
Cdd:cd03228 111 LLRDPPILILDEATSALDPETEALILEALRALA-KGKTVIVIAHRL-STIRDADRIIVLDDG 170
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
276-482 |
3.19e-17 |
|
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: 80.26 E-value: 3.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 276 QPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNhsaneainhgfalVTEERRSTGI--- 352
Cdd:cd03259 13 VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG-------------VPPERRNIGMvfq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 353 -YAyldigfnsLISNIQNYKNKVGLLDNSRMKSDTQ-----WVIDSMRVKTPGHRTqIGSLSGGNQQKVVIGRWLLTQPE 426
Cdd:cd03259 80 dYA--------LFPHLTVAENIAFGLKLRGVPKAEIrarvrELLELVGLEGLLNRY-PHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 507082969 427 ILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEG 207
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
25-226 |
4.74e-17 |
|
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: 80.35 E-value: 4.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 25 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEaLENGISMVHQELNLvLQRS 104
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAS-LRRQIGLVSQDVFL-FNDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 105 VMDNMwlgRYPTKGmfVDQDKMYRDTKAIF---------DELDIDIDPRArvGTLSVSQMQMIEIAKAFSYDAKIVIMDE 175
Cdd:cd03251 92 VAENI---AYGRPG--ATREEVEEAARAANahefimelpEGYDTVIGERG--VKLSGGQRQRIAIARALLKDPPILILDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 507082969 176 PTSSL---TEKEVNhlfTIIRKLKERGCGIVyISHKMEEIFQlCDEITVLRDGQ 226
Cdd:cd03251 165 ATSALdteSERLVQ---AALERLMKNRTTFV-IAHRLSTIEN-ADRIVVLEDGK 213
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
238-485 |
5.36e-17 |
|
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: 84.12 E-value: 5.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 238 MDKIISMMVGRSLNQRFPDKENKPGEVilQVRNLT----SLRQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIR 313
Cdd:COG2274 448 LDDILDLPPEREEGRSKLSLPRLKGDI--ELENVSfrypGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLY 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 314 EKSSGTITLHGKKINNHSANEainhgfaLvteeRRSTGIY---AYLdigFN-SLISNIqnyknkvgLLDNSRMksDTQWV 389
Cdd:COG2274 526 EPTSGRILIDGIDLRQIDPAS-------L----RRQIGVVlqdVFL---FSgTIRENI--------TLGDPDA--TDEEI 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 390 IDSMRV--------KTP-GHRTQIG----SLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKD 456
Cdd:COG2274 582 IEAARLaglhdfieALPmGYDTVVGeggsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL-KG 660
|
250 260
....*....|....*....|....*....
gi 507082969 457 KGIIIISSEmPELLGITDRILVMSNGLVA 485
Cdd:COG2274 661 RTVIIIAHR-LSTIRLADRIIVLDKGRIV 688
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
25-243 |
7.08e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 80.55 E-value: 7.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 25 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEaLENGISMVHQEL-NLVLQR 103
Cdd:PRK13647 17 GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKW-VRSKVGLVFQDPdDQVFSS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 104 SVMDNMWLGrypTKGMFVDQDKMYRDTKAIFDELDI-DIDPRARVgTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTE 182
Cdd:PRK13647 96 TVWDDVAFG---PVNMGLDKDEVERRVEEALKAVRMwDFRDKPPY-HLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 507082969 183 KEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIATQPLEGLDMDKIIS 243
Cdd:PRK13647 172 RGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVE 232
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
279-482 |
8.52e-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: 79.62 E-value: 8.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 279 IRDISFDLHKGEILGIAGLVGAKRTDIVETLFG-IREKS--SGTITLHGKKINNHSANEAINHgfaLVTEERRSTGIYAY 355
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrVEGGGttSGQILFNGQPRKPDQFQKCVAY---VRQDDILLPGLTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 356 LDIGFNSLIS--NIQNYKNKVGLLDNSRMKSDTQWVIDSMRVKtpghrtqigSLSGGNQQKVVIGRWLLTQPEILMLDEP 433
Cdd:cd03234 100 ETLTYTAILRlpRKSSDAIRKKRVEDVLLRDLALTRIGGNLVK---------GISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 507082969 434 TRGIDVGAKFEIYQLIAELAKKDKgIIIISSEMP--ELLGITDRILVMSNG 482
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLARRNR-IVILTIHQPrsDLFRLFDRILLLSSG 220
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
26-226 |
1.06e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 79.74 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 26 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeidfHSAKeaLENGISMvHQELnlvlqrSV 105
Cdd:COG1134 39 FWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR----VSAL--LELGAGF-HPEL------TG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 106 MDNMWLGryptkGMFVDQDKmyRDTKAIFDELdID-------ID-PrarVGTLSvSQMQM-IEIAKAFSYDAKIVIMDEP 176
Cdd:COG1134 106 RENIYLN-----GRLLGLSR--KEIDEKFDEI-VEfaelgdfIDqP---VKTYS-SGMRArLAFAVATAVDPDILLVDEV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 507082969 177 TS----SLTEKevnhLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQ 226
Cdd:COG1134 174 LAvgdaAFQKK----CLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGR 223
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
3-226 |
1.21e-16 |
|
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: 79.11 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 3 STHTQSSGEYLLEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGK---EIDF 79
Cdd:cd03220 12 TYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvssLLGL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 80 HSAkealengismVHQELnlvlqrSVMDN-----MWLGRYPTkgmfvDQDKMYRDTKAiFDELDIDIDprARVGTLSvSQ 154
Cdd:cd03220 92 GGG----------FNPEL------TGRENiylngRLLGLSRK-----EIDEKIDEIIE-FSELGDFID--LPVKTYS-SG 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507082969 155 MQM-IEIAKAFSYDAKIVIMDEPTS----SLTEKEVNHlftiIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQ 226
Cdd:cd03220 147 MKArLAFAIATALEPDILLIDEVLAvgdaAFQEKCQRR----LRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGK 219
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
24-226 |
1.29e-16 |
|
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: 79.05 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 24 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKeALENGISMVHQElNLVLQR 103
Cdd:cd03248 25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK-YLHSKVSLVGQE-PVLFAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 104 SVMDNM--WLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLT 181
Cdd:cd03248 103 SLQDNIayGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 507082969 182 EKEVNHLFTIIRKLKERGCGIVyISHKMEEIfQLCDEITVLRDGQ 226
Cdd:cd03248 183 AESEQQVQQALYDWPERRTVLV-IAHRLSTV-ERADQILVLDGGR 225
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
13-229 |
1.40e-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: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEalengism 92
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWE-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 93 vhqelnLVLQRSVM-------------DNMWLGRYPtkgmfvdqdkmYRDTKAIFDELdididPR---ARVG-------- 148
Cdd:COG4559 73 ------LARRRAVLpqhsslafpftveEVVALGRAP-----------HGSSAAQDRQI-----VRealALVGlahlagrs 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 149 --TLSVSQMQMIEIAKAF-------SYDAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEI 219
Cdd:COG4559 131 yqTLSGGEQQRVQLARVLaqlwepvDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRI 210
|
250
....*....|
gi 507082969 220 TVLRDGQWIA 229
Cdd:COG4559 211 LLLHQGRLVA 220
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
25-226 |
1.47e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 78.76 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 25 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEA--LENGISMVHQELNLVLQ 102
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVpfLRRQIGMIFQDHHLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 103 RSVMDNMWLgryPTKGMFVDQDKMYRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTE 182
Cdd:PRK10908 94 RTVYDNVAI---PLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 507082969 183 KEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQ 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 |
1.63e-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: 79.07 E-value: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 28 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFhSAKEALENGISMVHQElNLVLQRSVMD 107
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLAL-ADPAWLRRQVGVVLQE-NVLFNRSIRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 108 NMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRA--RVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSL-TEKE 184
Cdd:cd03252 95 NIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVgeQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALdYESE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 507082969 185 VNhlftIIRKLKE--RGCGIVYISHKMEEIfQLCDEITVLRDGQ 226
Cdd:cd03252 175 HA----IMRNMHDicAGRTVIIIAHRLSTV-KNADRIIVMEKGR 213
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
33-236 |
1.77e-16 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 78.64 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 33 NLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEidfHSAKEALENGISMVHQELNLVLQRSVMDNMWLG 112
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD---LTALPPAERPVSMLFQENNLFPHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 113 RYPtkGMFVDQDkmyrDTKAIFDELD----IDIDPRaRVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHL 188
Cdd:COG3840 96 LRP--GLKLTAE----QRAQVEQALErvglAGLLDR-LPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEM 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 507082969 189 FTIIRKL-KERGCGIVYISHKMEEIFQLCDEITVLRDGQWIATQPLEGL 236
Cdd:COG3840 169 LDLVDELcRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
280-482 |
1.95e-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: 77.96 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 280 RDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANeainhgfalVTEERRSTGI------- 352
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKN---------INELRQKVGMvfqqfnl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 353 YAYLDIGFNSLISNIQNYK--------------NKVGLLDnsrmKSDtqwvidsmrvKTPGHrtqigsLSGGNQQKVVIG 418
Cdd:cd03262 88 FPHLTVLENITLAPIKVKGmskaeaeeralellEKVGLAD----KAD----------AYPAQ------LSGGQQQRVAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507082969 419 RWLLTQPEILMLDEPTRGID---VGakfEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:cd03262 148 RALAMNPKVMLFDEPTSALDpelVG---EVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
261-500 |
2.28e-16 |
|
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: 78.48 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 261 PGEVILQVRNLTSLR--QPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEAinh 338
Cdd:COG1127 1 MSEPMIEVRNLTKSFgdRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKEL--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 339 gfalvTEERRSTGI----YAYLD-------IGF---------NSLISNIQNYK-NKVGLLDnsrmksdtqwVIDSMrvkt 397
Cdd:COG1127 78 -----YELRRRIGMlfqgGALFDsltvfenVAFplrehtdlsEAEIRELVLEKlELVGLPG----------AADKM---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 398 PGhrtqigSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGID-VGAKfEIYQLIAELAKKDKG-IIIISSEMPELLGITDR 475
Cdd:COG1127 139 PS------ELSGGMRKRVALARALALDPEILLYDEPTAGLDpITSA-VIDELIRELRDELGLtSVVVTHDLDSAFAIADR 211
|
250 260
....*....|....*....|....*..
gi 507082969 476 ILVMSNG--LVAGIVDTKTTTQNEILR 500
Cdd:COG1127 212 VAVLADGkiIAEGTPEELLASDDPWVR 238
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
266-485 |
2.75e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 79.32 E-value: 2.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 266 LQVRNLTSLRQP-------SIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANeainh 338
Cdd:PRK13637 3 IKIENLTHIYMEgtpfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVK----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 339 gfalVTEERRSTGIY------------AYLDIGFNSliSNIQNYKNKVglldNSRMKSDTQWV---IDSMRVKTPGhrtq 403
Cdd:PRK13637 78 ----LSDIRKKVGLVfqypeyqlfeetIEKDIAFGP--INLGLSEEEI----ENRVKRAMNIVgldYEDYKDKSPF---- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 404 igSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSE-MPELLGITDRILVMSNG 482
Cdd:PRK13637 144 --ELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHsMEDVAKLADRIIVMNKG 221
|
...
gi 507082969 483 LVA 485
Cdd:PRK13637 222 KCE 224
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
13-230 |
3.40e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 78.58 E-value: 3.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSFP-GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFhSAKEALEngis 91
Cdd:PRK13639 1 ILETRDLKYSYPdGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKY-DKKSLLE---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 92 mVHQELNLVLQRSvmDNMWLGryPTkgmfVDQDKMYRDTKAIFDELDID---IDPRARVGT----------LSVSQMQMI 158
Cdd:PRK13639 76 -VRKTVGIVFQNP--DDQLFA--PT----VEEDVAFGPLNLGLSKEEVEkrvKEALKAVGMegfenkpphhLSGGQKKRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507082969 159 EIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIAT 230
Cdd:PRK13639 147 AIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKE 218
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
13-225 |
3.49e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 78.20 E-value: 3.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAkealENGIsm 92
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA----ERGV-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 93 VHQELNLVLQRSVMDNMWLGrYPTKGMfvdqDKMYRDTKA--IFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYDAKI 170
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNVAFG-LQLAGV----EKMQRLEIAhqMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 507082969 171 VIMDEPTSSL---TEKEVNHLftIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDG 225
Cdd:PRK11248 150 LLLDEPFGALdafTREQMQTL--LLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
263-482 |
5.19e-16 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 79.00 E-value: 5.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 263 EVILQVRNLT-SLRQP-----SIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKS---SGTITLHGKKINN---H 330
Cdd:PRK09473 10 DALLDVKDLRvTFSTPdgdvtAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNlpeK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 331 SANEAINHGFALVTEERRsTGIYAYLDIGfNSLISNIQNYK--NKVGLLDNS-RMksdtqwvIDSmrVKTPGHRTQIG-- 405
Cdd:PRK09473 90 ELNKLRAEQISMIFQDPM-TSLNPYMRVG-EQLMEVLMLHKgmSKAEAFEESvRM-------LDA--VKMPEARKRMKmy 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 406 --SLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK09473 159 phEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAG 238
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
30-484 |
5.21e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 80.52 E-value: 5.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 30 DNVNLKVRPHSIHALMGENGAGKST-------LLKCLFGIYQkdSGSILFQGKEIdFHSAKEALE----NGISMVHQE-- 96
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSVtalsilrLLPSPPVVYP--SGDIRFHGESL-LHASEQTLRgvrgNKIAMIFQEpm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 97 --LNLV--LQRSVMDNMWLGRyptkGMfvdqdkmyRDTKA---IFDELDididpraRVG-------------TLSVSQMQ 156
Cdd:PRK15134 103 vsLNPLhtLEKQLYEVLSLHR----GM--------RREAArgeILNCLD-------RVGirqaakrltdyphQLSGGERQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 157 MIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFTIIRKLK-ERGCGIVYISHKMEEIFQLCDEITVLRDGQWI---ATQP 232
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQqELNMGLLFITHNLSIVRKLADRVAVMQNGRCVeqnRAAT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 233 LEGLDMDKIISMMVGrSLNQRFPDKENKPGEVILQVRNLT---SLRQPSIR----------DISFDLHKGEILGIAGLVG 299
Cdd:PRK15134 244 LFSAPTHPYTQKLLN-SEPSGDPVPLPEPASPLLDVEQLQvafPIRKGILKrtvdhnvvvkNISFTLRPGETLGLVGESG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 300 A-KRTDIVETLFGIRekSSGTITLHGKKINNHS-----------------ANEAIN---------------HGFALVTEE 346
Cdd:PRK15134 323 SgKSTTGLALLRLIN--SQGEIWFDGQPLHNLNrrqllpvrhriqvvfqdPNSSLNprlnvlqiieeglrvHQPTLSAAQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 347 RRSTGIYAYldigfnslisniqnykNKVGLLDNSRmksdtqwvidsmrvktpgHRTQiGSLSGGNQQKVVIGRWLLTQPE 426
Cdd:PRK15134 401 REQQVIAVM----------------EEVGLDPETR------------------HRYP-AEFSGGQRQRIAIARALILKPS 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 507082969 427 ILMLDEPTRGIDVGAKFEIYQLIAELAKKDK-GIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:PRK15134 446 LIILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQVIVLRQGEV 504
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
266-482 |
5.71e-16 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 76.78 E-value: 5.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 266 LQVRNLTSLR--QPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSAneainhgfalv 343
Cdd:COG4619 1 LELEGLSFRVggKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPP----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 344 TEERRSTgiyAYL----DIGFNSLISNIQN-YKNKVGLLDNSRMKSDTQwvidsmRVKTPGH--RTQIGSLSGGNQQKVV 416
Cdd:COG4619 70 PEWRRQV---AYVpqepALWGGTVRDNLPFpFQLRERKFDRERALELLE------RLGLPPDilDKPVERLSGGERQRLA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507082969 417 IGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKDKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:COG4619 141 LIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
13-228 |
6.33e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 79.49 E-value: 6.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfhSAKEALENGISM 92
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL---SHVPPYQRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 93 VHQELNLVLQRSVMDNMWLGryptkgmfVDQDKMYRDtkaifdeldidiDPRARVG-----------------TLSVSQM 155
Cdd:PRK11607 96 MFQSYALFPHMTVEQNIAFG--------LKQDKLPKA------------EIASRVNemlglvhmqefakrkphQLSGGQR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507082969 156 QMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITVLRDGQWI 228
Cdd:PRK11607 156 QRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-245 |
6.45e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 80.22 E-value: 6.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 5 HTQSSGEYLLEMTGIN---KSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFG-IY-QKDSGSILFQGKEIDF 79
Cdd:NF040905 249 RTPKIGEVVFEVKNWTvyhPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGrSYgRNISGTVFKDGKEVDV 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 80 HSAKEALENGISMV---HQELNLVLQRSVMDNMWLGRYP--TKGMFVDQDKMYRDTKAIFDELDI---DIDprARVGTLS 151
Cdd:NF040905 329 STVSDAIDAGLAYVtedRKGYGLNLIDDIKRNITLANLGkvSRRGVIDENEEIKVAEEYRKKMNIktpSVF--QKVGNLS 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 152 VSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIATQ 231
Cdd:NF040905 407 GGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITGEL 486
|
250
....*....|....
gi 507082969 232 PLEGLDMDKIISMM 245
Cdd:NF040905 487 PREEASQERIMRLI 500
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
279-434 |
7.11e-16 |
|
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: 74.61 E-value: 7.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 279 IRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSAnEAINHGFALVTEErrstgiyayldi 358
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDER-KSLRKEIGYVFQD------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 359 gfNSLISNIQNYKN-----KVGLLDNSRMKSDTQWVIDSMRVKTPGHRT---QIGSLSGGNQQKVVIGRWLLTQPEILML 430
Cdd:pfam00005 68 --PQLFPRLTVRENlrlglLLKGLSKREKDARAEEALEKLGLGDLADRPvgeRPGTLSGGQRQRVAIARALLTKPKLLLL 145
|
....
gi 507082969 431 DEPT 434
Cdd:pfam00005 146 DEPT 149
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
281-487 |
8.76e-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: 78.62 E-value: 8.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 281 DISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSAneainhGFALVTEERRSTgiYAYLDIGF 360
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRK------GIFLPPEKRRIG--YVFQEARL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 361 NSLISNIQN----YKNKVGLLDNSRMKSDTQWV-IDSMRVKTPGhrtqigSLSGGNQQKVVIGRWLLTQPEILMLDEPTR 435
Cdd:TIGR02142 87 FPHLSVRGNlrygMKRARPSERRISFERVIELLgIGHLLGRLPG------RLSGGEKQRVAIGRALLSSPRLLLMDEPLA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 507082969 436 GIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVAGI 487
Cdd:TIGR02142 161 ALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAA 213
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
25-234 |
9.21e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 77.23 E-value: 9.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 25 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeidfhSAKEAL-ENGISMVHQ--ELNLVL 101
Cdd:PRK15056 19 GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQ-----PTRQALqKNLVAYVPQseEVDWSF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 102 QRSVMDNMWLGRYPTKGMFVDQDKmyRDTKAIFDELD-IDI-DPRAR-VGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTS 178
Cdd:PRK15056 94 PVLVEDVVMMGRYGHMGWLRRAKK--RDRQIVTAALArVDMvEFRHRqIGELSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 507082969 179 SLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDeITVLRDGQWIATQPLE 234
Cdd:PRK15056 172 GVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTE 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
13-226 |
1.33e-15 |
|
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: 79.34 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSFPG-----------VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIyQKDSGSILFQGKEIDFHS 81
Cdd:COG4172 275 LLEARDLKVWFPIkrglfrrtvghVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 82 AKE--ALENGISMVHQE----LNlvlQRsvmdnMWLGRYPTKGMFVDQDKMYRDTK-----AIFDELDIDIDPRAR-VGT 149
Cdd:COG4172 354 RRAlrPLRRRMQVVFQDpfgsLS---PR-----MTVGQIIAEGLRVHGPGLSAAERrarvaEALEEVGLDPAARHRyPHE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 150 LSVSQMQMIEIAKAFSYDAKIVIMDEPTSSL---TEKEVNHLFtiiRKL-KERGCGIVYISHKMEEIFQLCDEITVLRDG 225
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALdvsVQAQILDLL---RDLqREHGLAYLFISHDLAVVRALAHRVMVMKDG 502
|
.
gi 507082969 226 Q 226
Cdd:COG4172 503 K 503
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
272-484 |
1.42e-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: 76.08 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 272 TSLRQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSaneainhGFALVtEERRSTG 351
Cdd:cd03258 14 TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLS-------GKELR-KARRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 352 -IYAyldiGFNsLISNIQNYKNkVGL---LDNSRMKSDTQWVIDSMRVKTPGHRTQI--GSLSGGNQQKVVIGRWLLTQP 425
Cdd:cd03258 86 mIFQ----HFN-LLSSRTVFEN-VALpleIAGVPKAEIEERVLELLELVGLEDKADAypAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 426 EILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
7-226 |
2.19e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 77.68 E-value: 2.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 7 QSSGEYLLEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfhsakeal 86
Cdd:PRK09452 8 PSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI--------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 87 eNGISMVHQELNLVLQR-------SVMDNMWLGRyptkgmfvdqdKMYRDTKAifdeldiDIDPRA-------------- 145
Cdd:PRK09452 79 -THVPAENRHVNTVFQSyalfphmTVFENVAFGL-----------RMQKTPAA-------EITPRVmealrmvqleefaq 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 146 -RVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEK-------EVNHLftiIRKLkerGCGIVYISHKMEEIFQLCD 217
Cdd:PRK09452 140 rKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKlrkqmqnELKAL---QRKL---GITFVFVTHDQEEALTMSD 213
|
....*....
gi 507082969 218 EITVLRDGQ 226
Cdd:PRK09452 214 RIVVMRDGR 222
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
15-226 |
3.04e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 75.50 E-value: 3.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 15 EMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfHSAKEALENGISMVH 94
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVA-TTPSRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 95 QELNLVLQRSVMDNMWLGRYP-TKGMFVDQDKMYRDtKAIfDELDIDiDPRAR-VGTLSVSQMQMIEIAKAFSYDAKIVI 172
Cdd:COG4604 82 QENHINSRLTVRELVAFGRFPySKGRLTAEDREIID-EAI-AYLDLE-DLADRyLDELSGGQRQRAFIAMVLAQDTDYVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 507082969 173 MDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHkmeEI-FQLC--DEITVLRDGQ 226
Cdd:COG4604 159 LDEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLH---DInFASCyaDHIVAMKDGR 213
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
19-226 |
3.46e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 75.43 E-value: 3.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 19 INKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGS---ILFQGKEIDfHSAKEALENGISMVH- 94
Cdd:PRK09984 10 LAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshIELLGRTVQ-REGRLARDIRKSRANt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 95 ----QELNLVLQRSVMDNMWLGR------YPTKGMFVDQDKMYRDTKAIfDELDIDIDPRARVGTLSVSQMQMIEIAKAF 164
Cdd:PRK09984 89 gyifQQFNLVNRLSVLENVLIGAlgstpfWRTCFSWFTREQKQRALQAL-TRVGMVHFAHQRVSTLSGGQQQRVAIARAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507082969 165 SYDAKIVIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITVLRDGQ 226
Cdd:PRK09984 168 MQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGH 230
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
278-482 |
3.88e-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: 74.33 E-value: 3.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 278 SIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSaneainhgfalvTEERRSTGI---YA 354
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP------------REVRRRIGIvfqDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 355 YLD---IGFNSLI--SNIQNYKNkvglldnSRMKSDTQWVIDSMRVKTPGHRtQIGSLSGGNQQKVVIGRWLLTQPEILM 429
Cdd:cd03265 83 SVDdelTGWENLYihARLYGVPG-------AERRERIDELLDFVGLLEAADR-LVKTYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 507082969 430 LDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHG 208
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
14-210 |
4.14e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 75.05 E-value: 4.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHS---AKE--ALEN 88
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKtpsDKAirELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 89 GISMVHQELNLVLQRSVMDNmwLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYDA 168
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQN--LIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 507082969 169 KIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKME 210
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVE 202
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
276-482 |
4.15e-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: 4.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 276 QPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANE-AINHGFalvteerRSTGIYA 354
Cdd:cd03300 13 FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKrPVNTVF-------QNYALFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 355 YLDIGfnsliSNIQnYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRtQIGSLSGGNQQKVVIGRWLLTQPEILMLDEPT 434
Cdd:cd03300 86 HLTVF-----ENIA-FGLRLKKLPKAEIKERVAEALDLVQLEGYANR-KPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 507082969 435 RGIDV----GAKFEIYQLIAELakkdkGI--IIISSEMPELLGITDRILVMSNG 482
Cdd:cd03300 159 GALDLklrkDMQLELKRLQKEL-----GItfVFVTHDQEEALTMSDRIAVMNKG 207
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
26-229 |
5.74e-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: 74.29 E-value: 5.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 26 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkEIDFHSAKEALENgISMVH-QELNLVLQRS 104
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-LVPWKRRKKFLRR-IGVVFgQKTQLWWDLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 105 VMDNMWLgrypTKGMFVDQDKMYRDTKAIFDELdIDIDP--RARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTE 182
Cdd:cd03267 112 VIDSFYL----LAAIYDLPPARFKKRLDELSEL-LDLEEllDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 507082969 183 KEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITVLRDGQWIA 229
Cdd:cd03267 187 VAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLY 234
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
29-228 |
6.64e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 74.70 E-value: 6.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKC---LFGIYQ---KDSGSILFQGKEIdFHSAKEALENGISMVHQELNLVLQ 102
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVlnrLIEIYDskiKVDGKVLYFGKDI-FQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 103 RSVMDNMwlgRYPTKGMFVdqdKMYRDTKAIFDE------LDIDIDPR--ARVGTLSVSQMQMIEIAKAFSYDAKIVIMD 174
Cdd:PRK14246 105 LSIYDNI---AYPLKSHGI---KEKREIKKIVEEclrkvgLWKEVYDRlnSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 507082969 175 EPTSSLTEKEVNHLFTIIRKLKERgCGIVYISHKMEEIFQLCDEITVLRDGQWI 228
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
26-283 |
6.79e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 75.51 E-value: 6.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 26 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG-----KEIDFhsAKEalengISMVHQelnlv 100
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpfkRRKEF--ARR-----IGVVFG----- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 101 lQRS-------VMDNMWLGRyptkgmfvdqdKMYRDTKAIFDE--------LDID--IDPRARvgTLSVSQ-MQMiEIAK 162
Cdd:COG4586 103 -QRSqlwwdlpAIDSFRLLK-----------AIYRIPDAEYKKrldelvelLDLGelLDTPVR--QLSLGQrMRC-ELAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 163 AFSYDAKIVIMDEPTSSL---TEKEVNHLftiIRKL-KERGCGIVYISHKMEEIFQLCDEITVLRDGQWIATQPLEGL-- 236
Cdd:COG4586 168 ALLHRPKILFLDEPTIGLdvvSKEAIREF---LKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELke 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507082969 237 --DMDKIISMMVGRSLNQ-RFPD----KENKPGEVILQVRNLTS--------LRQPSIRDIS 283
Cdd:COG4586 245 rfGPYKTIVLELAEPVPPlELPRggevIEREGNRVRLEVDPRESlaevlarlLARYPVRDLT 306
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
4-217 |
8.21e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 74.43 E-value: 8.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 4 THTQSSGEYLLEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKC------LFGIYQKDsGSILFQGKEI 77
Cdd:PRK14243 1 TSTLNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndLIPGFRVE-GKVTFHGKNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 78 -DFHSAKEALENGISMVHQELNlVLQRSVMDNMWLGRYpTKGMFVDQDKMYRDT---KAIFDEldidIDPRARVGTLSVS 153
Cdd:PRK14243 80 yAPDVDPVEVRRRIGMVFQKPN-PFPKSIYDNIAYGAR-INGYKGDMDELVERSlrqAALWDE----VKDKLKQSGLSLS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507082969 154 --QMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCgIVYISHKMEEIFQLCD 217
Cdd:PRK14243 154 ggQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYT-IIIVTHNMQQAARVSD 218
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
266-485 |
8.28e-15 |
|
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: 74.14 E-value: 8.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 266 LQVRNLtSLRQPS----IRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINN--HSANEAINH- 338
Cdd:cd03256 1 IEVENL-SKTYPNgkkaLKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlkGKALRQLRRq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 339 ------GFALVteERRS------TGIYAYLDI--GFNSLISNIQNYK-----NKVGLLDNSRMKSDTqwvidsmrvktpg 399
Cdd:cd03256 80 igmifqQFNLI--ERLSvlenvlSGRLGRRSTwrSLFGLFPKEEKQRalaalERVGLLDKAYQRADQ------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 400 hrtqigsLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPEL-LGITDRILV 478
Cdd:cd03256 145 -------LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLaREYADRIVG 217
|
....*..
