|
Name |
Accession |
Description |
Interval |
E-value |
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
18-559 |
0e+00 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 560.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 18 LLKPFWLRKNNKTSVLLIIIILAMILGVVKIQVWLNDWNNDFFNALSQKETDKLWQLVLWFPALLGIFVLISVNKTWLIK 97
Cdd:COG4178 10 LARPYWRSEEKWKAWGLLALLLLLTLASVGLNVLLNFWNRDFYDALQARDAAAFWQQLGVFALLAAISILLAVYQTYLRQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 98 LLTIRWREWLTDYYLNRWFADKNYYFTQIYGEhkNTDNPDQRIAEDILLLISKTLSLSFGFIQSLSMLITFTVILWQSAG 177
Cdd:COG4178 90 RLQIRWREWLTERLLDRWLSNRAYYRLQLSGG--EIDNPDQRIAEDIRLFTETTLSLSLGLLSSVVTLISFIGILWSLSG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 178 TLSFTVGGTEWNIQGYMVYTVVLIVIGGTLFTHKVGKRIRPLNVEKQRSEATFRTNLVQHNKQAELIALSNAESLQRQEL 257
Cdd:COG4178 168 SLTFTLGGYSITIPGYMVWAALIYAIIGTLLTHLIGRPLIRLNFEQQRREADFRFALVRVRENAESIALYRGEAAERRRL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 258 RDNFHTIKENWHRLMNRQRWLDYWQNIYSRSLSVLPYFLLLPQFISGQINLGGLMKSRQAFMLVSNNLSWFIYKYDELAE 337
Cdd:COG4178 248 RRRFDAVIANWRRLIRRQRNLTFFTTGYGQLAVIFPILVAAPRYFAGEITLGGLMQAASAFGQVQGALSWFVDNYQSLAE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 338 LAAVIDRLYEFHQLTEQ---RPTNKPK---NCQHAVQVANASIRTPDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLK 411
Cdd:COG4178 328 WRATVDRLAGFEEALEAadaLPEAASRietSEDGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLR 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 412 TLSHCWPWFKGDISSPAG--SWYVSQTPLIKSGLLKEIIC-KALPLPVDDKSLSEVLHQVGLGKLAARIHDHDRWGDILS 488
Cdd:COG4178 408 AIAGLWPYGSGRIARPAGarVLFLPQRPYLPLGTLREALLyPATAEAFSDAELREALEAVGLGHLAERLDEEADWDQVLS 487
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446551198 489 SGEKQRIALARLILRRPKWIFLDETTSHLEEQEAIRLLRLVREKLPTSGVIMVTHQPGVWNLADDICDISA 559
Cdd:COG4178 488 LGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTG 558
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
367-558 |
2.30e-59 |
|
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: 194.68 E-value: 2.30e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 367 VQVANASIRTPDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDISSPAG--SWYVSQTPLIKSGLL 444
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGedLLFLPQRPYLPLGTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 445 KEIICKAlplpvddkslsevlhqvglgklaarihdhdrWGDILSSGEKQRIALARLILRRPKWIFLDETTSHLEEQEAIR 524
Cdd:cd03223 81 REQLIYP-------------------------------WDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDR 129
|
170 180 190
....*....|....*....|....*....|....
gi 446551198 525 LLRLVREKLPTsgVIMVTHQPGVWNLADDICDIS 558
Cdd:cd03223 130 LYQLLKELGIT--VISVGHRPSLWKFHDRVLDLD 161
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
148-554 |
2.36e-33 |
|
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: 134.96 E-value: 2.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 148 ISKTLS-LSFGFIQSLSMLITFTVILWQSAGTLSFTVGGTewniqgymvytVVLIVIGGTLFthkvGKRIRPLNVEKQRS 226
Cdd:COG2274 265 IREFLTgSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLL-----------IPLYVLLGLLF----QPRLRRLSREESEA 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 227 EATFRTNLVQHNKQAELIALSNAESLQRQELRDNFhtikENWHRLMNRQRWLDYWQNIYSRSLSVLPYFLLL----PQFI 302
Cdd:COG2274 330 SAKRQSLLVETLRGIETIKALGAESRFRRRWENLL----AKYLNARFKLRRLSNLLSTLSGLLQQLATVALLwlgaYLVI 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 303 SGQINLGGLMksrqAFMLVSNNLSW----FIYKYDELAELAAVIDRLYEFHQLTEQRPTNK----PKNCQHAVQVANASI 374
Cdd:COG2274 406 DGQLTLGQLI----AFNILSGRFLApvaqLIGLLQRFQDAKIALERLDDILDLPPEREEGRsklsLPRLKGDIELENVSF 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 375 R-TPDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDIS---------SPAgSW-----YVSQTPLI 439
Cdd:COG2274 482 RyPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILidgidlrqiDPA-SLrrqigVVLQDVFL 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 440 KSGLLKEIICKALPLpVDDKSLSEVLHQVGL--------GKLAARIHDHdrwGDILSSGEKQRIALARLILRRPKWIFLD 511
Cdd:COG2274 561 FSGTIRENITLGDPD-ATDEEIIEAARLAGLhdfiealpMGYDTVVGEG---GSNLSGGQRQRLAIARALLRNPRILILD 636
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 446551198 512 ETTSHLEEQEAIRLLRLVREKLPTSGVIMVTHQPGVWNLADDI 554
Cdd:COG2274 637 EATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRI 679
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
71-548 |
4.32e-33 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 134.11 E-value: 4.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 71 LWQLVLWFPALLGIFVLISVNKtWLIKLLTIRWREWLTDYYLNRWFADKNYYftQIYGEHKNTDNPDQRIAEDILLLISK 150
Cdd:TIGR00954 135 AWILFKWFLIAPPASFINSAIK-YLLKELKLRFRVRLTRYLYSKYLSGFTFY--KVSNLDSRIQNPDQLLTQDVEKFCDS 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 151 TLSLSFGFIQSLSMLITFTVILWQSAGTLSftvGGTEWniqGYMVYTVVLIviggTLFTHKVGKrirpLNVEKQRSEATF 230
Cdd:TIGR00954 212 VVELYSNLTKPILDVILYSFKLLTALGSVG---PAGLF---AYLFATGVVL----TKLRPPIGK----LTVEEQALEGEY 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 231 R---TNLVQHNkqaELIALSNAESLQRQELRDNFHTIKENWHRLMNRQRWLDYWQNIYSRSL-SVLPYFLLLPQFI---- 302
Cdd:TIGR00954 278 RyvhSRLIMNS---EEIAFYQGNKVEKETVMSSFYRLVEHLNLIIKFRFSYGFLDNIVAKYTwSAVGLVAVSIPIFdkth 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 303 --SGQINLGGLMK----SRQAFMLVSNNLSWFIYKYDELAELAAVIDRLYEFHQLTE----------------------Q 354
Cdd:TIGR00954 355 paFLEMSEEELMQefynNGRLLLKAADALGRLMLAGRDMTRLAGFTARVDTLLQVLDdvksgnfkrprveeiesgreggR 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 355 RPTNKPKNCQ-----HAVQVANASIRTPDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDISSPAG 429
Cdd:TIGR00954 435 NSNLVPGRGIveyqdNGIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAK 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 430 S--WYVSQTPLIKSGLLKEIICkaLPLPVD--------DKSLSEVLHQVGLGKLAAR------IHDhdrWGDILSSGEKQ 493
Cdd:TIGR00954 515 GklFYVPQRPYMTLGTLRDQII--YPDSSEdmkrrglsDKDLEQILDNVQLTHILEReggwsaVQD---WMDVLSGGEKQ 589
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 446551198 494 RIALARLILRRPKWIFLDETTSHLEEQEAIRLLRLVREKLPTsgVIMVTHQPGVW 548
Cdd:TIGR00954 590 RIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGIT--LFSVSHRKSLW 642
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
199-557 |
1.06e-32 |
|
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: 132.20 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 199 VLIVIGGTLFTHKVGKRIrplNVEKQRSEATFRTNLVQH-NKQAELIAlSNAEslqrQELRDNFHTIKENWHRLMNRQRW 277
Cdd:COG4987 166 LLAGLLLPLLAARLGRRA---GRRLAAARAALRARLTDLlQGAAELAA-YGAL----DRALARLDAAEARLAAAQRRLAR 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 278 LDYWqniySRSLSVLPYFLLL--------PQFISGQIN---LGGL----MKSRQAFMLVSNNLSwfiykydELAELAAVI 342
Cdd:COG4987 238 LSAL----AQALLQLAAGLAVvavlwlaaPLVAAGALSgplLALLvlaaLALFEALAPLPAAAQ-------HLGRVRAAA 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 343 DRLyefHQLTEQRP------TNKPKNCQHAVQVANASIRTPDN-KIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSH 415
Cdd:COG4987 307 RRL---NELLDAPPavtepaEPAPAPGGPSLELEDVSFRYPGAgRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLR 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 416 CWPWFKGDIS---SPAGSW----------YVSQTPLIKSGLLKEIICKALPlPVDDKSLSEVLHQVGLGKLAARIHDH-D 481
Cdd:COG4987 384 FLDPQSGSITlggVDLRDLdeddlrrriaVVPQRPHLFDTTLRENLRLARP-DATDEELWAALERVGLGDWLAALPDGlD 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 482 RW----GDILSSGEKQRIALARLILRRPKWIFLDETTSHLEEQEAIRLLRLVREKLPTSGVIMVTHQPGVWNLADDICDI 557
Cdd:COG4987 463 TWlgegGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVL 542
|
|
| PRK12369 |
PRK12369 |
putative transporter; Reviewed |
46-348 |
1.15e-30 |
|
putative transporter; Reviewed
Pssm-ID: 171443 [Multi-domain] Cd Length: 326 Bit Score: 122.10 E-value: 1.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 46 VKIQVWLNDWNNDFFNALSQKET-------DKLWQLVLWFPALLGIFVLISVNKTWLIKLLTIRWREWLTDYYLNRWFAD 118
Cdd:PRK12369 30 VSLNVAINEWYGDFYDLLQKAKIepnnhtaGDFWASILSFLAIAMPYVLIATVVDYFASHYAFRWREAMTFSYLKFWRNK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 119 KNyyftqiygehkNTDNPDQRIAEDILLLISKTLSLSFGFIQSLSMLITFTVILWQSAGTLSFTVGGtewNIQGYMVYTV 198
Cdd:PRK12369 110 RD-----------NIEGSSQRIQEDTYRFAKIMESLGLSFLRAIMTLIAFIPILWGLSDGVSLPFLK---DIPGSLVWIA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 199 VLIVIGGTLFTHKVGKRIRPLNVEKQRSEATFRTNLV-QHNKQAELIALSNAESLqrqelrdnFHTIKENWHRLMNRQRW 277
Cdd:PRK12369 176 LLISLGGLVISWFVGIKLPGLEYNNQKVEAAFRKELVyAEDDKKNYAKPETLIEL--------FTGLRFNYFRLFLHYGY 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446551198 278 LDYWQNIYSRSLSVLPYFLLLPQFISGQINLGGLMKSRQAFMLVSNNLSWFIYKYDELAELAAVIDRLYEF 348
Cdd:PRK12369 248 FNIWLISFSQMMVIVPYLIMAPGLFAGVITLGVLMQISNAFSQVRSSFSVFIRNWTTITELRSIYKRLKEF 318
|
|
| ABC_membrane_2 |
pfam06472 |
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family ... |
48-302 |
1.92e-30 |
|
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family of ABC transporters and shares sequence similarity with pfam00664. Mutations in this domain in Swiss:P28288 are believed responsible for Zellweger Syndrome-2; mutations in Swiss:P33897 are responsible for recessive X-linked adrenoleukodystrophy. A Saccharomyces cerevisiae homolog is involved in the import of long-chain fatty acids.
Pssm-ID: 399466 Cd Length: 269 Bit Score: 120.02 E-value: 1.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 48 IQVWLNDWNNDFFNALSQKETDKLWQLVLWFPALLGIFVLISVNKTWLIKLLTIRWREWLTDYYLNRWFADKNYYftQIY 127
Cdd:pfam06472 30 LSVLVAQLDGQIVKALVAKNGRGFIRLLLKWALLAVPASFVNSALKYLTQRLALRFRTRLTRHLHDEYLKGRTYY--KMS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 128 GEHKNTDNPDQRIAEDILLLISKTLSLSFGFIQSLSMLITFTVILWQSAGTLSftvggtewniqgymVYTVVLIVIGGTL 207
Cdd:pfam06472 108 NLDGRIDNPDQRITQDVEKFCSSLSDLYSNLLKPILDIILFTFRLWRLSGWRG--------------PAILFLYVLLSAV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 208 FTHKVGKRIRPLNVEKQRSEATFRTNLVQHNKQAELIALSNAESLQRQELRDNFHTIKENWHRLMNRQRWLDYWQNIYSR 287
Cdd:pfam06472 174 ILRRLSPPFGKLVAEEQKLEGEFRYLHSRLITNAEEIAFYRGEKREKKQLQRSFKSLIDHMRRILRRRLWYGFIEDFVLK 253
|
250
....*....|....*.
gi 446551198 288 SL-SVLPYFLLLPQFI 302
Cdd:pfam06472 254 YTwSILGYVLVALPIF 269
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
367-545 |
3.09e-30 |
|
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: 117.58 E-value: 3.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 367 VQVANASIRtPDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWP-------WFKGDISSPAGSW-----YVS 434
Cdd:COG4133 3 LEAENLSCR-RGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPpsagevlWNGEPIRDAREDYrrrlaYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 435 QTPLIKSGL-LKEII---CKALPLPVDDKSLSEVLHQVGLGKLAarihdhDRWGDILSSGEKQRIALARLILRRPKWIFL 510
Cdd:COG4133 82 HADGLKPELtVRENLrfwAALYGLRADREAIDEALEAVGLAGLA------DLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 446551198 511 DETTSHLEEQEAIRLLRLVREKLPTSG-VIMVTHQP 545
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHLARGGaVLLTTHQP 191
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
375-545 |
1.05e-28 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 113.37 E-value: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 375 RTPDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDI--------SSPAGSW-----YVSQTPliks 441
Cdd:COG4619 8 FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIyldgkplsAMPPPEWrrqvaYVPQEP---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 442 GLLKEIICKALPLP-------VDDKSLSEVLHQVGLGK--LAARIHDhdrwgdiLSSGEKQRIALARLILRRPKWIFLDE 512
Cdd:COG4619 84 ALWGGTVRDNLPFPfqlrerkFDRERALELLERLGLPPdiLDKPVER-------LSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 446551198 513 TTSHLEEQEAIRLLRLVREKLPTSG--VIMVTHQP 545
Cdd:COG4619 157 PTSALDPENTRRVEELLREYLAEEGraVLWVSHDP 191
|
|
| SbmA_BacA |
pfam05992 |
SbmA/BacA-like family; The Rhizobium meliloti bacA gene encodes a function that is essential ... |
46-348 |
1.15e-28 |
|
SbmA/BacA-like family; The Rhizobium meliloti bacA gene encodes a function that is essential for bacterial differentiation into bacteroids within plant cells in the symbiosis between R. meliloti and alfalfa. An Escherichia coli homolog of BacA, SbmA, is implicated in the uptake of microcins and bleomycin. This family is likely to be a subfamily of the ABC transporter family.