gi 507082969 479 MSNGLVA 485
Cdd:cd03256 218 LKDGRIV 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
27-228 |
8.42e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 74.87 E-value: 8.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 27 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALEN---GISMVHQ--ELNLvL 101
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKlrkKVSLVFQfpEAQL-F 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 102 QRSVMDNMWLGryPTKGMFVDQDKMYRDTKAI----FDELDIDIDPRarvgTLSVSQMQMIEIAKAFSYDAKIVIMDEPT 177
Cdd:PRK13641 100 ENTVLKDVEFG--PKNFGFSEDEAKEKALKWLkkvgLSEDLISKSPF----ELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 507082969 178 SSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWI 228
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
20-228 |
9.20e-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: 72.58 E-value: 9.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 20 NKSFPGVKA-LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFG--IYQKDSGSILFQGKEIDfhsaKEALENGISMVHQE 96
Cdd:cd03213 15 SSPSKSGKQlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLD----KRSFRKIIGYVPQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 97 LNLVLQRSVMDNMwlgryptkgMFVdqdkmyrdtkaifdeldididprARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEP 176
Cdd:cd03213 91 DILHPTLTVRETL---------MFA-----------------------AKLRGLSGGERKRVSIALELVSNPSLLFLDEP 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 507082969 177 TSSLTEKEVNHLFTIIRKLKERGCGIVYISHK-MEEIFQLCDEITVLRDGQWI 228
Cdd:cd03213 139 TSGLDSSSALQVMSLLRRLADTGRTIICSIHQpSSEIFELFDKLLLLSQGRVI 191
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
28-225 |
1.37e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 74.02 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 28 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEalengismVHQELNLVLQRSvmD 107
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEK--------LRKHIGIVFQNP--D 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 108 NMWLGR-------YPTKGMFVDQDKMYRDTKAIFDELDI----DIDPRArvgtLSVSQMQMIEIAKAFSYDAKIVIMDEP 176
Cdd:PRK13648 94 NQFVGSivkydvaFGLENHAVPYDEMHRRVSEALKQVDMleraDYEPNA----LSGGQKQRVAIAGVLALNPSVIILDEA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 507082969 177 TSSLTEKEVNHLFTIIRKLK-ERGCGIVYISHKMEEIFQlCDEITVLRDG 225
Cdd:PRK13648 170 TSMLDPDARQNLLDLVRKVKsEHNITIISITHDLSEAME-ADHVIVMNKG 218
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
25-226 |
1.39e-14 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 76.98 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 25 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfhSAKEALENGISMVHQELNLVLQRS 104
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE--TNLDAVRQSLGMCPQHNILFHHLT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 105 VMDNMwLGRYPTKGMfvDQDKMYRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKE 184
Cdd:TIGR01257 1020 VAEHI-LFYAQLKGR--SWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYS 1096
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 507082969 185 VNHLFTIIRKLKErGCGIVYISHKMEEIFQLCDEITVLRDGQ 226
Cdd:TIGR01257 1097 RRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGR 1137
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
265-479 |
1.91e-14 |
|
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: 74.32 E-value: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 265 ILQVRNL-TSLRQPS-----IRDISFDLHKGEILGIAG------------LVGakrtdivetLFGIREKSSGTITLHGKK 326
Cdd:COG0444 1 LLEVRNLkVYFPTRRgvvkaVDGVSFDVRRGETLGLVGesgsgkstlaraILG---------LLPPPGITSGEILFDGED 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 327 INNHSAneainhgfalvtEERRStgiYAYLDIG------FNSLisniqnykN---KVG-----LLDNSRMKSDTQW---V 389
Cdd:COG0444 72 LLKLSE------------KELRK---IRGREIQmifqdpMTSL--------NpvmTVGdqiaePLRIHGGLSKAEArerA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 390 IDSM-RVKTPGHRTQIGS----LSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIIS 463
Cdd:COG0444 129 IELLeRVGLPDPERRLDRypheLSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFIT 208
|
250
....*....|....*.
gi 507082969 464 SEMPELLGITDRILVM 479
Cdd:COG0444 209 HDLGVVAEIADRVAVM 224
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1-229 |
2.00e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 73.28 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 1 MVSTHTQSSGEYLLEmtgiNKSF--PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLfGIYQKDS-GSILFQGKEI 77
Cdd:PRK10575 1 MQEYTNHSDTTFALR----NVSFrvPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQPPSeGEILLDAQPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 78 DFHSAKeALENGISMVHQELNLVLQRSVMDNMWLGRYP---TKGMFVDQDKMYRDtKAIfdeLDIDIDPRAR--VGTLSV 152
Cdd:PRK10575 76 ESWSSK-AFARKVAYLPQQLPAAEGMTVRELVAIGRYPwhgALGRFGAADREKVE-EAI---SLVGLKPLAHrlVDSLSG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507082969 153 SQMQMIEIAKAFSYDAKIVIMDEPTSSL-TEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIA 229
Cdd:PRK10575 151 GERQRAWIAMLVAQDSRCLLLDEPTSALdIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIA 228
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
272-482 |
2.04e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 73.71 E-value: 2.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 272 TSLRQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEAINhgfalvtEERRSTG 351
Cdd:PRK13641 16 TPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLK-------KLRKKVS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 352 I---YAYLDIGFNSLISNIQNYKNKVGLLDNSRMKSDTQWV-----IDSMRVKTPGhrtqigSLSGGNQQKVVIGRWLLT 423
Cdd:PRK13641 89 LvfqFPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLkkvglSEDLISKSPF------ELSGGQMRRVAIAGVMAY 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 507082969 424 QPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK13641 163 EPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHG 221
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
276-485 |
2.30e-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: 72.24 E-value: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 276 QPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSaneainhgfalVTEERRSTGiYAY 355
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD-----------PADLRRNIG-YVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 356 LDIG--FNSLISNI---QNYKNKVGLLDNSRMKSDTQWVIDSMRvktpGHRTQIG----SLSGGNQQKVVIGRWLLTQPE 426
Cdd:cd03245 85 QDVTlfYGTLRDNItlgAPLADDERILRAAELAGVTDFVNKHPN----GLDLQIGergrGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 427 ILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIIISSEMPeLLGITDRILVMSNG-LVA 485
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPS-LLDLVDRIIVMDSGrIVA 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
263-486 |
3.46e-14 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 72.00 E-value: 3.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 263 EVILQVRNLT------SLRQPSIRDISFDLHKGEILGIAGLVGAKRTdiveTLF----GIREKSSGTITLHGKKINNHSA 332
Cdd:COG1136 2 SPLLELRNLTksygtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKS----TLLnilgGLDRPTSGEVLIDGQDISSLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 333 NEAinhgfalvTEERRSTgiyayldIGF-----NsLISN---IQNyknkVGL---LDNSRMKSDTQWVIDSM-RVKTPGH 400
Cdd:COG1136 78 REL--------ARLRRRH-------IGFvfqffN-LLPEltaLEN----VALpllLAGVSRKERRERARELLeRVGLGDR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 401 RTQ-IGSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVM 479
Cdd:COG1136 138 LDHrPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRL 217
|
....*..
gi 507082969 480 SNGLVAG 486
Cdd:COG1136 218 RDGRIVS 224
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-226 |
4.35e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 74.88 E-value: 4.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 25 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGI--YQkdsGSILFQG---KEIDFHSAKEALengiSMVHQELNL 99
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFlpYQ---GSLKINGielRELDPESWRKHL----SWVGQNPQL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 100 vLQRSVMDNMWLGRYPTKGMFVDQ--DKMYRD--TKAIFDELDIDIDPRArvGTLSVSQMQMIEIAKAFSYDAKIVIMDE 175
Cdd:PRK11174 435 -PHGTLRDNVLLGNPDASDEQLQQalENAWVSefLPLLPQGLDTPIGDQA--AGLSVGQAQRLALARALLQPCQLLLLDE 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 507082969 176 PTSSLTEKEVNHLFTIIRKLKERGCGIVyISHKMEEIFQlCDEITVLRDGQ 226
Cdd:PRK11174 512 PTASLDAHSEQLVMQALNAASRRQTTLM-VTHQLEDLAQ-WDQIWVMQDGQ 560
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
28-226 |
4.45e-14 |
|
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: 71.37 E-value: 4.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 28 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfHSAKEALENGISMVHQElNLVLQRSVMD 107
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDIS-KIGLHDLRSRISIIPQD-PVLFSGTIRS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 108 NM-WLGRYPtkgmfvdqDKMYRDT------KAIFDELDIDIDPRARVG--TLSVSQMQMIEIAKAFSYDAKIVIMDEPTS 178
Cdd:cd03244 97 NLdPFGEYS--------DEELWQAlervglKEFVESLPGGLDTVVEEGgeNLSVGQRQLLCLARALLRKSKILVLDEATA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 507082969 179 SL---TEKevnHLFTIIRKlKERGCGIVYISHKMEEIFQlCDEITVLRDGQ 226
Cdd:cd03244 169 SVdpeTDA---LIQKTIRE-AFKDCTVLTIAHRLDTIID-SDRILVLDKGR 214
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
12-229 |
4.95e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 72.53 E-value: 4.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 12 YLLEMTGINKSFPG-VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEalengi 90
Cdd:PRK13652 2 HLIETRDLCYSYSGsKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIRE------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 91 smVHQELNLVLQRSvmDNMWLGryPTkgmfVDQDKMYRDTKAIFDELDID------------IDPRARV-GTLSVSQMQM 157
Cdd:PRK13652 76 --VRKFVGLVFQNP--DDQIFS--PT----VEQDIAFGPINLGLDEETVAhrvssalhmlglEELRDRVpHHLSGGEKKR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507082969 158 IEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITVLRDGQWIA 229
Cdd:PRK13652 146 VAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVA 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-228 |
5.28e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 74.33 E-value: 5.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 9 SGEYLLEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFqGKEIDfhsakealen 88
Cdd:COG0488 311 LGKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK---------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 89 gISMVHQEL-NLVLQRSVMDNMW--------------LGRYptkgMFV--DQDKmyrdtkaifdeldididpraRVGTLS 151
Cdd:COG0488 380 -IGYFDQHQeELDPDKTVLDELRdgapggteqevrgyLGRF----LFSgdDAFK--------------------PVGVLS 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 152 V---SQMQMieiAKAFSYDAKIVIMDEPTssltekevNHL--FTiIRKLKE-----RGCgIVYISHKMEEIFQLCDEITV 221
Cdd:COG0488 435 GgekARLAL---AKLLLSPPNVLLLDEPT--------NHLdiET-LEALEEalddfPGT-VLLVSHDRYFLDRVATRILE 501
|
....*..
gi 507082969 222 LRDGQWI 228
Cdd:COG0488 502 FEDGGVR 508
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
13-235 |
5.55e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 72.33 E-value: 5.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSFP-GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENGIS 91
Cdd:PRK13644 1 MIRLENVSYSYPdGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 92 MVHQ--ELNLVlQRSVMDNMWLGrypTKGMFVDQDKMYRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYDAK 169
Cdd:PRK13644 81 IVFQnpETQFV-GRTVEEDLAFG---PENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507082969 170 IVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIfQLCDEITVLRDGQWIatqpLEG 235
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKIV----LEG 217
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
14-225 |
5.80e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 73.19 E-value: 5.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKealENGISMV 93
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR---DRKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 94 HQELNLVLQRSVMDNMWLG------RYPTKGMFVDQDKMyrdtkAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYD 167
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAFGltvlprRERPNAAAIKAKVT-----QLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 507082969 168 AKIVIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITVLRDG 225
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQG 213
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
25-234 |
6.22e-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: 70.63 E-value: 6.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 25 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGI--YQKDSGSILFQGKEIDFHSAKEALENGISMVHQELNLVLQ 102
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGIFLAFQYPPEIPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 103 RSVMDnmwLGRYPTKGmfvdqdkmyrdtkaifdeldididprarvgtLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTE 182
Cdd:cd03217 92 VKNAD---FLRYVNEG-------------------------------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 507082969 183 KEVNHLFTIIRKLKERGCGIVYISHKmEEIFQLC--DEITVLRDGQWIATQPLE 234
Cdd:cd03217 138 DALRLVAEVINKLREEGKSVLIITHY-QRLLDYIkpDRVHVLYDGRIVKSGDKE 190
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
27-228 |
6.46e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 72.08 E-value: 6.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 27 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEAlengISMVHQELNLVLQ---- 102
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKD----IKQIRKKVGLVFQfpes 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 103 ----RSVMDNMWLGRYPTKGMFVDQDKMYRDTKA---IFDELdIDIDPRarvgTLSVSQMQMIEIAKAFSYDAKIVIMDE 175
Cdd:PRK13649 97 qlfeETVLKDVAFGPQNFGVSQEEAEALAREKLAlvgISESL-FEKNPF----ELSGGQMRRVAIAGILAMEPKILVLDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 507082969 176 PTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWI 228
Cdd:PRK13649 172 PTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
27-226 |
6.47e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 72.00 E-value: 6.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 27 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKealengISMVHQELNLVLQrsvm 106
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVK------LSDIRKKVGLVFQ---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 107 dnmwlgrYPTKGMFvdQDKMYRDTKAIFDEL---DIDIDPRAR-----VG------------TLSVSQMQMIEIAKAFSY 166
Cdd:PRK13637 91 -------YPEYQLF--EETIEKDIAFGPINLglsEEEIENRVKramniVGldyedykdkspfELSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 507082969 167 DAKIVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITVLRDGQ 226
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIKELhKEYNMTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
22-186 |
7.56e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 73.84 E-value: 7.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 22 SFPGVK-ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSaKEALENGISMVHQELNLv 100
Cdd:PRK13657 343 SYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT-RASLRRNIAVVFQDAGL- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 101 LQRSVMDNMWLGRyPTkgmfVDQDKMYRDTKAI----F-----DELDIDIDPRARvgTLSVSQMQMIEIAKAFSYDAKIV 171
Cdd:PRK13657 421 FNRSIEDNIRVGR-PD----ATDEEMRAAAERAqahdFierkpDGYDTVVGERGR--QLSGGERQRLAIARALLKDPPIL 493
|
170
....*....|....*...
gi 507082969 172 IMDEPTSSL---TEKEVN 186
Cdd:PRK13657 494 ILDEATSALdveTEAKVK 511
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
263-482 |
8.34e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 72.15 E-value: 8.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 263 EVILQVRNLTSL--RQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHsANEAinhgf 340
Cdd:PRK13537 5 VAPIDFRNVEKRygDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSR-ARHA----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 341 alvteeRRSTGI---YAYLDIGFnSLISNIQNYKNKVGLlDNSRMKSDTQWVIDSMRVKTPGHrTQIGSLSGGNQQKVVI 417
Cdd:PRK13537 79 ------RQRVGVvpqFDNLDPDF-TVRENLLVFGRYFGL-SAAAARALVPPLLEFAKLENKAD-AKVGELSGGMKRRLTL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507082969 418 GRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK13537 150 ARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
13-222 |
8.76e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 70.51 E-value: 8.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAkEALENGISM 92
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP-EIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 93 VHQELNLvLQRSVMDNMWLgRYPTKGMFVDQDKMYRDTkAIFdELDIDIDPRaRVGTLSVSQMQMIEIAKAFSYDAKIVI 172
Cdd:PRK10247 86 CAQTPTL-FGDTVYDNLIF-PWQIRNQQPDPAIFLDDL-ERF-ALPDTILTK-NIAELSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 507082969 173 MDEPTSSLTE---KEVNHLftIIRKLKERGCGIVYISHKMEEIfQLCDEITVL 222
Cdd:PRK10247 161 LDEITSALDEsnkHNVNEI--IHRYVREQNIAVLWVTHDKDEI-NHADKVITL 210
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
27-234 |
9.81e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 71.58 E-value: 9.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 27 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI--DFHSAKEA--LENGISMVHQ--ELNLv 100
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpaNLKKIKEVkrLRKEIGLVFQfpEYQL- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 101 LQRSVMDNMWLGryPTKgMFVDQDKMYRDTKAIFDELDIDIDPRARVG-TLSVSQMQMIEIAKAFSYDAKIVIMDEPTSS 179
Cdd:PRK13645 104 FQETIEKDIAFG--PVN-LGENKQEAYKKVPELLKLVQLPEDYVKRSPfELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 507082969 180 LTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITVLRDGQWIAT-QPLE 234
Cdd:PRK13645 181 LDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIgSPFE 237
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
13-264 |
1.03e-13 |
|
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: 74.28 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSFPGVK--ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfhsakeaLENgI 90
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--------LTN-I 2007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 91 SMVHQELNLVLQRSVMDNMWLGR----YPTKGMFVDQDKMYRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSY 166
Cdd:TIGR01257 2008 SDVHQNMGYCPQFDAIDDLLTGRehlyLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIG 2087
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 167 DAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIATQPLEGLDMD----KII 242
Cdd:TIGR01257 2088 CPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKfgdgYIV 2167
|
250 260 270
....*....|....*....|....*....|
gi 507082969 243 SMMVGRSLNQRFPD--------KENKPGEV 264
Cdd:TIGR01257 2168 TMKIKSPKDDLLPDlnpveqffQGNFPGSV 2197
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
26-226 |
1.16e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 71.86 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 26 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIyQKDSGSI-----LFQGKEIDFHSAKEALE---NGISMVHQEL 97
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHVtadrfRWNGIDLLKLSPRERRKiigREIAMIFQEP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 98 NLVL------QRSVMDNMWLGRYptKGMFVdQDKMYRDTKAIfdELdididpRARVGT-------------LSVSQMQMI 158
Cdd:COG4170 99 SSCLdpsakiGDQLIEAIPSWTF--KGKWW-QRFKWRKKRAI--EL------LHRVGIkdhkdimnsypheLTEGECQKV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507082969 159 EIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITVLRDGQ 226
Cdd:COG4170 168 MIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLnQLQGTSILLISHDLESISQWADTITVLYCGQ 236
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
265-482 |
1.27e-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: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 265 ILQVRNLTSL--RQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINnhsanEAINHGFAL 342
Cdd:COG4152 1 MLELKGLTKRfgDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-----PEDRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 343 VTEERrstGIYAyldigfnslisniqnyKNKVG--------L--LDNSRMKSDTQWVIDsmRVKTPGHRT-QIGSLSGGN 411
Cdd:COG4152 76 LPEER---GLYP----------------KMKVGeqlvylarLkgLSKAEAKRRADEWLE--RLGLGDRANkKVEELSKGN 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507082969 412 QQKVVIGRWLLTQPEILMLDEPTRGID-VGAKfEIYQLIAELAKKDKgIIIISS---EMPELLgiTDRILVMSNG 482
Cdd:COG4152 135 QQKVQLIAALLHDPELLILDEPFSGLDpVNVE-LLKDVIRELAAKGT-TVIFSShqmELVEEL--CDRIVIINKG 205
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
277-485 |
1.30e-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: 69.75 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 277 PSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKInnhsaneainhGFALVTEERRSTGIYAYL 356
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI-----------STIPLEDLRSSLTIIPQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 357 DIGFNSLI-SNiqnyknkvglLDNSRMKSDTQwVIDSMRVKTPGHrtqigSLSGGNQQKVVIGRWLLTQPEILMLDEPTR 435
Cdd:cd03369 91 PTLFSGTIrSN----------LDPFDEYSDEE-IYGALRVSEGGL-----NLSQGQRQLLCLARALLKRPRVLVLDEATA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 507082969 436 GIDVGAKFEIYQLIAELAkKDKGIIIISSEMPELLGItDRILVMSNGLVA 485
Cdd:cd03369 155 SIDYATDALIQKTIREEF-TNSTILTIAHRLRTIIDY-DKILVMDAGEVK 202
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
255-482 |
1.47e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.97 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 255 PDKENKPGEVILQVRNLT------SLRQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITlHGKKIN 328
Cdd:PRK10261 2 PHSDELDARDVLAVENLNiafmqeQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQ-CDKMLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 329 NHSANEAINHGFALVTEERRSTGiyAYLDIGFNSLISNI-----------------QNYKNKVGLLDNSRMksdtqwvID 391
Cdd:PRK10261 81 RRRSRQVIELSEQSAAQMRHVRG--ADMAMIFQEPMTSLnpvftvgeqiaesirlhQGASREEAMVEAKRM-------LD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 392 SMRVktPGHRTQIG----SLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEM 466
Cdd:PRK10261 152 QVRI--PEAQTILSryphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDM 229
|
250
....*....|....*.
gi 507082969 467 PELLGITDRILVMSNG 482
Cdd:PRK10261 230 GVVAEIADRVLVMYQG 245
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
14-207 |
1.57e-13 |
|
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: 72.78 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPG-VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeIDFHSAKE-ALENGIS 91
Cdd:TIGR02868 335 LELRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDG--VPVSSLDQdEVRRRVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 92 MVHQELNLvLQRSVMDNMWLGRyPTkgmfVDQDKMYR---------DTKAIFDELDIDIDPRARvgTLSVSQMQMIEIAK 162
Cdd:TIGR02868 413 VCAQDAHL-FDTTVRENLRLAR-PD----ATDEELWAalervgladWLRALPDGLDTVLGEGGA--RLSGGERQRLALAR 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 507082969 163 AFSYDAKIVIMDEPTSSL---TEKEVnhLFTIIRKLKERgcGIVYISH 207
Cdd:TIGR02868 485 ALLADAPILLLDEPTEHLdaeTADEL--LEDLLAALSGR--TVVLITH 528
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
279-484 |
1.66e-13 |
|
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: 69.88 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 279 IRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNhsaneainhgfaLVTEERRSTGIyAYL-- 356
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITK------------LPMHKRARLGI-GYLpq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 357 -DIGFNSLiSNIQNyknkVGLLDNSRMKSDTQWV-----------IDSMRvKTPGhrtqiGSLSGGNQQKVVIGRWLLTQ 424
Cdd:cd03218 83 eASIFRKL-TVEEN----ILAVLEIRGLSKKEREekleelleefhITHLR-KSKA-----SSLSGGERRRVEIARALATN 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 425 PEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:cd03218 152 PKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKV 211
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
30-229 |
1.71e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 70.40 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 30 DNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENgISMVHQELNLVLQRSVMDNM 109
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-IGLLAQNATTPGDITVQELV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 110 WLGRYPTKGMFV-----DQDKMYRDTKAIfdelDIDIDPRARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKE 184
Cdd:PRK10253 103 ARGRYPHQPLFTrwrkeDEEAVTKAMQAT----GITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISH 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 507082969 185 VNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITVLRDGQWIA 229
Cdd:PRK10253 179 QIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVA 224
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
262-482 |
1.99e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 71.03 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 262 GEVILQVRNLTSL---RQP----SIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANE 334
Cdd:PRK13631 18 DDIILRVKNLYCVfdeKQEnelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 335 AINHGFAL-----VTEERRSTGI------YAYL------DIGFNSLISNIQNYknkvglldnsRMKSDTQWVIDSMRVKT 397
Cdd:PRK13631 98 ELITNPYSkkiknFKELRRRVSMvfqfpeYQLFkdtiekDIMFGPVALGVKKS----------EAKKLAKFYLNKMGLDD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 398 PGHRTQIGSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRIL 477
Cdd:PRK13631 168 SYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVI 247
|
....*
gi 507082969 478 VMSNG 482
Cdd:PRK13631 248 VMDKG 252
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
266-482 |
2.22e-13 |
|
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: 69.14 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 266 LQVRNLTSL--RQPSIRDISFDLHKGeILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHsaneainhgfalV 343
Cdd:cd03264 1 LQLENLTKRygKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQ------------P 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 344 TEERRSTGiyaYL--DIGFNSLISNIQ--NYKNKVGLLDNSRMKSDTQWVIDsmRVKTPGHRTQ-IGSLSGGNQQKVVIG 418
Cdd:cd03264 68 QKLRRRIG---YLpqEFGVYPNFTVREflDYIAWLKGIPSKEVKARVDEVLE--LVNLGDRAKKkIGSLSGGMRRRVGIA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507082969 419 RWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKDKgIIIISSEMPE-LLGITDRILVMSNG 482
Cdd:cd03264 143 QALVGDPSILIVDEPTAGLDPEERIRFRNLLSELG-EDR-IVILSTHIVEdVESLCNQVAVLNKG 205
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
263-482 |
2.47e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 70.43 E-value: 2.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 263 EVILQVRNLT----SLRQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSaneainh 338
Cdd:PRK13635 3 EEIIRVEHISfrypDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEET------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 339 gfalVTEERRSTGIYayldigfnslisnIQNYKNK-VGL---------LDNSRMKSDT-----QWVIDSMRVKTPGHRtQ 403
Cdd:PRK13635 76 ----VWDVRRQVGMV-------------FQNPDNQfVGAtvqddvafgLENIGVPREEmvervDQALRQVGMEDFLNR-E 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 404 IGSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIIISsempellgIT---------D 474
Cdd:PRK13635 138 PHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQL-KEQKGITVLS--------IThdldeaaqaD 208
|
....*...
gi 507082969 475 RILVMSNG 482
Cdd:PRK13635 209 RVIVMNKG 216
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
266-487 |
2.66e-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: 68.82 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 266 LQVRNLTSL--RQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEainHGFALV 343
Cdd:cd03301 1 VELENVTKRfgNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD---RDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 344 TEErrstgiYAyldigfnsLISNIQNYKN-KVGLldnsRMKSDTQWVIDSmRVKTPGHRTQIG--------SLSGGNQQK 414
Cdd:cd03301 78 FQN------YA--------LYPHMTVYDNiAFGL----KLRKVPKDEIDE-RVREVAELLQIEhlldrkpkQLSGGQRQR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507082969 415 VVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVAGI 487
Cdd:cd03301 139 VALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQI 212
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
14-229 |
2.74e-13 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 69.29 E-value: 2.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEID----FHSAKEalenG 89
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIThlpmHKRARL----G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 90 ISMVHQE------LnlvlqrSVMDNMWL---GRYPTKgmfvdqdkmyRDTKAIFDEL--DIDIDPRARV--GTLSVSQMQ 156
Cdd:COG1137 80 IGYLPQEasifrkL------TVEDNILAvleLRKLSK----------KEREERLEELleEFGITHLRKSkaYSLSGGERR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507082969 157 MIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIA 229
Cdd:COG1137 144 RVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLA 216
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
13-229 |
3.17e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 69.42 E-value: 3.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEaLENGISM 92
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAE-LARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 93 VHQELNLVLQRSVMDNMWLGRYPtkgmfvDQDKMYRDTKAIFDELdididprARVG----------TLSVSQMQMIEIAK 162
Cdd:PRK13548 81 LPQHSSLSFPFTVEEVVAMGRAP------HGLSRAEDDALVAAAL-------AQVDlahlagrdypQLSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507082969 163 AF------SYDAKIVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITVLRDGQWIA 229
Cdd:PRK13548 148 VLaqlwepDGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVA 221
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
266-482 |
3.19e-13 |
|
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: 67.72 E-value: 3.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 266 LQVRNLT----SLRQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKInnHSANEAINHGFA 341
Cdd:cd03247 1 LSINNVSfsypEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV--SDLEKALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 342 LVTEErrstgiyAYLdigFN-SLISNIqnyknkvglldnsrmksdtqwvidsmrvktpGHRtqigsLSGGNQQKVVIGRW 420
Cdd:cd03247 79 VLNQR-------PYL---FDtTLRNNL-------------------------------GRR-----FSGGERQRLALARI 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507082969 421 LLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIIISSempELLGIT--DRILVMSNG 482
Cdd:cd03247 113 LLQDAPIVLLDEPTVGLDPITERQLLSLIFEVL-KDKTLIWITH---HLTGIEhmDKILFLENG 172
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
404-487 |
3.94e-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: 70.51 E-value: 3.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 404 IGSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:COG4148 131 PATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQG 210
|
....*
gi 507082969 483 LVAGI 487
Cdd:COG4148 211 RVVAS 215
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
13-226 |
3.95e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 71.66 E-value: 3.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSFPGVK-----------ALDNVNLKVRPHSIHALMGENGAGKST----LLKCLfgiyqKDSGSILFQGKEI 77
Cdd:PRK15134 275 LLDVEQLQVAFPIRKgilkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 78 DFHSAKEAL--ENGISMVHQELNLVL--QRSVMDNMwlgrypTKGMFVDQDKM---YRDTKAI--FDELDIDIDPRARV- 147
Cdd:PRK15134 350 HNLNRRQLLpvRHRIQVVFQDPNSSLnpRLNVLQII------EEGLRVHQPTLsaaQREQQVIavMEEVGLDPETRHRYp 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 148 GTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITVLRDGQ 226
Cdd:PRK15134 424 AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGE 503
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
27-228 |
4.37e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 69.81 E-value: 4.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 27 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfHSAKEALengISMVHQELNLVLQ---- 102
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIT-HKTKDKY---IRPVRKRIGMVFQfpes 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 103 ----RSVMDNMWLGryPTK-GMFVDQDKMYrdtkaIFDELdIDIDPRARVGTLSVSQM---QM--IEIAKAFSYDAKIVI 172
Cdd:PRK13646 97 qlfeDTVEREIIFG--PKNfKMNLDEVKNY-----AHRLL-MDLGFSRDVMSQSPFQMsggQMrkIAIVSILAMNPDIIV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 507082969 173 MDEPTSSLTEKEVNHLFTIIRKLK-ERGCGIVYISHKMEEIFQLCDEITVLRDGQWI 228
Cdd:PRK13646 169 LDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIV 225
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
13-232 |
4.87e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 69.33 E-value: 4.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSFPGV---------KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDF--HS 81
Cdd:PRK10419 3 LLNVSGLSHHYAHGglsgkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 82 AKEALENGISMVHQE-LNLV-LQRSVmdnMWLGRYPTKGMfVDQDKMYRDTKAifDEL--DIDIDPR---ARVGTLSVSQ 154
Cdd:PRK10419 83 QRKAFRRDIQMVFQDsISAVnPRKTV---REIIREPLRHL-LSLDKAERLARA--SEMlrAVDLDDSvldKRPPQLSGGQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507082969 155 MQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITVLRDGQWIATQP 232
Cdd:PRK10419 157 LQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQP 235
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
267-484 |
5.51e-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: 69.21 E-value: 5.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 267 QVRNLTSLRqPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEAIN---HGFALV 343
Cdd:cd03294 29 EILKKTGQT-VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrKKISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 344 TEerrSTGIYAYLdigfnSLISNIQnYKNKV-GLLDNSRMKSDTQwVIDSMRVKTPGHRtQIGSLSGGNQQKVVIGRWLL 422
Cdd:cd03294 108 FQ---SFALLPHR-----TVLENVA-FGLEVqGVPRAEREERAAE-ALELVGLEGWEHK-YPDELSGGMQQRVGLARALA 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507082969 423 TQPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKDKGIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:cd03294 177 VDPDILLMDEAFSALDPLIRREMQDELLRLqAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
14-226 |
6.09e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 70.13 E-value: 6.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfhsAKEALEN-GISM 92
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV----THRSIQQrDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 93 VHQELNLVLQRSVMDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYDAKIVI 172
Cdd:PRK11432 83 VFQSYALFPHMSLGENV---GYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 507082969 173 MDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITVLRDGQ 226
Cdd:PRK11432 160 FDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGK 214
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
27-226 |
6.10e-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: 67.82 E-value: 6.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 27 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfHSAKEALENGISMVHQELNLvLQRSVM 106
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIS-TIPLEDLRSSLTIIPQDPTL-FSGTIR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 107 DNmwlgryptkgmfVDQDKMYRDTKaIFDELDIdidprARVG-TLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLtEKEV 185
Cdd:cd03369 100 SN------------LDPFDEYSDEE-IYGALRV-----SEGGlNLSQGQRQLLCLARALLKRPRVLVLDEATASI-DYAT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 507082969 186 NHLFT-IIRKLKErGCGIVYISHKMEEIFQlCDEITVLRDGQ 226
Cdd:cd03369 161 DALIQkTIREEFT-NSTILTIAHRLRTIID-YDKILVMDAGE 200
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
277-482 |
7.76e-13 |
|
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: 68.13 E-value: 7.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 277 PSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHG----KKINNHSANEAINHGfalvteeRRSTGI 352
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlvpwKRRKKFLRRIGVVFG-------QKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 353 YaylDI----GFNsLISNIQNyknkvglLDNSRMKSDTQWVIDSMRVkTPGHRTQIGSLSGGNQQKVVIGRWLLTQPEIL 428
Cdd:cd03267 108 W---DLpvidSFY-LLAAIYD-------LPPARFKKRLDELSELLDL-EELLDTPVRQLSLGQRMRAEIAAALLHEPEIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 507082969 429 MLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISS-EMPELLGITDRILVMSNG 482
Cdd:cd03267 176 FLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTShYMKDIEALARRVLVIDKG 230
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-236 |
8.35e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 68.58 E-value: 8.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 16 MTGINKS--FPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQK-----DSGSILFQGKEIDFHSAKEALEN 88
Cdd:PRK14271 22 MAAVNLTlgFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRDVLEFRR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 89 GISMVHQELNlVLQRSVMDNMWLGRYPTKgmFVDQDKMYRDTKAIFDELDIDIDPRARVGT----LSVSQMQMIEIAKAF 164
Cdd:PRK14271 102 RVGMLFQRPN-PFPMSIMDNVLAGVRAHK--LVPRKEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507082969 165 SYDAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERgCGIVYISHKMEEIFQLCDEITVLRDGQWIATQPLEGL 236
Cdd:PRK14271 179 AVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
28-229 |
9.39e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 68.67 E-value: 9.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 28 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGS---ILFQGKEIDfhsakealENGISMVHQELNLVLQRS 104
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLT--------AKTVWDIREKVGIVFQNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 105 vmDNMWLGR-------YPTKGMFVDQDKMYRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPT 177
Cdd:PRK13640 94 --DNQFVGAtvgddvaFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDEST 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 507082969 178 SSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIfQLCDEITVLRDGQWIA 229
Cdd:PRK13640 172 SMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLA 223
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
279-482 |
1.43e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 67.23 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 279 IRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEAINHGFALVTEErrsTGIYAYLDI 358
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQE---ASIFRRLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 359 gFNSLISNIQNYKNkvglLDNSRMKSDTQWVIDSMRVKtpgH-RTQIG-SLSGGNQQKVVIGRWLLTQPEILMLDEPTRG 436
Cdd:PRK10895 96 -YDNLMAVLQIRDD----LSAEQREDRANELMEEFHIE---HlRDSMGqSLSGGERRRVEIARALAANPKFILLDEPFAG 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 507082969 437 IDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK10895 168 VDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQG 213
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
276-482 |
1.45e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 68.70 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 276 QPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINnhsaneainhgfALVTEERRSTGI--- 352
Cdd:PRK13536 54 KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP------------ARARLARARIGVvpq 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 353 YAYLDIGFnSLISNIQNYKNKVGLldNSRmksDTQWVIDSM----RVKTPGHrTQIGSLSGGNQQKVVIGRWLLTQPEIL 428
Cdd:PRK13536 122 FDNLDLEF-TVRENLLVFGRYFGM--STR---EIEAVIPSLlefaRLESKAD-ARVSDLSGGMKRRLTLARALINDPQLL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 507082969 429 MLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK13536 195 ILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
265-506 |
1.70e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 67.80 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 265 ILQVRNLtSLRQP----SIRDISFDLHKGEILGIAGLVGAKRTdiveTLF----GIREKSSGTITLHGKKI--NNHSANE 334
Cdd:PRK13639 1 ILETRDL-KYSYPdgteALKGINFKAEKGEMVALLGPNGAGKS----TLFlhfnGILKPTSGEVLIKGEPIkyDKKSLLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 335 AI-----------NHGFALVTEErrstgiyaylDIGFNSLisNIQNYKNKVglldNSRMKSDTQWVIDSMRVKTPGHRtq 403
Cdd:PRK13639 76 VRktvgivfqnpdDQLFAPTVEE----------DVAFGPL--NLGLSKEEV----EKRVKEALKAVGMEGFENKPPHH-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 404 igsLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKkdKGI-IIISSEMPELLGI-TDRILVMSN 481
Cdd:PRK13639 138 ---LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNK--EGItIIISTHDVDLVPVyADKVYVMSD 212
|
250 260
....*....|....*....|....*.
gi 507082969 482 G-LVAGIVDTKTTTQNEILRLASLHL 506
Cdd:PRK13639 213 GkIIKEGTPKEVFSDIETIRKANLRL 238
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
18-234 |
1.75e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 68.90 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 18 GINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfhsAKEALENGISMVHQEL 97
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN---DVPPAERGVGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 98 NLVLQRSVMDNMWLGrypTKGMFVDQDKMYRDTKAIFDELD----IDIDPRArvgtLSVSQMQMIEIAKAFSYDAKIVIM 173
Cdd:PRK11000 85 ALYPHLSVAENMSFG---LKLAGAKKEEINQRVNQVAEVLQlahlLDRKPKA----LSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507082969 174 DEPTSSLTEK-EVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLrDGQWIAT--QPLE 234
Cdd:PRK11000 158 DEPLSNLDAAlRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVL-DAGRVAQvgKPLE 220
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
284-485 |
1.81e-12 |
|
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: 66.36 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 284 FDLH--KGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKkinNHSANEAINHGFALVTEErrsTGIYAYLDIGFN 361
Cdd:cd03298 17 FDLTfaQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV---DVTAAPPADRPVSMLFQE---NNLFAHLTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 362 slisniqnyknkVGLLDNSRMKSDTQwviDSMRVKTPGHRTQI--------GSLSGGNQQKVVIGRWLLTQPEILMLDEP 433
Cdd:cd03298 91 ------------VGLGLSPGLKLTAE---DRQAIEVALARVGLaglekrlpGELSGGERQRVALARVLVRDKPVLLLDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 507082969 434 TRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPE-LLGITDRILVMSNGLVA 485
Cdd:cd03298 156 FAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEdAKRLAQRVVFLDNGRIA 208
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
21-226 |
2.40e-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: 2.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 21 KSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeidfhsakealenGISMVHQE---L 97
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------------SIAYVSQEpwiQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 98 NlvlqRSVMDNMWLGRYptkgmfVDQDKmYRDT-KAIFDELDIDIDP---RARVG----TLSVSQMQMIEIAKAFSYDAK 169
Cdd:cd03250 79 N----GTIRENILFGKP------FDEER-YEKViKACALEPDLEILPdgdLTEIGekgiNLSGGQKQRISLARAVYSDAD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 507082969 170 IVIMDEPTSSLTEKEVNHLFT--IIRKLKERGCgIVYISHKMEEIFQlCDEITVLRDGQ 226
Cdd:cd03250 148 IYLLDDPLSAVDAHVGRHIFEncILGLLLNNKT-RILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
405-484 |
2.72e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 67.98 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 405 GSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGL 483
Cdd:PRK11144 127 GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGK 206
|
.
gi 507082969 484 V 484
Cdd:PRK11144 207 V 207
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
277-495 |
2.90e-12 |
|
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: 66.49 E-value: 2.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 277 PSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEAINHgFALVTEErrstgiyAYL 356
Cdd:cd03251 16 PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQ-IGLVSQD-------VFL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 357 digFNSLISNIQNYknkvGLLDNSRMKsdtqwVIDSMRV--------KTP-GHRTQIGS----LSGGNQQKVVIGRWLLT 423
Cdd:cd03251 88 ---FNDTVAENIAY----GRPGATREE-----VEEAARAanahefimELPeGYDTVIGErgvkLSGGQRQRIAIARALLK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507082969 424 QPEILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIIISSEMPELLGItDRILVMSNGlvaGIVDTKTTTQ 495
Cdd:cd03251 156 DPPILILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRLSTIENA-DRIVVLEDG---KIVERGTHEE 222
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
406-485 |
3.26e-12 |
|
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: 65.26 E-value: 3.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 406 SLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIII----SSEMPELLgitDRILVMSN 481
Cdd:cd03213 111 GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSihqpSSEIFELF---DKLLLLSQ 187
|
....
gi 507082969 482 GLVA 485
Cdd:cd03213 188 GRVI 191
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
276-485 |
3.29e-12 |
|
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: 66.10 E-value: 3.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 276 QPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNhsaneainhgfalVTEE--RRSTGIY 353
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIRE-------------VTLDslRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 354 AYLDIGFNSLIS-NIQnYKNkVGLLDNSRMKSDTQWVIDSMRVKTP-GHRTQIGS----LSGGNQQKVVIGRWLLTQPEI 427
Cdd:cd03253 81 PQDTVLFNDTIGyNIR-YGR-PDATDEEVIEAAKAAQIHDKIMRFPdGYDTIVGErglkLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 507082969 428 LMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIIISSEMPELLGiTDRILVMSNGLVA 485
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIVN-ADKIIVLKDGRIV 214
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
278-502 |
7.72e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 65.67 E-value: 7.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 278 SIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNH---------SANEAINHGFALVTEERR 348
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAlqknlvayvPQSEEVDWSFPVLVEDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 349 STGIYAYLdigfnslisniqnyknkvGLLDNSRmKSDTQWVIDSM-RVKTPGHR-TQIGSLSGGNQQKVVIGRWLLTQPE 426
Cdd:PRK15056 102 MMGRYGHM------------------GWLRRAK-KRDRQIVTAALaRVDMVEFRhRQIGELSGGQKKRVFLARAIAQQGQ 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507082969 427 ILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRIlVMSNGLVAGIVDTKTTTQNEILRLA 502
Cdd:PRK15056 163 VILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASGPTETTFTAENLELA 237
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
13-230 |
8.20e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 65.33 E-value: 8.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKE---IDFHSAKEA---- 85
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlRDLYALSEAerrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 86 ---LENGIsmVHQ--ELNLVLQRSVMDN-----MWLGryptkgmfvdqDKMYRDTKAI----FDELDID---IDPRARvg 148
Cdd:PRK11701 86 llrTEWGF--VHQhpRDGLRMQVSAGGNigerlMAVG-----------ARHYGDIRATagdwLERVEIDaarIDDLPT-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 149 TLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITVLRDGQW 227
Cdd:PRK11701 151 TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
...
gi 507082969 228 IAT 230
Cdd:PRK11701 231 VES 233
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
266-489 |
8.31e-12 |
|
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: 64.80 E-value: 8.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 266 LQVRNLT------SLRQPSIRDISFDLHKGEILGIAGLVGAKRTdiveTLF----GIREKSSGTITLHGKKINNHSANEA 335
Cdd:cd03293 1 LEVRNVSktygggGGAVTALEDISLSVEEGEFVALVGPSGCGKS----TLLriiaGLERPTSGEVLVDGEPVTGPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 336 I---------------NHGFAL-----VTEERRSTGIyAYLDigfnslisniqnyknKVGLLDNSRmksdtqwvidsmrv 395
Cdd:cd03293 77 YvfqqdallpwltvldNVALGLelqgvPKAEARERAE-ELLE---------------LVGLSGFEN-------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 396 KTPGhrtqigSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKD-KGIIIISSEMPELLGITD 474
Cdd:cd03293 127 AYPH------QLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgKTVLLVTHDIDEAVFLAD 200
|
250
....*....|....*..
gi 507082969 475 RILVMSN--GLVAGIVD 489
Cdd:cd03293 201 RVVVLSArpGRIVAEVE 217
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
278-484 |
8.32e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 65.54 E-value: 8.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 278 SIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEAINH-GFALVTEERRSTGIYAYL 356
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHiGIVFQNPDNQFVGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 357 DIGFnSLISNIQNYKNkvglldnsrMKSDTQWVI-DSMRVKTPGHRTQigSLSGGNQQKVVIGRWLLTQPEILMLDEPTR 435
Cdd:PRK13648 104 DVAF-GLENHAVPYDE---------MHRRVSEALkQVDMLERADYEPN--ALSGGQKQRVAIAGVLALNPSVIILDEATS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 507082969 436 GIDVGAKFEIYQLIAEL-AKKDKGIIIISSEMPELLGiTDRILVMSNGLV 484
Cdd:PRK13648 172 MLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAME-ADHVIVMNKGTV 220
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
266-484 |
9.10e-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: 65.05 E-value: 9.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 266 LQVRNLTSL--RQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEAiNHGF--- 340
Cdd:cd03296 3 IEVRNVSKRfgDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER-NVGFvfq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 341 --ALVteeRRSTgiyAYLDIGFNSLISNIQNYKNKvglldnSRMKSDTQWVIDSMRVKTPGHR--TQigsLSGGNQQKVV 416
Cdd:cd03296 82 hyALF---RHMT---VFDNVAFGLRVKPRSERPPE------AEIRAKVHELLKLVQLDWLADRypAQ---LSGGQRQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 417 IGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGI--IIISSEMPELLGITDRILVMSNGLV 484
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRL-HDELHVttVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
404-496 |
1.00e-11 |
|
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: 65.11 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 404 IGSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIIS---SEMPEllGITdRILVM 479
Cdd:COG1119 140 FGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgAPTLVLVThhvEEIPP--GIT-HVLLL 216
|
90
....*....|....*....
gi 507082969 480 SNGLV--AGIVDTKTTTQN 496
Cdd:COG1119 217 KDGRVvaAGPKEEVLTSEN 235
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
276-487 |
1.09e-11 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 67.11 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 276 QPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEAINHgFALVTEErrstgiyAY 355
Cdd:COG1132 353 RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQ-IGVVPQD-------TF 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 356 LdigFN-SLISNIqnyknKVGLLDNSRmksdtQWVIDSMRV--------KTP-GHRTQIG----SLSGGNQQKVVIGRWL 421
Cdd:COG1132 425 L---FSgTIRENI-----RYGRPDATD-----EEVEEAAKAaqahefieALPdGYDTVVGergvNLSGGQRQRIAIARAL 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507082969 422 LTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIIIS---SempellgiT----DRILVMSNGLVAGI 487
Cdd:COG1132 492 LKDPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAhrlS--------TirnaDRILVLDDGRIVEQ 555
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
265-506 |
1.18e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 65.25 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 265 ILQVRNLtSLRQP----SIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINnHSAN------E 334
Cdd:PRK13636 5 ILKVEEL-NYNYSdgthALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKglmklrE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 335 AINHGFALVTEERRSTGIYAylDIGFNSLisNIQNYKNKV-GLLDNSRMKSDtqwvIDSMRVKtPGHrtqigSLSGGNQQ 413
Cdd:PRK13636 83 SVGMVFQDPDNQLFSASVYQ--DVSFGAV--NLKLPEDEVrKRVDNALKRTG----IEHLKDK-PTH-----CLSFGQKK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 414 KVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV---AGIvd 489
Cdd:PRK13636 149 RVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVilqGNP-- 226
|
250
....*....|....*..
gi 507082969 490 TKTTTQNEILRLASLHL 506
Cdd:PRK13636 227 KEVFAEKEMLRKVNLRL 243
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
27-243 |
1.27e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 65.06 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 27 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDS-----GSILFQGKEI-DFHSAKEALENGISMVHQELNLv 100
Cdd:PRK14258 21 KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyERRVNLNRLRRQVSMVHPKPNL- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 101 LQRSVMDNM-----WLGRYPTKGMFVDQDKMYRDTKaIFDELDIDIDPRARvgTLSVSQMQMIEIAKAFSYDAKIVIMDE 175
Cdd:PRK14258 100 FPMSVYDNVaygvkIVGWRPKLEIDDIVESALKDAD-LWDEIKHKIHKSAL--DLSGGQQQRLCIARALAVKPKVLLMDE 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507082969 176 PTSSLTEKEVNHLFTIIRKLKERG-CGIVYISHKMEEIFQLCDEITVLRDGQWIATQPLEGLDMDKIIS 243
Cdd:PRK14258 177 PCFGLDPIASMKVESLIQSLRLRSeLTMVIVSHNLHQVSRLSDFTAFFKGNENRIGQLVEFGLTKKIFN 245
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
265-482 |
1.44e-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: 67.35 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 265 ILQVRNLTSL----RQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKInnhsaneainhgF 340
Cdd:TIGR01257 1937 ILRLNELTKVysgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI------------L 2004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 341 ALVTEERRSTGIYAYLDiGFNSLISNIQN---YKNKVGLlDNSRMKSDTQWVIDSMRVKTPGHRTQiGSLSGGNQQKVVI 417
Cdd:TIGR01257 2005 TNISDVHQNMGYCPQFD-AIDDLLTGREHlylYARLRGV-PAEEIEKVANWSIQSLGLSLYADRLA-GTYSGGNKRKLST 2081
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507082969 418 GRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:TIGR01257 2082 AIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
275-477 |
1.51e-11 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 63.41 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 275 RQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKK----INNHSAneaINHGFALVTEERRST 350
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGArvayVPQRSE---VPDSLPLTVRDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 351 GIYAyldigfnslisniqnyknKVGLLDNSRmKSDTQWVIDSM-RVKTPG--HRtQIGSLSGGNQQKVVIGRWLLTQPEI 427
Cdd:NF040873 81 GRWA------------------RRGLWRRLT-RDDRAAVDDALeRVGLADlaGR-QLGELSGGQRQRALLAQGLAQEADL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 507082969 428 LMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRIL 477
Cdd:NF040873 141 LLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVL 190
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
265-489 |
1.68e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 64.56 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 265 ILQVRNLTSLRQPSI--RDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSAneainhgFAL 342
Cdd:PRK11701 6 LLSVRGLTKLYGPRKgcRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDL-------YAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 343 VTEERRstgIYAYLDIGFN------------SLISNIQNYKNKVGLLDNSRMKSD-TQWVidsMRVKTPGHRT--QIGSL 407
Cdd:PRK11701 79 SEAERR---RLLRTEWGFVhqhprdglrmqvSAGGNIGERLMAVGARHYGDIRATaGDWL---ERVEIDAARIddLPTTF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 408 SGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKDKGIIIISSEM--PELLgiTDRILVMSNGLV 484
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLavARLL--AHRLLVMKQGRV 230
|
....*..
gi 507082969 485 --AGIVD 489
Cdd:PRK11701 231 veSGLTD 237
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
31-234 |
1.83e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 65.67 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 31 NVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeIDFHSakealENGISM---------VHQELNLVL 101
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGR-VLFDA-----EKGICLppekrrigyVFQDARLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 102 QRSVMDNMWLGryptkgmfvdqdkMYRDTKAIFDELD--IDIDPR-ARV-GTLSVSQMQMIEIAKAFSYDAKIVIMDEPT 177
Cdd:PRK11144 90 HYKVRGNLRYG-------------MAKSMVAQFDKIValLGIEPLlDRYpGSLSGGEKQRVAIGRALLTAPELLLMDEPL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 507082969 178 SSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITVLRDGQWIATQPLE 234
Cdd:PRK11144 157 ASLDLPRKRELLPYLERLaREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLE 214
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-229 |
1.91e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 66.39 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 3 STHTQSSGEYLLEMTGINKSFPG--VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFH 80
Cdd:PRK11160 328 TTSTAAADQVSLTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADY 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 81 SaKEALENGISMVHQELNLvLQRSVMDNMWLGryptkgmfvdqdkmyrDTKAIFDELdidIDPRARVG------------ 148
Cdd:PRK11160 408 S-EAALRQAISVVSQRVHL-FSATLRDNLLLA----------------APNASDEAL---IEVLQQVGleklleddkgln 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 149 --------TLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSL---TEKEVNHLftiirkLKERGCG--IVYISHKMEEIFQL 215
Cdd:PRK11160 467 awlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLdaeTERQILEL------LAEHAQNktVLMITHRLTGLEQF 540
|
250
....*....|....