Pssm-ID: 461797 [Multi-domain] Cd Length: 314 Bit Score: 115.98 E-value: 1.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 46 VKIQVWLNDWNNDFF----NALSQKET---DKLWQLVLWFPALLGIFVLISVNKTWLIKLLTIRWREWLTDYYLNRWFAD 118
Cdd:pfam05992 23 VQVDVAINAWYGPFYdliqKALASPNAvtiGEFYASLLVFLGIAFIYVTIAVLNLFFVSHYVFRWRTAMNDYYTSHWQQL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 119 KnyyftQIYGEhkntdnpDQRIAEDILLLISKTLSLSFGFIQSLSMLITFTVILWQ-SAGTLSFTVGGtewNIQGYMVYT 197
Cdd:pfam05992 103 R-----HIEGA-------SQRVQEDTMRFASIVEDLGVSLVRAIMTLIAFLPVLFGlSKHVPVLPIIG---DIPHSLVWA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 198 VVLIVIGGTLFTHKVGKRIRPLNVEKQRSEATFRTNLVqhnkqaelIALSNAESLQRQELRDNFHTIKENWHRLMNRQRW 277
Cdd:pfam05992 168 AVVWSLGGTVFLAVVGIKLPGLEFNNQKVEAAYRKELV--------YGEDDATRATPKTLKELFSDVRKNYFRLYFHYMY 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446551198 278 LDYWQNIYSRSLSVLPYFLLLPQFISGQINLGGLMKSRQAFMLVSNNLSWFIYKYDELAELAAVIDRLYEF 348
Cdd:pfam05992 240 FNIARIFYLQLDNLFGYIFLAPSIVAGKITLGVMQQITNVFGKVRGSFQYLINSWTTIVELMSIYKRLRAF 310
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
340-554 |
1.48e-28 |
|
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: 119.86 E-value: 1.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 340 AVIDRLYEFHQLTEQRPTNK----PKNCQHAVQVANASIRTPDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSH 415
Cdd:COG4988 306 AAAEKIFALLDAPEPAAPAGtaplPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 416 CWPWFKGDI--------SSPAGSW-----YVSQTPLIKSGLLKEIICKALPlPVDDKSLSEVLHQVGL--------GKLA 474
Cdd:COG4988 386 FLPPYSGSIlingvdlsDLDPASWrrqiaWVPQNPYLFAGTIRENLRLGRP-DASDEELEAALEAAGLdefvaalpDGLD 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 475 ARIHDHdrwGDILSSGEKQRIALARLILRRPKWIFLDETTSHLEEQEAIRLLRLVREKLPTSGVIMVTHQPGVWNLADDI 554
Cdd:COG4988 465 TPLGEG---GRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRI 541
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
138-543 |
2.64e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 116.03 E-value: 2.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 138 QRIAEDI-LLLISKTLSLSFGF----------------IQSLSMLITFTVI-LWQSAGTLSFTVGgtewniqgYMVYT-- 197
Cdd:COG1132 90 QRVVADLrRDLFEHLLRLPLSFfdrrrtgdllsrltndVDAVEQFLAHGLPqLVRSVVTLIGALV--------VLFVIdw 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 198 -----VVLIVIGGTLFTHKVGKRIRPLNVEKQRSEATFrTNLVQHNKQ-AELIALSNAESLQRQELRDNFHTIKENWHRL 271
Cdd:COG1132 162 rlaliVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAEL-NGRLQESLSgIRVVKAFGREERELERFREANEELRRANLRA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 272 MNRQRWLDYWQNIYSRSLSVLPYFLLLPQFISGQINLGGLMksrqAFMLVSNNLSW----FIYKYDELAELAAVIDRLYE 347
Cdd:COG1132 241 ARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLV----AFILYLLRLFGplrqLANVLNQLQRALASAERIFE 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 348 F----HQLTEQRPTNKPKNCQHAVQVANASIRTPDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKG- 422
Cdd:COG1132 317 LldepPEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGr 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 423 ------DISS-PAGSW-----YVSQTPLIKSGLLKEIICKALPlPVDDKSLSEVLHqvglgklAARIHDH---------- 480
Cdd:COG1132 397 ilidgvDIRDlTLESLrrqigVVPQDTFLFSGTIRENIRYGRP-DATDEEVEEAAK-------AAQAHEFiealpdgydt 468
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446551198 481 ---DRwGDILSSGEKQRIALARLILRRPKWIFLDETTSHL----EE--QEAIRllRLVREKlpTsgVIMVTH 543
Cdd:COG1132 469 vvgER-GVNLSGGQRQRIAIARALLKDPPILILDEATSALdtetEAliQEALE--RLMKGR--T--TIVIAH 533
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
368-556 |
6.03e-27 |
|
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: 107.52 E-value: 6.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 368 QVANASIRTpDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDIsspagswYVSQTPlIKSGLLKEI 447
Cdd:cd03214 1 EVENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEI-------LLDGKD-LASLSPKEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 448 ICK-ALplpvddksLSEVLHQVGLGKLAARIHDHdrwgdiLSSGEKQRIALARLILRRPKWIFLDETTSHLEEQEAIRLL 526
Cdd:cd03214 72 ARKiAY--------VPQALELLGLAHLADRPFNE------LSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELL 137
|
170 180 190
....*....|....*....|....*....|..
gi 446551198 527 RLVREKLPTSG--VIMVTHQPgvwNLADDICD 556
Cdd:cd03214 138 ELLRRLARERGktVVMVLHDL---NLAARYAD 166
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
366-557 |
9.26e-27 |
|
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: 113.92 E-value: 9.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 366 AVQVANASIRTPDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDIS---------SPAGSW----Y 432
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAvngvpladaDADSWRdqiaW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 433 VSQTPLIKSGLLKEIICKALPlPVDDKSLSEVLHQVGLGKLAA--------RIHDHdrwGDILSSGEKQRIALARLILRR 504
Cdd:TIGR02857 401 VPQHPFLFAGTIAENIRLARP-DASDAEIREALERAGLDEFVAalpqgldtPIGEG---GAGLSGGQAQRLALARAFLRD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446551198 505 PKWIFLDETTSHLEEQEAIRLLRLVREKLPTSGVIMVTHQPGVWNLADDICDI 557
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
378-561 |
1.23e-26 |
|
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: 108.59 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 378 DNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDIS---SPAGSW----------YVSQTPLIKSGLL 444
Cdd:COG1120 12 GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgRDLASLsrrelarriaYVPQEPPAPFGLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 445 -KEIIckAL-----------PLPVDDKSLSEVLHQVGLGKLAARIHDHdrwgdiLSSGEKQRIALARLILRRPKWIFLDE 512
Cdd:COG1120 92 vRELV--ALgryphlglfgrPSAEDREAVEEALERTGLEHLADRPVDE------LSGGERQRVLIARALAQEPPLLLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446551198 513 TTSHLEEQEAIRLLRLVREKLPTSG--VIMVTHQPgvwNLADDICDISAVL 561
Cdd:COG1120 164 PTSHLDLAHQLEVLELLRRLARERGrtVVMVLHDL---NLAARYADRLVLL 211
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
368-554 |
3.72e-25 |
|
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: 102.29 E-value: 3.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 368 QVANASIRTPDNK-IILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDI---SSPAGSWYVSQtpliksgl 443
Cdd:cd03246 2 EVENVSFRYPGAEpPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVrldGADISQWDPNE-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 444 LKEIICKalpLPVDDKSLSevlhqvglGKLAarihdhdrwGDILSSGEKQRIALARLILRRPKWIFLDETTSHLEEQEAI 523
Cdd:cd03246 74 LGDHVGY---LPQDDELFS--------GSIA---------ENILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGER 133
|
170 180 190
....*....|....*....|....*....|..
gi 446551198 524 RLLRLVRE-KLPTSGVIMVTHQPGVWNLADDI 554
Cdd:cd03246 134 ALNQAIAAlKAAGATRIVIAHRPETLASADRI 165
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
377-554 |
4.35e-25 |
|
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: 101.69 E-value: 4.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 377 PDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDI--------SSPAGSW-----YVSQTPLIKSGL 443
Cdd:cd03228 12 GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIlidgvdlrDLDLESLrkniaYVPQDPFLFSGT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 444 LKEiickalplpvddkslsevlhqvglgklaarihdhdrwgDILSSGEKQRIALARLILRRPKWIFLDETTSHLEEQEAI 523
Cdd:cd03228 92 IRE--------------------------------------NILSGGQRQRIAIARALLRDPPILILDEATSALDPETEA 133
|
170 180 190
....*....|....*....|....*....|.
gi 446551198 524 RLLRLVREKLPTSGVIMVTHQPGVWNLADDI 554
Cdd:cd03228 134 LILEALRALAKGKTVIVIAHRLSTIRDADRI 164
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
369-545 |
2.54e-23 |
|
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: 103.59 E-value: 2.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 369 VANASIRTPDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDIS---SPAGSW----------YVSQ 435
Cdd:TIGR02868 337 LRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTldgVPVSSLdqdevrrrvsVCAQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 436 TPLIKSGLLKEIICKALPlPVDDKSLSEVLHQVGLGKLAARIHD-HDRW----GDILSSGEKQRIALARLILRRPKWIFL 510
Cdd:TIGR02868 417 DAHLFDTTVRENLRLARP-DATDEELWAALERVGLADWLRALPDgLDTVlgegGARLSGGERQRLALARALLADAPILLL 495
|
170 180 190
....*....|....*....|....*....|....*
gi 446551198 511 DETTSHLEEQEAIRLLRLVREKLPTSGVIMVTHQP 545
Cdd:TIGR02868 496 DEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
368-561 |
9.93e-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: 94.62 E-value: 9.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 368 QVANASIRTPDNKIiLENLNFHVSPGKWLLLKGYSGAGKTTLLKTLShcwpwfkGDISSPAGSWYVsqtpliksgllkei 447
Cdd:cd00267 1 EIENLSFRYGGRTA-LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIA-------GLLKPTSGEILI-------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 448 ickaLPLPVDDKSLSEVLHQVGLgklaarIHDhdrwgdiLSSGEKQRIALARLILRRPKWIFLDETTSHLEEQEAIRLLR 527
Cdd:cd00267 59 ----DGKDIAKLPLEELRRRIGY------VPQ-------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLE 121
|
170 180 190
....*....|....*....|....*....|....*
gi 446551198 528 LVREKLPT-SGVIMVTHQPgvwNLADDICDISAVL 561
Cdd:cd00267 122 LLRELAEEgRTVIIVTHDP---ELAELAADRVIVL 153
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
367-543 |
3.55e-22 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 95.12 E-value: 3.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 367 VQVANASIRTPDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLShcwpwfkGDISSPAGSWYVSQTPLIKsglLKE 446
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLY-------GEERPTSGQVLVNGQDLSR---LKR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 447 -----------II---CK-----------ALPLPVDDKS-------LSEVLHQVGL-GKLAARIHdhdrwgdILSSGEKQ 493
Cdd:COG2884 72 reipylrrrigVVfqdFRllpdrtvyenvALPLRVTGKSrkeirrrVREVLDLVGLsDKAKALPH-------ELSGGEQQ 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446551198 494 RIALARLILRRPKWIFLDETTSHLEEQEAIRLLRLVRE--KLPTSgVIMVTH 543
Cdd:COG2884 145 RVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEinRRGTT-VLIATH 195
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
367-556 |
1.49e-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: 93.55 E-value: 1.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 367 VQVANASIRTPDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDIS------SPAGSW-------YV 433
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLvdgkdiTKKNLRelrrkvgLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 434 SQTP---LIKSGLLKEII--CKALPLPVD--DKSLSEVLHQVGLGKLAAR-IHDhdrwgdiLSSGEKQRIALARLILRRP 505
Cdd:COG1122 81 FQNPddqLFAPTVEEDVAfgPENLGLPREeiRERVEEALELVGLEHLADRpPHE-------LSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446551198 506 KWIFLDETTSHLEEQEAIRLLRLVREkLPTSG--VIMVTHQPgvwNLADDICD 556
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKR-LNKEGktVIIVTHDL---DLVAELAD 202
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
368-554 |
1.96e-21 |
|
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: 92.53 E-value: 1.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 368 QVANASIRTPD-NKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDI--------SSPAGSW-----YV 433
Cdd:cd03225 1 ELKNLSFSYPDgARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVlvdgkdltKLSLKELrrkvgLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 434 SQTP---LIKSGLLKEII--CKALPLPVDD--KSLSEVLHQVGLGKLAAR-IHDhdrwgdiLSSGEKQRIALARLILRRP 505
Cdd:cd03225 81 FQNPddqFFGPTVEEEVAfgLENLGLPEEEieERVEEALELVGLEGLRDRsPFT-------LSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446551198 506 KWIFLDETTSHLEEQEAIRLLRLVReKLPTSG--VIMVTHQP-GVWNLADDI 554
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLK-KLKAEGktIIIVTHDLdLLLELADRV 204
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
368-561 |
4.52e-21 |
|
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: 91.83 E-value: 4.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 368 QVANASIRTpDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDIS----SPAGSW----YVSQTP-- 437
Cdd:cd03235 1 EVEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgkPLEKERkrigYVPQRRsi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 438 ----------LIKSGLLKEIICKALPLPVDDKSLSEVLHQVGLGKLAARIHDHdrwgdiLSSGEKQRIALARLILRRPKW 507
Cdd:cd03235 80 drdfpisvrdVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGE------LSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446551198 508 IFLDETTSHLEEQEAIRLLRLVREkLPTSG--VIMVTHQpgvWNLADDICDISAVL 561
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRE-LRREGmtILVVTHD---LGLVLEYFDRVLLL 205
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
365-554 |
7.98e-21 |
|
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: 91.11 E-value: 7.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 365 HAVQVANASIRTPDNKI-ILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLS---------------HCWPWFKGDISSPA 428
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIpALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAglykptsgsvlldgtDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 429 GswYVSQTPLIKSGLLKEIICKALPLpVDDKSLSEVLHQVGLGKLAARiHDH-------DRwGDILSSGEKQRIALARLI 501
Cdd:cd03245 81 G--YVPQDVTLFYGTLRDNITLGAPL-ADDERILRAAELAGVTDFVNK-HPNgldlqigER-GRGLSGGQRQAVALARAL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446551198 502 LRRPKWIFLDETTSHLEEQEAIRLLRLVREKLPTSGVIMVTHQPGVWNLADDI 554
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRI 208
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
382-555 |
5.44e-20 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 88.86 E-value: 5.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 382 ILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLS---HCWPwFKGDISSPAGSWYvSQTPLIksgllkEIIckalpLPVDD 458
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAgalKGTP-VAGCVDVPDNQFG-REASLI------DAI-----GRKGD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 459 KSLS-EVLHQVGLGKLAA--RIHDHdrwgdiLSSGEKQRIALARLILRRPKWIFLDETTSHLEEQEAIR----LLRLVRE 531
Cdd:COG2401 112 FKDAvELLNAVGLSDAVLwlRRFKE------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRvarnLQKLARR 185
|
170 180
....*....|....*....|....*
gi 446551198 532 KLPTsgVIMVTHQPGVWN-LADDIC 555
Cdd:COG2401 186 AGIT--LVVATHHYDVIDdLQPDLL 208
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
383-515 |
6.59e-20 |
|
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: 86.55 E-value: 6.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 383 LENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSH-------------------CWPWFKGDISspagswYVSQTPLIKSGL 443
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGllsptegtilldgqdltddERKSLRKEIG------YVFQDPQLFPRL 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446551198 444 -LKEII-----CKALPLPVDDKSLSEVLHQVGLGKLAARIHDhdRWGDILSSGEKQRIALARLILRRPKWIFLDETTS 515
Cdd:pfam00005 75 tVRENLrlgllLKGLSKREKDARAEEALEKLGLGDLADRPVG--ERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
349-543 |
8.52e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 92.97 E-value: 8.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 349 HQLTEQRP------TNKPKNCQHAVQVANASIRTPD-NKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFK 421
Cdd:PRK11160 315 NEITEQKPevtfptTSTAAADQVSLTLNNVSFTYPDqPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 422 GDIS---SPAGSW----------YVSQTPLIKSGLLKEIICKALPLPVDDKsLSEVLHQVGLGKLAARIHDHDRW----G 484
Cdd:PRK11160 395 GEILlngQPIADYseaalrqaisVVSQRVHLFSATLRDNLLLAAPNASDEA-LIEVLQQVGLEKLLEDDKGLNAWlgegG 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446551198 485 DILSSGEKQRIALARLILRRPKWIFLDETTSHLE---EQEAIRLLR-LVREKLptsgVIMVTH 543
Cdd:PRK11160 474 RQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDaetERQILELLAeHAQNKT----VLMITH 532
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
364-554 |
4.85e-19 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 86.68 E-value: 4.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 364 QHAVQVANASIRTpDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDIS----SPAGSW----YVSQ 435
Cdd:COG1121 4 MPAIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRlfgkPPRRARrrigYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 436 TP------------LIKSGLLKEIICKALPLPVDDKSLSEVLHQVGLGKLAAR-IHDhdrwgdiLSSGEKQRIALARLIL 502
Cdd:COG1121 83 RAevdwdfpitvrdVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRpIGE-------LSGGQQQRVLLARALA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446551198 503 RRPKWIFLDETTSHLEE--QEAI-RLLR-LVREKLptsGVIMVTHQPG-VWNLADDI 554
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAatEEALyELLReLRREGK---TILVVTHDLGaVREYFDRV 209
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
379-545 |
7.70e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 84.93 E-value: 7.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 379 NKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDISSPAG----SWYVSQTPLI--KSGllkeiiCKAl 452
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGdiddPDVAEACHYLghRNA------MKP- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 453 PLPV-------------DDKSLSEVLHQVGLGKLAarihdHDRWGDiLSSGEKQRIALARLIL-RRPKWIfLDETTSHLE 518
Cdd:PRK13539 87 ALTVaenlefwaaflggEELDIAAALEAVGLAPLA-----HLPFGY-LSAGQKRRVALARLLVsNRPIWI-LDEPTAALD 159
|
170 180
....*....|....*....|....*...