gi 507082969 216 cDEITVLRDGQWIA 229
Cdd:PRK11160 541 -DRICVMDNGQIIE 553
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
12-77 |
2.52e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 63.89 E-value: 2.52e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507082969 12 YLLEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFG--IYQKDSGSILFQGKEI 77
Cdd:CHL00131 6 PILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESI 73
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-77 |
2.52e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 63.95 E-value: 2.52e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507082969 14 LEMTGINKSF-PG----VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI 77
Cdd:COG1101 2 LELKNLSKTFnPGtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV 70
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
27-228 |
2.56e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 64.03 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 27 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKD-----SGSILFQGKEIdfHSAKE---ALENGISMVHQELN 98
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNI--YSPRTdtvDLRKEIGMVFQQPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 99 lVLQRSVMDNMWLGrYPTKGMfvdQDKMYRDT--------KAIFDELDiDIDPRARVGtLSVSQMQMIEIAKAFSYDAKI 170
Cdd:PRK14239 97 -PFPMSIYENVVYG-LRLKGI---KDKQVLDEavekslkgASIWDEVK-DRLHDSALG-LSGGQQQRVCIARVLATSPKI 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 507082969 171 VIMDEPTSSLTEKEVNHLFTIIRKLKERGCgIVYISHKMEEIFQLCDEITVLRDGQWI 228
Cdd:PRK14239 170 ILLDEPTSALDPISAGKIEETLLGLKDDYT-MLLVTRSMQQASRISDRTGFFLDGDLI 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
266-479 |
2.75e-11 |
|
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: 65.77 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 266 LQVRNLTSL---RQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINnhSANEAINHG-FA 341
Cdd:TIGR02857 322 LEFSGVSVAypgRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLA--DADADSWRDqIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 342 LVTEerrSTGIYAyldigfNSLISNIQNYKN--KVGLLDNSRMKSDTQWVIDSMRvktPGHRTQIGS----LSGGNQQKV 415
Cdd:TIGR02857 400 WVPQ---HPFLFA------GTIAENIRLARPdaSDAEIREALERAGLDEFVAALP---QGLDTPIGEggagLSGGQAQRL 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507082969 416 VIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIisSEMPELLGITDRILVM 479
Cdd:TIGR02857 468 ALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLV--THRLALAALADRIVVL 529
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
265-486 |
2.86e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 63.51 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 265 ILQVRNLT-SLRQ-PSIRDISFDLHKGEILGIAGLVGAKRTdiveTLF----GIREKSSGTITLHGKKINNHSANEAINH 338
Cdd:COG1137 3 TLEAENLVkSYGKrTVVKDVSLEVNQGEIVGLLGPNGAGKT----TTFymivGLVKPDSGRIFLDGEDITHLPMHKRARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 339 GFALVTEE----RRST---GIYAYLDIgfnsLISNIQNYKNKV-GLLDNSRmksdtqwvIDSMRvKTPGHrtqigSLSGG 410
Cdd:COG1137 79 GIGYLPQEasifRKLTvedNILAVLEL----RKLSKKEREERLeELLEEFG--------ITHLR-KSKAY-----SLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 411 NQQKVVIGRWLLTQPEILMLDEPTRGID---VGakfEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG--LVA 485
Cdd:COG1137 141 ERRRVEIARALATNPKFILLDEPFAGVDpiaVA---DIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGkvLAE 217
|
.
gi 507082969 486 G 486
Cdd:COG1137 218 G 218
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
24-225 |
3.18e-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: 63.12 E-value: 3.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 24 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEA-LENGISMVH-QELNLVL 101
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrSRNRYSVAYaAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 102 QRSVMDNMWLGRYPTKGMFvdqdKMYRDTKAIfdELDIDIDP---RARVG----TLSVSQMQMIEIAKAFSYDAKIVIMD 174
Cdd:cd03290 92 NATVEENITFGSPFNKQRY----KAVTDACSL--QPDIDLLPfgdQTEIGergiNLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 507082969 175 EPTSSLTEKEVNHLFT--IIRKLKERGCGIVYISHKMEEIFQlCDEITVLRDG 225
Cdd:cd03290 166 DPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
279-484 |
3.43e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 63.45 E-value: 3.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 279 IRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKIN---NHSANEAINHGFALVTEERRSTGIYAY 355
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrDKDGQLKVADKNQLRLLRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 356 LDI-GFNSLISNIQNYKNKVGLLDNSRMKS------DTQWVIDSMRVKTPGHrtqigsLSGGNQQKVVIGRWLLTQPEIL 428
Cdd:PRK10619 101 FNLwSHMTVLENVMEAPIQVLGLSKQEAREravkylAKVGIDERAQGKYPVH------LSGGQQQRVSIARALAMEPEVL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 507082969 429 MLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:PRK10619 175 LFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
261-489 |
3.77e-11 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 63.57 E-value: 3.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 261 PGEVILQVRNLT------SLRQPSIRDISFDLHKGE---ILG------------IAGLVGAkrtdivetlfgirekSSGT 319
Cdd:COG1116 3 AAAPALELRGVSkrfptgGGGVTALDDVSLTVAAGEfvaLVGpsgcgkstllrlIAGLEKP---------------TSGE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 320 ITLHGKKINNHSANEAI---------------NHGFAL-----VTEERRSTgIYAYLDigfnslisniqnyknKVGLLD- 378
Cdd:COG1116 68 VLVDGKPVTGPGPDRGVvfqepallpwltvldNVALGLelrgvPKAERRER-ARELLE---------------LVGLAGf 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 379 -NSRmksdtqwvidsmrvktPGhrtqigSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKD 456
Cdd:COG1116 132 eDAY----------------PH------QLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETG 189
|
250 260 270
....*....|....*....|....*....|....*..
gi 507082969 457 KGIIIISSEMPE--LLGitDRILVMSN--GLVAGIVD 489
Cdd:COG1116 190 KTVLFVTHDVDEavFLA--DRVVVLSArpGRIVEEID 224
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
14-228 |
4.61e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 65.04 E-value: 4.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPG--VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKeALENGIS 91
Cdd:PRK11176 342 IEFRNVTFTYPGkeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLA-SLRNQVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 92 MVHQELNLvLQRSVMDNMwlgRYPTKGMFVDQD-----KMYRDTKAIfDELDIDIDprARVG----TLSVSQMQMIEIAK 162
Cdd:PRK11176 421 LVSQNVHL-FNDTIANNI---AYARTEQYSREQieeaaRMAYAMDFI-NKMDNGLD--TVIGengvLLSGGQRQRIAIAR 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507082969 163 AFSYDAKIVIMDEPTSSL-TEKEvNHLFTIIRKLKERGCGIVyISHKMEEIFQlCDEITVLRDGQWI 228
Cdd:PRK11176 494 ALLRDSPILILDEATSALdTESE-RAIQAALDELQKNRTSLV-IAHRLSTIEK-ADEILVVEDGEIV 557
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
275-495 |
5.02e-11 |
|
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: 63.29 E-value: 5.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 275 RQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKIN--NHSANEAINHGFALVTEE------ 346
Cdd:TIGR02769 23 RAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYqlDRKQRRAFRRDVQLVFQDspsavn 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 347 -RRSTGiyayldigfNSLISNIQNYKNkvglLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGNQQKVVIGRWLLTQP 425
Cdd:TIGR02769 103 pRMTVR---------QIIGEPLRHLTS----LDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKP 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507082969 426 EILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGI--IIISSEMPELLGITDRILVMSNGlvaGIVDTKTTTQ 495
Cdd:TIGR02769 170 KLIVLDEAVSNLDMVLQAVILELLRKL-QQAFGTayLFITHDLRLVQSFCQRVAVMDKG---QIVEECDVAQ 237
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
27-230 |
5.49e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 63.50 E-value: 5.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 27 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFH-SAKE--ALENGISMVHQ--ELNLvL 101
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGkKNKKlkPLRKKVGIVFQfpEHQL-F 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 102 QRSVMDNMWLGryPTKgmF-VDQDKMYRDTKAIFDELDIDIDPRARVG-TLSVSQMQMIEIAKAFSYDAKIVIMDEPTSS 179
Cdd:PRK13634 100 EETVEKDICFG--PMN--FgVSEEDAKQKAREMIELVGLPEELLARSPfELSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 507082969 180 LT---EKEVNHLFTIIRKlkERGCGIVYISHKMEEIFQLCDEITVLRDGQWIAT 230
Cdd:PRK13634 176 LDpkgRKEMMEMFYKLHK--EKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQ 227
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
27-229 |
5.51e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 63.60 E-value: 5.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 27 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSIlfqgKEIDFHSAKEALENGISMVHQELNLVLQ---- 102
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKV----TVGDIVVSSTSKQKEIKPVRKKVGVVFQfpes 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 103 ----RSVMDNMWLG-------RYPTKGMFVDQDKMYRDTKAIFDELDIDidprarvgtLSVSQMQMIEIAKAFSYDAKIV 171
Cdd:PRK13643 96 qlfeETVLKDVAFGpqnfgipKEKAEKIAAEKLEMVGLADEFWEKSPFE---------LSGGQMRRVAIAGILAMEPEVL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 507082969 172 IMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIA 229
Cdd:PRK13643 167 VLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIIS 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
276-484 |
5.65e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 64.48 E-value: 5.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 276 QPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEAinhgfalvteERRSTGIYAY 355
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAA----------SRRVASVPQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 356 LDIGFNSLISNIQNYKNKVGLLDNSRMKSDTQWVIDSM--RVKTPGHRTQ-IGSLSGGNQQKVVIGRWLLTQPEILMLDE 432
Cdd:PRK09536 86 TSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAmeRTGVAQFADRpVTSLSGGERQRVLLARALAQATPVLLLDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 507082969 433 PTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:PRK09536 166 PTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
266-474 |
6.44e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 62.75 E-value: 6.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 266 LQVRNLTSL--RQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIRE-----KSSGTITLHGKKINNHSAN-EAIN 337
Cdd:PRK14258 8 IKVNNLSFYydTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIYERRVNlNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 338 HGFALVTEERRSTGIYAYLDIGFNSlisNIQNYKNKVGLLD--NSRMKSDTQWviDSMRVKTpgHRTQIgSLSGGNQQKV 415
Cdd:PRK14258 88 RQVSMVHPKPNLFPMSVYDNVAYGV---KIVGWRPKLEIDDivESALKDADLW--DEIKHKI--HKSAL-DLSGGQQQRL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 416 VIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELA-KKDKGIIIISSEMPELLGITD 474
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSD 219
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
281-477 |
6.95e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.44 E-value: 6.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 281 DISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTItlhgkkinNHSANEAINHgfalVTEErrstgiyAYLDIGF 360
Cdd:PRK09544 22 DVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------KRNGKLRIGY----VPQK-------LYLDTTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 361 NSLISNIQNYKNKVglldnsrMKSDTQWVIDsmRVKTpGHRTQ--IGSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGID 438
Cdd:PRK09544 83 PLTVNRFLRLRPGT-------KKEDILPALK--RVQA-GHLIDapMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 507082969 439 VGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRIL 477
Cdd:PRK09544 153 VNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVL 192
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
277-484 |
1.03e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 62.31 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 277 PSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEAINH--GFALVTEERRSTGIYA 354
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKlvGIVFQNPETQFVGRTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 355 YLDIGF---NSLISNIQNYKnkvgLLDnsRMKSDTQwvIDSMRVKTPGhrtqigSLSGGNQQKVVIGRWLLTQPEILMLD 431
Cdd:PRK13644 96 EEDLAFgpeNLCLPPIEIRK----RVD--RALAEIG--LEKYRHRSPK------TLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 507082969 432 EPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPElLGITDRILVMSNGLV 484
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKI 213
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-229 |
1.06e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 62.34 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 11 EYLLEMTGINKSFPGVK--ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEaLEN 88
Cdd:PRK13635 3 EEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWD-VRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 89 GISMVHQEL-NLVLQRSVMDNMWLGrYPTKGmfVDQDKMYRDTKAIFDELDI----DIDPrARvgtLSVSQMQMIEIAKA 163
Cdd:PRK13635 82 QVGMVFQNPdNQFVGATVQDDVAFG-LENIG--VPREEMVERVDQALRQVGMedflNREP-HR---LSGGQKQRVAIAGV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507082969 164 FSYDAKIVIMDEPTSSLTEKEVNHLFTIIRKLK-ERGCGIVYISHKMEEIFQlCDEITVLRDGQWIA 229
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGRREVLETVRQLKeQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILE 220
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
281-482 |
1.24e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 62.79 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 281 DISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANE------------------AINHGFAL 342
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDrkvgfvfqhyalfrhmtvFDNIAFGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 343 VTEERRSTGIYAYLDIGFNSLISNIQnyknkvglLDNSRMKSDTQwvidsmrvktpghrtqigsLSGGNQQKVVIGRWLL 422
Cdd:PRK10851 100 TVLPRRERPNAAAIKAKVTQLLEMVQ--------LAHLADRYPAQ-------------------LSGGQKQRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 507082969 423 TQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGI-IIISSEMPELLGITDRILVMSNG 482
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTsVFVTHDQEEAMEVADRVVVMSQG 213
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
27-209 |
1.29e-10 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 61.98 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 27 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIY-----QKDSGSILFQGKEIdfHSAK---EALENGISMVHQELN 98
Cdd:COG1117 25 QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlipgARVEGEILLDGEDI--YDPDvdvVELRRRVGMVFQKPN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 99 LvLQRSVMDNMWLGrYPTKGMfvdQDKMYRDTK--------AIFDELDIDIDPRArvGTLSVSQMQMIEIAKAFSYDAKI 170
Cdd:COG1117 103 P-FPKSIYDNVAYG-LRLHGI---KSKSELDEIveeslrkaALWDEVKDRLKKSA--LGLSGGQQQRLCIARALAVEPEV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 507082969 171 VIMDEPTSSL----TEKevnhlftI---IRKLKERgCGIVYISHKM 209
Cdd:COG1117 176 LLMDEPTSALdpisTAK-------IeelILELKKD-YTIVIVTHNM 213
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
261-458 |
1.36e-10 |
|
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: 63.53 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 261 PGEVILQVRNLTSLR---QPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGkkINNHSANEAIN 337
Cdd:TIGR02868 330 LGKPTLELRDLSAGYpgaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDG--VPVSSLDQDEV 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 338 HGFALVTEERrstgiyAYL---DIGFNSLISN-------IQNYKNKVGLLDnsrmksdtqWVidsmRVKTPGHRTQIG-- 405
Cdd:TIGR02868 408 RRRVSVCAQD------AHLfdtTVRENLRLARpdatdeeLWAALERVGLAD---------WL----RALPDGLDTVLGeg 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 507082969 406 --SLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEiyqLIAELAKKDKG 458
Cdd:TIGR02868 469 gaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADE---LLEDLLAALSG 520
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
279-485 |
1.41e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 63.53 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 279 IRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKS---SGTITLHGKKINnhsaneainhgfalvteERRSTGIYAY 355
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPID-----------------AKEMRAISAY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 356 L---DIGFNSLisNIQNYKNKVGLLdnsRMKSDT---------QWVIDSMRVKTPGHrTQIG------SLSGGNQQKVVI 417
Cdd:TIGR00955 104 VqqdDLFIPTL--TVREHLMFQAHL---RMPRRVtkkekrervDEVLQALGLRKCAN-TRIGvpgrvkGLSGGERKRLAF 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507082969 418 GRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIII----SSEMPELLgitDRILVMSNGLVA 485
Cdd:TIGR00955 178 ASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTihqpSSELFELF---DKIILMAEGRVA 246
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
281-482 |
1.61e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 61.18 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 281 DISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINnHSANEAINHGFALvteeRRSTG-------IY 353
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFD-FSKTPSDKAIREL----RRNVGmvfqqynLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 354 AYLdigfnSLISNIQNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIgSLSGGNQQKVVIGRWLLTQPEILMLDEP 433
Cdd:PRK11124 95 PHL-----TVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPL-HLSGGQQQRVAIARALMMEPQVLLFDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 507082969 434 TRGIDVGAKFEIYQLIAELAkkDKGI--IIISSEMPELLGITDRILVMSNG 482
Cdd:PRK11124 169 TAALDPEITAQIVSIIRELA--ETGItqVIVTHEVEVARKTASRVVYMENG 217
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
263-482 |
1.78e-10 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 61.59 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 263 EVILQVRNLtSLR---QPSIRDISFDLHKGEILGIAGLVGA-KRT---------DIVETLfgireKSSGTITLHGKKINN 329
Cdd:COG1117 9 EPKIEVRNL-NVYygdKQALKDINLDIPENKVTALIGPSGCgKSTllrclnrmnDLIPGA-----RVEGEILLDGEDIYD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 330 HSANeainhgfalVTEERRSTG------------IY---AYldiGFNslisnIQNYKNK-------------VGLLDNsr 381
Cdd:COG1117 83 PDVD---------VVELRRRVGmvfqkpnpfpksIYdnvAY---GLR-----LHGIKSKseldeiveeslrkAALWDE-- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 382 mksdtqwVIDsmRVKTPGhrtqiGSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIII 461
Cdd:COG1117 144 -------VKD--RLKKSA-----LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL-KKDYTIVI 208
|
250 260
....*....|....*....|.
gi 507082969 462 ISSEMPELLGITDRILVMSNG 482
Cdd:COG1117 209 VTHNMQQAARVSDYTAFFYLG 229
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
21-228 |
1.89e-10 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 60.35 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 21 KSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGI---YQKDSGSILFQGkeidfHSAKEALEngismvhqel 97
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegNVSVEGDIHYNG-----IPYKEFAE---------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 98 nlvlqrsvmdnmwlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPR--ARVGTLSVSQMQMIEIAKAFSYDAKIVIMDE 175
Cdd:cd03233 80 ---------------KYPGEIIYVSEEDVHFPTLTVRETLDFALRCKgnEFVRGISGGERKRVSIAEALVSRASVLCWDN 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 507082969 176 PTSSLTEKEVNHLFTIIRKL--KERGCGIVYISHKMEEIFQLCDEITVLRDGQWI 228
Cdd:cd03233 145 STRGLDSSTALEILKCIRTMadVLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
264-485 |
1.96e-10 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 61.33 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 264 VILQVRNLT-SL-RQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEAINH--- 338
Cdd:PRK13548 1 AMLEARNLSvRLgGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRrav 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 339 -------GFALVTEErrstgiyayldigfnslisniqnyknkV---GLLDNSRMKSDTQWVIDSMRVKTP----GHRtQI 404
Cdd:PRK13548 81 lpqhsslSFPFTVEE---------------------------VvamGRAPHGLSRAEDDALVAAALAQVDlahlAGR-DY 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 405 GSLSGGNQQKVVIGRwLLTQ-------PEILMLDEPTRGIDVGAKFEIYQLIAELAKKDK-GIIIIssempeL--LGIT- 473
Cdd:PRK13548 133 PQLSGGEQQRVQLAR-VLAQlwepdgpPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGlAVIVV------LhdLNLAa 205
|
250
....*....|....*.
gi 507082969 474 ---DRILVMSNG-LVA 485
Cdd:PRK13548 206 ryaDRIVLLHQGrLVA 221
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
277-484 |
2.00e-10 |
|
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: 60.95 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 277 PSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSaNEAINHGFALVTEERRSTGiyayl 356
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE-HKYLHSKVSLVGQEPVLFA----- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 357 digfNSLISNIqnyknKVGLLDNSRM-------KSDTQWVIDSMRvktPGHRTQIGS----LSGGNQQKVVIGRWLLTQP 425
Cdd:cd03248 102 ----RSLQDNI-----AYGLQSCSFEcvkeaaqKAHAHSFISELA---SGYDTEVGEkgsqLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 507082969 426 EILMLDEPTRGIDVGAKFEIYQLIAElAKKDKGIIIISSEMpELLGITDRILVMSNGLV 484
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQALYD-WPERRTVLVIAHRL-STVERADQILVLDGGRI 226
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
275-500 |
2.05e-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: 61.16 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 275 RQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSaneainhgfalVTEERRSTGiYA 354
Cdd:cd03295 13 GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQD-----------PVELRRKIG-YV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 355 YLDIGFNSLISNIQNYKNKVGLLDNSRMKSDTqwvidsmRVKT--------PGHRTQ--IGSLSGGNQQKVVIGRWLLTQ 424
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRE-------RADEllalvgldPAEFADryPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507082969 425 PEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVAgIVDTKtttqNEILR 500
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIV-QVGTP----DEILR 225
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
29-225 |
2.43e-10 |
|
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: 59.95 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGiyQKDSGSIlfqgkeidfhsakealENGISMVHQELNLVLQRSVmdn 108
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVI----------------TGEILINGRPLDKNFQRST--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 109 mwlgryptkgMFVDQDKMYRDTKAIFDELDIDIDPRArvgtLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHL 188
Cdd:cd03232 82 ----------GYVEQQDVHSPNLTVREALRFSALLRG----LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNI 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 507082969 189 FTIIRKLKERGCGIV-YISHKMEEIFQLCDEITVLRDG 225
Cdd:cd03232 148 VRFLKKLADSGQAILcTIHQPSASIFEKFDRLLLLKRG 185
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
26-225 |
2.70e-10 |
|
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: 60.36 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 26 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKD---SGSILFQGKEIDFHSAKEAlengISMVHQELNLVLQ 102
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPDQFQKC----VAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 103 RSV------MDNMWLGRYPTKGmfvdQDKMYRDTKAIFDELDIDIDpRARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEP 176
Cdd:cd03234 96 LTVretltyTAILRLPRKSSDA----IRKKRVEDVLLRDLALTRIG-GNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 507082969 177 TSSLTEKEVNHLFTIIRKLKERGCGIVYISHK-MEEIFQLCDEITVLRDG 225
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLARRNRIVILTIHQpRSDLFRLFDRILLLSSG 220
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
279-485 |
3.18e-10 |
|
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: 60.19 E-value: 3.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 279 IRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGkkinnhsaneainHGFALVTEE--RRSTGIYAYL 356
Cdd:cd03252 18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDG-------------HDLALADPAwlRRQVGVVLQE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 357 DIGFN-SLISNIQnyknkvglLDNSRMksDTQWVIDSMRV--------KTP-GHRTQIG----SLSGGNQQKVVIGRWLL 422
Cdd:cd03252 85 NVLFNrSIRDNIA--------LADPGM--SMERVIEAAKLagahdfisELPeGYDTIVGeqgaGLSGGQRQRIAIARALI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507082969 423 TQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIIISSEMPELLGiTDRILVMSNGLVA 485
Cdd:cd03252 155 HNPRILIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIV 215
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
277-484 |
3.49e-10 |
|
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: 59.73 E-value: 3.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 277 PSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEainhgfalVTEERRSTGIyAYL 356
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRA--------IPYLRRKIGV-VFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 357 DigfNSLISNIQNYKN---------KVGLLDNSRMKSDTQWVIDSMRvktpgHRTQIGSLSGGNQQKVVIGRWLLTQPEI 427
Cdd:cd03292 86 D---FRLLPDRNVYENvafalevtgVPPREIRKRVPAALELVGLSHK-----HRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 507082969 428 LMLDEPTRGIDVGAKFEIYQLIAELAKKDKgIIIISSEMPELLGITD-RILVMSNGLV 484
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKINKAGT-TVVVATHAKELVDTTRhRVIALERGKL 214
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
263-496 |
3.94e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 60.17 E-value: 3.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 263 EVILQVRNLTSL--RQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIRE-----KSSGTITLHGKKINNHSANEA 335
Cdd:PRK14239 3 EPILQVSDLSVYynKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSPRTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 336 -INHGFALVTEERRSTGIYAYLDIGFNSLISNIqnyKNKvGLLDNSRMKSDTQWVIDSmRVKTPGHRTQIGsLSGGNQQK 414
Cdd:PRK14239 83 dLRKEIGMVFQQPNPFPMSIYENVVYGLRLKGI---KDK-QVLDEAVEKSLKGASIWD-EVKDRLHDSALG-LSGGQQQR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 415 VVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTKTTT 494
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMF 235
|
..
gi 507082969 495 QN 496
Cdd:PRK14239 236 MN 237
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
29-235 |
4.05e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 59.83 E-value: 4.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHS--AKEALENG-ISMVHQELNLVLQRSV 105
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaAKAELRNQkLGFIYQFHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 106 MDNMWL-----GRYPTKGmfvdQDKMYRDTKAIfdeldiDIDPRA--RVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTS 178
Cdd:PRK11629 105 LENVAMplligKKKPAEI----NSRALEMLAAV------GLEHRAnhRPSELSGGERQRVAIARALVNNPRLVLADEPTG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 507082969 179 SLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITvLRDGQWIATQPLEG 235
Cdd:PRK11629 175 NLDARNADSIFQLLGELNRLqGTAFLVVTHDLQLAKRMSRQLE-MRDGRLTAELSLMG 231
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
266-497 |
4.19e-10 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 59.77 E-value: 4.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 266 LQVRNLTSLRQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKkinNHSANEAINHGFALVTE 345
Cdd:COG3840 2 LRLDDLTYRYGDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQ---DLTALPPAERPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 346 ErrstgiyayldigfNSLISNIQNYKNkVGLLDNSRMK-SDTQWVidsmRVKTPGHRTQI--------GSLSGGNQQKVV 416
Cdd:COG3840 79 E--------------NNLFPHLTVAQN-IGLGLRPGLKlTAEQRA----QVEQALERVGLaglldrlpGQLSGGQRQRVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 417 IGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPE-LLGITDRILVMSNGLVAGIVDTKTTTQ 495
Cdd:COG3840 140 LARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEdAARIADRVLLVADGRIAADGPTAALLD 219
|
..
gi 507082969 496 NE 497
Cdd:COG3840 220 GE 221
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
29-226 |
4.64e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 60.52 E-value: 4.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEaLENGISMVHQEL-NLVLQRSVMD 107
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWD-IRHKIGMVFQNPdNQFVGATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 108 NMWLGrYPTKGM-FVDQDKMYRDTKAIFDELDIDIDPRARvgtLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVN 186
Cdd:PRK13650 102 DVAFG-LENKGIpHEEMKERVNEALELVGMQDFKEREPAR---LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 507082969 187 HLFTIIRKLKER-GCGIVYISHKMEEIfQLCDEITVLRDGQ 226
Cdd:PRK13650 178 ELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQ 217
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
26-236 |
4.75e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 60.97 E-value: 4.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 26 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIyQKDSGSIL---FQGKEIDF-----HSAKEALENGISMVHQEL 97
Cdd:PRK15093 20 VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTadrMRFDDIDLlrlspRERRKLVGHNVSMIFQEP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 98 NLVLQ------RSVMDNM----WLGRYPtkgmfvdQDKMYRDTKAIfdEL--DIDI-DPRARVGT----LSVSQMQMIEI 160
Cdd:PRK15093 99 QSCLDpservgRQLMQNIpgwtYKGRWW-------QRFGWRKRRAI--ELlhRVGIkDHKDAMRSfpyeLTEGECQKVMI 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507082969 161 AKAFSYDAKIVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITVLRDGQWIATQPLEGL 236
Cdd:PRK15093 170 AIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKEL 246
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
14-238 |
4.99e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 60.08 E-value: 4.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILfqGKEIDFHSAKEalenGISMV 93
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL--AGTAPLAEARE----DTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 94 HQELNLVLQRSVMDNMWLGrypTKGmfvdqdkMYRDtkAIFDELD-IDIDPRAR--VGTLSVSQMQMIEIAKAFSYDAKI 170
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGLG---LKG-------QWRD--AALQALAaVGLADRANewPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 507082969 171 VIMDEP---TSSLTEKEVNHLftIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWiatqpleGLDM 238
Cdd:PRK11247 155 LLLDEPlgaLDALTRIEMQDL--IESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI-------GLDL 216
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
266-484 |
5.47e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 59.76 E-value: 5.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 266 LQVRNLTSL--RQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINnhsANEAINHGFALV 343
Cdd:PRK11264 4 IEVKNLVKKfhGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITID---TARSLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 344 TEERRSTGiyaYLDIGFN-----SLISNIqnYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGS-LSGGNQQKVVI 417
Cdd:PRK11264 81 RQLRQHVG---FVFQNFNlfphrTVLENI--IEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRrLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507082969 418 GRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
265-482 |
6.98e-10 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 60.50 E-value: 6.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 265 ILQVRNLTsLR---QPSIRDISFDLHKGEI---LG------------IAGLvgakrtdivETLfgirekSSGTITLHGKK 326
Cdd:COG3842 5 ALELENVS-KRygdVTALDDVSLSIEPGEFvalLGpsgcgkttllrmIAGF---------ETP------DSGRILLDGRD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 327 INNhsaneainhgfalVTEERRSTGI----YA---YLD----IGFnslisniqnyknkvGL----LDNSRMKSDTQWVID 391
Cdd:COG3842 69 VTG-------------LPPEKRNVGMvfqdYAlfpHLTvaenVAF--------------GLrmrgVPKAEIRARVAELLE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 392 SMRVKTPGHRtQIGSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKdkgiiiissempelLG 471
Cdd:COG3842 122 LVGLEGLADR-YPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRE--------------LG 186
|
250 260
....*....|....*....|....*.
gi 507082969 472 IT---------------DRILVMSNG 482
Cdd:COG3842 187 ITfiyvthdqeealalaDRIAVMNDG 212
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
259-482 |
7.57e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 59.06 E-value: 7.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 259 NKPgevILQVRNLTSLRQPS------IRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSA 332
Cdd:PRK11629 2 NKI---LLQCDNLCKRYQEGsvqtdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 333 N---EAINH--GFalvteerrstgIYAyldigFNSLISNIQNYKNKVG--LLDNSRMKSDTQWVIDSMRVKTPGHRTQ-- 403
Cdd:PRK11629 79 AakaELRNQklGF-----------IYQ-----FHHLLPDFTALENVAMplLIGKKKPAEINSRALEMLAAVGLEHRANhr 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507082969 404 IGSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK11629 143 PSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDG 221
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
9-258 |
8.72e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 60.43 E-value: 8.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 9 SGEYLLEMTGINKsfpGVKaldNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALE- 87
Cdd:PRK10070 30 SKEQILEKTGLSL---GVK---DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 88 --NGISMVHQELNLVLQRSVMDNMWLGrYPTKGMFVDQdkmyRDTKAI--FDELDIDIDPRARVGTLSVSQMQMIEIAKA 163
Cdd:PRK10070 104 rrKKIAMVFQSFALMPHMTVLDNTAFG-MELAGINAEE----RREKALdaLRQVGLENYAHSYPDELSGGMRQRVGLARA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 164 FSYDAKIVIMDEPTSS---LTEKEVNHLFTIIRKLKERgcGIVYISHKMEEIFQLCDEITVLRDGQWIAT-QPLEGLD-- 237
Cdd:PRK10070 179 LAINPDILLMDEAFSAldpLIRTEMQDELVKLQAKHQR--TIVFISHDLDEAMRIGDRIAIMQNGEVVQVgTPDEILNnp 256
|
250 260
....*....|....*....|..
gi 507082969 238 -MDKIISMMVGRSLNQRFPDKE 258
Cdd:PRK10070 257 aNDYVRTFFRGVDISQVFSAKD 278
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
13-208 |
9.14e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.42 E-value: 9.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfhsakealeNGISM 92
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK---------KDLCT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 93 VHQELNLVLQRSVMD-NMWLgryptkgmfvdQDKMYRDTKaiFDELDIDIDPRARV-----------GTLSVSQMQMIEI 160
Cdd:PRK13540 72 YQKQLCFVGHRSGINpYLTL-----------RENCLYDIH--FSPGAVGITELCRLfslehlidypcGLLSSGQKRQVAL 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 507082969 161 AKAFSYDAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHK 208
Cdd:PRK13540 139 LRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
27-222 |
9.25e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 60.11 E-value: 9.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 27 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKE--ALENGISMVHQE----LNlv 100
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEwrAVRSDIQMIFQDplasLN-- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 101 lqrsvmDNMWLGRYPTKGMFVDQDKMYRDT-----KAIFdeldididprARVGTL-----------SVSQMQMIEIAKAF 164
Cdd:PRK15079 113 ------PRMTIGEIIAEPLRTYHPKLSRQEvkdrvKAMM----------LKVGLLpnlinryphefSGGQCQRIGIARAL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 507082969 165 SYDAKIVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITVL 222
Cdd:PRK15079 177 ILEPKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVM 235
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
279-499 |
9.61e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 60.43 E-value: 9.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 279 IRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHG---KKINNHSANEAINHGFALVTEERRSTGIYAY 355
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELREVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 356 LD-IGFNSLISNIQNYKNKVGLLDNSRmksdtQWVIDSMRVKTPGHrtqigsLSGGNQQKVVIGRWLLTQPEILMLDEPT 434
Cdd:PRK10070 124 LDnTAFGMELAGINAEERREKALDALR-----QVGLENYAHSYPDE------LSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507082969 435 RGIDVGAKFEIYQLIAEL-AKKDKGIIIISSEMPELLGITDRILVMSNGLVagivdTKTTTQNEIL 499
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV-----VQVGTPDEIL 253
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
33-226 |
9.83e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 58.83 E-value: 9.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 33 NLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEidfHSAKEALENGISMVHQELNLVLQRSVMDNMWLG 112
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD---HTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 113 RYPTKGMFVDQDKMYRDtkaIFDELDIDiDPRARV-GTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFTI 191
Cdd:PRK10771 96 LNPGLKLNAAQREKLHA---IARQMGIE-DLLARLpGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTL 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 507082969 192 IRKL-KERGCGIVYISHKMEEIFQLCDEITVLRDGQ 226
Cdd:PRK10771 172 VSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGR 207
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
10-207 |
9.90e-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: 60.72 E-value: 9.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 10 GEYLLEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFqGKEIDFHS---AKEAL 86
Cdd:TIGR03719 319 GDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLAYvdqSRDAL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 87 ENGISmVHQELN------LVLQRSVMDNMWLGRYPTKGmfVDQDKmyrdtkaifdeldididpraRVGTLSVSQMQMIEI 160
Cdd:TIGR03719 398 DPNKT-VWEEISggldiiKLGKREIPSRAYVGRFNFKG--SDQQK--------------------KVGQLSGGERNRVHL 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 507082969 161 AKAFSYDAKIVIMDEPTSSLtekEVNHLftiiRKLKER-----GCGIVyISH 207
Cdd:TIGR03719 455 AKTLKSGGNVLLLDEPTNDL---DVETL----RALEEAllnfaGCAVV-ISH 498
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
279-487 |
1.17e-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: 58.63 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 279 IRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEAInhgfalVTEErrstgiYAYLdi 358
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV------VFQN------YSLL-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 359 gfnSLISNIQNYKNKVGLLDNSRMKSDTQWVID---SMRVKTPGHRTQIGSLSGGNQQKVVIGRWLLTQPEILMLDEPTR 435
Cdd:TIGR01184 67 ---PWLTVRENIALAVDRVLPDLSKSERRAIVEehiALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFG 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 507082969 436 GIDVGAKFEIYQLIAELAKKDK-GIIIISSEMPELLGITDRILVMSNGLVAGI 487
Cdd:TIGR01184 144 ALDALTRGNLQEELMQIWEEHRvTVLMVTHDVDEALLLSDRVVMLTNGPAANI 196
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
266-482 |
1.46e-09 |
|
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: 60.50 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 266 LQVRNLT----SLRQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEAINHgFA 341
Cdd:TIGR02203 331 VEFRNVTfrypGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQ-VA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 342 LVTEErrstgiyAYLdigFNSLISNIQNYkNKVGLLDNSRMKS-----DTQWVIDSMrvktP-GHRTQIGS----LSGGN 411
Cdd:TIGR02203 410 LVSQD-------VVL---FNDTIANNIAY-GRTEQADRAEIERalaaaYAQDFVDKL----PlGLDTPIGEngvlLSGGQ 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507082969 412 QQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISsempELLGI--TDRILVMSNG 482
Cdd:TIGR02203 475 RQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAH----RLSTIekADRIVVMDDG 543
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
29-207 |
1.53e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.05 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSakealengismvhqelnlvlQRSVMDN 108
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGR--------------------EASLIDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 109 MWLGRYPTKGMFVDQDKMYRDTKAIfdeldididpRARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSL---TEKEV 185
Cdd:COG2401 106 IGRKGDFKDAVELLNAVGLSDAVLW----------LRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLdrqTAKRV 175
|
170 180
....*....|....*....|...
gi 507082969 186 NHlftIIRKL-KERGCGIVYISH 207
Cdd:COG2401 176 AR---NLQKLaRRAGITLVVATH 195
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
14-70 |
1.55e-09 |
|
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: 56.30 E-value: 1.55e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 507082969 14 LEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSI 70
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV 57
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
407-481 |
1.61e-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: 56.78 E-value: 1.61e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507082969 407 LSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIaelakKDKGIIIIS-SEMPELLGITDRILVMSN 481
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL-----KELGITVISvGHRPSLWKFHDRVLDLDG 162
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
24-226 |
1.67e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 60.76 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 24 PGVK-ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfhsakeaLENGISMVHQELNLVLQ 102
Cdd:PLN03232 1246 PGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDV--------AKFGLTDLRRVLSIIPQ 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 103 RSVMDNmwlgryPTKGMFVDQDKMYRDT-----------KAIFDELDIDIDPRARVG--TLSVSQMQMIEIAKAFSYDAK 169
Cdd:PLN03232 1318 SPVLFS------GTVRFNIDPFSEHNDAdlwealerahiKDVIDRNPFGLDAEVSEGgeNFSVGQRQLLSLARALLRRSK 1391
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 507082969 170 IVIMDEPTSSLtekEVNHLFTIIRKLKE--RGCGIVYISHKMEEIFQlCDEITVLRDGQ 226
Cdd:PLN03232 1392 ILVLDEATASV---DVRTDSLIQRTIREefKSCTMLVIAHRLNTIID-CDKILVLSSGQ 1446
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
13-232 |
1.70e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 60.12 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSFPG----VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfhsakeALEN 88
Cdd:PRK10535 4 LLELKDIRRSYPSgeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVA------TLDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 89 G---------ISMVHQELNLVLQRSVMDNMwlgryPTKGMFVDQDKMYRDTKAIFDELDIDIDPRA--RVGTLSVSQMQM 157
Cdd:PRK10535 78 DalaqlrrehFGFIFQRYHLLSHLTAAQNV-----EVPAVYAGLERKQRLLRAQELLQRLGLEDRVeyQPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507082969 158 IEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKmEEIFQLCDEITVLRDGQWIATQP 232
Cdd:PRK10535 153 VSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIVRNPP 226
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
266-482 |
1.71e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 60.03 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 266 LQVRNLT----SLRQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEAINHgFA 341
Cdd:PRK11176 342 IEFRNVTftypGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQ-VA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 342 LVTEErrstgiyAYLdigFNSLISNIQNYK-----NKVGLLDNSRMKSDTQWvIDSMRvktPGHRTQIG----SLSGGNQ 412
Cdd:PRK11176 421 LVSQN-------VHL---FNDTIANNIAYArteqySREQIEEAARMAYAMDF-INKMD---NGLDTVIGengvLLSGGQR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 413 QKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIIISSEMPELLGiTDRILVMSNG 482
Cdd:PRK11176 487 QRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEK-ADEILVVEDG 554
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
266-480 |
1.76e-09 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 58.33 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 266 LQVRNLtSLR-------QPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEAI-- 336
Cdd:COG4525 4 LTVRHV-SVRypgggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGVvf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 337 -------------NHGFAL----VTEERRSTGIYAYLDigfnslisniqnyknKVGLLDNsrmksdtqwvidsmrvktpg 399
Cdd:COG4525 83 qkdallpwlnvldNVAFGLrlrgVPKAERRARAEELLA---------------LVGLADF-------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 400 HRTQIGSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKDKGIIIISSEMPELLGITDRILV 478
Cdd:COG4525 128 ARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEALFLATRLVV 207
|
..
gi 507082969 479 MS 480
Cdd:COG4525 208 MS 209
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
315-499 |
1.86e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.43 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 315 KSSGTITLHGKKINNHSANEAINHgFALVTEERRSTGIYAYLDIGFNSLISNIQNYKN--KVGLLDNsrmksdtqwVIDS 392
Cdd:PTZ00265 1274 KNSGKILLDGVDICDYNLKDLRNL-FSIVSQEPMLFNMSIYENIKFGKEDATREDVKRacKFAAIDE---------FIES 1343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 393 MRVKtpgHRTQIG----SLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMP 467
Cdd:PTZ00265 1344 LPNK---YDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKaDKTIITIAHRIA 1420
|
170 180 190
....*....|....*....|....*....|..
gi 507082969 468 ElLGITDRILVMSNGLVAGIVDTKTTTQNEIL 499
Cdd:PTZ00265 1421 S-IKRSDKIVVFNNPDRTGSFVQAHGTHEELL 1451
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
26-230 |
1.93e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 59.09 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 26 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSI----LFQGKEIDFHSAKEA-----------LENGI 90
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELITNpyskkiknfkeLRRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 91 SMVHQ--ELNL---VLQRSVMdnmwlgrYPTKGMFVDQDKMYRDTKAIFDELDIDID--PRARVGtLSVSQMQMIEIAKA 163
Cdd:PRK13631 119 SMVFQfpEYQLfkdTIEKDIM-------FGPVALGVKKSEAKKLAKFYLNKMGLDDSylERSPFG-LSGGQKRRVAIAGI 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507082969 164 FSYDAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIAT 230
Cdd:PRK13631 191 LAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKT 257
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-268 |
1.95e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.51 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGiyQKDSGSILFQGKEIDFHSAKEALENGISMVHQELNLVLQRSVMDN 108
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVITGGDRLVNGRPLDSSFQRSIGYVQQQDLHLPTSTVRES 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 109 MWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRARVGT----LSVSQMQMIEIAKAFSYDAK-IVIMDEPTSSLTEK 183
Cdd:TIGR00956 857 LRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVpgegLNVEQRKRLTIGVELVAKPKlLLFLDEPTSGLDSQ 936
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 184 EVNHLFTIIRKLKERGCGIVYISHKME-EIFQLCDEITVL-RDGQWIATQPLeGLDMDKIISMMvGRSLNQRFPDKENkP 261
Cdd:TIGR00956 937 TAWSICKLMRKLADHGQAILCTIHQPSaILFEEFDRLLLLqKGGQTVYFGDL-GENSHTIINYF-EKHGAPKCPEDAN-P 1013
|
....*..
gi 507082969 262 GEVILQV 268
Cdd:TIGR00956 1014 AEWMLEV 1020
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
277-482 |
2.03e-09 |
|
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: 58.01 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 277 PSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEAINHgFALVTEErrsTGIYAyl 356
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM-IGVVLQD---TFLFS-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 357 digfNSLISNIqnyknKVGLLDNSrmksDTQWVIDSMRV-------KTP-GHRTQIG----SLSGGNQQKVVIGRWLLTQ 424
Cdd:cd03254 91 ----GTIMENI-----RLGRPNAT----DEEVIEAAKEAgahdfimKLPnGYDTVLGenggNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 507082969 425 PEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIIISSEMPELLGiTDRILVMSNG 482
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKN-ADKILVLDDG 213
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
250-482 |
2.26e-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: 60.41 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 250 LNQRFPDKENkPGEVI-LQVRNLTSLRQPSIR------DISFdlHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITL 322
Cdd:TIGR01257 913 INDSFFEREL-PGLVPgVCVKNLVKIFEPSGRpavdrlNITF--YENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLV 989
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 323 HGKKInnHSANEAInhgfalvteeRRSTGIYAYLDIGFNSLI--SNIQNYKNKVGlldnsRMKSDTQWVIDSMRVKTPGH 400
Cdd:TIGR01257 990 GGKDI--ETNLDAV----------RQSLGMCPQHNILFHHLTvaEHILFYAQLKG-----RSWEEAQLEMEAMLEDTGLH 1052
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 401 RT---QIGSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIIISSEMPELLGITDRIL 477
Cdd:TIGR01257 1053 HKrneEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIA 1131
|
....*
gi 507082969 478 VMSNG 482
Cdd:TIGR01257 1132 IISQG 1136
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-232 |
2.30e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 59.87 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 6 TQSSGEYLLEMTGINKSFP-----------GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG 74
Cdd:PRK10261 306 TVVDGEPILQVRNLVTRFPlrsgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 75 KEIDFHSAK--EALENGISMVHQELNLVLQ------RSVMDnmwlgryPTKGMFVDQDKMYRDTKAIFDEldididpraR 146
Cdd:PRK10261 386 QRIDTLSPGklQALRRDIQFIFQDPYASLDprqtvgDSIME-------PLRVHGLLPGKAAAARVAWLLE---------R 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 147 VGTL-----------SVSQMQMIEIAKAFSYDAKIVIMDEPTSSLtekEVNHLFTIIRKL----KERGCGIVYISHKMEE 211
Cdd:PRK10261 450 VGLLpehawryphefSGGQRQRICIARALALNPKVIIADEAVSAL---DVSIRGQIINLLldlqRDFGIAYLFISHDMAV 526
|
250 260
....*....|....*....|.
gi 507082969 212 IFQLCDEITVLRDGQWIATQP 232
Cdd:PRK10261 527 VERISHRVAVMYLGQIVEIGP 547
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
44-207 |
2.43e-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: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 44 LMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEAlENGISMVHQE-LNLVLqrSVMDNM-WLGRyptkgmfv 121
Cdd:cd03231 31 VTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIA-RGLLYLGHAPgIKTTL--SVLENLrFWHA-------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 122 dqdkmYRDTKAIFDELDiDIDPRA----RVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFTIIRKLKE 197
Cdd:cd03231 100 -----DHSDEQVEEALA-RVGLNGfedrPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCA 173
|
170
....*....|
gi 507082969 198 RGCGIVYISH 207
Cdd:cd03231 174 RGGMVVLTTH 183
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
253-482 |
2.47e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 59.45 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 253 RFPDKEN-KPGEVILQVRNLT----SLRQPSIRDISFDLHKGEILGIAGLVGAKRTdiveTLFGI--RE--KSSGTITLH 323
Cdd:PRK11160 325 TFPTTSTaAADQVSLTLNNVSftypDQPQPVLKGLSLQIKAGEKVALLGRTGCGKS----TLLQLltRAwdPQQGEILLN 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 324 GKKINNHSaNEAINHGFALVTEErrstgiyayLDIGFNSLISNIQNYK------------NKVGL---LDNSrmKSDTQW 388
Cdd:PRK11160 401 GQPIADYS-EAALRQAISVVSQR---------VHLFSATLRDNLLLAApnasdealievlQQVGLeklLEDD--KGLNAW 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 389 VIDsmrvktpGHRTqigsLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIIISSempE 468
Cdd:PRK11160 469 LGE-------GGRQ----LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITH---R 533
|
250
....*....|....*.
gi 507082969 469 LLGIT--DRILVMSNG 482
Cdd:PRK11160 534 LTGLEqfDRICVMDNG 549
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
265-485 |
2.54e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 58.10 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 265 ILQVRNLTSL--RQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEAINHgFAL 342
Cdd:PRK11231 2 TLRTENLTVGygTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARR-LAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 343 -----VTEErrstgiyaylDIGFNSLISNIQN-YKNKVGlldnsRMKSDtqwviDSMRVKTPGHRTQI--------GSLS 408
Cdd:PRK11231 81 lpqhhLTPE----------GITVRELVAYGRSpWLSLWG-----RLSAE-----DNARVNQAMEQTRInhladrrlTDLS 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507082969 409 GGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG-LVA 485
Cdd:PRK11231 141 GGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGhVMA 218
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
256-482 |
2.91e-09 |
|
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: 59.92 E-value: 2.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 256 DKENKP--GEVILQVRNLTSLRQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITlHGKKINNHSAN 333
Cdd:TIGR01271 417 NKARKQpnGDDGLFFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK-HSGRISFSPQT 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 334 EAINHG-------FALVTEERRSTGIyayldIGFNSLISNIQNYKNKvglldnsrmksdtqwvidsmrVKTPGHRTQIgS 406
Cdd:TIGR01271 496 SWIMPGtikdniiFGLSYDEYRYTSV-----IKACQLEEDIALFPEK---------------------DKTVLGEGGI-T 548
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507082969 407 LSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQ--LIAELAKKDKgiIIISSEMpELLGITDRILVMSNG 482
Cdd:TIGR01271 549 LSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFEscLCKLMSNKTR--ILVTSKL-EHLKKADKILLLHEG 623
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
279-482 |
2.97e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 57.75 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 279 IRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIRE------KSSGTITLHGKKINNHSANEAINHGFALVTEERRSTGI 352
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 353 YAYLDIGFNSLISNIQNYKNKVGLLDNSrMKSDTQWVIDSMRVKTPGHRtqigsLSGGNQQKVVIGRWLLTQPEILMLDE 432
Cdd:PRK14246 106 SIYDNIAYPLKSHGIKEKREIKKIVEEC-LRKVGLWKEVYDRLNSPASQ-----LSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 507082969 433 PTRGIDVGAKFEIYQLIAELaKKDKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITEL-KNEIAIVIVSHNPQQVARVADYVAFLYNG 228
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
250-482 |
3.14e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 58.69 E-value: 3.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 250 LNQRFPDKENKPGEV---ILQVRNLTSL--RQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHG 324
Cdd:PRK11607 1 MNDAIPRPQAKTRKAltpLLEIRNLTKSfdGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 325 KKINNHSA-NEAINHGFalvteerRSTGIYAYLDIGFNSLISNIQNYKNKVGLldNSRMKSDTQWVIDSMRVKTPGHRtq 403
Cdd:PRK11607 81 VDLSHVPPyQRPINMMF-------QSYALFPHMTVEQNIAFGLKQDKLPKAEI--ASRVNEMLGLVHMQEFAKRKPHQ-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 404 igsLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEI-YQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK11607 150 ---LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRG 226
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
266-482 |
4.08e-09 |
|
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: 56.32 E-value: 4.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 266 LQVRNLT-------SLRQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGkkinnhsaneainh 338
Cdd:cd03250 1 ISVEDASftwdsgeQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 339 GFALVTEErrstgiyAYLdigFN-SLISNI--------QNYKnKVglLDNSRMKSDtqwvIDSMrvkTPGHRTQIG---- 405
Cdd:cd03250 67 SIAYVSQE-------PWI---QNgTIRENIlfgkpfdeERYE-KV--IKACALEPD----LEIL---PDGDLTEIGekgi 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 406 SLSGGNQQKVVIGRWLLTQPEILMLDEPTRGID--VGAK-FEiyQLIAELAKKDKGIIIISSEMpELLGITDRILVMSNG 482
Cdd:cd03250 127 NLSGGQKQRISLARAVYSDADIYLLDDPLSAVDahVGRHiFE--NCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNG 203
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
407-482 |
4.17e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 57.87 E-value: 4.17e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507082969 407 LSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELA-KKDKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK13646 146 MSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEG 222
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
263-474 |
4.23e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 57.48 E-value: 4.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 263 EVILQVRNLTSL--RQPSIRDISFDLHKGEILGIAGLVG-AKRT---------DIVETLfgireKSSGTITLHGKKINNH 330
Cdd:PRK14243 8 ETVLRTENLNVYygSFLAVKNVWLDIPKNQITAFIGPSGcGKSTilrcfnrlnDLIPGF-----RVEGKVTFHGKNLYAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 331 SANEAinhgfalvtEERRSTGIY----------AYLDIGFNSlisNIQNYKNKVGLLDNSRMKSDTQW--VIDSMRvktp 398
Cdd:PRK14243 83 DVDPV---------EVRRRIGMVfqkpnpfpksIYDNIAYGA---RINGYKGDMDELVERSLRQAALWdeVKDKLK---- 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507082969 399 ghrtQIG-SLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIIISSEMPELLGITD 474
Cdd:PRK14243 147 ----QSGlSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL-KEQYTIIIVTHNMQQAARVSD 218
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
280-484 |
4.32e-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: 56.93 E-value: 4.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 280 RDISFDLHKGEILGIAGLVGAKRTdiveTLfgIR------EKSSGTITLHGKKINNHSANeaINH-----GF-------- 340
Cdd:COG1126 18 KGISLDVEKGEVVVIIGPSGSGKS----TL--LRcinlleEPDSGTITVDGEDLTDSKKD--INKlrrkvGMvfqqfnlf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 341 -----------ALVT------EERRSTGIyAYLDigfnslisniqnyknKVGLLDnsrmKSDtqwvidsmrvKTPGhrtq 403
Cdd:COG1126 90 phltvlenvtlAPIKvkkmskAEAEERAM-ELLE---------------RVGLAD----KAD----------AYPA---- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 404 igSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGID---VGakfEIYQLIAELAKKDKGIIIISSEMpellG----ITDRI 476
Cdd:COG1126 136 --QLSGGQQQRVAIARALAMEPKVMLFDEPTSALDpelVG---EVLDVMRDLAKEGMTMVVVTHEM----GfareVADRV 206
|
....*...