gi 446551198 519 EQEAIRLLRLVREKLPTSG-VIMVTHQP 545
Cdd:PRK13539 160 AAAVALFAELIRAHLAQGGiVIAATHIP 187
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
379-554 |
1.54e-18 |
|
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: 84.58 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 379 NKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDI--------SSPAGSW-----YVSQTPLIKSGLLK 445
Cdd:cd03254 15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIlidgidirDISRKSLrsmigVVLQDTFLFSGTIM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 446 EIICKALPLPvDDKSLSEVLHQVGLGKLAAR-IHDHDRW----GDILSSGEKQRIALARLILRRPKWIFLDETTSHL--- 517
Cdd:cd03254 95 ENIRLGRPNA-TDEEVIEAAKEAGAHDFIMKlPNGYDTVlgenGGNLSQGERQLLAIARAMLRDPKILILDEATSNIdte 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446551198 518 -EE--QEAIRLLRLVReklpTSgvIMVTHQPGVWNLADDI 554
Cdd:cd03254 174 tEKliQEALEKLMKGR----TS--IIIAHRLSTIKNADKI 207
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
368-556 |
2.09e-18 |
|
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: 83.85 E-value: 2.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 368 QVANASIRTPDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLShcwpwfkGDISSPAGS----------------- 430
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILA-------GLIKESSGSillngkpikakerrksi 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 431 WYVSQTP---LIKSGLLKEIICKALPLPVDDKSLSEVLHQVGLGKLAARiHDHDrwgdiLSSGEKQRIALARLILRRPKW 507
Cdd:cd03226 74 GYVMQDVdyqLFTDSVREELLLGLKELDAGNEQAETVLKDLDLYALKER-HPLS-----LSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446551198 508 IFLDETTSHLEEQEAIRLLRLVRE-KLPTSGVIMVTHQPgvwNLADDICD 556
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRElAAQGKAVIVITHDY---EFLAKVCD 194
|
|
| SbmA |
COG1133 |
Peptide antibiotic transporter SbmA/BacA, ABC-type permease family [Defense mechanisms]; |
46-356 |
3.83e-18 |
|
Peptide antibiotic transporter SbmA/BacA, ABC-type permease family [Defense mechanisms];
Pssm-ID: 440748 Cd Length: 408 Bit Score: 86.90 E-value: 3.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 46 VKIQVWLNDWNNDFF----NALSQK---ETDKLWQLVLWFPALLGIFVLISVNKTWLIKLLTIRWREWLTDYYLNRWfad 118
Cdd:COG1133 106 VQVSVAINAWYGPFYdliqKALSKPgsvTIADFYGQMLTFLGIALIAVTVGVLNAFFVSHYVFRWRTAMNDYYMAHW--- 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 119 knyyftqiygEH-KNTDNPDQRIAEDILLLISKTLSLSFGFIQSLSMLITFTVILWqsagTLSFTVggTEWNIQGYMVYT 197
Cdd:COG1133 183 ----------PRlRHIEGASQRVQEDTMRFASIVEGLGVSFIDAVMTLIAFLPVLW----ALSQHV--TELPIIGEVPYS 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 198 VVLIVIG----GTLFTHKVGKRIRPLNVEKQRSEATFRTNLVqhnkqaelIALSNAESLQRQELRDNFHTIKENWHRLmn 273
Cdd:COG1133 247 LVWAAIFwslfGTVLLALVGIKLPGLEFRNQRVEAAYRKELV--------YGEDDAERAQPPTVRELFSNVRRNYFRL-- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 274 rqrwldYWQNIY---SRSL-----SVLPYFLLLPQFISGQINLGGLMKSRQAFMLVSNNLSWFIYKYDELAELAAVIDRL 345
Cdd:COG1133 317 ------YFHYLYfnvARYLylqadNIFPLFILVPSIVAGKITLGLMQQISNAFGQVRSSFQYLVNSWTTIVELLSIYKRL 390
|
330
....*....|.
gi 446551198 346 YEFHQLTEQRP 356
Cdd:COG1133 391 RAFEAAIDDEP 401
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
378-554 |
4.74e-18 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 82.95 E-value: 4.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 378 DNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLS-----------------HCWPWFKGDISspagswYVSQTPL-- 438
Cdd:cd03259 11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAglerpdsgeilidgrdvTGVPPERRNIG------MVFQDYAlf 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 439 --------IKSGLLKeiicKALPLPVDDKSLSEVLHQVGLGklaariHDHDRWGDILSSGEKQRIALARLILRRPKWIFL 510
Cdd:cd03259 85 phltvaenIAFGLKL----RGVPKAEIRARVRELLELVGLE------GLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446551198 511 DETTSHLEEQEAIRLLRLVREKLPTSG--VIMVTHQPG-VWNLADDI 554
Cdd:cd03259 155 DEPLSALDAKLREELREELKELQRELGitTIYVTHDQEeALALADRI 201
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
222-554 |
7.26e-18 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 86.63 E-value: 7.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 222 EKQRSEATfrTNLVQHNKQAElIALSNAESLQRQELRDNfhtIKENWHRLmnRQRWLDyWQNIYSRSLSVL----PYFLL 297
Cdd:TIGR01842 166 KKPLKEAT--EASIRANNLAD-SALRNAEVIEAMGMMGN---LTKRWGRF--HSKYLS-AQSAASDRAGMLsnlsKYFRI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 298 LPQF----------ISGQINlGGLMKSRQAFM---------LVSNNLSWF--IYKYDELAELaavidrlyeFHQLTEQRP 356
Cdd:TIGR01842 237 VLQSlvlglgaylaIDGEIT-PGMMIAGSILVgralapidgAIGGWKQFSgaRQAYKRLNEL---------LANYPSRDP 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 357 TNKPKNCQHAVQVANASIRTPD-NKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDI---SSPAGSW- 431
Cdd:TIGR01842 307 AMPLPEPEGHLSVENVTIVPPGgKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVrldGADLKQWd 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 432 ---------YVSQTPLIKSGLLKEIICKaLPLPVDDKSLSEVLHQVGLGKLAARIHD-HDRW----GDILSSGEKQRIAL 497
Cdd:TIGR01842 387 retfgkhigYLPQDVELFPGTVAENIAR-FGENADPEKIIEAAKLAGVHELILRLPDgYDTVigpgGATLSGGQRQRIAL 465
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 446551198 498 ARLILRRPKWIFLDETTSHLEEQEAIRLLR-LVREKLPTSGVIMVTHQPGVWNLADDI 554
Cdd:TIGR01842 466 ARALYGDPKLVVLDEPNSNLDEEGEQALANaIKALKARGITVVVITHRPSLLGCVDKI 523
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
378-545 |
8.86e-18 |
|
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: 81.77 E-value: 8.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 378 DNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDISSP-------AGSW-----YVSQTPLIKSGLLK 445
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNggpldfqRDSIargllYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 446 EIICKALPLPVDDKSLSEVLHQVGLGKLaarihdHDRWGDILSSGEKQRIALARLIL-RRPKWIfLDETTSHLEEQEAIR 524
Cdd:cd03231 91 LENLRFWHADHSDEQVEEALARVGLNGF------EDRPVAQLSAGQQRRVALARLLLsGRPLWI-LDEPTTALDKAGVAR 163
|
170 180
....*....|....*....|..
gi 446551198 525 LLRLVREKLPTSG-VIMVTHQP 545
Cdd:cd03231 164 FAEAMAGHCARGGmVVLTTHQD 185
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
378-545 |
9.56e-18 |
|
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: 81.64 E-value: 9.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 378 DNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDISSP-------AGSW-----YVSQTPLIKSGL-- 443
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNgtplaeqRDEPhenilYLGHLPGLKPELsa 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 444 LKEIICKALPLPVDDKSLSEVLHQVGLGKLAarihdhDRWGDILSSGEKQRIALARLIL-RRPKWIfLDETTSHLEEQEA 522
Cdd:TIGR01189 91 LENLHFWAAIHGGAQRTIEDALAAVGLTGFE------DLPAAQLSAGQQRRLALARLWLsRRPLWI-LDEPTTALDKAGV 163
|
170 180
....*....|....*....|....
gi 446551198 523 IRLLRLVREKLPTSG-VIMVTHQP 545
Cdd:TIGR01189 164 ALLAGLLRAHLARGGiVLLTTHQD 187
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
382-558 |
1.17e-17 |
|
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: 81.77 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 382 ILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLShcwpwfkGDISSPAGSWYVSQTPLIKSG------------------- 442
Cdd:cd03255 19 ALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILG-------GLDRPTSGEVRVDGTDISKLSekelaafrrrhigfvfqsf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 443 -LLKEIICK---ALPLPVDDKSLSE-------VLHQVGLGklaariHDHDRWGDILSSGEKQRIALARLILRRPKWIFLD 511
Cdd:cd03255 92 nLLPDLTALenvELPLLLAGVPKKErreraeeLLERVGLG------DRLNHYPSELSGGQQQRVAIARALANDPKIILAD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446551198 512 ETTSHLEEQEAIRLLRLVREKLPTSG--VIMVTHQPGVWNLADDICDIS 558
Cdd:cd03255 166 EPTGNLDSETGKEVMELLRELNKEAGttIVVVTHDPELAEYADRIIELR 214
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
364-554 |
1.74e-17 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 85.57 E-value: 1.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 364 QHAVQVANASIRTP-DNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKG-------DISSpagsW---- 431
Cdd:COG4618 328 KGRLSVENLTVVPPgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGsvrldgaDLSQ----Wdree 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 432 ------YVSQTPLIKSGLLKEIICKaLPLPVDDKslseVLHqvglgklAARIHD-HD-----------RWGD---ILSSG 490
Cdd:COG4618 404 lgrhigYLPQDVELFDGTIAENIAR-FGDADPEK----VVA-------AAKLAGvHEmilrlpdgydtRIGEggaRLSGG 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446551198 491 EKQRIALARLILRRPKWIFLDETTSHLEEQ-EA--IRLLRLVREKLPTsgVIMVTHQPGVWNLADDI 554
Cdd:COG4618 472 QRQRIGLARALYGDPRLVVLDEPNSNLDDEgEAalAAAIRALKARGAT--VVVITHRPSLLAAVDKL 536
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
366-543 |
1.85e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 82.13 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 366 AVQVANASIRTpDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLShcwpwfkGDISSPAGSWYVSQTPL--IKSGL 443
Cdd:PRK13548 2 MLEARNLSVRL-GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALS-------GELSPDSGEVRLNGRPLadWSPAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 444 L-------------------KEII-CKALPLPV----DDKSLSEVLHQVGLGKLAARIHDHdrwgdiLSSGEKQRIALAR 499
Cdd:PRK13548 74 LarrravlpqhsslsfpftvEEVVaMGRAPHGLsraeDDALVAAALAQVDLAHLAGRDYPQ------LSGGEQQRVQLAR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446551198 500 LILR------RPKWIFLDETTSHLEEQEAIRLLRLVREKLPTSG--VIMVTH 543
Cdd:PRK13548 148 VLAQlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGlaVIVVLH 199
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
367-543 |
3.48e-17 |
|
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: 80.62 E-value: 3.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 367 VQVANASIR-TPDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDI----------------SSPAG 429
Cdd:cd03244 3 IEFKNVSLRyRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSIlidgvdiskiglhdlrSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 430 swyVSQTPLIKSGLLKEIICkalPLPV-DDKSLSEVLHQVGL--------GKLAARIHDHdrwGDILSSGEKQRIALARL 500
Cdd:cd03244 83 ---IPQDPVLFSGTIRSNLD---PFGEySDEELWQALERVGLkefveslpGGLDTVVEEG---GENLSVGQRQLLCLARA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446551198 501 ILRRPKWIFLDETTSHLEEQEAIRLLRLVREKLPTSGVIMVTH 543
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAH 196
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
367-561 |
6.13e-17 |
|
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: 80.24 E-value: 6.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 367 VQVANASIRTPDNKI---ILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWP------WFKG-DISSPAGSW----- 431
Cdd:cd03257 2 LEVKNLSVSFPTGGGsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKptsgsiIFDGkDLLKLSRRLrkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 432 ----YVSQTPLikSGL-----LKEIICKAL-----PLPVDDKSLSEVLHQVGLGKLAARIHD--HDrwgdiLSSGEKQRI 495
Cdd:cd03257 82 keiqMVFQDPM--SSLnprmtIGEQIAEPLrihgkLSKKEARKEAVLLLLVGVGLPEEVLNRypHE-----LSGGQRQRV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446551198 496 ALARLILRRPKWIFLDETTSHLE---EQEAIRLLRLVREKLPTSgVIMVTHQPGVwnlADDICDISAVL 561
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDvsvQAQILDLLKKLQEELGLT-LLFITHDLGV---VAKIADRVAVM 219
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
367-554 |
7.58e-17 |
|
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: 79.05 E-value: 7.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 367 VQVANASIRTPDNKI----ILENLNFHVSPGKWLLLKGYSGAGKTTLLKTL---SHCwpwFKGDISSPAGSWYVSQTPLI 439
Cdd:cd03250 1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgeLEK---LSGSVSVPGSIAYVSQEPWI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 440 KSGLLKEIICKALPLpvDDKSLSEVLHQVGLGKLAARIHDHDRW-----GDILSSGEKQRIALARLILRRPKWIFLD--- 511
Cdd:cd03250 78 QNGTIRENILFGKPF--DEERYEKVIKACALEPDLEILPDGDLTeigekGINLSGGQKQRISLARAVYSDADIYLLDdpl 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446551198 512 -----ETTSHLEEQEAIRLLRLVReklpTsgVIMVTHQPGVWNLADDI 554
Cdd:cd03250 156 savdaHVGRHIFENCILGLLLNNK----T--RILVTHQLQLLPHADQI 197
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
364-561 |
1.36e-16 |
|
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: 82.64 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 364 QHAVQVANASIRTPDNKI-ILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWP---------WFKG-DISSPAGSW- 431
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggrisgevLLDGrDLLELSEALr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 432 -----YVSQTP---LIKSGLLKEII--CKALPLPVDD--KSLSEVLHQVGLGKLAarihdhDRWGDILSSGEKQRIALAR 499
Cdd:COG1123 82 grrigMVFQDPmtqLNPVTVGDQIAeaLENLGLSRAEarARVLELLEAVGLERRL------DRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446551198 500 LILRRPKWIFLDETTSHLE---EQEAIRLLRLVREKLPTSgVIMVTHQPGVwnlADDICDISAVL 561
Cdd:COG1123 156 ALALDPDLLIADEPTTALDvttQAEILDLLRELQRERGTT-VLLITHDLGV---VAEIADRVVVM 216
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
366-545 |
1.96e-16 |
|
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: 78.97 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 366 AVQVANASIRTpDNKIILENLNFHVSPG-KWLLLkGYSGAGKTTLLKTLS--HcWPWFKGDIS---SPAGSW-------- 431
Cdd:COG1119 3 LLELRNVTVRR-GGKTILDDISWTVKPGeHWAIL-GPNGAGKSTLLSLITgdL-PPTYGNDVRlfgERRGGEdvwelrkr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 432 --YVS---QTPLIKSGLLKEIICKAL---------PLPVDDKSLSEVLHQVGLGKLAARihdhdRWGDiLSSGEKQRIAL 497
Cdd:COG1119 80 igLVSpalQLRFPRDETVLDVVLSGFfdsiglyrePTDEQRERARELLELLGLAHLADR-----PFGT-LSQGEQRRVLI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446551198 498 ARLILRRPKWIFLDETTSHLEEQEAIRLLRLVRE--KLPTSGVIMVTHQP 545
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHV 203
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
380-554 |
2.11e-16 |
|
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: 78.47 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 380 KIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLS---HCWPWFKGDI------SSPAgSW-----YVSQTPLIKSGL-L 444
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQIlfngqpRKPD-QFqkcvaYVRQDDILLPGLtV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 445 KEII--CKALPLPV--DDKSLSEVLHQVGLGKLAARIHDHDRWGDIlSSGEKQRIALARLILRRPKWIFLDETTSHLEEQ 520
Cdd:cd03234 99 RETLtyTAILRLPRksSDAIRKKRVEDVLLRDLALTRIGGNLVKGI-SGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 446551198 521 EAIRLLRLVREkLPTSG--VIMVTHQPG--VWNLADDI 554
Cdd:cd03234 178 TALNLVSTLSQ-LARRNriVILTIHQPRsdLFRLFDRI 214
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
367-554 |
3.82e-16 |
|
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: 76.46 E-value: 3.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 367 VQVANASIRTPDnKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLShcwpwfkGDISSPAGSWYVSQTPLIKSGLLKE 446
Cdd:cd03229 1 LELKNVSKRYGQ-KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIA-------GLEEPDSGSILIDGEDLTDLEDELP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 447 IICKALPLPVDDKSL---SEVLHQVGLGklaarihdhdrwgdiLSSGEKQRIALARLILRRPKWIFLDETTSHLE---EQ 520
Cdd:cd03229 73 PLRRRIGMVFQDFALfphLTVLENIALG---------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDpitRR 137
|
170 180 190
....*....|....*....|....*....|....*
gi 446551198 521 EAIRLLRLVREKLPTSgVIMVTHQPG-VWNLADDI 554
Cdd:cd03229 138 EVRALLKSLQAQLGIT-VVLVTHDLDeAARLADRV 171
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
373-555 |
4.29e-16 |
|
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: 76.82 E-value: 4.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 373 SIRTPDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLShcwpwfkGDISSPA--GSWYVSQTPLIKSgLLKEIICK 450
Cdd:cd03213 15 SSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALA-------GRRTGLGvsGEVLINGRPLDKR-SFRKIIGY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 451 AlplPVDDKSLS-----EVLHqvglgkLAARIHDhdrwgdiLSSGEKQRIALARLILRRPKWIFLDETTSHLEEQEAIRL 525
Cdd:cd03213 87 V---PQDDILHPtltvrETLM------FAAKLRG-------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQV 150
|
170 180 190
....*....|....*....|....*....|....