gi 507082969 477 LVMSNGLV 484
Cdd:COG1126 207 VFMDGGRI 214
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
407-500 |
4.67e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 57.72 E-value: 4.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 407 LSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAK-KDKGIIIISSEMPELLGITDRILVMSNGLVA 485
Cdd:PRK13634 146 LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTHSMEDAARYADQIVVMHKGTVF 225
|
90
....*....|....*
gi 507082969 486 givdtKTTTQNEILR 500
Cdd:PRK13634 226 -----LQGTPREIFA 235
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
277-484 |
4.73e-09 |
|
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: 58.98 E-value: 4.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 277 PSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINN---HSANEAINHgfaLVTEERRSTGiy 353
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDidrHTLRQFINY---LPQEPYIFSG-- 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 354 AYLDigfNSLISNIQNYKNK--VGLLDNSRMKSDtqwvIDSMRVktpGHRTQI----GSLSGGNQQKVVIGRWLLTQPEI 427
Cdd:TIGR01193 563 SILE---NLLLGAKENVSQDeiWAACEIAEIKDD----IENMPL---GYQTELseegSSISGGQKQRIALARALLTDSKV 632
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 507082969 428 LMLDEPTRGIDVGAKFEIYQLIAELakKDKGIIIISSEMpELLGITDRILVMSNGLV 484
Cdd:TIGR01193 633 LILDESTSNLDTITEKKIVNNLLNL--QDKTIIFVAHRL-SVAKQSDKIIVLDHGKI 686
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
265-484 |
5.11e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 57.43 E-value: 5.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 265 ILQVRNLT-----SLRQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEaINHG 339
Cdd:PRK13650 4 IIEVKNLTfkykeDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWD-IRHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 340 FALVTE--ERRSTGIYAYLDIGF---------NSLISNIQNYKNKVGLLDnsrmksdtqwvidsMRVKTPGHrtqigsLS 408
Cdd:PRK13650 83 IGMVFQnpDNQFVGATVEDDVAFglenkgiphEEMKERVNEALELVGMQD--------------FKEREPAR------LS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507082969 409 GGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIIIS--SEMPElLGITDRILVMSNGLV 484
Cdd:PRK13650 143 GGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGI-RDDYQMTVISitHDLDE-VALSDRVLVMKNGQV 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
29-226 |
5.47e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 56.71 E-value: 5.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGK---EIDFHSAKEALENGISMVHQELNLVLQRSV 105
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQplhQMDEEARAKLRAKHVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 106 MDNMWLgryPT--KGMFVDQDKmyRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLT-- 181
Cdd:PRK10584 106 LENVEL---PAllRGESSRQSR--NGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDrq 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 507082969 182 --EKEVNHLFTIIRklkERGCGIVYISHKmEEIFQLCDEITVLRDGQ 226
Cdd:PRK10584 181 tgDKIADLLFSLNR---EHGTTLILVTHD-LQLAARCDRRLRLVNGQ 223
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
275-484 |
5.91e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 58.43 E-value: 5.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 275 RQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSAnEAINHGFALVTEErrstgiyA 354
Cdd:PRK13657 347 SRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTR-ASLRRNIAVVFQD-------A 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 355 YLdigFNSLIS-NIQnyknkVGLLDNS----RMKSDTQWVIDSMRVKTPGHRTQIG----SLSGGNQQKVVIGRWLLTQP 425
Cdd:PRK13657 419 GL---FNRSIEdNIR-----VGRPDATdeemRAAAERAQAHDFIERKPDGYDTVVGergrQLSGGERQRLAIARALLKDP 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 507082969 426 EILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIIISSEMPELLGiTDRILVMSNGLV 484
Cdd:PRK13657 491 PILILDEATSALDVETEAKVKAALDEL-MKGRTTFIIAHRLSTVRN-ADRILVFDNGRV 547
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
13-95 |
6.11e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 56.72 E-value: 6.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGI--YQKDSGSILFQGKEIDFHSAKEALENGI 90
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
....*
gi 507082969 91 SMVHQ 95
Cdd:PRK09580 81 FMAFQ 85
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
276-482 |
6.27e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 56.63 E-value: 6.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 276 QPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSA-------NEAI--------NHGF 340
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAergvvfqNEGLlpwrnvqdNVAF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 341 AL-----VTEERRSTGiyayldigfnslisniQNYKNKVGLldnsrmksdtqwvidsmrvKTPGHRtQIGSLSGGNQQKV 415
Cdd:PRK11248 94 GLqlagvEKMQRLEIA----------------HQMLKKVGL-------------------EGAEKR-YIWQLSGGQRQRV 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507082969 416 VIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKDKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK11248 138 GIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
276-485 |
6.31e-09 |
|
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: 56.35 E-value: 6.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 276 QPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINnHSANEAINHGFALVTEErrstgiyAY 355
Cdd:cd03244 17 PPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDIS-KIGLHDLRSRISIIPQD-------PV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 356 LDIGfnSLISN-----------IQNYKNKVGLLDnsrmksdtqwVIDSMRVKTPGHRTQIGS-LSGGNQQKVVIGRWLLT 423
Cdd:cd03244 89 LFSG--TIRSNldpfgeysdeeLWQALERVGLKE----------FVESLPGGLDTVVEEGGEnLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507082969 424 QPEILMLDEPTRGIDVGAKFEIYQLIAElAKKDKGIIIISSEMPELLGiTDRILVMSNGLVA 485
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLDTIID-SDRILVLDKGRVV 216
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
405-482 |
6.53e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 56.84 E-value: 6.53e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507082969 405 GSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK14247 145 GKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLEL-KKDMTIVLVTHFPQQAARISDYVAFLYKG 221
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
276-484 |
8.04e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 56.55 E-value: 8.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 276 QPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKIN-NHSANEAINHGFALVTEERRSTGIYA 354
Cdd:PRK13638 14 EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDySKRGLLALRQQVATVFQDPEQQIFYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 355 YLDigfnsliSNIQNYKNKVGLLDN--SRMKSDTQWVIDSMRVKtpghRTQIGSLSGGNQQKVVIGRWLLTQPEILMLDE 432
Cdd:PRK13638 94 DID-------SDIAFSLRNLGVPEAeiTRRVDEALTLVDAQHFR----HQPIQCLSHGQKKRVAIAGALVLQARYLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 507082969 433 PTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:PRK13638 163 PTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQI 214
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
261-482 |
8.80e-09 |
|
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: 55.90 E-value: 8.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 261 PGEVILQVRNLT-SLRQPS-----IRDISFDLHKGEILGIAGLVGAKRTdiveTLFGI----REKSSGTITLHGKKInnh 330
Cdd:COG4181 4 SSAPIIELRGLTkTVGTGAgeltiLKGISLEVEAGESVAIVGASGSGKS----TLLGLlaglDRPTSGTVRLAGQDL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 331 saneainhgFALvTEERRSTGIYAYLDIGFNS--LISN------------IQNYKN----------KVGLldnsrmksdt 386
Cdd:COG4181 77 ---------FAL-DEDARARLRARHVGFVFQSfqLLPTltalenvmlpleLAGRRDarararalleRVGL---------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 387 qwvidsmrvktpGHRTQ--IGSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGID--VGAKfeIYQLIAELaKKDKG--II 460
Cdd:COG4181 137 ------------GHRLDhyPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDaaTGEQ--IIDLLFEL-NRERGttLV 201
|
250 260
....*....|....*....|..
gi 507082969 461 IISSEmPELLGITDRILVMSNG 482
Cdd:COG4181 202 LVTHD-PALAARCDRVLRLRAG 222
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
407-482 |
9.55e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 57.89 E-value: 9.55e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507082969 407 LSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAElakKDKGIIIIS-SEMPELLGITDRILVMSNG 482
Cdd:COG4178 486 LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE---ELPGTTVISvGHRSTLAAFHDRVLELTGD 559
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
41-229 |
1.04e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 56.09 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 41 IHaLMGENGAGKSTLLKCLFGIYQKdSGSILFQGKEIDFHSAKEalengisMVHQELNLVLQRSVMDNM----WLGRY-P 115
Cdd:PRK03695 25 LH-LVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAE-------LARHRAYLSQQQTPPFAMpvfqYLTLHqP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 116 TKGMFVDQDKMYRDtkaIFDELDIDiDPRAR-VGTLSVSQMQMIEIAKAF-------SYDAKIVIMDEPTSSLTEKEVNH 187
Cdd:PRK03695 96 DKTRTEAVASALNE---VAEALGLD-DKLGRsVNQLSGGEWQRVRLAAVVlqvwpdiNPAGQLLLLDEPMNSLDVAQQAA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 507082969 188 LFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIA 229
Cdd:PRK03695 172 LDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLA 213
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-234 |
1.10e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 56.00 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 11 EYLLEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQ-----KDSGSILFQGKEIdFHSAKEA 85
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNI-YSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 86 LE--NGISMVHQELNLVLQRSVMDNMWLGrYPTKGMFVDQDKMYRDTK------AIFDELDIDIDPRArvGTLSVSQMQM 157
Cdd:PRK14267 81 IEvrREVGMVFQYPNPFPHLTIYDNVAIG-VKLNGLVKSKKELDERVEwalkkaALWDEVKDRLNDYP--SNLSGGQRQR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507082969 158 IEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERgCGIVYISHKMEEIFQLCDEITVLRDGQWIATQPLE 234
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTR 233
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
266-467 |
1.69e-08 |
|
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: 54.81 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 266 LQVRNLTSLR--QPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKInnHSANEAINHGFALV 343
Cdd:cd03231 1 LEADELTCERdgRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL--DFQRDSIARGLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 344 TEErrsTGIYAYLdigfnSLISNIQNYKNkvgllDNSRmksDTQW-VIDSMRVKTPGHRTqIGSLSGGNQQKVVIGRWLL 422
Cdd:cd03231 79 GHA---PGIKTTL-----SVLENLRFWHA-----DHSD---EQVEeALARVGLNGFEDRP-VAQLSAGQQRRVALARLLL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 507082969 423 TQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDkGIIIISSEMP 467
Cdd:cd03231 142 SGRPLWILDEPTTALDKAGVARFAEAMAGHCARG-GMVVLTTHQD 185
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
13-222 |
1.74e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 55.51 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEidfhsakealenGISM 92
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKL------------RIGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 93 VHQELNL--VLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIfdeldididpRARVGTLSVSQMQMIEIAKAFSYDAKI 170
Cdd:PRK09544 72 VPQKLYLdtTLPLTVNRFLRLRPGTKKEDILPALKRVQAGHLI----------DAPMQKLSGGETQRVLLARALLNRPQL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 507082969 171 VIMDEPTSSLtekEVN---HLFTIIRKLK-ERGCGIVYISHKMEEIFQLCDEITVL 222
Cdd:PRK09544 142 LVLDEPTQGV---DVNgqvALYDLIDQLRrELDCAVLMVSHDLHLVMAKTDEVLCL 194
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
13-226 |
1.96e-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: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSFPG----VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfhsakeAL-E 87
Cdd:COG4181 8 IIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLF------ALdE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 88 NG--------ISMVHQELNLVLQRSVMDNMWLgryPTkgmfvdqdkmyrdtkaifdELDIDIDPRAR-------VG---- 148
Cdd:COG4181 82 DArarlrarhVGFVFQSFQLLPTLTALENVML---PL-------------------ELAGRRDARARarallerVGlghr 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 149 ------TLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNH----LFTIIRklkERGCGIVYISHKmEEIFQLCDE 218
Cdd:COG4181 140 ldhypaQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQiidlLFELNR---ERGTTLVLVTHD-PALAARCDR 215
|
....*...
gi 507082969 219 ITVLRDGQ 226
Cdd:COG4181 216 VLRLRAGR 223
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
266-482 |
1.99e-08 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 55.92 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 266 LQVRNLT-SLRQ-PSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHsaneainhgfaLV 343
Cdd:COG1118 3 IEVRNISkRFGSfTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTN-----------LP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 344 TEERRstgiyayldIGFNSlisniQNY---------KN-----KVGLLDNSRMKSDTQWVIDSMRVKTPGHR--TQigsL 407
Cdd:COG1118 72 PRERR---------VGFVF-----QHYalfphmtvaENiafglRVRPPSKAEIRARVEELLELVQLEGLADRypSQ---L 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507082969 408 SGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISS---EmpELLGITDRILVMSNG 482
Cdd:COG1118 135 SGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVThdqE--EALELADRVVVMNQG 210
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
407-482 |
2.26e-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: 54.19 E-value: 2.26e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507082969 407 LSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKG--IIIISSEMPELLGITDRILVMSNG 482
Cdd:cd03233 119 ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTttFVSLYQASDEIYDLFDKVLVLYEG 196
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
407-482 |
2.34e-08 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 55.02 E-value: 2.34e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507082969 407 LSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKkdKGI--IIISSEMPELLGITDRILVMSNG 482
Cdd:COG4161 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQ--TGItqVIVTHEVEFARKVASQVVYMEKG 217
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
276-461 |
2.53e-08 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 54.29 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 276 QPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEA----------------INH- 338
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIpylrrrigvvfqdfrlLPDr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 339 ------GFAL-VTEERRS---TGIYAYLDigfnslisniqnyknKVGLLDnsRMKsdtqwvidsmrvKTPGHrtqigsLS 408
Cdd:COG2884 95 tvyenvALPLrVTGKSRKeirRRVREVLD---------------LVGLSD--KAK------------ALPHE------LS 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 507082969 409 GGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIII 461
Cdd:COG2884 140 GGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLI 192
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
26-222 |
2.60e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 55.74 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 26 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHS--AKEALENGISMVHQ-------- 95
Cdd:PRK11308 28 VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeAQKLLRQKIQIVFQnpygslnp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 96 ------------ELNLVLQRS--------VMDNMWL-----GRYPTkgMFvdqdkmyrdtkaifdeldididprarvgtl 150
Cdd:PRK11308 108 rkkvgqileeplLINTSLSAAerrekalaMMAKVGLrpehyDRYPH--MF------------------------------ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507082969 151 SVSQMQMIEIAKAFSYDAKIVIMDEPTSSL---TEKEVNHLFTIIRklKERGCGIVYISHKMEEIFQLCDEITVL 222
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALdvsVQAQVLNLMMDLQ--QELGLSYVFISHDLSVVEHIADEVMVM 228
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
407-485 |
2.89e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 54.71 E-value: 2.89e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507082969 407 LSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVA 485
Cdd:PRK09493 137 LSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIA 215
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
14-188 |
3.09e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.05 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILF----------QGKEIDFhsak 83
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWsenanigyyaQDHAYDF---- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 84 ealENGIsmvhqelnlvlqrSVMDnmWLGRYPTKGmfvDQDKMYRDT--KAIFDELDIdidpRARVGTLS-VSQMQMIeI 160
Cdd:PRK15064 396 ---ENDL-------------TLFD--WMSQWRQEG---DDEQAVRGTlgRLLFSQDDI----KKSVKVLSgGEKGRML-F 449
|
170 180
....*....|....*....|....*...
gi 507082969 161 AKAFSYDAKIVIMDEPTssltekevNHL 188
Cdd:PRK15064 450 GKLMMQKPNVLVMDEPT--------NHM 469
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
281-482 |
3.43e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 55.12 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 281 DISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEAINhgfalvtEERRSTGI---YAYLD 357
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIK-------PVRKKVGVvfqFPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 358 IGFNSLISNIQNYKNKVGLLDNSRMKsdtqwvIDSMRVKTPGHRTQIGS-----LSGGNQQKVVIGRWLLTQPEILMLDE 432
Cdd:PRK13643 97 LFEETVLKDVAFGPQNFGIPKEKAEK------IAAEKLEMVGLADEFWEkspfeLSGGQMRRVAIAGILAMEPEVLVLDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 507082969 433 PTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK13643 171 PTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKG 220
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
29-229 |
3.46e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.83 E-value: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYqkdSGSILFQGKEI--DFHSAKEALENGISMVHQELNLVLQR--- 103
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDL---TGGGAPRGARVtgDVTLNGEPLAAIDAPRLARLRAVLPQaaq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 104 -----SVMDNMWLGRYPTKGMfvDQDKMYRDTKAIFDELDI-DIDPRAR--VGTLSVSQMQMIEIAKAFSY--------- 166
Cdd:PRK13547 94 pafafSAREIVLLGRYPHARR--AGALTHRDGEIAWQALALaGATALVGrdVTTLSGGELARVQFARVLAQlwpphdaaq 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507082969 167 DAKIVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITVLRDGQWIA 229
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDPNLAARHADRIAMLADGAIVA 235
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
406-485 |
3.50e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 55.42 E-value: 3.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 406 SLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:PRK11000 133 ALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
.
gi 507082969 485 A 485
Cdd:PRK11000 213 A 213
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
263-482 |
4.27e-08 |
|
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: 53.98 E-value: 4.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 263 EVILQVRNLT---------SLRQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLH--GKKINNHS 331
Cdd:COG4778 2 TTLLEVENLSktftlhlqgGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdGGWVDLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 332 ANEAInhgfalVTEERRSTgiyayldIGFNS--LisniqnyknKV------------GLLDNSRMKSDTQwvidsMRVKT 397
Cdd:COG4778 82 ASPRE------ILALRRRT-------IGYVSqfL---------RViprvsaldvvaePLLERGVDREEAR-----ARARE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 398 PGHRTQI---------GSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPE 468
Cdd:COG4778 135 LLARLNLperlwdlppATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEV 214
|
250
....*....|....
gi 507082969 469 LLGITDRILVMSNG 482
Cdd:COG4778 215 REAVADRVVDVTPF 228
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
272-482 |
4.27e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 54.37 E-value: 4.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 272 TSLRQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEAINH-----GFALVTEE 346
Cdd:PRK13649 16 TPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQirkkvGLVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 347 RRSTGIYAYLDIGFNSlisniQNY---KNKVGLLdnSRMKSDTQWVIDSMRVKTPGhrtqigSLSGGNQQKVVIGRWLLT 423
Cdd:PRK13649 96 SQLFEETVLKDVAFGP-----QNFgvsQEEAEAL--AREKLALVGISESLFEKNPF------ELSGGQMRRVAIAGILAM 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 507082969 424 QPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK13649 163 EPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKG 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
407-495 |
5.44e-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: 55.46 E-value: 5.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 407 LSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDK-GIIIISSEmpelLGI----TDRILVMSN 481
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGmALLLITHD----LGVvrrfADRVAVMRQ 232
|
90
....*....|....
gi 507082969 482 GLvagIVDTKTTTQ 495
Cdd:COG4172 233 GE---IVEQGPTAE 243
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
407-492 |
5.45e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 54.32 E-value: 5.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 407 LSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVag 486
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKI-- 243
|
....*.
gi 507082969 487 IVDTKT 492
Cdd:PRK13651 244 IKDGDT 249
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
405-463 |
5.67e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 53.69 E-value: 5.67e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 405 GSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGID-VGAKfEIYQLIAELaKKDKGIIIIS 463
Cdd:PRK14267 148 SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDpVGTA-KIEELLFEL-KKEYTIVLVT 205
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
390-482 |
5.91e-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: 51.68 E-value: 5.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 390 IDSMRVKTPGHRTQigsLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAkfeIYQLIAELAKKDKGIIIISSEmPEL 469
Cdd:cd03221 57 VTWGSTVKIGYFEQ---LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLES---IEALEEALKEYPGTVILVSHD-RYF 129
|
90
....*....|....
gi 507082969 470 L-GITDRILVMSNG 482
Cdd:cd03221 130 LdQVATKIIELEDG 143
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
258-479 |
6.94e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 54.33 E-value: 6.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 258 ENKpgEVILQVRNLT---SLR-------QPS-----IRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITL 322
Cdd:PRK15079 3 EGK--KVLLEVADLKvhfDIKdgkqwfwQPPktlkaVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 323 HGKKINNHSANE--AINHGFALVTEE-------RRSTG-IYA------YLDIGFNSLISNIQNYKNKVGLLDNsrmksdt 386
Cdd:PRK15079 81 LGKDLLGMKDDEwrAVRSDIQMIFQDplaslnpRMTIGeIIAeplrtyHPKLSRQEVKDRVKAMMLKVGLLPN------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 387 qwVIDsmrvKTPgHRtqigsLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSE 465
Cdd:PRK15079 154 --LIN----RYP-HE-----FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHD 221
|
250
....*....|....
gi 507082969 466 MPELLGITDRILVM 479
Cdd:PRK15079 222 LAVVKHISDRVLVM 235
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
276-484 |
7.03e-08 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 55.11 E-value: 7.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 276 QPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKInnhsanEAINHGFAlvteeRRSTGIYAY 355
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL------VQYDHHYL-----HRQVALVGQ 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 356 LDIGFN-SLISNIQ---NYKNKVGLLdNSRMKSDTQWVIDSMrvkTPGHRTQIGS----LSGGNQQKVVIGRWLLTQPEI 427
Cdd:TIGR00958 563 EPVLFSgSVRENIAyglTDTPDEEIM-AAAKAANAHDFIMEF---PNGYDTEVGEkgsqLSGGQKQRIAIARALVRKPRV 638
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 507082969 428 LMLDEPTRGIDVgakfEIYQLIAELAK-KDKGIIIISSEMPeLLGITDRILVMSNGLV 484
Cdd:TIGR00958 639 LILDEATSALDA----ECEQLLQESRSrASRTVLLIAHRLS-TVERADQILVLKKGSV 691
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
258-487 |
7.35e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 54.57 E-value: 7.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 258 ENKPgevILQVRNLTSL--RQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSAnea 335
Cdd:PRK09452 10 SLSP---LVELRGISKSfdGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPA--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 336 inhgfalvteERRstgiyaYLDIGFNS--LISNIQNYKN-KVGLldnsRMKSD-----TQWVIDSMR-VKTPGHRTQ-IG 405
Cdd:PRK09452 84 ----------ENR------HVNTVFQSyaLFPHMTVFENvAFGL----RMQKTpaaeiTPRVMEALRmVQLEEFAQRkPH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 406 SLSGGNQQKVVIGRWLLTQPEILMLDEPTRGID----VGAKFEIYQLIAELakkdkGI--IIISSEMPELLGITDRILVM 479
Cdd:PRK09452 144 QLSGGQQQRVAIARAVVNKPKVLLLDESLSALDyklrKQMQNELKALQRKL-----GItfVFVTHDQEEALTMSDRIVVM 218
|
....*...
gi 507082969 480 SNGLVAGI 487
Cdd:PRK09452 219 RDGRIEQD 226
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
270-482 |
8.61e-08 |
|
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: 53.71 E-value: 8.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 270 NLTSLRQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITlHGKKINNHSANEAINHGfalVTEERRS 349
Cdd:cd03291 44 NLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK-HSGRISFSSQFSWIMPG---TIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 350 TGIyAYLDIGFNSLISNIQNYKNKVGLLDNSrmksdtqwvidsmrvKTPGHRTQIgSLSGGNQQKVVIGRWLLTQPEILM 429
Cdd:cd03291 120 FGV-SYDEYRYKSVVKACQLEEDITKFPEKD---------------NTVLGEGGI-TLSGGQRARISLARAVYKDADLYL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 507082969 430 LDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMpELLGITDRILVMSNG 482
Cdd:cd03291 183 LDSPFGYLDVFTEKEIFESCVCKLMANKTRILVTSKM-EHLKKADKILILHEG 234
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
11-226 |
8.89e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 53.25 E-value: 8.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 11 EYLLEMTGINKSF---------PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHS 81
Cdd:PRK15112 2 ETLLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 82 AKEALENgISMVHQELNLVL---QR--SVMDnmwlgrYPTKgMFVDQDKMYRDtKAIFDELdididprARVG-------- 148
Cdd:PRK15112 82 YSYRSQR-IRMIFQDPSTSLnprQRisQILD------FPLR-LNTDLEPEQRE-KQIIETL-------RQVGllpdhasy 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 149 ---TLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITVLRD 224
Cdd:PRK15112 146 yphMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQ 225
|
..
gi 507082969 225 GQ 226
Cdd:PRK15112 226 GE 227
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
8-109 |
9.36e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 53.23 E-value: 9.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 8 SSGEYLLEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALE 87
Cdd:PRK11831 2 QSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYT 81
|
90 100
....*....|....*....|....
gi 507082969 88 --NGISMVHQELNLVLQRSVMDNM 109
Cdd:PRK11831 82 vrKRMSMLFQSGALFTDMNVFDNV 105
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
279-485 |
9.81e-08 |
|
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: 52.92 E-value: 9.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 279 IRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKinnhSANEAINHGF--ALVTEErrstgiyayl 356
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV----SSLLGLGGGFnpELTGRE---------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 357 DIGFNSLISNiqnyknkvglLDNSRMKSDTQWVID--------SMRVKTpghrtqigsLSGGNQQKVVIGRWLLTQPEIL 428
Cdd:cd03220 104 NIYLNGRLLG----------LSRKEIDEKIDEIIEfselgdfiDLPVKT---------YSSGMKARLAFAIATALEPDIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 429 MLDEptrGIDVG-AKFEI--YQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVA 485
Cdd:cd03220 165 LIDE---VLAVGdAAFQEkcQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
277-485 |
1.01e-07 |
|
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: 54.95 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 277 PSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKK--------INNHSANEAINHGFALVTEERR 348
Cdd:TIGR00957 652 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVayvpqqawIQNDSLRENILFGKALNEKYYQ 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 349 STgiyayldigfnslisniqnyknkvglLDNSRMKSDtqwvidsMRVKTPGHRTQIG----SLSGGNQQKVVIGRWLLTQ 424
Cdd:TIGR00957 732 QV--------------------------LEACALLPD-------LEILPSGDRTEIGekgvNLSGGQKQRVSLARAVYSN 778
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507082969 425 PEILMLDEPTRGIDVGAKFEIYQLI--AELAKKDKGIIIISSEMpELLGITDRILVMSNGLVA 485
Cdd:TIGR00957 779 ADIYLFDDPLSAVDAHVGKHIFEHVigPEGVLKNKTRILVTHGI-SYLPQVDVIIVMSGGKIS 840
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
265-482 |
1.06e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 53.17 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 265 ILQVRNLTSLRQP-----SIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSA-NEAINH 338
Cdd:PRK13642 4 ILEVENLVFKYEKesdvnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 339 GFALVTEERRSTGIYAYLDIGFNSLISNIQNyKNKVGLLDNSRMksdtqwVIDSMRVKTpghrTQIGSLSGGNQQKVVIG 418
Cdd:PRK13642 84 GMVFQNPDNQFVGATVEDDVAFGMENQGIPR-EEMIKRVDEALL------AVNMLDFKT----REPARLSGGQKQRVAVA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507082969 419 RWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELakKDK---GIIIISSEMPELLGiTDRILVMSNG 482
Cdd:PRK13642 153 GIIALRPEIIILDESTSMLDPTGRQEIMRVIHEI--KEKyqlTVLSITHDLDEAAS-SDRILVMKAG 216
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
29-207 |
1.07e-07 |
|
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: 51.39 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQkdsgsiLFQGKeIDFHSAKEALengismvhqelnLVLQRSvmdn 108
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWP------WGSGR-IGMPEGEDLL------------FLPQRP---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 109 mwlgrYPTKGMFVDQdkmyrdtkaifdeLdidIDPRARVgtLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHL 188
Cdd:cd03223 74 -----YLPLGTLREQ-------------L---IYPWDDV--LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRL 130
|
170
....*....|....*....
gi 507082969 189 FtiiRKLKERGCGIVYISH 207
Cdd:cd03223 131 Y---QLLKELGITVISVGH 146
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
28-228 |
1.08e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 53.17 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 28 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfhsakeALENGISMVHQELNLVLQRSvmD 107
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDT-------SDEENLWDIRNKAGMVFQNP--D 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 108 NMWLGryptkgMFVDQDkmyrdtkAIFDELDIDIDP---RARVGT-----------------LSVSQMQMIEIAKAFSYD 167
Cdd:PRK13633 96 NQIVA------TIVEED-------VAFGPENLGIPPeeiRERVDEslkkvgmyeyrrhaphlLSGGQKQRVAIAGILAMR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507082969 168 AKIVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQlCDEITVLRDGQWI 228
Cdd:PRK13633 163 PECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVV 223
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
29-226 |
1.22e-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: 54.44 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfHSAKEALENGISMVHQElnLVL-QRSVMD 107
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIR-DVTQASLRAAIGIVPQD--TVLfNDTIAY 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 108 NMWLGRyPTkgmfVDQDKMYRDTKAIfdELD--IDIDPR---ARVG----TLSVSQMQMIEIAKAFSYDAKIVIMDEPTS 178
Cdd:COG5265 451 NIAYGR-PD----ASEEEVEAAARAA--QIHdfIESLPDgydTRVGerglKLSGGEKQRVAIARTLLKNPPILIFDEATS 523
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 507082969 179 SL---TEKEvnhlftIIRKLKE--RGCGIVYISHKMEEIfQLCDEITVLRDGQ 226
Cdd:COG5265 524 ALdsrTERA------IQAALREvaRGRTTLVIAHRLSTI-VDADEILVLEAGR 569
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
65-231 |
1.35e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.65 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 65 KDSGSILFQGKEIDFHSAKEaLENGISMVHQElNLVLQRSVMDNMWLGRyptkgmfvdQDKMYRDTK-----AIFDEL-- 137
Cdd:PTZ00265 1274 KNSGKILLDGVDICDYNLKD-LRNLFSIVSQE-PMLFNMSIYENIKFGK---------EDATREDVKrackfAAIDEFie 1342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 138 ------DIDIDPRARvgTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSL---TEKEVNHLFTIIRKLKERgcGIVYISHK 208
Cdd:PTZ00265 1343 slpnkyDTNVGPYGK--SLSGGQKQRIAIARALLREPKILLLDEATSSLdsnSEKLIEKTIVDIKDKADK--TIITIAHR 1418
|
170 180
....*....|....*....|....*..
gi 507082969 209 MEEIfQLCDEITVL----RDGQWIATQ 231
Cdd:PTZ00265 1419 IASI-KRSDKIVVFnnpdRTGSFVQAH 1444
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
407-484 |
1.63e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 52.78 E-value: 1.63e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507082969 407 LSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDK-GIIIISSEMPELLGiTDRILVMSNGLV 484
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGiTIILITHYMEEAVE-ADRIIVMDSGKV 222
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
289-482 |
1.79e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 53.73 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 289 GEILGIAGLVGAKRTDIVETLFGIREKSS--GTITLHGKKINNHSANEAinhGFalVTEERRstgIYAYLDIG----FNS 362
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILKRT---GF--VTQDDI---LYPHLTVRetlvFCS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 363 LISniqnyknkvglLDNSRMKSDTQWVIDSMRVK---TPGHRTQIGS-----LSGGNQQKVVIGRWLLTQPEILMLDEPT 434
Cdd:PLN03211 166 LLR-----------LPKSLTKQEKILVAESVISElglTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPT 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 507082969 435 RGIDVGAKFEIYQLIAELAKKDKgIIIISSEMP--ELLGITDRILVMSNG 482
Cdd:PLN03211 235 SGLDATAAYRLVLTLGSLAQKGK-TIVTSMHQPssRVYQMFDSVLVLSEG 283
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
277-484 |
1.90e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.21 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 277 PSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNhsaneainhgFALvTEERRSTGIYAYL 356
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAK----------FGL-TDLRRVLSIIPQS 1318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 357 DIGFNSLIS-NIQNYK--NKVGL---LDNSRMKsdtqwviDSMRVKTPGHRTQIG----SLSGGNQQKVVIGRWLLTQPE 426
Cdd:PLN03232 1319 PVLFSGTVRfNIDPFSehNDADLweaLERAHIK-------DVIDRNPFGLDAEVSeggeNFSVGQRQLLSLARALLRRSK 1391
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 507082969 427 ILMLDEPTRGIDVGAKFEIYQLIAElAKKDKGIIIISSEMPELLGiTDRILVMSNGLV 484
Cdd:PLN03232 1392 ILVLDEATASVDVRTDSLIQRTIRE-EFKSCTMLVIAHRLNTIID-CDKILVLSSGQV 1447
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
29-229 |
1.93e-07 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 52.15 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKdSGSILFQGKEIDFHSAKEalengismvhqelnLVLQRSvmdn 108
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAE--------------LARHRA---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 109 mWLGR--YPTKGMFVDQ-----------DKMYRDTKA-IFDELDIDiDPRAR-VGTLSVSQMQMIEIAKAF-------SY 166
Cdd:COG4138 73 -YLSQqqSPPFAMPVFQylalhqpagasSEAVEQLLAqLAEALGLE-DKLSRpLTQLSGGEWQRVRLAAVLlqvwptiNP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507082969 167 DAKIVIMDEPTSSLtekEVNH---LFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIA 229
Cdd:COG4138 151 EGQLLLLDEPMNSL---DVAQqaaLDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVA 213
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
277-482 |
2.42e-07 |
|
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: 51.56 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 277 PSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEAINHG-FALVTEERRSTGIYAY 355
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNrYSVAYAAQKPWLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 356 LD--IGFNSLIsNIQNYKnkvGLLDNSRMKSDtqwvIDSMRVktpGHRTQIG----SLSGGNQQKVVIGRWLLTQPEILM 429
Cdd:cd03290 95 VEenITFGSPF-NKQRYK---AVTDACSLQPD----IDLLPF---GDQTEIGergiNLSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 507082969 430 LDEPTRGIDVGAKFEIYQL-IAELAKKDKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:cd03290 164 LDDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
263-484 |
2.49e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 52.10 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 263 EVILQVRNLTSL---------RQ--PSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITlhgkkINNHS 331
Cdd:PRK15112 2 ETLLEVRNLSKTfryrtgwfrRQtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELL-----IDDHP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 332 ANEAiNHGFalvteerRSTGIYAYLDIGFNSLisniqNYKNKVG-LLD-----NSRMKSDT--QWVIDSMRvktpghrtQ 403
Cdd:PRK15112 77 LHFG-DYSY-------RSQRIRMIFQDPSTSL-----NPRQRISqILDfplrlNTDLEPEQreKQIIETLR--------Q 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 404 IG-----------SLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKdKGI--IIISSEMPELL 470
Cdd:PRK15112 136 VGllpdhasyyphMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEK-QGIsyIYVTQHLGMMK 214
|
250
....*....|....
gi 507082969 471 GITDRILVMSNGLV 484
Cdd:PRK15112 215 HISDQVLVMHQGEV 228
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
275-482 |
2.76e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 52.11 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 275 RQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGI---REKSSGTITLHGKKINNHSANEAINH-GFALVTEERRST 350
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAKTVWDIREKvGIVFQNPDNQFV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 351 GIYAYLDIGF---------NSLISNIQNYKNKVGLLDnsrmksdtqwVIDSmrvktpghrtQIGSLSGGNQQKVVIGRWL 421
Cdd:PRK13640 99 GATVGDDVAFglenravprPEMIKIVRDVLADVGMLD----------YIDS----------EPANLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507082969 422 LTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIIIS--SEMPELLGiTDRILVMSNG 482
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKL-KKKNNLTVISitHDIDEANM-ADQVLVLDDG 219
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
280-458 |
2.95e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 51.91 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 280 RDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEaINHGFALVTEERRSTGiyaylDIG 359
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE-VARRIGLLAQNATTPG-----DIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 360 FNSLISNiQNYKNKvGLLDNSRmKSDTQWVIDSMRVKTPGH--RTQIGSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGI 437
Cdd:PRK10253 98 VQELVAR-GRYPHQ-PLFTRWR-KEDEEAVTKAMQATGITHlaDQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180
....*....|....*....|.
gi 507082969 438 DVGAKFEIYQLIAELaKKDKG 458
Cdd:PRK10253 175 DISHQIDLLELLSEL-NREKG 194
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
276-484 |
3.32e-07 |
|
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: 51.39 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 276 QPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEAINHgFALVTEERrstgiyay 355
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQ-IGLVSQEP-------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 356 lDIGFNSLISNIQNYKNKVglLDNSRMKSDTQWVIDSMRVKTP-GHRTQIG----SLSGGNQQKVVIGRWLLTQPEILML 430
Cdd:cd03249 87 -VLFDGTIAENIRYGKPDA--TDEEVEEAAKKANIHDFIMSLPdGYDTLVGergsQLSGGQKQRIAIARALLRNPKILLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 507082969 431 DEPTRGIDVGAKFEIYQLIaELAKKDKGIIIISSempELLGI--TDRILVMSNGLV 484
Cdd:cd03249 164 DEATSALDAESEKLVQEAL-DRAMKGRTTIVIAH---RLSTIrnADLIAVLQNGQV 215
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
11-439 |
3.52e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 52.63 E-value: 3.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 11 EYLLEMTGINKSFPGVKA-LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIyQKDsgsilFQGKeidfhsAKEALENG 89
Cdd:TIGR03719 2 QYIYTMNRVSKVVPPKKEiLKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-DKD-----FNGE------ARPQPGIK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 90 ISMVHQELNLVLQRSVMDNMWLGRYPTKGMFVDQDKM---YRDTKAIFDEL--------DI-------DIDPR------- 144
Cdd:TIGR03719 70 VGYLPQEPQLDPTKTVRENVEEGVAEIKDALDRFNEIsakYAEPDADFDKLaaeqaelqEIidaadawDLDSQleiamda 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 145 -------ARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEV----NHLF----TI----------------IR 193
Cdd:TIGR03719 150 lrcppwdADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVawleRHLQeypgTVvavthdryfldnvagwIL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 194 KLkERGCGIVYISH------------KMEEIFQLCDEITVLRDGQWIATQP-------------LEGLdmdkiismmvgr 248
Cdd:TIGR03719 230 EL-DRGRGIPWEGNysswleqkqkrlEQEEKEESARQKTLKRELEWVRQSPkgrqakskarlarYEEL------------ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 249 sLNQRFPDKENK------PGE----VILQVRNLTSL--RQPSIRDISFDLHKGEILGIAGLVGAKRTdiveTLF----GI 312
Cdd:TIGR03719 297 -LSQEFQKRNETaeiyipPGPrlgdKVIEAENLTKAfgDKLLIDDLSFKLPPGGIVGVIGPNGAGKS----TLFrmitGQ 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 313 REKSSGTITLhGKKI-------------NNHSANEAINHGFALVTEERRSTGIYAYLDiGFnslisniqNYKNkvglldn 379
Cdd:TIGR03719 372 EQPDSGTIEI-GETVklayvdqsrdaldPNKTVWEEISGGLDIIKLGKREIPSRAYVG-RF--------NFKG------- 434
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 380 srmkSDTQwvidsmrvktpghrTQIGSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDV 439
Cdd:TIGR03719 435 ----SDQQ--------------KKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV 476
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
280-484 |
4.20e-07 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 52.00 E-value: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 280 RDISFDLHKGEILGIAGLVGAKRTdiveTLfgIR-----EK-SSGTITLHGKKINNHSANEainhgfaLVtEERRSTGIy 353
Cdd:COG1135 22 DDVSLTIEKGEIFGIIGYSGAGKS----TL--IRcinllERpTSGSVLVDGVDLTALSERE-------LR-AARRKIGM- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 354 ayldI--GFNsLISN------------IQNYKNK------------VGLLDnsrmKSD---TQwvidsmrvktpghrtqi 404
Cdd:COG1135 87 ----IfqHFN-LLSSrtvaenvalpleIAGVPKAeirkrvaellelVGLSD----KADaypSQ----------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 405 gsLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGL 483
Cdd:COG1135 141 --LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGR 218
|
.
gi 507082969 484 V 484
Cdd:COG1135 219 I 219
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
390-506 |
5.06e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 51.34 E-value: 5.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 390 IDSMRVKTPGHrtqigsLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPEL 469
Cdd:PRK13652 127 LEELRDRVPHH------LSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDL 200
|
90 100 110
....*....|....*....|....*....|....*....
gi 507082969 470 LG-ITDRILVMSNG-LVAGIVDTKTTTQNEILRLASLHL 506
Cdd:PRK13652 201 VPeMADYIYVMDKGrIVAYGTVEEIFLQPDLLARVHLDL 239
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
29-271 |
5.32e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.54 E-value: 5.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGiyQKDSGSILFQGKEIDFHSAKEALENgISMVHQELNL-----VLQR 103
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGDIRISGFPKKQETFAR-ISGYCEQNDIhspqvTVRE 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 104 SVMDNMWLgRYPT------KGMFVDQdkmyrdtkaIFDELDIDIDPRARVGT-----LSVSQMQMIEIAKAFSYDAKIVI 172
Cdd:PLN03140 973 SLIYSAFL-RLPKevskeeKMMFVDE---------VMELVELDNLKDAIVGLpgvtgLSTEQRKRLTIAVELVANPSIIF 1042
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 173 MDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKME-EIFQLCDEITVL-RDGQWIATQPLeGLDMDKIISMMVGRSL 250
Cdd:PLN03140 1043 MDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLMkRGGQVIYSGPL-GRNSHKIIEYFEAIPG 1121
|
250 260
....*....|....*....|.
gi 507082969 251 NQRFPDKENkPGEVILQVRNL 271
Cdd:PLN03140 1122 VPKIKEKYN-PATWMLEVSSL 1141
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
275-486 |
6.24e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 50.26 E-value: 6.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 275 RQpSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEainhgfalVTEERRSTGIY- 353
Cdd:PRK10908 15 RQ-ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRE--------VPFLRRQIGMIf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 354 ----------AYLDIGFNSLISN---------IQNYKNKVGLLDNSRmksdtqwvidSMRVKtpghrtqigsLSGGNQQK 414
Cdd:PRK10908 86 qdhhllmdrtVYDNVAIPLIIAGasgddirrrVSAALDKVGLLDKAK----------NFPIQ----------LSGGEQQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507082969 415 VVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAG 486
Cdd:PRK10908 146 VGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHG 217
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
407-482 |
7.19e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 50.86 E-value: 7.19e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507082969 407 LSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKdKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDG 238
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
406-484 |
7.79e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 50.45 E-value: 7.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 406 SLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDK-GIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:PRK11247 133 ALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGfTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
407-484 |
8.07e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 50.90 E-value: 8.07e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507082969 407 LSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDK-GIIIISSEMPELLGITDRILVMSNGLV 484
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENmALVLITHDLALVAEAAHKIIVMYAGQV 232
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
265-506 |
8.71e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 50.50 E-value: 8.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 265 ILQVRNLTsLRQP----SIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEaINHGF 340
Cdd:PRK13647 4 IIEVEDLH-FRYKdgtkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKW-VRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 341 ALVTEER-----RSTgiyAYLDIGFNSLISNI--QNYKNKVG-LLDNSRMKSdtqwvidsMRVKTPGHrtqigsLSGGNQ 412
Cdd:PRK13647 82 GLVFQDPddqvfSST---VWDDVAFGPVNMGLdkDEVERRVEeALKAVRMWD--------FRDKPPYH------LSYGQK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 413 QKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTKT 492
Cdd:PRK13647 145 KRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSL 224
|
250
....*....|....
gi 507082969 493 TTQNEILRLASLHL 506
Cdd:PRK13647 225 LTDEDIVEQAGLRL 238
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
261-479 |
8.75e-07 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 50.89 E-value: 8.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 261 PGEVILQVRNLT--------SLRQPS-----IRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKI 327
Cdd:COG4608 3 MAEPLLEVRDLKkhfpvrggLFGRTVgvvkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 328 NNHSANEainhgfalVTEERRSTGI-----YAyldigfnSLisniqnyknkvglldNSRMKsdtqwVIDS----MRVKTP 398
Cdd:COG4608 83 TGLSGRE--------LRPLRRRMQMvfqdpYA-------SL---------------NPRMT-----VGDIiaepLRIHGL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 399 GHRTQIGS----------------------LSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKD 456
Cdd:COG4608 128 ASKAERRErvaellelvglrpehadrypheFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDL-QDE 206
|
250 260
....*....|....*....|....*....
gi 507082969 457 KGI--IIISSEmpelLG----ITDRILVM 479
Cdd:COG4608 207 LGLtyLFISHD----LSvvrhISDRVAVM 231
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
29-206 |
8.82e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 49.49 E-value: 8.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEAL-----ENGismVHQELnlvlqr 103
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAChylghRNA---MKPAL------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 104 SVMDNM--WLGRYPTKGMFVDqdkmyrDTKAIFDELDIdIDPRArvGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLT 181
Cdd:PRK13539 89 TVAENLefWAAFLGGEELDIA------AALEAVGLAPL-AHLPF--GYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
170 180
....*....|....*....|....*
gi 507082969 182 EKEVNHLFTIIRKLKERGcGIVYIS 206
Cdd:PRK13539 160 AAAVALFAELIRAHLAQG-GIVIAA 183
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
43-207 |
1.00e-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: 49.28 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 43 ALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfHSAKEALENGISMVHQE-LNLVLqrSVMDNM-WLGRyptkgMF 120
Cdd:TIGR01189 30 QVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA-EQRDEPHENILYLGHLPgLKPEL--SALENLhFWAA-----IH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 121 VDQDKMYRDTKAIFDELDIDIDPrarVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGC 200
Cdd:TIGR01189 102 GGAQRTIEDALAAVGLTGFEDLP---AAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLARGG 178
|
....*..
gi 507082969 201 GIVYISH 207
Cdd:TIGR01189 179 IVLLTTH 185
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
283-479 |
1.11e-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: 50.06 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 283 SFDLHK------GEILGIAGLVGAKRTDIVETLFGIREKSSGTitlHGKK------INNHSANEAINHGFALVTEERRST 350
Cdd:cd03236 14 SFKLHRlpvpreGQVLGLVGPNGIGKSTALKILAGKLKPNLGK---FDDPpdwdeiLDEFRGSELQNYFTKLLEGDVKVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 351 GIYAYLDigfnsLISNiqNYKNKVGLLDNSRMKSDTQ-WVIDSMRVKTPGHRtQIGSLSGGNQQKVVIGRWLLTQPEILM 429
Cdd:cd03236 91 VKPQYVD-----LIPK--AVKGKVGELLKKKDERGKLdELVDQLELRHVLDR-NIDQLSGGELQRVAIAAALARDADFYF 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 507082969 430 LDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVM 479
Cdd:cd03236 163 FDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
407-484 |
1.13e-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: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 407 LSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDvgAKFEIyQLIAELAK--KDKGIIII--SSEMPELLGITDRILVMSNG 482
Cdd:COG3839 134 LSGGQRQRVALGRALVREPKVFLLDEPLSNLD--AKLRV-EMRAEIKRlhRRLGTTTIyvTHDQVEAMTLADRIAVMNDG 210
|
..
gi 507082969 483 LV 484
Cdd:COG3839 211 RI 212
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
28-226 |
1.19e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 51.25 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 28 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfHSAKEALENGISMVHQELNLvLQRSVMD 107
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLT-KLQLDSWRSRLAVVSQTPFL-FSDTVAN 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 108 NMWLGRyPTkgmfVDQDKMYRDTKAIFDELDIDIDPRA---RVG----TLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSL 180
Cdd:PRK10789 408 NIALGR-PD----ATQQEIEHVARLASVHDDILRLPQGydtEVGergvMLSGGQKQRISIARALLLNAEILILDDALSAV 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 507082969 181 ---TEKEvnhlftIIRKLKERGCG-IVYIS-HKMEEIFQlCDEITVLRDGQ 226
Cdd:PRK10789 483 dgrTEHQ------ILHNLRQWGEGrTVIISaHRLSALTE-ASEILVMQHGH 526
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
26-228 |
1.19e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 50.09 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 26 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEaLENGISMVHQEL-NLVLQRS 104
Cdd:PRK13642 20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWN-LRRKIGMVFQNPdNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 105 VMDNMWLGrYPTKGMfVDQDKMYRDTKAIF--DELDIDIDPRARvgtLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTE 182
Cdd:PRK13642 99 VEDDVAFG-MENQGI-PREEMIKRVDEALLavNMLDFKTREPAR---LSGGQKQRVAVAGIIALRPEIIILDESTSMLDP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 507082969 183 KEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQlCDEITVLRDGQWI 228
Cdd:PRK13642 174 TGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEII 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
272-503 |
1.29e-06 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 50.07 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 272 TSLRQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKIN--NHSANEAINHGFALVTEE--- 346
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAklNRAQRKAFRRDIQMVFQDsis 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 347 ----RRSTGiyAYLDIGFNSLISniqnyknkvglLDNSRMKSDTQWVIDSMRVkTPGHRTQI-GSLSGGNQQKVVIGRWL 421
Cdd:PRK10419 101 avnpRKTVR--EIIREPLRHLLS-----------LDKAERLARASEMLRAVDL-DDSVLDKRpPQLSGGQLQRVCLARAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 422 LTQPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKDKGIIIISSEMPELLGITDRILVMSNGlvaGIVDTKTTTqnEILR 500
Cdd:PRK10419 167 AVEPKLLILDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITHDLRLVERFCQRVMVMDNG---QIVETQPVG--DKLT 241
|
...
gi 507082969 501 LAS 503
Cdd:PRK10419 242 FSS 244
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-180 |
1.35e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.10 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 6 TQSSGEYLLEMTGINKSFPGVKALDNVNLKV-RPHSIhALMGENGAGKSTLLKCLFGIYQKDSGSILFQGK-EID-FHSA 82
Cdd:PRK11147 312 ASRSGKIVFEMENVNYQIDGKQLVKDFSAQVqRGDKI-ALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlEVAyFDQH 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 83 KEALEngismvhqelnlvLQRSVMDNMWLGRyptkgmfvdQDKMY--RDTKAIFDELDIDIDP-RAR--VGTLSVSQMQM 157
Cdd:PRK11147 391 RAELD-------------PEKTVMDNLAEGK---------QEVMVngRPRHVLGYLQDFLFHPkRAMtpVKALSGGERNR 448
|
170 180
....*....|....*....|...
gi 507082969 158 IEIAKAFSYDAKIVIMDEPTSSL 180
Cdd:PRK11147 449 LLLARLFLKPSNLLILDEPTNDL 471
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
407-487 |
1.95e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 49.62 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 407 LSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVA 485
Cdd:PRK13645 151 LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVI 230
|
..
gi 507082969 486 GI 487
Cdd:PRK13645 231 SI 232
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
172-438 |
2.10e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.01 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 172 IMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIATQPLEGLDMDKIISMMV--GRS 249
Cdd:PRK10938 158 ILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQALVAQLAhsEQL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 250 LNQRFPDKENKPGEVIL-QVRNLTSLR--------QPSIRDISFDLHKGEILGIAGLVGAKRTDIVE------------- 307
Cdd:PRK10938 238 EGVQLPEPDEPSARHALpANEPRIVLNngvvsyndRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSlitgdhpqgysnd 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 308 -TLFGIREKSSGTITLHGKKINNHSAneainhgfALVTEERRSTG-----IYAYLD-IGFNSLISniqnyknkvgllDNS 380
Cdd:PRK10938 318 lTLFGRRRGSGETIWDIKKHIGYVSS--------SLHLDYRVSTSvrnviLSGFFDsIGIYQAVS------------DRQ 377
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507082969 381 RMKSDtQWV----IDSMRVKTPGHrtqigSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGID 438
Cdd:PRK10938 378 QKLAQ-QWLdilgIDKRTADAPFH-----SLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
280-482 |
2.34e-06 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 49.41 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 280 RDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEainhgfalVTEERRSTG-IYAYldi 358
Cdd:PRK11153 22 NNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKE--------LRKARRQIGmIFQH--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 359 gFNSLIS-----NI-----------QNYKNKVG-LLDnsrmksdtqwvidsmRVKTPGHRTQIGS-LSGGNQQKVVIGRW 420
Cdd:PRK11153 91 -FNLLSSrtvfdNValplelagtpkAEIKARVTeLLE---------------LVGLSDKADRYPAqLSGGQKQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507082969 421 LLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDK-GIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK11153 155 LASNPKVLLCDEATSALDPATTRSILELLKDINRELGlTIVLITHEMDVVKRICDRVAVIDAG 217
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
266-474 |
2.63e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 48.33 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 266 LQVRNLTSLRQPSI--RDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSANEAInhgfalv 343
Cdd:PRK13539 3 LEGEDLACVRGGRVlfSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAC------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 344 teerrstgiyAYL---DiGFNSLISNIQNYKNKVGLLDNSRmkSDTQWVIDSMRVKTPGHRtQIGSLSGGNQQKVVIGRW 420
Cdd:PRK13539 76 ----------HYLghrN-AMKPALTVAENLEFWAAFLGGEE--LDIAAALEAVGLAPLAHL-PFGYLSAGQKRRVALARL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 507082969 421 LLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDkGIIIISSEMPelLGITD 474
Cdd:PRK13539 142 LVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQG-GIVIAATHIP--LGLPG 192
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
265-482 |
2.76e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 49.42 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 265 ILQVRNLT----SLRQP--SIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIrEKSSGTITLHGKKINN--------H 330
Cdd:PRK15093 3 LLDIRNLTiefkTSDGWvkAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTADRMRFDDidllrlspR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 331 SANEAINHGFALVTEERRSTgiyayLD----IGfNSLISNIQNYKNKvglldnSRMKSDTQW----VIDSM-RVKTPGHR 401
Cdd:PRK15093 82 ERRKLVGHNVSMIFQEPQSC-----LDpserVG-RQLMQNIPGWTYK------GRWWQRFGWrkrrAIELLhRVGIKDHK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 402 TQIGS----LSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDK-GIIIISSEMPELLGITDRI 476
Cdd:PRK15093 150 DAMRSfpyeLTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNtTILLISHDLQMLSQWADKI 229
|
....*.
gi 507082969 477 LVMSNG 482
Cdd:PRK15093 230 NVLYCG 235
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
421-482 |
2.85e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 49.32 E-value: 2.85e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507082969 421 LLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISS-EMPELLGITDRILVMSNG 482
Cdd:COG4586 169 LLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTShDMDDIEALCDRVIVIDHG 231
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
407-485 |
3.10e-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: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 407 LSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIIsSEMPELLG--ITDRILVMSNGLV 484
Cdd:cd03217 105 FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLII-THYQRLLDyiKPDRVHVLYDGRI 183
|
.
gi 507082969 485 A 485
Cdd:cd03217 184 V 184
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
275-485 |
3.79e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 49.33 E-value: 3.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 275 RQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINnHSANEAINHGFALVteerrSTGIYA 354
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLT-KLQLDSWRSRLAVV-----SQTPFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 355 YLDigfnSLISNI--------QNYKNKVGLLDNsrmksdtqwVIDSMRVKTPGHRTQIGS----LSGGNQQKVVIGRWLL 422
Cdd:PRK10789 401 FSD----TVANNIalgrpdatQQEIEHVARLAS---------VHDDILRLPQGYDTEVGErgvmLSGGQKQRISIARALL 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507082969 423 TQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKgiIIISSEMPELLGITDRILVMSNGLVA 485
Cdd:PRK10789 468 LNAEILILDDALSAVDGRTEHQILHNLRQWGEGRT--VIISAHRLSALTEASEILVMQHGHIA 528
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
30-203 |
4.97e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 47.49 E-value: 4.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 30 DNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfHSAKEALengismvHQELnlvlqrsvmdnM 109
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI--RRQRDEY-------HQDL-----------L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 110 WLGRYP-TKGM--------FVDQDKMYRDTKAIFDELdididprARVG----------TLSVSQMQMIEIAKAFSYDAKI 170
Cdd:PRK13538 78 YLGHQPgIKTEltalenlrFYQRLHGPGDDEALWEAL-------AQVGlagfedvpvrQLSAGQQRRVALARLWLTRAPL 150
|
170 180 190
....*....|....*....|....*....|...
gi 507082969 171 VIMDEPTSSLTEKEVNHLFTIIRKLKERGcGIV 203
Cdd:PRK13538 151 WILDEPFTAIDKQGVARLEALLAQHAEQG-GMV 182
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
10-70 |
5.08e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.96 E-value: 5.08e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507082969 10 GEYLLEMTGINKSFpGVKAL-DNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSI 70
Cdd:PRK11819 321 GDKVIEAENLSKSF-GDRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
275-485 |
5.16e-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: 49.05 E-value: 5.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 275 RQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNhsaneainhgfalVTEE--RRSTGI 352
Cdd:COG5265 370 ERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRD-------------VTQAslRAAIGI 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 353 YAYLDIGFN-SLISNIQnYknkvGLLDNS--------RMKSdtqwvIDSMRVKTP-GHRTQIGS----LSGGNQQKVVIG 418
Cdd:COG5265 437 VPQDTVLFNdTIAYNIA-Y----GRPDASeeeveaaaRAAQ-----IHDFIESLPdGYDTRVGErglkLSGGEKQRVAIA 506
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507082969 419 RWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIII----SSempellgIT--DRILVMSNGLVA 485
Cdd:COG5265 507 RTLLKNPPILIFDEATSALDSRTERAIQAALREVA-RGRTTLVIahrlST-------IVdaDEILVLEAGRIV 571
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
400-481 |
5.60e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.26 E-value: 5.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 400 HRTQIGS----LSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDR 475
Cdd:PTZ00265 569 YETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYANT 648
|
....*.
gi 507082969 476 ILVMSN 481
Cdd:PTZ00265 649 IFVLSN 654
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
26-212 |
5.89e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.26 E-value: 5.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 26 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQgkeiDFHSAKEA----LENGISMVHQElNLVL 101
Cdd:PTZ00265 398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN----DSHNLKDInlkwWRSKIGVVSQD-PLLF 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 102 QRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAR----------------------------------- 146
Cdd:PTZ00265 473 SNSIKNNIKYSLYSLKDLEALSNYYNEDGNDSQENKNKRNSCRAKcagdlndmsnttdsneliemrknyqtikdsevvdv 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 147 --------------------VGT----LSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGI 202
Cdd:PTZ00265 553 skkvlihdfvsalpdkyetlVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRI 632
|
250
....*....|.