gi 446551198 526 LRLVReKLPTSG--VIMVTHQPG--VWNLADDIC 555
Cdd:cd03213 151 MSLLR-RLADTGrtIICSIHQPSseIFELFDKLL 183
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
376-561 |
4.87e-16 |
|
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: 77.62 E-value: 4.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 376 TPDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKG-------DISSPAGS---------WYVSQT-PL 438
Cdd:cd03258 14 TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGsvlvdgtDLTLLSGKelrkarrriGMIFQHfNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 439 IKSGLLKEIIckALPLPVDDKSLSEV-------LHQVGLGklaariHDHDRWGDILSSGEKQRIALARLILRRPKWIFLD 511
Cdd:cd03258 94 LSSRTVFENV--ALPLEIAGVPKAEIeervlelLELVGLE------DKADAYPAQLSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446551198 512 ETTSHLEE---QEAIRLLRLVREKL-PTsgVIMVTHQPGVwnlADDICDISAVL 561
Cdd:cd03258 166 EATSALDPettQSILALLRDINRELgLT--IVLITHEMEV---VKRICDRVAVM 214
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
371-543 |
6.92e-16 |
|
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: 76.68 E-value: 6.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 371 NASIRTPDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLShcwpwfkGDISSPAGSWYVSQTPLikSGLLKEIICK 450
Cdd:cd03292 5 NVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIY-------KEELPTSGTIRVNGQDV--SDLRGRAIPY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 451 ------------------------ALPLPVDD-------KSLSEVLHQVGLGklaariHDHDRWGDILSSGEKQRIALAR 499
Cdd:cd03292 76 lrrkigvvfqdfrllpdrnvyenvAFALEVTGvppreirKRVPAALELVGLS------HKHRALPAELSGGEQQRVAIAR 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446551198 500 LILRRPKWIFLDETTSHLEEQEAIRLLRLVrEKLPTSG--VIMVTH 543
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTWEIMNLL-KKINKAGttVVVATH 194
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
377-533 |
8.81e-16 |
|
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: 76.81 E-value: 8.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 377 PDNKIiLENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKG-------DISSPAGSW------YVSQTPLIKSGL 443
Cdd:cd03249 14 PDVPI-LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGeilldgvDIRDLNLRWlrsqigLVSQEPVLFDGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 444 LKEIICKALPlpvdDKSLSEVLHQVGLgklaARIHDH-------------DRwGDILSSGEKQRIALARLILRRPKWIFL 510
Cdd:cd03249 93 IAENIRYGKP----DATDEEVEEAAKK----ANIHDFimslpdgydtlvgER-GSQLSGGQKQRIAIARALLRNPKILLL 163
|
170 180
....*....|....*....|....
gi 446551198 511 DETTSHLE-EQEAIrllrlVREKL 533
Cdd:cd03249 164 DEATSALDaESEKL-----VQEAL 182
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
368-556 |
1.10e-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: 76.84 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 368 QVANASIRTPDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLShcwpwfkGDISSPAGSWYV---SQTPLIKSGL- 443
Cdd:cd03256 2 EVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLN-------GLVEPTSGSVLIdgtDINKLKGKALr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 444 ---------------------LKEIICKALP-----------LPVDDKSL-SEVLHQVGLGKLAARihdhdRwGDILSSG 490
Cdd:cd03256 75 qlrrqigmifqqfnlierlsvLENVLSGRLGrrstwrslfglFPKEEKQRaLAALERVGLLDKAYQ-----R-ADQLSGG 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446551198 491 EKQRIALARLILRRPKWIFLDETTSHLEEQEAIRLLRLVREKLPTSG--VIMVTHQPgvwNLADDICD 556
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGitVIVSLHQV---DLAREYAD 213
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
367-543 |
1.24e-15 |
|
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: 75.04 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 367 VQVANASIRTPDN-KIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLShcwpwfkGDISSPAGSWYVSQTPLIK-SGLL 444
Cdd:cd03247 1 LSINNVSFSYPEQeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLT-------GDLKPQQGEITLDGVPVSDlEKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 445 KEIICkalplpvddkslseVLHQvglgklaaRIHDHD-----RWGDILSSGEKQRIALARLILRRPKWIFLDETTSHLEE 519
Cdd:cd03247 74 SSLIS--------------VLNQ--------RPYLFDttlrnNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDP 131
|
170 180
....*....|....*....|....
gi 446551198 520 QEAIRLLRLVREKLPTSGVIMVTH 543
Cdd:cd03247 132 ITERQLLSLIFEVLKDKTLIWITH 155
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
378-561 |
1.36e-15 |
|
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: 76.39 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 378 DNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLShcwpwfkGDISSPAGSWYVSQTPLIK--SGLLKEIICK----- 450
Cdd:cd03261 11 GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIV-------GLLRPDSGEVLIDGEDISGlsEAELYRLRRRmgmlf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 451 ---------------ALPL--------PVDDKSLSEVLHQVGLGklaariHDHDRWGDILSSGEKQRIALARLILRRPKW 507
Cdd:cd03261 84 qsgalfdsltvfenvAFPLrehtrlseEEIREIVLEKLEAVGLR------GAEDLYPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446551198 508 IFLDETTSHLE---EQEAIRLLRLVREKLPTSgVIMVTHQpgvWNLADDICDISAVL 561
Cdd:cd03261 158 LLYDEPTAGLDpiaSGVIDDLIRSLKKELGLT-SIMVTHD---LDTAFAIADRIAVL 210
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
380-543 |
1.68e-15 |
|
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: 75.59 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 380 KIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDIS---------SPAGSwYVSQTPLI---KSgLLKEI 447
Cdd:cd03293 17 VTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLvdgepvtgpGPDRG-YVFQQDALlpwLT-VLDNV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 448 ickALPL---PVDDKSL----SEVLHQVGLGKLAarihdhDRWGDILSSGEKQRIALARLILRRPKWIFLDETTSHLEEQ 520
Cdd:cd03293 95 ---ALGLelqGVPKAEAreraEELLELVGLSGFE------NAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDAL 165
|
170 180
....*....|....*....|....*..
gi 446551198 521 --EAIR--LLRLVREKLPTsgVIMVTH 543
Cdd:cd03293 166 trEQLQeeLLDIWRETGKT--VLLVTH 190
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
382-552 |
1.88e-15 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 75.85 E-value: 1.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 382 ILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLShC--WP-----WFKG-DIS--SPA----------GswYVSQT----- 436
Cdd:COG1136 23 ALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILG-GldRPtsgevLIDGqDISslSERelarlrrrhiG--FVFQFfnllp 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 437 ----------PLIKSGllkeiickaLPLPVDDKSLSEVLHQVGLGKLA-ARIHDhdrwgdiLSSGEKQRIALARLILRRP 505
Cdd:COG1136 100 eltalenvalPLLLAG---------VSRKERRERARELLERVGLGDRLdHRPSQ-------LSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446551198 506 KWIFLDETTSHLEEQ---EAIRLLR-LVREKlpTSGVIMVTHQPGVWNLAD 552
Cdd:COG1136 164 KLILADEPTGNLDSKtgeEVLELLReLNREL--GTTIVMVTHDPELAARAD 212
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
378-556 |
2.09e-15 |
|
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: 76.05 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 378 DNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLS------------------HCWPWFKGDISspagswYVSQTPLI 439
Cdd:COG4555 12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAgllkpdsgsilidgedvrKEPREARRQIG------VLPDERGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 440 KSGL-LKEII---CKALPLPVDD--KSLSEVLHQVGLGKLAARihdhdRWGDiLSSGEKQRIALARLILRRPKWIFLDET 513
Cdd:COG4555 86 YDRLtVRENIryfAELYGLFDEElkKRIEELIELLGLEEFLDR-----RVGE-LSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446551198 514 TSHLeEQEAIRLLRLVREKLPTSG--VIMVTHQPgvwNLADDICD 556
Cdd:COG4555 160 TNGL-DVMARRLLREILRALKKEGktVLFSSHIM---QEVEALCD 200
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
378-556 |
2.22e-15 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 75.87 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 378 DNKIILENLNFHVSPGKWL-LLkGYSGAGKTTLLKTLShcwpwfkG--------------DISSPAGSW-----YVSQTP 437
Cdd:COG1131 11 GDKTALDGVSLTVEPGEIFgLL-GPNGAGKTTTIRMLL-------GllrptsgevrvlgeDVARDPAEVrrrigYVPQEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 438 LIKSGL-LKEII-----CKALPLPVDDKSLSEVLHQVGLGKLAARIHDHdrwgdiLSSGEKQRIALARLILRRPKWIFLD 511
Cdd:COG1131 83 ALYPDLtVRENLrffarLYGLPRKEARERIDELLELFGLTDAADRKVGT------LSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446551198 512 ETTSHLEEQEAIRLLRLVREkLPTSG--VIMVTHqpgvwNL--ADDICD 556
Cdd:COG1131 157 EPTSGLDPEARRELWELLRE-LAAEGktVLLSTH-----YLeeAERLCD 199
|
|
| PRK11098 |
PRK11098 |
peptide antibiotic transporter SbmA; |
46-356 |
3.96e-15 |
|
peptide antibiotic transporter SbmA;
Pssm-ID: 182960 Cd Length: 409 Bit Score: 77.35 E-value: 3.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 46 VKIQVWLNDWNNDFF----NALSQKETDKLWQLVLWFPALLGI---FVLISVNKTWLIKLLTIRWREWLTDYYLNRWfad 118
Cdd:PRK11098 105 VQVSVAVNAWYAPFYdliqTALSSPGKVTIGQFYSEVGVFLGIaliAVVISVLNNFFVSHYVFRWRTAMNEYYMAHW--- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 119 knYYFTQIYGehkntdnPDQRIAEDILLLISKTLSLSFGFIQSLSMLITFTVILWQsagtLSFTVggTEWNIQGYMVYTV 198
Cdd:PRK11098 182 --QKLRHIEG-------AAQRVQEDTMRFASTLENLGVSFINAIMTLIAFLPVLVT----LSAHV--PELPIVGHIPYGL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 199 VLIVI----GGTLFTHKVGKRIRPLNVEKQRSEATFRTNLVqhnkqaelIALSNAESLQRQELRDNFHTIKENWHRLmnr 274
Cdd:PRK11098 247 VIAAIvwslFGTGLLAVVGIKLPGLEFKNQRVEAAYRKELV--------YGEDDADRATPPTVRELFSNVRKNYFRL--- 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 275 qrwldYWQNIY---SRSL-----SVLPYFLLLPQFISGQINLGGLMKSRQAFMLVSNNLSWFIYKYDELAELAAVIDRLY 346
Cdd:PRK11098 316 -----YFHYMYfniARILylqvdNVFGLFLLFPSIVAGTITLGLMTQITNVFGQVRGSFQYLINSWTTIVELLSIYKRLR 390
|
330
....*....|
gi 446551198 347 EFHQLTEQRP 356
Cdd:PRK11098 391 SFEAALDGEP 400
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
372-545 |
4.88e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 74.07 E-value: 4.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 372 ASIRtpDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDISspagsW-----------------YVS 434
Cdd:PRK13538 8 ACER--DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVL-----WqgepirrqrdeyhqdllYLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 435 QTPLIKSGLLKE---IICKALPLPVDDKSLSEVLHQVGLGK---LAARIhdhdrwgdiLSSGEKQRIALARLIL-RRPKW 507
Cdd:PRK13538 81 HQPGIKTELTALenlRFYQRLHGPGDDEALWEALAQVGLAGfedVPVRQ---------LSAGQQRRVALARLWLtRAPLW 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 446551198 508 IfLDETTSHLEEQEAIRLLRLVREKLPTSG-VIMVTHQP 545
Cdd:PRK13538 152 I-LDEPFTAIDKQGVARLEALLAQHAEQGGmVILTTHQD 189
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
379-556 |
5.36e-15 |
|
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: 72.82 E-value: 5.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 379 NKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLShcwpwfkGDISSPAGSWYVSQTPLIKSGL-LKEIICkALP---- 453
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIIL-------GLLKPDSGEIKVLGKDIKKEPEeVKRRIG-YLPeeps 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 454 LPvDDKSLSEVLHqvglgklaarihdhdrwgdiLSSGEKQRIALARLILRRPKWIFLDETTSHLEEQEAIRLLRLVREkL 533
Cdd:cd03230 84 LY-ENLTVRENLK--------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRE-L 141
|
170 180
....*....|....*....|....*
gi 446551198 534 PTSG--VIMVTHqpgVWNLADDICD 556
Cdd:cd03230 142 KKEGktILLSSH---ILEEAERLCD 163
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
366-543 |
1.23e-14 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 73.97 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 366 AVQVANASIR---TPDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLShcwpwfkG--------------DISSPA 428
Cdd:COG1116 7 ALELRGVSKRfptGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIA-------GlekptsgevlvdgkPVTGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 429 GSW-YVSQTPLiksgLL-----KEIIckALPLPVDDKSLSEV-------LHQVGLGKLAarihdhDRWGDILSSGEKQRI 495
Cdd:COG1116 80 PDRgVVFQEPA----LLpwltvLDNV--ALGLELRGVPKAERrerarelLELVGLAGFE------DAYPHQLSGGMRQRV 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446551198 496 ALARLILRRPKWIFLDE--------TTSHLEEQeairLLRLVREKLPTsgVIMVTH 543
Cdd:COG1116 148 AIARALANDPEVLLMDEpfgaldalTRERLQDE----LLRLWQETGKT--VLFVTH 197
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
378-554 |
1.34e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 73.21 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 378 DNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTL-SHCWP-----WFKG-DISSPAGSWY---VS---QTPLiksgLL 444
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVaSLISPtsgtlLFEGeDISTLKPEIYrqqVSycaQTPT----LF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 445 KEIICKALPLP-------VDDKSLSEVLHQVGLGK--LAARIHDhdrwgdiLSSGEKQRIALARLILRRPKWIFLDETTS 515
Cdd:PRK10247 94 GDTVYDNLIFPwqirnqqPDPAIFLDDLERFALPDtiLTKNIAE-------LSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446551198 516 HLEEQ------EAIRllRLVREKlpTSGVIMVTHQPGVWNLADDI 554
Cdd:PRK10247 167 ALDESnkhnvnEIIH--RYVREQ--NIAVLWVTHDKDEINHADKV 207
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
343-544 |
2.19e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 76.04 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 343 DRLYEF--HQLTEQRPTNKPKNCQHAVQVA--NASIRTPDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWP 418
Cdd:PRK11174 322 ESLVTFleTPLAHPQQGEKELASNDPVTIEaeDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 419 wFKGDI--------SSPAGSW-----YVSQTPLIKSGLLKEIICKALPLPVDDK--------SLSEVLHQVGLGkLAARI 477
Cdd:PRK11174 402 -YQGSLkingielrELDPESWrkhlsWVGQNPQLPHGTLRDNVLLGNPDASDEQlqqalenaWVSEFLPLLPQG-LDTPI 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446551198 478 HDHdrwGDILSSGEKQRIALARLILRRPKWIFLDETTSHLEEQEAIRLLRLVREKLPTSGVIMVTHQ 544
Cdd:PRK11174 480 GDQ---AAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQ 543
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
383-554 |
2.53e-14 |
|
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: 70.92 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 383 LENLNFHVSPGKWLLLKGYSGAGKTTLLKTLShcwpwfkGDISSPAGSWYVSQTPL-IKSgllkeiICKALPLPVddksl 461
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILS-------GLYKPDSGEILVDGKEVsFAS------PRDARRAGI----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 462 sEVLHQvglgklaarihdhdrwgdiLSSGEKQRIALARLILRRPKWIFLDETTSHLEEQEAIRLLRLVReKLPTSG--VI 539
Cdd:cd03216 78 -AMVYQ-------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIR-RLRAQGvaVI 136
|
170
....*....|....*.
gi 446551198 540 MVTHQPG-VWNLADDI 554
Cdd:cd03216 137 FISHRLDeVFEIADRV 152
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
360-554 |
2.65e-14 |
|
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: 72.50 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 360 PKNCQHAVQVANASI--RTPDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDI---SSPAGSW--- 431
Cdd:cd03248 5 PDHLKGIVKFQNVTFayPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVlldGKPISQYehk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 432 -------YVSQTPLIKSGLLKEIICKALPlpvdDKSLSEVLhqvglgKLAARIHDHD--------------RWGDILSSG 490
Cdd:cd03248 85 ylhskvsLVGQEPVLFARSLQDNIAYGLQ----SCSFECVK------EAAQKAHAHSfiselasgydtevgEKGSQLSGG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446551198 491 EKQRIALARLILRRPKWIFLDETTSHLEEQEAIRLLRLVREKLPTSGVIMVTHQPGVWNLADDI 554
Cdd:cd03248 155 QKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQI 218
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
377-543 |
3.07e-14 |
|
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: 72.26 E-value: 3.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 377 PDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLshcwpwFK-GDISSpaGSWYVSQTPlIKSgllkeiickalplp 455
Cdd:cd03253 11 DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLL------FRfYDVSS--GSILIDGQD-IRE-------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 456 VDDKSLSE---------------VLHQVGLGKL------------AARIHDH-------------DRwGDILSSGEKQRI 495
Cdd:cd03253 68 VTLDSLRRaigvvpqdtvlfndtIGYNIRYGRPdatdeevieaakAAQIHDKimrfpdgydtivgER-GLKLSGGEKQRV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446551198 496 ALARLILRRPKWIFLDETTSHLE---EQEAIRLLRLVREKLPTsgvIMVTH 543
Cdd:cd03253 147 AIARAILKNPPILLLDEATSALDthtEREIQAALRDVSKGRTT---IVIAH 194
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
127-520 |
6.01e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 74.76 E-value: 6.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 127 YGEHKnTDNPDQRIAEDILLlISKTLSLSFG-FIQSLSMLITFTVILWQSAGTLSFtvggtewniqgymvytVVLIVIGG 205
Cdd:TIGR00958 252 FDENK-TGELTSRLSSDTQT-MSRSLSLNVNvLLRNLVMLLGLLGFMLWLSPRLTM----------------VTLINLPL 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 206 TLFTHKV-GKRIRPLNVEKQrsEATFRTNlvqhnkQAELIALSN--------AESLQRQELRDNFHTIKEnwhrlMNRQR 276
Cdd:TIGR00958 314 VFLAEKVfGKRYQLLSEELQ--EAVAKAN------QVAEEALSGmrtvrsfaAEEGEASRFKEALEETLQ-----LNKRK 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 277 WLDYWQNIYSRSLSVLPYFLLLpQFISGQINLGGLMKSRQ--AFML----VSNNLSWFIYKYDELAELAAVIDRLYEFHQ 350
Cdd:TIGR00958 381 ALAYAGYLWTTSVLGMLIQVLV-LYYGGQLVLTGKVSSGNlvSFLLyqeqLGEAVRVLSYVYSGMMQAVGASEKVFEYLD 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 351 LTEQRPTN---KPKNCQHAVQVANASIRTPD--NKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKG--- 422
Cdd:TIGR00958 460 RKPNIPLTgtlAPLNLEGLIEFQDVSFSYPNrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGqvl 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 423 ----DISSPAGSWY------VSQTPLIKSGLLKEIICKALPLPVDDKSLSEVlhqvglgkLAARIHDH------------ 480
Cdd:TIGR00958 540 ldgvPLVQYDHHYLhrqvalVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAA--------KAANAHDFimefpngydtev 611
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 446551198 481 DRWGDILSSGEKQRIALARLILRRPKWIFLDETTSHLEEQ 520
Cdd:TIGR00958 612 GEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAE 651
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
383-554 |
1.01e-13 |
|
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: 70.83 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 383 LENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDIS---------SPA--GSWYVSQTPL----------IKS 441
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILlngkditnlPPEkrDISYVPQNYAlfphmtvyknIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 442 GLLKEIICKalplPVDDKSLSEVLHQVGLGKLAarihdhDRWGDILSSGEKQRIALARLILRRPKWIFLDETTSHLEEQ- 520
Cdd:cd03299 95 GLKKRKVDK----KEIERKVLEIAEMLGIDHLL------NRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRt 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 446551198 521 --EAIRLLRLVREKLPTSgVIMVTH-QPGVWNLADDI 554
Cdd:cd03299 165 keKLREELKKIRKEFGVT-VLHVTHdFEEAWALADKV 200
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
376-533 |
1.21e-13 |
|
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: 70.72 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 376 TPDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWpwfkgDISSpaGS--------------------WYVSQ 435
Cdd:cd03251 11 PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFY-----DVDS--GRilidghdvrdytlaslrrqiGLVSQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 436 TPLIKSGLLKEIICKALPlpvdDKSLSEVLHqvglgklAARI-HDHD---------------RwGDILSSGEKQRIALAR 499
Cdd:cd03251 84 DVFLFNDTVAENIAYGRP----GATREEVEE-------AARAaNAHEfimelpegydtvigeR-GVKLSGGQRQRIAIAR 151
|
170 180 190
....*....|....*....|....*....|....*
gi 446551198 500 LILRRPKWIFLDETTSHLE-EQEairllRLVREKL 533
Cdd:cd03251 152 ALLKDPPILILDEATSALDtESE-----RLVQAAL 181
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
377-554 |
1.42e-13 |
|
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: 70.59 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 377 PDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKG-------DISSPAGSWY------VSQTPLIKSGL 443
Cdd:cd03252 12 PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGrvlvdghDLALADPAWLrrqvgvVLQENVLFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 444 LKEIICKALPLPvddkSLSEVLHqvglgklAARIHD-HD--------------RWGDILSSGEKQRIALARLILRRPKWI 508
Cdd:cd03252 92 IRDNIALADPGM----SMERVIE-------AAKLAGaHDfiselpegydtivgEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446551198 509 FLDETTSHLEEQEAIRLLRLVREKLPTSGVIMVTHQPGVWNLADDI 554
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRI 206
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
366-532 |
1.44e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 73.21 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 366 AVQVANASIRTPDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDI---SSPAGSW----------Y 432
Cdd:PRK10790 340 RIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIrldGRPLSSLshsvlrqgvaM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 433 VSQTPLIKSGLLKEIIckALPLPVDDKSLSEVLHQVGLGKLAARIHD--HDRWGD---ILSSGEKQRIALARLILRRPKW 507
Cdd:PRK10790 420 VQQDPVVLADTFLANV--TLGRDISEEQVWQALETVQLAELARSLPDglYTPLGEqgnNLSVGQKQLLALARVLVQTPQI 497
|
170 180
....*....|....*....|....*...
gi 446551198 508 IFLDETTSHLE---EQEAIRLLRLVREK 532
Cdd:PRK10790 498 LILDEATANIDsgtEQAIQQALAAVREH 525
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
342-555 |
1.79e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 73.16 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 342 IDRLYEFHQLTEQRPTNKPKNCQHAVQvanasirtPDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPwfK 421
Cdd:TIGR00955 8 SDVFGRVAQDGSWKQLVSRLRGCFCRE--------RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSP--K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 422 G-DISS-------PAGSW-------YVSQTPL-IKSGLLKE--IICKALPLPVDDKS------LSEVLHQVGLGKLA-AR 476
Cdd:TIGR00955 78 GvKGSGsvllngmPIDAKemraisaYVQQDDLfIPTLTVREhlMFQAHLRMPRRVTKkekrerVDEVLQALGLRKCAnTR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 477 IHDHDRWGDiLSSGEKQRIALARLILRRPKWIFLDETTSHLEEQEAIRLLRLVReKLPTSG--VIMVTHQPG--VWNLAD 552
Cdd:TIGR00955 158 IGVPGRVKG-LSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLK-GLAQKGktIICTIHQPSseLFELFD 235
|
...
gi 446551198 553 DIC 555
Cdd:TIGR00955 236 KII 238
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
367-543 |
6.60e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 69.27 E-value: 6.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 367 VQVANASIRTPDN-KIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDIS------SPAGSW-------Y 432
Cdd:PRK13635 6 IRVEHISFRYPDAaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITvggmvlSEETVWdvrrqvgM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 433 VSQTP----------------LIKSGLlkeiickalplPVDD--KSLSEVLHQVGLGKLAARIHDHdrwgdiLSSGEKQR 494
Cdd:PRK13635 86 VFQNPdnqfvgatvqddvafgLENIGV-----------PREEmvERVDQALRQVGMEDFLNREPHR------LSGGQKQR 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446551198 495 IALARLILRRPKWIFLDETTSHLEEQ------EAIRllRLVREKLPTsgVIMVTH 543
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDPRgrrevlETVR--QLKEQKGIT--VLSITH 199
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
378-543 |
8.68e-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: 67.60 E-value: 8.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 378 DNKIILENLNFHVSPGKWLLLkGYSGAGKTTLLKTLSHCWP------WFKG-DISSPAGSW-----YVSQTPLIKS---- 441
Cdd:cd03264 11 GKKRALDGVSLTLGPGMYGLL-GPNGAGKTTLMRILATLTPpssgtiRIDGqDVLKQPQKLrrrigYLPQEFGVYPnftv 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 442 -------GLLKEIICKALPLPVDdkslsEVLHQVGLGKlaariHDHDRWGDiLSSGEKQRIALARLILRRPKWIFLDETT 514
Cdd:cd03264 90 refldyiAWLKGIPSKEVKARVD-----EVLELVNLGD-----RAKKKIGS-LSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180
....*....|....*....|....*....
gi 446551198 515 SHLEEQEAIRLLRLVREKLPTSGVIMVTH 543
Cdd:cd03264 159 AGLDPEERIRFRNLLSELGEDRIVILSTH 187
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
336-561 |
9.21e-13 |
|
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: 70.70 E-value: 9.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 336 AELAAVIDRLYEFHQLTEQRPTNKPkncqhAVQVANAS----IRTPDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLK 411
Cdd:COG1123 235 QALAAVPRLGAARGRAAPAAAAAEP-----LLEVRNLSkrypVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLAR 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 412 TLSHCWP------WFKG-DISSPAGSW---------YVSQTP---LIKSGLLKEIICKAL----PLPVDD--KSLSEVLH 466
Cdd:COG1123 310 LLLGLLRptsgsiLFDGkDLTKLSRRSlrelrrrvqMVFQDPyssLNPRMTVGDIIAEPLrlhgLLSRAErrERVAELLE 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 467 QVGLGKLAARIHDHDrwgdiLSSGEKQRIALARLILRRPKWIFLDETTSHLEE--QEAI-RLLRLVREKLPTSgVIMVTH 543
Cdd:COG1123 390 RVGLPPDLADRYPHE-----LSGGQRQRVAIARALALEPKLLILDEPTSALDVsvQAQIlNLLRDLQRELGLT-YLFISH 463
|
250 260
....*....|....*....|
gi 446551198 544 qpgvwNLA--DDICDISAVL 561
Cdd:COG1123 464 -----DLAvvRYIADRVAVM 478
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
378-561 |
1.67e-12 |
|
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: 67.31 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 378 DNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLShcwpwfkGDISSPAGSWYVSQTPLIKSGL--LKEIICK----- 450
Cdd:COG1127 16 GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLII-------GLLRPDSGEILVDGQDITGLSEkeLYELRRRigmlf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 451 ---------------ALPL---PVDDKSL-----SEVLHQVGLGklaariHDHDRWGDILSSGEKQRIALAR-LILRrPK 506
Cdd:COG1127 89 qggalfdsltvfenvAFPLrehTDLSEAEirelvLEKLELVGLP------GAADKMPSELSGGMRKRVALARaLALD-PE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446551198 507 WIFLDETTSHLEEQEAIRLLRLVRE---KLPTSgVIMVTHQ-PGVWNLADDIcdisAVL 561
Cdd:COG1127 162 ILLYDEPTAGLDPITSAVIDELIRElrdELGLT-SVVVTHDlDSAFAIADRV----AVL 215
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
367-544 |
2.13e-12 |
|
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: 66.28 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 367 VQVANASIR-TPDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKG-------DISS-PAGSW-----Y 432
Cdd:cd03369 7 IEVENLSVRyAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGkieidgiDISTiPLEDLrssltI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 433 VSQTPLIKSGLLKeiickaLPLPV----DDKSLSEVLhQVGLGklaarihdhdrwGDILSSGEKQRIALARLILRRPKWI 508
Cdd:cd03369 87 IPQDPTLFSGTIR------SNLDPfdeySDEEIYGAL-RVSEG------------GLNLSQGQRQLLCLARALLKRPRVL 147
|
170 180 190
....*....|....*....|....*....|....*.
gi 446551198 509 FLDETTSHLEEQEAIRLLRLVREKLPTSGVIMVTHQ 544
Cdd:cd03369 148 VLDEATASIDYATDALIQKTIREEFTNSTILTIAHR 183
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
381-545 |
2.66e-12 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 66.70 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 381 IILENL-----------NFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDIS---------SPAgswyvsQTPLik 440
Cdd:COG3840 2 LRLDDLtyrygdfplrfDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILwngqdltalPPA------ERPV-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 441 SGLLKE------------I---ICKALPLPVDDKS-LSEVLHQVGLGKLAarihdhDRWGDILSSGEKQRIALARLILR- 503
Cdd:COG3840 74 SMLFQEnnlfphltvaqnIglgLRPGLKLTAEQRAqVEQALERVGLAGLL------DRLPGQLSGGQRQRVALARCLVRk 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446551198 504 RPKWIfLDETTSHLE---EQEAIRLLR-LVREKLPTsgVIMVTHQP 545
Cdd:COG3840 148 RPILL-LDEPFSALDpalRQEMLDLVDeLCRERGLT--VLMVTHDP 190
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
392-555 |
2.92e-12 |
|
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: 66.16 E-value: 2.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 392 PGKWLLLKGYSGAGKTTLLKTLShcwpwfkGDISSPAGSWYVSQTPLIKS-------------GLL------------KE 446
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIA-------GLEKPDGGTIVLNGTVLFDSrkkinlppqqrkiGLVfqqyalfphlnvRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 447 IICKALPLP---VDDKSLSEVLHQVGLGKLAarihdhDRWGDILSSGEKQRIALARLILRRPKWIFLDETTSHLEEQEAI 523
Cdd:cd03297 95 NLAFGLKRKrnrEDRISVDELLDLLGLDHLL------NRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 446551198 524 RLLRLVRE-----KLPtsgVIMVTHQPG-VWNLADDIC 555
Cdd:cd03297 169 QLLPELKQikknlNIP---VIFVTHDLSeAEYLADRIV 203
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
380-543 |
3.72e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 68.55 E-value: 3.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 380 KIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDISSPAGsW---YVSQTPLIKSGL-LKEIICKALPlP 455
Cdd:COG0488 11 RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG-LrigYLPQEPPLDDDLtVLDTVLDGDA-E 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 456 VDD--KSLSEVLHQVG--------LGKLAARIHDHDRWG-----------------------DILSSGEKQRIALARLIL 502
Cdd:COG0488 89 LRAleAELEELEAKLAepdedlerLAELQEEFEALGGWEaearaeeilsglgfpeedldrpvSELSGGWRRRVALARALL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446551198 503 RRPKWIFLDETTSHLEEqEAIRLLR--LVREKlptSGVIMVTH 543
Cdd:COG0488 169 SEPDLLLLDEPTNHLDL-ESIEWLEefLKNYP---GTVLVVSH 207
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
378-543 |
6.20e-12 |
|
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: 65.34 E-value: 6.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 378 DNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLShcwpwfkGDISSPAGSWYVSQTPLIKSGLLK------------ 445
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIA-------GFETPTSGEILLDGKDITNLPPHKrpvntvfqnyal 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 446 -------EIICKALPLPVDDKS-----LSEVLHQVGLGKLAAR-IHDhdrwgdiLSSGEKQRIALARLILRRPKWIFLDE 512
Cdd:cd03300 84 fphltvfENIAFGLRLKKLPKAeikerVAEALDLVQLEGYANRkPSQ-------LSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 446551198 513 TTSHLE----EQEAIRLLRLVREKLPTsgVIMVTH 543
Cdd:cd03300 157 PLGALDlklrKDMQLELKRLQKELGIT--FVFVTH 189
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
383-547 |
9.13e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 64.90 E-value: 9.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 383 LENLNFHVSPGKWLLLKGYSGAGKTTLLKTL------SHCWPWFKG-DISSPAGSwyvsQTPLIKSG----------LLK 445
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLIcgierpSAGKIWFSGhDITRLKNR----EVPFLRRQigmifqdhhlLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 446 EIICK--ALPLPVDDKSLSEVLHQVGLGKLAARIHDHDRWGDI-LSSGEKQRIALARLILRRPKWIFLDETTSHLEEQEA 522
Cdd:PRK10908 94 RTVYDnvAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIqLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALS 173
|
170 180
....*....|....*....|....*..
gi 446551198 523 IRLLRLVrEKLPTSG--VIMVTHQPGV 547
Cdd:PRK10908 174 EGILRLF-EEFNRVGvtVLMATHDIGL 199
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
383-543 |
1.09e-11 |
|
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: 64.79 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 383 LENLNFHVSPGKWLLLKGYSGAGKTTLLKTLShcwpwfkgDISSPA-GSWYVSQTPLIKSGLLKEIICK---ALP-LPVD 457
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLIS--------GLAQPTsGGVILEGKQITEPGPDRMVVFQnysLLPwLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 458 DK---SLSEVLHQVGLGKLAARIHDH----------DRWGDILSSGEKQRIALARLILRRPKWIFLDE--------TTSH 516
Cdd:TIGR01184 73 ENialAVDRVLPDLSKSERRAIVEEHialvglteaaDKRPGQLSGGMKQRVAIARALSIRPKVLLLDEpfgaldalTRGN 152
|
170 180
....*....|....*....|....*..