gi 507082969 203 -VYISHKMEEI 212
Cdd:PTZ00265 633 tIIIAHRLSTI 643
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
14-253 |
6.23e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.19 E-value: 6.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAG--KSTLLKCLFGiyqKDSGSILFqgKEIDFHSAKEALENGIS 91
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPW--RF*TWCANRRALRRTIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 92 MvHQELNLVLQRSV--MDNMWLgryptKGMFVDQDKmyRDTKAIFDELDIDIDPRARVG----TLSVSQMQMIEIAKAFS 165
Cdd:NF000106 89 *-HRPVR*GRRESFsgRENLYM-----IGR*LDLSR--KDARARADELLERFSLTEAAGraaaKYSGGMRRRLDLAASMI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 166 YDAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWIATQpleglDMDKIISMM 245
Cdd:NF000106 161 GRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADG-----KVDELKTKV 235
|
....*...
gi 507082969 246 VGRSLNQR 253
Cdd:NF000106 236 GGRTLQIR 243
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
266-482 |
6.39e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 47.77 E-value: 6.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 266 LQVRNLT-SLRQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIR----EKSSGTITLHGKKInnhSANEAINHGF 340
Cdd:PRK10418 5 IELRNIAlQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGRVLLDGKPV---APCALRGRKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 341 ALVTEERRStgiyayldiGFNSLiSNIQNYKNKVgLLDNSRMKSDTQwVIDSMRVKTPGHRTQIGSL-----SGGNQQKV 415
Cdd:PRK10418 82 ATIMQNPRS---------AFNPL-HTMHTHARET-CLALGKPADDAT-LTAALEAVGLENAARVLKLypfemSGGMLQRM 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507082969 416 VIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKDKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHG 217
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
29-226 |
7.70e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.97 E-value: 7.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfhsakeaLENGISMVHQELNLVLQRSVM-- 106
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDI--------SKFGLMDLRKVLGIIPQAPVLfs 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 107 ---------------DNMW--LGRYPTKgmfvdqDKMYRDTKAifdeLDIDIdprARVG-TLSVSQMQMIEIAKAFSYDA 168
Cdd:PLN03130 1327 gtvrfnldpfnehndADLWesLERAHLK------DVIRRNSLG----LDAEV---SEAGeNFSVGQRQLLSLARALLRRS 1393
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 169 KIVIMDEPTSSLtekEVNHLFTIIRKLKE--RGCGIVYISHKMEEIFQlCDEITVLRDGQ 226
Cdd:PLN03130 1394 KILVLDEATAAV---DVRTDALIQKTIREefKSCTMLIIAHRLNTIID-CDRILVLDAGR 1449
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
402-439 |
8.58e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.41 E-value: 8.58e-06
10 20 30
....*....|....*....|....*....|....*...
gi 507082969 402 TQIGSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDV 439
Cdd:PRK11147 152 AALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI 189
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
14-236 |
8.86e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 47.39 E-value: 8.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPGVkALDNVNLKVRPHSIHALMGENGAGKStlLKC--LFGIY----QKDSGSILFQGKEIdfhsAKEALE 87
Cdd:PRK10418 5 IELRNIALQAAQP-LVHGVSLTLQRGRVLALVGGSGSGKS--LTCaaALGILpagvRQTAGRVLLDGKPV----APCALR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 88 nGISMVhqelnLVLQ--RSVMD---NM---------WLGRYPTKGMFVdqdkmyrdtkAIFDELDIDiDPrARVGTLSVS 153
Cdd:PRK10418 78 -GRKIA-----TIMQnpRSAFNplhTMhtharetclALGKPADDATLT----------AALEAVGLE-NA-ARVLKLYPF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 154 QM-----QMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITVLRDGQW 227
Cdd:PRK10418 140 EMsggmlQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
....*....
gi 507082969 228 IATQPLEGL 236
Cdd:PRK10418 220 VEQGDVETL 228
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
407-479 |
1.04e-05 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 47.59 E-value: 1.04e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507082969 407 LSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAK-KDKGIIIISSEMPELLGITDRILVM 479
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVL 232
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
13-207 |
1.33e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.64 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 13 LLEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILF-----------------QGK 75
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYeqdlivarlqqdpprnvEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 76 EIDFHSA-----KEALENgismVHQELNLVLQRSvMDNMwLGRYPTKGMFVDQDKMYRDTKAIFDELD-IDIDPRARVGT 149
Cdd:PRK11147 83 VYDFVAEgieeqAEYLKR----YHDISHLVETDP-SEKN-LNELAKLQEQLDHHNLWQLENRINEVLAqLGLDPDAALSS 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507082969 150 LSVSQMQMIEIAKAFSYDAKIVIMDEPTssltekevNHL-FTIIRKLKE-----RGCgIVYISH 207
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPT--------NHLdIETIEWLEGflktfQGS-IIFISH 211
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
404-496 |
1.49e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 46.46 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 404 IGSLSGGNQQKV-VIGRWLLTQPEI------LMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRI 476
Cdd:PRK03695 124 VNQLSGGEWQRVrLAAVVLQVWPDInpagqlLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRV 203
|
90 100
....*....|....*....|..
gi 507082969 477 LVMSNG--LVAGIVDTKTTTQN 496
Cdd:PRK03695 204 WLLKQGklLASGRRDEVLTPEN 225
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
281-485 |
2.43e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 46.50 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 281 DISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKkinnhsanEAINHGFALVTEERRSTGI-----YAY 355
Cdd:PRK11308 33 GVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQ--------DLLKADPEAQKLLRQKIQIvfqnpYGS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 356 LdigfnslisniqNYKNKVG------LLDNSRM--KSDTQWVIDSMRvkTPGHRTQIGS-----LSGGNQQKVVIGRWLL 422
Cdd:PRK11308 105 L------------NPRKKVGqileepLLINTSLsaAERREKALAMMA--KVGLRPEHYDryphmFSGGQRQRIAIARALM 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507082969 423 TQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGI--IIISSEMPELLGITDRILVMSNGLVA 485
Cdd:PRK11308 171 LDPDVVVADEPVSALDVSVQAQVLNLMMDL-QQELGLsyVFISHDLSVVEHIADEVMVMYLGRCV 234
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
404-462 |
2.45e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 46.70 E-value: 2.45e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 507082969 404 IGSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIII 462
Cdd:COG1245 210 ISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVV 268
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
407-481 |
2.91e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.55 E-value: 2.91e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507082969 407 LSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSN 481
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLAD 210
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
260-484 |
3.32e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.89 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 260 KPGEVILQVRN-----LTSLRQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFG-IREKSSGTITLHGKkinnhsan 333
Cdd:PLN03232 609 QPGAPAISIKNgyfswDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGS-------- 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 334 eainhgfalvteerrstgiyayldIGFNSLISNIQNYKNKVGLLDNSRMKSDTQW-VIDSMRVKT-----PGH-RTQIG- 405
Cdd:PLN03232 681 ------------------------VAYVPQVSWIFNATVRENILFGSDFESERYWrAIDVTALQHdldllPGRdLTEIGe 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 406 ---SLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMpELLGITDRILVMSNG 482
Cdd:PLN03232 737 rgvNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQL-HFLPLMDRIILVSEG 815
|
..
gi 507082969 483 LV 484
Cdd:PLN03232 816 MI 817
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
29-226 |
3.58e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 46.41 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDS--GSILFQGKEIdfhsAKEALENgISMVHQELNLVLQRSVM 106
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKP----TKQILKR-TGFVTQDDILYPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 107 DNM---WLGRYPTKgmFVDQDKMyRDTKAIFDELDIDIDPRARVGT-----LSVSQMQMIEIAKAFSYDAKIVIMDEPTS 178
Cdd:PLN03211 159 ETLvfcSLLRLPKS--LTKQEKI-LVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 507082969 179 SLTEKEVNHLFTIIRKLKERGCGIVYISHK-MEEIFQLCDEITVLRDGQ 226
Cdd:PLN03211 236 GLDATAAYRLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
29-78 |
3.98e-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: 3.98e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 507082969 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKD---SGSILFQGKEID 78
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLT 69
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
403-484 |
4.18e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 45.99 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 403 QIGSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAElAKKDKGIIIISSEMPELLGItDRILVMSNG 482
Cdd:PRK11174 482 QAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNA-ASRRQTTLMVTHQLEDLAQW-DQIWVMQDG 559
|
..
gi 507082969 483 LV 484
Cdd:PRK11174 560 QI 561
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
407-482 |
4.89e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 44.77 E-value: 4.89e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507082969 407 LSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:PRK10584 147 LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNG 222
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
266-464 |
5.94e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 44.02 E-value: 5.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 266 LQVRNLTSLRQPSI--RDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKInnHSANEAINH----- 338
Cdd:PRK13538 2 LEARNLACERDERIlfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI--RRQRDEYHQdllyl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 339 GFAlvteerrsTGIYAYL----DIGFNSLISN------IQNYKNKVGLLDnsrmksdtqwvidsmRVKTPghrtqIGSLS 408
Cdd:PRK13538 80 GHQ--------PGIKTELtaleNLRFYQRLHGpgddeaLWEALAQVGLAG---------------FEDVP-----VRQLS 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 507082969 409 GGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDkGIIIISS 464
Cdd:PRK13538 132 AGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQG-GMVILTT 186
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
27-210 |
6.46e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.09 E-value: 6.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 27 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfHSAKEALengiSMVHQELNLVLQRSVM 106
Cdd:PRK13541 14 KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNIN-NIAKPYC----TYIGHNLGLKLEMTVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 107 DN--MWLGRYPTKGMFVDQDKMYRdtkaIFDELDididprARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKE 184
Cdd:PRK13541 89 ENlkFWSEIYNSAETLYAAIHYFK----LHDLLD------EKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKEN 158
|
170 180
....*....|....*....|....*.
gi 507082969 185 VNHLFTIIrKLKERGCGIVYISHKME 210
Cdd:PRK13541 159 RDLLNNLI-VMKANSGGIVLLSSHLE 183
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
407-482 |
6.48e-05 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 45.10 E-value: 6.48e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507082969 407 LSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKdKGI--IIISSEMPELLGITDRILVMSNG 482
Cdd:PRK11432 137 ISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQ-FNItsLYVTHDQSEAFAVSDTVIVMNKG 213
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
424-463 |
7.44e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.50 E-value: 7.44e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 507082969 424 QPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIIS 463
Cdd:NF033858 415 KPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFIS 454
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
405-485 |
9.15e-05 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 43.80 E-value: 9.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 405 GSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKDKGIIIISSEMPELLGITDRILVMSNGL 483
Cdd:PRK10771 128 GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGR 207
|
..
gi 507082969 484 VA 485
Cdd:PRK10771 208 IA 209
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
403-482 |
1.01e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 45.10 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 403 QIGSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEmPELLGITDRILVMSNG 482
Cdd:PRK10535 141 QPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDG 219
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
28-78 |
1.62e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 44.19 E-value: 1.62e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 507082969 28 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEID 78
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT 388
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
263-484 |
1.74e-04 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 43.46 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 263 EVILQVRNL--TSLRQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGI--REKSSGT-ITLHGKKINNHSAneain 337
Cdd:PRK09984 2 QTIIRVEKLakTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitGDKSAGShIELLGRTVQREGR----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 338 hgfaLVTEERRSTGIYAYLDIGFNsLISNIQNYKNK-VGLLDNSRM-KSDTQWVIDSMRVKTPGHRTQIG---------- 405
Cdd:PRK09984 77 ----LARDIRKSRANTGYIFQQFN-LVNRLSVLENVlIGALGSTPFwRTCFSWFTREQKQRALQALTRVGmvhfahqrvs 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 406 SLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDkGIIIISS--EMPELLGITDRILVMSNGL 483
Cdd:PRK09984 152 TLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQND-GITVVVTlhQVDYALRYCERIVALRQGH 230
|
.
gi 507082969 484 V 484
Cdd:PRK09984 231 V 231
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
257-462 |
1.94e-04 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 42.78 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 257 KENKPgevILQVRNL--TSLRQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSAnE 334
Cdd:PRK10247 2 QENSP---LLQLQNVgyLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP-E 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 335 AINHGFALVTEERRSTGIYAYLDIGFNSLISNIQNYKNKvgLLDnsrmksdtqwviDSMRVKTPGHRTQ--IGSLSGGNQ 412
Cdd:PRK10247 78 IYRQQVSYCAQTPTLFGDTVYDNLIFPWQIRNQQPDPAI--FLD------------DLERFALPDTILTknIAELSGGEK 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 507082969 413 QKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIII 462
Cdd:PRK10247 144 QRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYV-REQNIAVL 192
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
6-180 |
2.12e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.03 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 6 TQSSGEYLLEMTGINKSFPGVKaldnvnLKVRPHSIHA-----LMGENGAGKSTLLKCLFGIYQKDSGSILFQGK----- 75
Cdd:PRK13409 333 DESERETLVEYPDLTKKLGDFS------LEVEGGEIYEgevigIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKisykp 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 76 ---EIDFH--------SAKEALENgiSMVHQELN--LVLQRsVMDNmwlgryptkgmfvdqdkmyrdtkaifdeldidid 142
Cdd:PRK13409 407 qyiKPDYDgtvedllrSITDDLGS--SYYKSEIIkpLQLER-LLDK---------------------------------- 449
|
170 180 190
....*....|....*....|....*....|....*...
gi 507082969 143 praRVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSL 180
Cdd:PRK13409 450 ---NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHL 484
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
29-225 |
2.20e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 44.20 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFG-IYQKDSGSILFQGKeidfhsakealengISMVHQeLNLVLQRSVMD 107
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGS--------------VAYVPQ-VSWIFNATVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 108 NMWLGRYptkgmfVDQDKMYRDTKAIFDELDIDIDP---RARVG----TLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSL 180
Cdd:PLN03232 698 NILFGSD------FESERYWRAIDVTALQHDLDLLPgrdLTEIGergvNISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 507082969 181 TEKEVNHLFTIIRKLKERGCGIVYISHKMeEIFQLCDEITVLRDG 225
Cdd:PLN03232 772 DAHVAHQVFDSCMKDELKGKTRVLVTNQL-HFLPLMDRIILVSEG 815
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
29-226 |
2.84e-04 |
|
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: 43.78 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGiyqkdsgsilfqgkEIDFHSAKEALENGISMVHQEL---NLVLQRSV 105
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLA--------------EMDKVEGHVHMKGSVAYVPQQAwiqNDSLRENI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 106 MDNMWLgryptkgmfvdQDKMYRDT-KAIFDELDIDIDP---RARVG----TLSVSQMQMIEIAKAFSYDAKIVIMDEPT 177
Cdd:TIGR00957 720 LFGKAL-----------NEKYYQQVlEACALLPDLEILPsgdRTEIGekgvNLSGGQKQRVSLARAVYSNADIYLFDDPL 788
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 507082969 178 SSLTEKEVNHLFTII------RKLKERgcgiVYISHKMEEIFQLcDEITVLRDGQ 226
Cdd:TIGR00957 789 SAVDAHVGKHIFEHVigpegvLKNKTR----ILVTHGISYLPQV-DVIIVMSGGK 838
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-180 |
2.93e-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: 43.62 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 2 VSTHTQSSGEY-LLEMTGINKSFPGVKaldnvnLKVRPHSIH-----ALMGENGAGKSTLLKCLFGIYQKDSGSILFQGK 75
Cdd:COG1245 329 VHAPRREKEEEtLVEYPDLTKSYGGFS------LEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 76 eidfhsakealengISMVHQELNLVLQRSVMDNMwlgRYPTKGMFvdQDKMYRDTkaIFDELDIDIDPRARVGTLSVSQM 155
Cdd:COG1245 403 --------------ISYKPQYISPDYDGTVEEFL---RSANTDDF--GSSYYKTE--IIKPLGLEKLLDKNVKDLSGGEL 461
|
170 180
....*....|....*....|....*
gi 507082969 156 QMIEIAKAFSYDAKIVIMDEPTSSL 180
Cdd:COG1245 462 QRVAIAACLSRDADLYLLDEPSAHL 486
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
402-434 |
3.09e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.18 E-value: 3.09e-04
10 20 30
....*....|....*....|....*....|...
gi 507082969 402 TQIGSLSGGNQQKVVIGRWLLTQPEILMLDEPT 434
Cdd:PRK11819 159 AKVTKLSGGERRRVALCRLLLEKPDMLLLDEPT 191
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
404-462 |
3.60e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.26 E-value: 3.60e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 507082969 404 IGSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIII 462
Cdd:PRK13409 210 ISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELA-EGKYVLVV 267
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
149-230 |
3.85e-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: 42.22 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 149 TLSVSQMQMIEIAKAFSYDAK---IVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIfQLCDEITVL--- 222
Cdd:cd03271 169 TLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVI-KCADWIIDLgpe 247
|
90
....*....|.
gi 507082969 223 ---RDGQWIAT 230
Cdd:cd03271 248 ggdGGGQVVAS 258
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
406-485 |
3.90e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.31 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 406 SLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAkfeIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVA 485
Cdd:PLN03073 627 TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA---VEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVT 703
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
13-70 |
4.00e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.23 E-value: 4.00e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 507082969 13 LLEMTGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSI 70
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI 369
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
280-482 |
4.01e-04 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 41.99 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 280 RDISFDLHKGEILGIAGLVGAKRTdiveTLF----GIREKSSGTITLHGKkinnhsaneainhgfalvteerrstgIYAY 355
Cdd:COG1134 43 KDVSFEVERGESVGIIGRNGAGKS----TLLkliaGILEPTSGRVEVNGR--------------------------VSAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 356 LDI--GFNSLISNIQNyknkVGLldNSRM----KSDTQWVIDS------------MRVKT--PGHRTQIG-SLSggnqqk 414
Cdd:COG1134 93 LELgaGFHPELTGREN----IYL--NGRLlglsRKEIDEKFDEivefaelgdfidQPVKTysSGMRARLAfAVA------ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 507082969 415 vvigrwLLTQPEILMLDEptrGIDVG-AKFEI--YQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:COG1134 161 ------TAVDPDILLVDE---VLAVGdAAFQKkcLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKG 222
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
407-482 |
4.12e-04 |
|
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: 41.46 E-value: 4.12e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507082969 407 LSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIII-ISSEMPELLGITDRILVMSNG 482
Cdd:cd03232 109 LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCtIHQPSASIFEKFDRLLLLKRG 185
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
27-228 |
4.27e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 42.38 E-value: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 27 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFHSAKEALENG----------------- 89
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEKVleklviqktrfkkikki 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 90 ------ISMVHQ--ELNLVLQRSVMDNMWLGRyptkGMFVDQDKMYRDTKAIFDELDIDID--PRARVGtLSVSQMQMIE 159
Cdd:PRK13651 101 keirrrVGVVFQfaEYQLFEQTIEKDIIFGPV----SMGVSKEEAKKRAAKYIELVGLDESylQRSPFE-LSGGQKRRVA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507082969 160 IAKAFSYDAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQWI 228
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKII 244
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
14-234 |
4.33e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 42.52 E-value: 4.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 14 LEMTGINKSFPG-VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfhsAKEALENGISM 92
Cdd:PRK11650 4 LKLQAVRKSYDGkTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVN---ELEPADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 93 VHQELNLVLQRSVMDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELDI----DIDPRArvgtLSVSQMQMIEIAKAFSYDA 168
Cdd:PRK11650 81 VFQNYALYPHMSVRENM---AYGLKIRGMPKAEIEERVAEAARILELepllDRKPRE----LSGGQRQRVAMGRAIVREP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507082969 169 KIVIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITVLRDGQ--WIATqPLE 234
Cdd:PRK11650 154 AVFLFDEPLSNLDAKLRVQMRLEIQRLHRRlKTTSLYVTHDQVEAMTLADRVVVMNGGVaeQIGT-PVE 221
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
43-478 |
5.36e-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: 42.46 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 43 ALMGENGAGKSTLLKCL-------FGIYQKDSG--SIL--FQGKEIDFHSAKEAlENGISMVH--QELNL---VLQRSVM 106
Cdd:COG1245 103 GILGPNGIGKSTALKILsgelkpnLGDYDEEPSwdEVLkrFRGTELQDYFKKLA-NGEIKVAHkpQYVDLipkVFKGTVR 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 107 DnmWLGRyptkgmfVDQDKMYRDtkaIFDELDID--IDprARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKE 184
Cdd:COG1245 182 E--LLEK-------VDERGKLDE---LAEKLGLEniLD--RDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQ 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 185 VNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVL--RDGQW-IATQPLegldmdkiiSMMVG---------RSLNQ 252
Cdd:COG1245 248 RLNVARLIRELAEEGKYVLVVEHDLAILDYLADYVHILygEPGVYgVVSKPK---------SVRVGinqyldgylPEENV 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 253 RF----------PDKENKPGEVILQVRNLT-SLRQPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTIT 321
Cdd:COG1245 319 RIrdepiefevhAPRREKEEETLVEYPDLTkSYGGFSLEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 322 LhGKKINnhsaneainhgfalvteerrstgiYA--YLDIGFN----SLISNIQNYKnkvglLDNSRMKSDtqwVIDSMRV 395
Cdd:COG1245 399 E-DLKIS------------------------YKpqYISPDYDgtveEFLRSANTDD-----FGSSYYKTE---IIKPLGL 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 396 KtPGHRTQIGSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELA-KKDKGIIIISSEMPELLGITD 474
Cdd:COG1245 446 E-KLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAeNRGKTAMVVDHDIYLIDYISD 524
|
....
gi 507082969 475 RILV 478
Cdd:COG1245 525 RLMV 528
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
408-482 |
6.02e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 41.55 E-value: 6.02e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507082969 408 SGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIIsSEMPELLG--ITDRILVMSNG 482
Cdd:CHL00131 153 SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILI-THYQRLLDyiKPDYVHVMQNG 228
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
11-62 |
6.79e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.41 E-value: 6.79e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 507082969 11 EYLLEMTGINKSFPGVKA-LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGI 62
Cdd:PRK11819 4 QYIYTMNRVSKVVPPKKQiLKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV 56
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
149-212 |
7.47e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.31 E-value: 7.47e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507082969 149 TLSVSQMQMIEIAKAFSYDAK---IVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEI 212
Cdd:TIGR00630 829 TLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVI 895
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
148-219 |
7.50e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 40.38 E-value: 7.50e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507082969 148 GTLSVSQMQMIEIAK--AFSYDAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKmEEIFQLCDEI 219
Cdd:cd03238 86 STLSGGELQRVKLASelFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN-LDVLSSADWI 158
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
408-505 |
9.17e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 41.64 E-value: 9.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 408 SGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVA-- 485
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIad 225
|
90 100
....*....|....*....|.
gi 507082969 486 GIVDT-KTTTQNEILRLASLH 505
Cdd:NF000106 226 GKVDElKTKVGGRTLQIRPAH 246
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
407-474 |
9.58e-04 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 40.90 E-value: 9.58e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 407 LSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGI--IIISSEMPELLGITD 474
Cdd:PRK11831 144 LSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISEL-NSALGVtcVVVSHDVPEVLSIAD 212
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
266-482 |
9.60e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 41.63 E-value: 9.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 266 LQVRNLT-SLR--QPSIRDISFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSSGTITLHGKKINNHSaNEAINHGFAL 342
Cdd:PRK10790 341 IDIDNVSfAYRddNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS-HSVLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 343 VTEER--RSTGIYAYLDIGFNslISNIQNYK--NKVGLLDNSRMKSDtqwvidsmrvktpGHRTQIG----SLSGGNQQK 414
Cdd:PRK10790 420 VQQDPvvLADTFLANVTLGRD--ISEEQVWQalETVQLAELARSLPD-------------GLYTPLGeqgnNLSVGQKQL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 415 VVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIIS--SEMPEllgiTDRILVMSNG 482
Cdd:PRK10790 485 LALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHrlSTIVE----ADTILVLHRG 550
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
391-478 |
1.31e-03 |
|
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: 39.86 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 391 DSMRVKTPGHRTQIGSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPEL 469
Cdd:cd03222 56 DEWDGITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEgKKTALVVEHDLAVL 135
|
....*....
gi 507082969 470 LGITDRILV 478
Cdd:cd03222 136 DYLSDRIHV 144
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
28-226 |
1.53e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.03 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 28 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeidfhSAKEALENGISMvhqelnlvlQRSVMD 107
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS-----AALIAISSGLNG---------QLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 108 NMWLgryptKG--MFVDQDKMYRDTKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEV 185
Cdd:PRK13545 105 NIEL-----KGlmMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFT 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 507082969 186 NHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITVLRDGQ 226
Cdd:PRK13545 180 KKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQ 220
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
406-500 |
1.84e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 406 SLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAkfeIYQLIAELAKKDKGIIIISSEMpELLG--ITDRILVMSNGL 483
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA---VLWLETYLLKWPKTFIVVSHAR-EFLNtvVTDILHLHGQKL 419
|
90
....*....|....*....
gi 507082969 484 VA--GIVDTKTTTQNEILR 500
Cdd:PLN03073 420 VTykGDYDTFERTREEQLK 438
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
390-463 |
1.91e-03 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 40.16 E-value: 1.91e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507082969 390 IDSMRVKTPGHRTqIGSLSGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKdKGIIIIS 463
Cdd:PRK10575 132 ISLVGLKPLAHRL-VDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQE-RGLTVIA 203
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
29-74 |
2.02e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.92 E-value: 2.02e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 507082969 29 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG 74
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG 62
|
|
| 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 507082969 46 GENGAGKSTLLKCLFGIYQKDSGSIlfqgkEIDFHSAKEA 85
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQI-----QIDGKTATRG 78
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
103-222 |
3.84e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.20 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 103 RSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFdELDIDIDPRAR-VGTLSVSQMQMIEIAKAFSYDAK---IVIMDEPTS 178
Cdd:PRK00635 763 KNIADILEMTAYEAEKFFLDEPSIHEKIHALC-SLGLDYLPLGRpLSSLSGGEIQRLKLAYELLAPSKkptLYVLDEPTT 841
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 507082969 179 SLTEKEVNHLFTIIRKLKERGCGIVYISHKMeEIFQLCDEITVL 222
Cdd:PRK00635 842 GLHTHDIKALIYVLQSLTHQGHTVVIIEHNM-HVVKVADYVLEL 884
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
408-482 |
4.06e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 40.09 E-value: 4.06e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507082969 408 SGGNQQKVVIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAK--KDKGIIIISSEMPELLGITDRILVMSNG 482
Cdd:TIGR00956 211 SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANilDTTPLVAIYQCSQDAYELFDKVIVLYEG 287
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
43-212 |
5.91e-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: 37.35 E-value: 5.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 43 ALMGENGAGKSTLLKCLFGIYQKDSGSILfqgkeidfhsakealengismvhqelnlvlqrsvmdnmwlgryptkgmFVD 122
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELGPPGGGVI------------------------------------------------YID 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507082969 123 QDKMYRDTKAIFDELDIDIDPRArvgtLSVSQMQMIEIAKAFSYDAKIVIMDEPTSSLTEKEVNHLF------TIIRKLK 196
Cdd:smart00382 38 GEDILEEVLDQLLLIIVGGKKAS----GSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelrLLLLLKS 113
|
170
....*....|....*.
gi 507082969 197 ERGCGIVYISHKMEEI 212
Cdd:smart00382 114 EKNLTVILTTNDEKDL 129
|
|
| |