gi 446551198 517 LEEQeairLLRLVREKLPTsgVIMVTH 543
Cdd:TIGR01184 153 LQEE----LMQIWEEHRVT--VLMVTH 173
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
358-556 |
1.69e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 64.81 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 358 NKPKNCQHAVQVANASIRTPDnKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDI---SSPAGSW--- 431
Cdd:PRK10575 3 EYTNHSDTTFALRNVSFRVPG-RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIlldAQPLESWssk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 432 -------YV-SQTPLIKSGLLKEIIC-------KAL-PLPVDDKS-LSEVLHQVGLGKLAARIHDHdrwgdiLSSGEKQR 494
Cdd:PRK10575 82 afarkvaYLpQQLPAAEGMTVRELVAigrypwhGALgRFGAADREkVEEAISLVGLKPLAHRLVDS------LSGGERQR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446551198 495 IALARLILRRPKWIFLDETTSHLEEQEAIRLL----RLVREKLPTsgVIMVTHQpgvWNLADDICD 556
Cdd:PRK10575 156 AWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLalvhRLSQERGLT--VIAVLHD---INMAARYCD 216
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
378-543 |
2.12e-11 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 65.50 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 378 DNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLS-HCWP-----WFKG-DISS------PAGswYVSQTPL------ 438
Cdd:COG3842 16 GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAgFETPdsgriLLDGrDVTGlppekrNVG--MVFQDYAlfphlt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 439 ----IKSGLlkeiicKALPLPVDD--KSLSEVLHQVGLGKLAAR-IHDhdrwgdiLSSGEKQRIALARLILRRPKWIFLD 511
Cdd:COG3842 94 vaenVAFGL------RMRGVPKAEirARVAELLELVGLEGLADRyPHQ-------LSGGQQQRVALARALAPEPRVLLLD 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 446551198 512 ETTSHLEEQ--EAIR--LLRLVREkLPTSgVIMVTH 543
Cdd:COG3842 161 EPLSALDAKlrEEMReeLRRLQRE-LGIT-FIYVTH 194
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
378-543 |
2.18e-11 |
|
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: 61.70 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 378 DNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDISSPAGSW--YVSQtpliksgllkeiickalplp 455
Cdd:cd03221 11 GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKigYFEQ-------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 456 vddkslsevlhqvglgklaarihdhdrwgdiLSSGEKQRIALARLILRRPKWIFLDETTSHLEEqEAIRLLRLVREKLPt 535
Cdd:cd03221 71 -------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDL-ESIEALEEALKEYP- 117
|
....*...
gi 446551198 536 SGVIMVTH 543
Cdd:cd03221 118 GTVILVSH 125
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
260-544 |
3.56e-11 |
|
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: 66.47 E-value: 3.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 260 NFHTikENWHRLMNRQRWLDYWQNIysrslsVLPYFLLLPQFIS--------GQInlgGLMKSRQafMLVSNNLSWFIYK 331
Cdd:TIGR01271 1095 NLHT--ANWFLYLSTLRWFQMRIDI------IFVFFFIAVTFIAigtnqdgeGEV---GIILTLA--MNILSTLQWAVNS 1161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 332 YDELAELAAVIDRLYEFHQL--TEQRPTN--KPKNCQHAVQVANASIR------------------TPDNKIILENLNFH 389
Cdd:TIGR01271 1162 SIDVDGLMRSVSRVFKFIDLpqEEPRPSGggGKYQLSTVLVIENPHAQkcwpsggqmdvqgltakyTEAGRAVLQDLSFS 1241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 390 VSPGKWLLLKGYSGAGKTTLLKTLSHCWPwFKGDISSPAGSW-------------YVSQTPLIKSGLLKeiicKALPlPV 456
Cdd:TIGR01271 1242 VEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWnsvtlqtwrkafgVIPQKVFIFSGTFR----KNLD-PY 1315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 457 D---DKSLSEVLHQVGL--------GKLAARIHDHdrwGDILSSGEKQRIALARLILRRPKWIFLDETTSHLEEQEAIRL 525
Cdd:TIGR01271 1316 EqwsDEEIWKVAEEVGLksvieqfpDKLDFVLVDG---GYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQII 1392
|
330
....*....|....*....
gi 446551198 526 LRLVREKLPTSGVIMVTHQ 544
Cdd:TIGR01271 1393 RKTLKQSFSNCTVILSEHR 1411
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
378-554 |
4.20e-11 |
|
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: 62.66 E-value: 4.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 378 DNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDISspAGSWYVSQTPLIKSGL-------------- 443
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIY--IGGRDVTDLPPKDRDIamvfqnyalyphmt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 444 LKEIIckALPLPVDDKSLSEVLHQVglgKLAARI----HDHDRWGDILSSGEKQRIALARLILRRPKWIFLDETTS---- 515
Cdd:cd03301 89 VYDNI--AFGLKLRKVPKDEIDERV---REVAELlqieHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSnlda 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446551198 516 HLEEQEAIRLLRLVREKLPTsgVIMVTH-QPGVWNLADDI 554
Cdd:cd03301 164 KLRVQMRAELKRLQQRLGTT--TIYVTHdQVEAMTMADRI 201
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
379-554 |
5.53e-11 |
|
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: 62.23 E-value: 5.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 379 NKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDISSPAGSWYVSQTPLIKSGLLKE------------ 446
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEapgfypnltare 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 447 -IICKALPLPVDDKSLSEVLHQVGLGKlaariHDHDRWGDiLSSGEKQRIALARLILRRPKWIFLDETTSHLEEqEAIRL 525
Cdd:cd03268 92 nLRLLARLLGIRKKRIDEVLDVVGLKD-----SAKKKVKG-FSLGMKQRLGIALALLGNPDLLILDEPTNGLDP-DGIKE 164
|
170 180 190
....*....|....*....|....*....|..
gi 446551198 526 LRLVREKLPTSG--VIMVTHQPG-VWNLADDI 554
Cdd:cd03268 165 LRELILSLRDQGitVLISSHLLSeIQKVADRI 196
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
379-543 |
5.55e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 63.16 E-value: 5.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 379 NKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLShcwpwfkGDISSPAGSWYVSQTPLIK-----------SGLL--K 445
Cdd:PRK11247 24 ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLA-------GLETPSAGELLAGTAPLAEaredtrlmfqdARLLpwK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 446 EIICK-ALPLPVD--DKSLsEVLHQVGLgklAARIHDhdrWGDILSSGEKQRIALARLILRRPKWIFLDE------TTSH 516
Cdd:PRK11247 97 KVIDNvGLGLKGQwrDAAL-QALAAVGL---ADRANE---WPAALSGGQKQRVALARALIHRPGLLLLDEplgaldALTR 169
|
170 180
....*....|....*....|....*..
gi 446551198 517 LEEQEAIRllRLVREKLPTsgVIMVTH 543
Cdd:PRK11247 170 IEMQDLIE--SLWQQHGFT--VLLVTH 192
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
382-561 |
9.07e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 64.09 E-value: 9.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 382 ILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLshcwpwfKGDISSPAGSWYVSQTPlIKSGLLKEIICKALPLP------ 455
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAI-------NGTLTPTAGTVLVAGDD-VEALSARAASRRVASVPqdtsls 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 456 -------------------------VDDKSLSEVLHQVGLGKLAarihdhDRWGDILSSGEKQRIALARLILRRPKWIFL 510
Cdd:PRK09536 90 fefdvrqvvemgrtphrsrfdtwteTDRAAVERAMERTGVAQFA------DRPVTSLSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446551198 511 DETTSHLEEQEAIRLLRLVREkLPTSG--VIMVTHQpgvWNLADDICDISAVL 561
Cdd:PRK09536 164 DEPTASLDINHQVRTLELVRR-LVDDGktAVAAIHD---LDLAARYCDELVLL 212
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
366-554 |
1.16e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 62.51 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 366 AVQVANASIRTPDNKI-ILENLNFHVSPGKWLLLKGYSGAGKTTLLK---------------------TLSHCWPWfkgD 423
Cdd:PRK13640 5 IVEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKlinglllpddnpnskitvdgiTLTAKTVW---D 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 424 ISSPAGswYVSQTPL-----------IKSGLLKeiicKALPLPVDDKSLSEVLHQVGLGKLAarihdhDRWGDILSSGEK 492
Cdd:PRK13640 82 IREKVG--IVFQNPDnqfvgatvgddVAFGLEN----RAVPRPEMIKIVRDVLADVGMLDYI------DSEPANLSGGQK 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446551198 493 QRIALARLILRRPKWIFLDETTSHLEEQEAIRLLRLVREKLPTSG--VIMVTHQPGVWNLADDI 554
Cdd:PRK13640 150 QRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNltVISITHDIDEANMADQV 213
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
378-555 |
2.53e-10 |
|
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: 60.66 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 378 DNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKT---LSHCWP--------WFKG-DISSPAGSWY--------VSQTP 437
Cdd:cd03260 11 GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLlnrLNDLIPgapdegevLLDGkDIYDLDVDVLelrrrvgmVFQKP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 438 LIKSGLLKEIIckALPLPV----DDKSLSE----VLHQVGL-GKLAARIHDHDrwgdiLSSGEKQRIALARLILRRPKWI 508
Cdd:cd03260 91 NPFPGSIYDNV--AYGLRLhgikLKEELDErveeALRKAALwDEVKDRLHALG-----LSGGQQQRLCLARALANEPEVL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446551198 509 FLDETTSHLEEQEAIRLLRLVREKLPTSGVIMVTHQPG-VWNLADDIC 555
Cdd:cd03260 164 LLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQqAARVADRTA 211
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
367-543 |
3.63e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 60.86 E-value: 3.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 367 VQVANASIRTPDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKtlsHcwpwFKGDISSPAGSWYVSQTPLI--KSGLL 444
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFL---H----FNGILKPTSGEVLIKGEPIKydKKSLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 445 K--------------EIICKA-----------LPLPVDD--KSLSEVLHQVGLGKLAARIHDHdrwgdiLSSGEKQRIAL 497
Cdd:PRK13639 75 EvrktvgivfqnpddQLFAPTveedvafgplnLGLSKEEveKRVKEALKAVGMEGFENKPPHH------LSGGQKKRVAI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446551198 498 ARLILRRPKWIFLDETTSHLEEQEAIRLLRLVREkLPTSG--VIMVTH 543
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYD-LNKEGitIIISTH 195
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
367-544 |
3.94e-10 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 61.02 E-value: 3.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 367 VQVANASIR-TPDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWpWFKGDISSPAGSW-------------Y 432
Cdd:cd03289 3 MTVKDLTAKyTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGVSWnsvplqkwrkafgV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 433 VSQTPLIKSGLLKeiicKALPlPV---DDKSLSEVLHQVGL--------GKLAARIHDHdrwGDILSSGEKQRIALARLI 501
Cdd:cd03289 82 IPQKVFIFSGTFR----KNLD-PYgkwSDEEIWKVAEEVGLksvieqfpGQLDFVLVDG---GCVLSHGHKQLMCLARSV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446551198 502 LRRPKWIFLDETTSHLEEQEAIRLLRLVREKLPTSGVIMVTHQ 544
Cdd:cd03289 154 LSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHR 196
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
378-543 |
5.12e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 60.52 E-value: 5.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 378 DNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDIS------SPAGSW-------YVSQTPL------ 438
Cdd:PRK13650 18 QEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIidgdllTEENVWdirhkigMVFQNPDnqfvga 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 439 -----IKSGLLKeiicKALPLPVDDKSLSEVLHQVGLGKLAarihdhDRWGDILSSGEKQRIALARLILRRPKWIFLDET 513
Cdd:PRK13650 98 tveddVAFGLEN----KGIPHEEMKERVNEALELVGMQDFK------EREPARLSGGQKQRVAIAGAVAMRPKIIILDEA 167
|
170 180 190
....*....|....*....|....*....|...
gi 446551198 514 TSHLE---EQEAIRLLRLVREKLPTSgVIMVTH 543
Cdd:PRK13650 168 TSMLDpegRLELIKTIKGIRDDYQMT-VISITH 199
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
375-530 |
5.16e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.03 E-value: 5.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 375 RTPDNKIILENLNFHVSPGKWLLLKGYSGAGKTT----LLKTL-SHCWPWFKGdisSPAGSW-------------YVSQT 436
Cdd:PRK15134 294 RTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLInSQGEIWFDG---QPLHNLnrrqllpvrhriqVVFQD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 437 PliKSGL-----LKEIIckALPLPVDDKSLS---------EVLHQVGLGklAARIHdhdRWGDILSSGEKQRIALARLIL 502
Cdd:PRK15134 371 P--NSSLnprlnVLQII--EEGLRVHQPTLSaaqreqqviAVMEEVGLD--PETRH---RYPAEFSGGQRQRIAIARALI 441
|
170 180
....*....|....*....|....*...
gi 446551198 503 RRPKWIFLDETTSHLEEQEAIRLLRLVR 530
Cdd:PRK15134 442 LKPSLIILDEPTSSLDKTVQAQILALLK 469
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
455-545 |
8.19e-10 |
|
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: 59.04 E-value: 8.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 455 PVDDKSLSEVLHQVGLGKLAARIHDHdrwgdiLSSGEKQRIALARLILRRPKWIFLDETTSHLEEQEAIRLLRLV----R 530
Cdd:cd03298 103 AEDRQAIEVALARVGLAGLEKRLPGE------LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVldlhA 176
|
90
....*....|....*
gi 446551198 531 EKLPTsgVIMVTHQP 545
Cdd:cd03298 177 ETKMT--VLMVTHQP 189
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
378-545 |
9.48e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 59.31 E-value: 9.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 378 DNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLS-HcwP---------WFKG-DIS--SP-----AGSWYVSQTPL- 438
Cdd:COG0396 11 EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMgH--PkyevtsgsiLLDGeDILelSPderarAGIFLAFQYPVe 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 439 IK----SGLLKEII----CKALPLPVDDKSLSEVLHQVGLGKLAArihdhDRW---GdiLSSGEKQRIALARLILRRPKW 507
Cdd:COG0396 89 IPgvsvSNFLRTALnarrGEELSAREFLKLLKEKMKELGLDEDFL-----DRYvneG--FSGGEKKRNEILQMLLLEPKL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446551198 508 IFLDETTSHLeEQEAIRLLRLVREKL--PTSGVIMVTHQP 545
Cdd:COG0396 162 AILDETDSGL-DIDALRIVAEGVNKLrsPDRGILIITHYQ 200
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
361-545 |
9.91e-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: 58.41 E-value: 9.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 361 KNCQHAVQVANasirtpDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHcwpwfKGDISSPAGSWYVSQTPLIK 440
Cdd:cd03232 7 KNLNYTVPVKG------GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG-----RKTAGVITGEILINGRPLDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 441 SgLLKEI-ICKALPLPVDDKSLSEVLhqvglgKLAARIHDhdrwgdiLSSGEKQRIALARLILRRPKWIFLDETTSHLEE 519
Cdd:cd03232 76 N-FQRSTgYVEQQDVHSPNLTVREAL------RFSALLRG-------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
170 180
....*....|....*....|....*...
gi 446551198 520 QEAIRLLRLVReKLPTSG--VIMVTHQP 545
Cdd:cd03232 142 QAAYNIVRFLK-KLADSGqaILCTIHQP 168
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
365-544 |
1.15e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 59.43 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 365 HAVQVANASIRTPDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKtlsHcwpwFKGDISSPAGSWYVSQTPLIKS--- 441
Cdd:PRK13652 2 HLIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFR---H----FNGILKPTSGSVLIRGEPITKEnir 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 442 ------GLL--------------KEIICKALPLPVDDKSL----SEVLHQVGLGKLAARIHDHdrwgdiLSSGEKQRIAL 497
Cdd:PRK13652 75 evrkfvGLVfqnpddqifsptveQDIAFGPINLGLDEETVahrvSSALHMLGLEELRDRVPHH------LSGGEKKRVAI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446551198 498 ARLILRRPKWIFLDETTSHLEEQEAIRLLRLVREKLPTSG--VIMVTHQ 544
Cdd:PRK13652 149 AGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGmtVIFSTHQ 197
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
392-555 |
1.88e-09 |
|
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: 58.53 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 392 PGKWLLLKGYSGAGKTTLLKTLS---------HCWP--W------FKG-------------DISSPAGSWYVSQTPLIKS 441
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAgklkpnlgkFDDPpdWdeildeFRGselqnyftkllegDVKVIVKPQYVDLIPKAVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 442 GLLKEIICKalplpVDDK-SLSEVLHQVGLGKLAarihdhDRWGDILSSGEKQRIALARLILRRPKWIFLDETTSHLEEQ 520
Cdd:cd03236 105 GKVGELLKK-----KDERgKLDELVDQLELRHVL------DRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 446551198 521 EAIRLLRLVREKL-PTSGVIMVTHQPGVWN-LADDIC 555
Cdd:cd03236 174 QRLNAARLIRELAeDDNYVLVVEHDLAVLDyLSDYIH 210
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
377-543 |
2.08e-09 |
|
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: 59.95 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 377 PDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDISSPAGS--WYVSQTP-LIKSGLLKEIICKALP 453
Cdd:TIGR03719 15 PPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIkvGYLPQEPqLDPTKTVRENVEEGVA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 454 LPVDD-KSLSEVLHQVG------------LGKLAARI-----HDHDRWGDI----------------LSSGEKQRIALAR 499
Cdd:TIGR03719 95 EIKDAlDRFNEISAKYAepdadfdklaaeQAELQEIIdaadaWDLDSQLEIamdalrcppwdadvtkLSGGERRRVALCR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446551198 500 LILRRPKWIFLDETTSHLEEQEAIRLLRLVREKLPTsgVIMVTH 543
Cdd:TIGR03719 175 LLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGT--VVAVTH 216
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
366-554 |
2.47e-09 |
|
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: 58.12 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 366 AVQVANASIRTPDNKIiLENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDIsspagsWY----VSQTPL--- 438
Cdd:cd03296 2 SIEVRNVSKRFGDFVA-LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTI------LFggedATDVPVqer 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 439 --------------------IKSGLLKEIICKALPLPVDDKSLSEVLHQVGLGKLAarihdhDRWGDILSSGEKQRIALA 498
Cdd:cd03296 75 nvgfvfqhyalfrhmtvfdnVAFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLA------DRYPAQLSGGQRQRVALA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 499 RLILRRPKWIFLDETTSHLEEQ---EAIRLLRLVREKLPTSGViMVTH-QPGVWNLADDI 554
Cdd:cd03296 149 RALAVEPKVLLLDEPFGALDAKvrkELRRWLRRLHDELHVTTV-FVTHdQEEALEVADRV 207
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
379-552 |
2.66e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 57.27 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 379 NKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDISSPAGS------WYVSQTPLI--KSGL-----LK 445
Cdd:PRK13540 13 DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSikkdlcTYQKQLCFVghRSGInpyltLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 446 EIICKALPLPVDDKSLSEVLHQVGLGklaariHDHDRWGDILSSGEKQRIALARLILRRPKWIFLDETTSHLEEQEAIRL 525
Cdd:PRK13540 93 ENCLYDIHFSPGAVGITELCRLFSLE------HLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTI 166
|
170 180
....*....|....*....|....*...
gi 446551198 526 LRLVREKLPTSGVIMVT-HQPGVWNLAD 552
Cdd:PRK13540 167 ITKIQEHRAKGGAVLLTsHQDLPLNKAD 194
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
378-554 |
2.86e-09 |
|
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: 57.15 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 378 DNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCwP---------WFKG-DIS--SP-----AGSWYVSQTPLIK 440
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-PkyevtegeiLFKGeDITdlPPeerarLGIFLAFQYPPEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 441 SGLlkeiickalplpvddkSLSEVLHQVGLGklaarihdhdrwgdiLSSGEKQRIALARLILRRPKWIFLDETTSHLeEQ 520
Cdd:cd03217 90 PGV----------------KNADFLRYVNEG---------------FSGGEKKRNEILQLLLLEPDLAILDEPDSGL-DI 137
|
170 180 190
....*....|....*....|....*....|....*.
gi 446551198 521 EAIRLLRLVREKL--PTSGVIMVTHQPgvwNLADDI 554
Cdd:cd03217 138 DALRLVAEVINKLreEGKSVLIITHYQ---RLLDYI 170
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
400-552 |
3.75e-09 |
|
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: 58.57 E-value: 3.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 400 GYSGAGKTTLLKTLS--------HC----WPWFKGDisspAGSW---------YVSQTPL----------IKSGLlkeii 448
Cdd:COG4148 32 GPSGSGKTTLLRAIAglerpdsgRIrlggEVLQDSA----RGIFlpphrrrigYVFQEARlfphlsvrgnLLYGR----- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 449 cKALPLPVDDKSLSEVLHQVGLGKLAarihdhDRWGDILSSGEKQRIALARLILRRPKWIFLDETTSHLEE---QEAIRL 525
Cdd:COG4148 103 -KRAPRAERRISFDEVVELLGIGHLL------DRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLarkAEILPY 175
|
170 180 190
....*....|....*....|....*....|
gi 446551198 526 L-RLVRE-KLPtsgVIMVTHQPG-VWNLAD 552
Cdd:COG4148 176 LeRLRDElDIP---ILYVSHSLDeVARLAD 202
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
382-554 |
4.24e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.91 E-value: 4.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 382 ILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDIS---------SPA-----GSWYVSQTPLIKSGL-LKE 446
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEiggnpcarlTPAkahqlGIYLVPQEPLLFPNLsVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 447 IICKALPLPVDDKS-LSEVLHQVGlgklaarIH-DHDRWGDILSSGEKQRIALARLILRRPKWIFLDETTSHLEEQEAIR 524
Cdd:PRK15439 106 NILFGLPKRQASMQkMKQLLAALG-------CQlDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETER 178
|
170 180 190
....*....|....*....|....*....|..
gi 446551198 525 LLRLVREKLPTS-GVIMVTHQ-PGVWNLADDI 554
Cdd:PRK15439 179 LFSRIRELLAQGvGIVFISHKlPEIRQLADRI 210
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
382-542 |
5.31e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 56.40 E-value: 5.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 382 ILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLShcwpwfkGDISSPAGSWYVSQTPLIKSGLLKEI-ICKALPLPVDDKS 460
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLA-------GLLHVESGQIQIDGKTATRGDRSRFMaYLGHLPGLKADLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 461 LSEVLHQV-GL-GKLAAR----------IHDH-DRWGDILSSGEKQRIALARLILR-RPKWIfLDETTSHLeEQEAIRLL 526
Cdd:PRK13543 99 TLENLHFLcGLhGRRAKQmpgsalaivgLAGYeDTLVRQLSAGQKKRLALARLWLSpAPLWL-LDEPYANL-DLEGITLV 176
|
170
....*....|....*..
gi 446551198 527 -RLVREKLPTSGVIMVT 542
Cdd:PRK13543 177 nRMISAHLRGGGAALVT 193
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
382-547 |
5.54e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 56.95 E-value: 5.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 382 ILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDISSPAGSWYVSQTPLIKSGL------------------ 443
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKAIRelrrnvgmvfqqynlwph 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 444 ------LKEIICKALPLpVDDKSLSEVLhqvglgKLAARIH--DH-DRWGDILSSGEKQRIALARLILRRPKWIFLDETT 514
Cdd:PRK11124 97 ltvqqnLIEAPCRVLGL-SKDQALARAE------KLLERLRlkPYaDRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPT 169
|
170 180 190
....*....|....*....|....*....|....*
gi 446551198 515 SHLEEQEAIRLLRLVREkLPTSGV--IMVTHQPGV 547
Cdd:PRK11124 170 AALDPEITAQIVSIIRE-LAETGItqVIVTHEVEV 203
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
379-561 |
8.83e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 56.56 E-value: 8.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 379 NKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDI----------SSPAGSWYVS---QTPLIKSGL-L 444
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVflgdkpismlSSRQLARRLAllpQHHLTPEGItV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 445 KEIICKA----LP----LPVDDKSLSEV-LHQVGLGKLAarihdhDRWGDILSSGEKQRIALARLILRRPKWIFLDETTS 515
Cdd:PRK11231 94 RELVAYGrspwLSlwgrLSAEDNARVNQaMEQTRINHLA------DRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTT 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446551198 516 HLEEQEAIRLLRLVREkLPTSG--VIMVTHQpgvWNLADDICDISAVL 561
Cdd:PRK11231 168 YLDINHQVELMRLMRE-LNTQGktVVTVLHD---LNQASRYCDHLVVL 211
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
463-545 |
1.34e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 55.56 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 463 EVLHQVGLGK----LAARihdhdrwgdiLSSGEKQRIALARLILRRPKWIFLDETTSHLEEQEAIR----LLRLVREKLP 534
Cdd:PRK10584 129 ALLEQLGLGKrldhLPAQ----------LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKiadlLFSLNREHGT 198
|
90
....*....|.
gi 446551198 535 TsgVIMVTHQP 545
Cdd:PRK10584 199 T--LILVTHDL 207
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
382-546 |
1.54e-08 |
|
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: 55.23 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 382 ILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDIsspagswYVSQTPLIKSG-LLKEIICK---------- 450
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTI-------IIDGLKLTDDKkNINELRQKvgmvfqqfnl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 451 -----AL------PLPVDDKSLSEV-------LHQVGLgklaarIHDHDRWGDILSSGEKQRIALARLILRRPKWIFLDE 512
Cdd:cd03262 88 fphltVLenitlaPIKVKGMSKAEAeeralelLEKVGL------ADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDE 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 446551198 513 TTSHLEEQEAIRLLRLVREkLPTSGVIM--VTHQPG 546
Cdd:cd03262 162 PTSALDPELVGEVLDVMKD-LAEEGMTMvvVTHEMG 196
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
383-554 |
2.08e-08 |
|
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: 55.14 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 383 LENLNFHVSPGKWLLLKGYSGAGKTTLLKTLShcwpwfkGDISSPAGSWY-----VSQTP---LIKSGL----------- 443
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLIS-------GFLRPTSGSVLfdgedITGLPpheIARLGIgrtfqiprlfp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 444 ---------------LKEIICKALPLPVDDKSLS---EVLHQVGLGKLAARIhdhdrwGDILSSGEKQRIALARLILRRP 505
Cdd:cd03219 89 eltvlenvmvaaqarTGSGLLLARARREEREAREraeELLERVGLADLADRP------AGELSYGQQRRLEIARALATDP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446551198 506 KWIFLDETTSHLEEQEAIRLLRLVREkLPTSG--VIMVTH-QPGVWNLADDI 554
Cdd:cd03219 163 KLLLLDEPAAGLNPEETEELAELIRE-LRERGitVLLVEHdMDVVMSLADRV 213
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
364-533 |
2.53e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 55.88 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 364 QHAVQVANASIRTPDNKIIlENLNFHVSPGKWLLLKGYSGAGKTTLLKTLShcwpwfkGDISSPAGSWYVSQTPLIKSGL 443
Cdd:PRK11432 4 KNFVVLKNITKRFGSNTVI-DNLNLTIKQGTMVTLLGPSGCGKTTVLRLVA-------GLEKPTEGQIFIDGEDVTHRSI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 444 LKEIIC----------------------KALPLPVDD--KSLSEVLHQVGLGKLAarihdhDRWGDILSSGEKQRIALAR 499
Cdd:PRK11432 76 QQRDICmvfqsyalfphmslgenvgyglKMLGVPKEErkQRVKEALELVDLAGFE------DRYVDQISGGQQQRVALAR 149
|
170 180 190
....*....|....*....|....*....|....
gi 446551198 500 LILRRPKWIFLDETTSHLEEQeairLLRLVREKL 533
Cdd:PRK11432 150 ALILKPKVLLFDEPLSNLDAN----LRRSMREKI 179
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
381-552 |
2.73e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 54.59 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 381 IILENL-----------NFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDI---------SSPAgswyvsQTPLik 440
Cdd:PRK10771 2 LKLTDItwlyhhlpmrfDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtlngqdhttTPPS------RRPV-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 441 SGLLKE------------I---ICKALPLPVDDK-SLSEVLHQVGLGKLAARIHDHdrwgdiLSSGEKQRIALARLILRR 504
Cdd:PRK10771 74 SMLFQEnnlfshltvaqnIglgLNPGLKLNAAQReKLHAIARQMGIEDLLARLPGQ------LSGGQRQRVALARCLVRE 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446551198 505 PKWIFLDETTSHLE---EQEAIRLLRLV-REKLPTsgVIMVTHqpgvwNLAD 552
Cdd:PRK10771 148 QPILLLDEPFSALDpalRQEMLTLVSQVcQERQLT--LLMVSH-----SLED 192
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
344-522 |
2.86e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 56.51 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 344 RLYEFHQL------TEQRPTNK-PKNCQHAVQVANASIRTPDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHC 416
Cdd:PRK13657 305 KLEEFFEVedavpdVRDPPGAIdLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRV 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 417 WPWFKG-------DISSpagswyVSQTPLIKS--------GLLKEIICKALPLPVDDKSLSEVLhqvglgKLAARIHDHD 481
Cdd:PRK13657 385 FDPQSGrilidgtDIRT------VTRASLRRNiavvfqdaGLFNRSIEDNIRVGRPDATDEEMR------AAAERAQAHD 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446551198 482 ---------------RwGDILSSGEKQRIALARLILRRPKWIFLDETTSHLE-EQEA 522
Cdd:PRK13657 453 fierkpdgydtvvgeR-GRQLSGGERQRLAIARALLKDPPILILDEATSALDvETEA 508
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
383-559 |
2.92e-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: 54.36 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 383 LENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDIS-SPAGSW--------------------YVSQtpliks 441
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILvRHDGGWvdlaqaspreilalrrrtigYVSQ------ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 442 gLLKeiickALP----LPVddksLSEVLHQVGLGKLAARihdhDRWGDIL-----------------SSGEKQRIALARL 500
Cdd:COG4778 101 -FLR-----VIPrvsaLDV----VAEPLLERGVDREEAR----ARARELLarlnlperlwdlppatfSGGEQQRVNIARG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446551198 501 ILRRPKWIFLDETTSHLEEQEAIRLLRLVREKLPT-SGVIMVTHQPGVWN-LADDICDISA 559
Cdd:COG4778 167 FIADPPLLLLDEPTASLDAANRAVVVELIEEAKARgTAIIGIFHDEEVREaVADRVVDVTP 227
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
383-557 |
3.87e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.09 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 383 LENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPW--FKGDIsspagswYVSQTPLIKSGlLKE-------IICKALP 453
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHgtYEGEI-------IFEGEELQASN-IRDteragiaIIHQELA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 454 LpVDDKSLSE-------------------------VLHQVGLGklaarIHDHDRWGDiLSSGEKQRIALARLILRRPKWI 508
Cdd:PRK13549 93 L-VKELSVLEniflgneitpggimdydamylraqkLLAQLKLD-----INPATPVGN-LGLGQQQLVEIAKALNKQARLL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446551198 509 FLDETTSHLEEQEAIRLLRLVREkLPTSGV--IMVTHQPG-VWNLADDICDI 557
Cdd:PRK13549 166 ILDEPTASLTESETAVLLDIIRD-LKAHGIacIYISHKLNeVKAISDTICVI 216
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
382-527 |
4.00e-08 |
|
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: 53.98 E-value: 4.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 382 ILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDIS---------SP-----AGSWYVSQTPLIKSGL---- 443
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRfdgrditglPPherarAGIGYVPEGRRIFPELtvee 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 444 -------------LKEIICKALPL-PVddksLSEVLHQVGlgklaarihdhdrwGDiLSSGEKQRIALARLILRRPKWIF 509
Cdd:cd03224 95 nlllgayarrrakRKARLERVYELfPR----LKERRKQLA--------------GT-LSGGEQQMLAIARALMSRPKLLL 155
|
170 180
....*....|....*....|....
gi 446551198 510 LDETTSHL-----EE-QEAIRLLR 527
Cdd:cd03224 156 LDEPSEGLapkivEEiFEAIRELR 179
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
380-561 |
4.00e-08 |
|
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: 54.05 E-value: 4.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 380 KIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLShcwpwfkGDISSPAGSWYVSQTPLIKSG--LLKEI-IC------- 449
Cdd:cd03263 15 KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLT-------GELRPTSGTAYINGYSIRTDRkaARQSLgYCpqfdalf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 450 ---------------KALPLPVDDKSLSEVLHQVGLGKLA-ARIHDhdrwgdiLSSGEKQRIALARLILRRPKWIFLDET 513
Cdd:cd03263 88 deltvrehlrfyarlKGLPKSEIKEEVELLLRVLGLTDKAnKRART-------LSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446551198 514 TSHLEEQEAIRLLRLVREKLPTSGVIMVTHQPgvwNLADDICDISAVL 561
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGRSIILTTHSM---DEAEALCDRIAIM 205
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
382-543 |
4.71e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 54.05 E-value: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 382 ILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLshcwpwfkGDISSP-AGSWYVSQTPLIKSG------------------ 442
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLL--------GGLDTPtSGDVIFNGQPMSKLSsaakaelrnqklgfiyqf 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 443 --LLKE-----------IICKALPLPVDDKSLsEVLHQVGLGKLAarihdHDRWGDiLSSGEKQRIALARLILRRPKWIF 509
Cdd:PRK11629 96 hhLLPDftalenvamplLIGKKKPAEINSRAL-EMLAAVGLEHRA-----NHRPSE-LSGGERQRVAIARALVNNPRLVL 168
|
170 180 190
....*....|....*....|....*....|....*.
gi 446551198 510 LDETTSHLEEQEAIRLLRLVRE--KLPTSGVIMVTH 543
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGElnRLQGTAFLVVTH 204
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
329-543 |
6.15e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.64 E-value: 6.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 329 IYKYDELAELAAVI-DRLYEFHQLTeqrPTNKPKncQHAVQVANASIRTPDNKIILENLNFHVSPGKWLLLKGYSGAGKT 407
Cdd:PLN03073 475 IKALDRLGHVDAVVnDPDYKFEFPT---PDDRPG--PPIISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKS 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 408 TLLKTLShcwpwfkGDISSPAGSwyVSQTPLIKSGLLKEIICKAL-----PLPVDDKSLSEVLHQvglgKLAARIHDHDR 482
Cdd:PLN03073 550 TILKLIS-------GELQPSSGT--VFRSAKVRMAVFSQHHVDGLdlssnPLLYMMRCFPGVPEQ----KLRAHLGSFGV 616
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446551198 483 WGDI-------LSSGEKQRIALARLILRRPKWIFLDETTSHLEEQEAIRLLR-LVrekLPTSGVIMVTH 543
Cdd:PLN03073 617 TGNLalqpmytLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQgLV---LFQGGVLMVSH 682
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
371-554 |
6.17e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 55.49 E-value: 6.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 371 NASIRT---PDN-KIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDI---SSPA-----GSW-----YV 433
Cdd:PRK10789 315 DVNIRQftyPQTdHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIrfhDIPLtklqlDSWrsrlaVV 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 434 SQTPLIKSGLLKEIIckALPLPvdDKSLSEVLHQVGLgklaARIHDH-------------DRwGDILSSGEKQRIALARL 500
Cdd:PRK10789 395 SQTPFLFSDTVANNI--ALGRP--DATQQEIEHVARL----ASVHDDilrlpqgydtevgER-GVMLSGGQKQRISIARA 465
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446551198 501 ILRRPKWIFLDETTSHLE---EQEAIRLLRLVREKlptSGVIMVTHQPGVWNLADDI 554
Cdd:PRK10789 466 LLLNAEILILDDALSAVDgrtEHQILHNLRQWGEG---RTVIISAHRLSALTEASEI 519
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
378-517 |
6.31e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 55.46 E-value: 6.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 378 DNKIILENLNFHVSPG-KWLLLkGYSGAGKTTLLKTLShcwpwfkGDISSPAGS--W-------YVSQtpliKSGLLKEi 447
Cdd:COG0488 326 GDKTLLDDLSLRIDRGdRIGLI-GPNGAGKSTLLKLLA-------GELEPDSGTvkLgetvkigYFDQ----HQEELDP- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 448 ickalplpvdDKSLSEVLHQVGLGKLAARIH-----------DHDRWGDILSSGEKQRIALARLILRRPKWIFLDETTSH 516
Cdd:COG0488 393 ----------DKTVLDELRDGAPGGTEQEVRgylgrflfsgdDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNH 462
|
.
gi 446551198 517 L 517
Cdd:COG0488 463 L 463
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
375-545 |
6.65e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 55.27 E-value: 6.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 375 RTPDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTL-----SHCwpwFKGDISSPAG---------SWYVSQTPLIK 440
Cdd:PLN03211 76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALagriqGNN---FTGTILANNRkptkqilkrTGFVTQDDILY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 441 SGL-LKE--IICKALPLPvddKSLSE---------VLHQVGLGKLAARIHDHDRWGDIlSSGEKQRIALARLILRRPKWI 508
Cdd:PLN03211 153 PHLtVREtlVFCSLLRLP---KSLTKqekilvaesVISELGLTKCENTIIGNSFIRGI-SGGERKRVSIAHEMLINPSLL 228
|
170 180 190
....*....|....*....|....*....|....*....
gi 446551198 509 FLDETTSHLEEQEAIRLLrLVREKLPTSGVIMVT--HQP 545
Cdd:PLN03211 229 ILDEPTSGLDATAAYRLV-LTLGSLAQKGKTIVTsmHQP 266
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
378-543 |
6.80e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 54.95 E-value: 6.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 378 DNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLShcwpwfkGDISSPAGSWY-----VSQTPLIKS----------- 441
Cdd:PRK09452 25 DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIA-------GFETPDSGRIMldgqdITHVPAENRhvntvfqsyal 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 442 ------------GLLkeiiCKALPLPVDDKSLSEVLHQVGLGKLAAR-IHDhdrwgdiLSSGEKQRIALARLILRRPKWI 508
Cdd:PRK09452 98 fphmtvfenvafGLR----MQKTPAAEITPRVMEALRMVQLEEFAQRkPHQ-------LSGGQQQRVAIARAVVNKPKVL 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 446551198 509 FLDETTSHLE----EQEAIRLLRLVREKLPTsgVIMVTH 543
Cdd:PRK09452 167 LLDESLSALDyklrKQMQNELKALQRKLGIT--FVFVTH 203
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
383-547 |
7.16e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 53.78 E-value: 7.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 383 LENLNFHVSPGKWLLLKGYSGAGKTTLLKTLS-HCWPwFKGDIS--SPAGSW--------------------YVSQTPLi 439
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSaRLAP-DAGEVHyrMRDGQLrdlyalseaerrrllrtewgFVHQHPR- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 440 kSGLLKEIICKAlplpvddkSLSEVLHQVG--------------LGKL---AARIHDHDRwgdILSSGEKQRIALARLIL 502
Cdd:PRK11701 100 -DGLRMQVSAGG--------NIGERLMAVGarhygdiratagdwLERVeidAARIDDLPT---TFSGGMQQRLQIARNLV 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446551198 503 RRPKWIFLDETTSHLEEQEAIRLLRLVREKLPTSG--VIMVTHQPGV 547
Cdd:PRK11701 168 THPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGlaVVIVTHDLAV 214
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
342-524 |
8.52e-08 |
|
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: 54.83 E-value: 8.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 342 IDRLYEfhqLTEQRPTNKPKNCQHAVQVANASIR--------TPDNKIiLENLNFHVSPGKWLLLKGYSGAGKTTLLKTL 413
Cdd:COG5265 329 MERMFD---LLDQPPEVADAPDAPPLVVGGGEVRfenvsfgyDPERPI-LKGVSFEVPAGKTVAIVGPSGAGKSTLARLL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 414 shcwpwFK------G-------DISSpagswyVSQTPLIKS-GL-----------LKEIICKALPlpvdDKSLSEVLHqv 468
Cdd:COG5265 405 ------FRfydvtsGrilidgqDIRD------VTQASLRAAiGIvpqdtvlfndtIAYNIAYGRP----DASEEEVEA-- 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446551198 469 glgklAAR---IHDH-----DRW-------GDILSSGEKQRIALARLILRRPKWIFLDETTSHL------EEQEAIR 524
Cdd:COG5265 467 -----AARaaqIHDFieslpDGYdtrvgerGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALdsrterAIQAALR 538
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
378-561 |
1.02e-07 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 53.92 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 378 DNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLShcwpwfkG--DISSpaGSWY------------------VSQT- 436
Cdd:COG3839 14 GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIA-------GleDPTS--GEILiggrdvtdlppkdrniamVFQSy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 437 --------------PLIKSGLLKEIIckalplpvdDKSLSEVLHQVGLGKLAarihdhDRWGDILSSGEKQRIALARLIL 502
Cdd:COG3839 85 alyphmtvyeniafPLKLRKVPKAEI---------DRRVREAAELLGLEDLL------DRKPKQLSGGQRQRVALGRALV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446551198 503 RRPKWIFLDETTSHLEEQ--EAIR--LLRLVREkLPTSgVIMVTH-QPGVWNLADDIcdisAVL 561
Cdd:COG3839 150 REPKVFLLDEPLSNLDAKlrVEMRaeIKRLHRR-LGTT-TIYVTHdQVEAMTLADRI----AVM 207
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
383-543 |
1.04e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 53.56 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 383 LENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDIS------SPAGSW-------YVSQTPliKSGLLKEIIC 449
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKidgellTAENVWnlrrkigMVFQNP--DNQFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 450 KALPLPVDDKSL--SEVLHQVGLGKLAARIHD-HDRWGDILSSGEKQRIALARLILRRPKWIFLDETTSHLE---EQEAI 523
Cdd:PRK13642 101 DDVAFGMENQGIprEEMIKRVDEALLAVNMLDfKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDptgRQEIM 180
|
170 180
....*....|....*....|
gi 446551198 524 RLLRLVREKLPTSgVIMVTH 543
Cdd:PRK13642 181 RVIHEIKEKYQLT-VLSITH 199
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
383-543 |
1.10e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 54.65 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 383 LENLNFHVSPGKWLLLKGYSGAGKTTLLKTLS-HCWP-----WFKG---DISSP-----AGSWYVSQ------------- 435
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYgLYQPdsgeiLIDGkpvRIRSPrdaiaLGIGMVHQhfmlvpnltvaen 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 436 ----TPLIKSGLL------KEI--ICKALPLPVDdkslsevlhqvglgkLAARIHDhdrwgdiLSSGEKQRIALARLILR 503
Cdd:COG3845 101 ivlgLEPTKGGRLdrkaarARIreLSERYGLDVD---------------PDAKVED-------LSVGEQQRVEILKALYR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446551198 504 RPKWIFLDETTSHLEEQEAIRLLRLVReKLPTSG--VIMVTH 543
Cdd:COG3845 159 GARILILDEPTAVLTPQEADELFEILR-RLAAEGksIIFITH 199
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
378-545 |
1.33e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 53.13 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 378 DNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDISSPAGSWY----VSQTPLIKsgLLKEI---ICK 450
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdIFQIDAIK--LRKEVgmvFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 451 ALPLP----------------VDDKS-----LSEVLHQVGLGKlaaRIHDH-DRWGDILSSGEKQRIALARLILRRPKWI 508
Cdd:PRK14246 99 PNPFPhlsiydniayplkshgIKEKReikkiVEECLRKVGLWK---EVYDRlNSPASQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190
....*....|....*....|....*....|....*..
gi 446551198 509 FLDETTSHLEEQEAIRLLRLVREKLPTSGVIMVTHQP 545
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNP 212
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
449-554 |
1.37e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 52.78 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 449 CKALPLPVDDKSLSEVLHQVGLGKlAARIhdHDRWGDILSSGEKQRIALARLILRRPKWIFLDETTSHLEEQEAIRLL-- 526
Cdd:PRK10418 106 CLALGKPADDATLTAALEAVGLEN-AARV--LKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILdl 182
|
90 100 110
....*....|....*....|....*....|.
gi 446551198 527 --RLVREKLPtsGVIMVTHQPG-VWNLADDI 554
Cdd:PRK10418 183 leSIVQKRAL--GMLLVTHDMGvVARLADDV 211
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
365-559 |
1.74e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.74 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 365 HAVQVANASiRTPDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLShcwpwfkGDISSPAGS--W-------YVSQ 435
Cdd:PRK15064 318 NALEVENLT-KGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLV-------GELEPDSGTvkWsenanigYYAQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 436 --TPLIKSGL-LKEIICKALPLPVDDKSLSEVLhqvglGKLAARIHDHDRWGDILSSGEKQRIALARLILRRPKWIFLDE 512
Cdd:PRK15064 390 dhAYDFENDLtLFDWMSQWRQEGDDEQAVRGTL-----GRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDE 464
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446551198 513 TTSHLeEQEAIRLLRLVREKLPTSgVIMVTH-QPGVWNLADDICDISA 559
Cdd:PRK15064 465 PTNHM-DMESIESLNMALEKYEGT-LIFVSHdREFVSSLATRIIEITP 510
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
379-543 |
1.82e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 52.42 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 379 NKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDISSPAG--SWYVSQT-------PLIKSG--LLKEI 447
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKlrIGYVPQKlyldttlPLTVNRflRLRPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 448 ICKALPLPVDDKSLSEVLHQVGLGKLaarihdhdrwgdilSSGEKQRIALARLILRRPKWIFLDETTSHLEEQEAIRLLR 527
Cdd:PRK09544 96 TKKEDILPALKRVQAGHLIDAPMQKL--------------SGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYD 161
|
170
....*....|....*....
gi 446551198 528 LV---REKLpTSGVIMVTH 543
Cdd:PRK09544 162 LIdqlRREL-DCAVLMVSH 179
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
382-543 |
2.14e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 53.16 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 382 ILENLNFHVSPGKWLLLKGYSGAGKTTLLKTL------SHCWPWFKG-DISS------PAGswYVSQT-PLIKSGLLKEI 447
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIaglehqTSGHIRFHGtDVSRlhardrKVG--FVFQHyALFRHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 448 ICKALP-LP--------VDDKSLSEVLHQVGLGKLAarihdhDRWGDILSSGEKQRIALARLILRRPKWIFLDETTSHLE 518
Cdd:PRK10851 95 IAFGLTvLPrrerpnaaAIKAKVTQLLEMVQLAHLA------DRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
170 180
....*....|....*....|....*...
gi 446551198 519 EQ---EAIRLLRLVREKLPTSGViMVTH 543
Cdd:PRK10851 169 AQvrkELRRWLRQLHEELKFTSV-FVTH 195
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
463-543 |
2.17e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 53.48 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 463 EVLHQVGLG-KLAARIHDhdrwgdiLSSGEKQRIALARLILRRPKWIFLDETTSHLEEQEAIRLLRLVREkLPTSGV--I 539
Cdd:COG1129 123 ELLARLGLDiDPDTPVGD-------LSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRR-LKAQGVaiI 194
|
....
gi 446551198 540 MVTH 543
Cdd:COG1129 195 YISH 198
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
382-544 |
3.67e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.44 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 382 ILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDISSPAGSW-------------YVSQTPLIKSGLLKEII 448
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVakfgltdlrrvlsIIPQSPVLFSGTVRFNI 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 449 CkalPLPV-DDKSLSEVLHQVGLGK--------LAARIHDHdrwGDILSSGEKQRIALARLILRRPKWIFLDETTSHLEE 519
Cdd:PLN03232 1331 D---PFSEhNDADLWEALERAHIKDvidrnpfgLDAEVSEG---GENFSVGQRQLLSLARALLRRSKILVLDEATASVDV 1404
|
170 180
....*....|....*....|....*
gi 446551198 520 QEAIRLLRLVREKLPTSGVIMVTHQ 544
Cdd:PLN03232 1405 RTDSLIQRTIREEFKSCTMLVIAHR 1429
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
382-520 |
3.91e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.11 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 382 ILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDI--------SSPAGSWY------VSQTPLIKSGLLKEI 447
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIiindshnlKDINLKWWrskigvVSQDPLLFSNSIKNN 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 448 ICKALPLPVDDKSLSEVLHQVGL------------------------------GKLAAR-------------------IH 478
Cdd:PTZ00265 480 IKYSLYSLKDLEALSNYYNEDGNdsqenknkrnscrakcagdlndmsnttdsnELIEMRknyqtikdsevvdvskkvlIH 559
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446551198 479 DH-----DRWGDI-------LSSGEKQRIALARLILRRPKWIFLDETTSHLEEQ 520
Cdd:PTZ00265 560 DFvsalpDKYETLvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
383-547 |
4.30e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 51.71 E-value: 4.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 383 LENLNFHVSPGKWLLLKGYSGAGKTTLLKTLShcwpwfkGDISSPAGSWYVSQTPL------IKSGLLKEI--------- 447
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLA-------GMIEPTSGELLIDDHPLhfgdysYRSQRIRMIfqdpstsln 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 448 ----ICKALPLPV----------DDKSLSEVLHQVGLGKLAARIHDHdrwgdILSSGEKQRIALARLILRRPKWIFLDET 513
Cdd:PRK15112 102 prqrISQILDFPLrlntdlepeqREKQIIETLRQVGLLPDHASYYPH-----MLAPGQKQRLGLARALILRPKVIIADEA 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 446551198 514 TSHLEEQEAIRLLRLVREKLPTSGV--IMVTHQPGV 547
Cdd:PRK15112 177 LASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGM 212
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
375-561 |
5.52e-07 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 51.73 E-value: 5.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 375 RTPDNKII-LENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHcwpwfkgdISSP-AGSWYVSQ---TPLIKSGLLKE--- 446
Cdd:PRK11153 12 PQGGRTIHaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINL--------LERPtSGRVLVDGqdlTALSEKELRKArrq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 447 --IICK--------------ALPLPVD-------DKSLSEVLHQVGLGklaariHDHDRWGDILSSGEKQRIALARLILR 503
Cdd:PRK11153 84 igMIFQhfnllssrtvfdnvALPLELAgtpkaeiKARVTELLELVGLS------DKADRYPAQLSGGQKQRVAIARALAS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446551198 504 RPKWIFLDETTSHLEEQ--EAI-RLLRLVREKLPTSgVIMVTHQPGVwnlADDICDISAVL 561
Cdd:PRK11153 158 NPKVLLCDEATSALDPAttRSIlELLKDINRELGLT-IVLITHEMDV---VKRICDRVAVI 214
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
383-556 |
5.89e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 51.27 E-value: 5.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 383 LENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKG-----DISSPAGSWYVSQTPLIK----------SGLLKEI 447
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGkvtvgDIVVSSTSKQKEIKPVRKkvgvvfqfpeSQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 448 ICKALPL-PVD--------DKSLSEVLHQVGLGKlaarihdhDRWGDI---LSSGEKQRIALARLILRRPKWIFLDETTS 515
Cdd:PRK13643 102 VLKDVAFgPQNfgipkekaEKIAAEKLEMVGLAD--------EFWEKSpfeLSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446551198 516 HLEEQEAIRLLRLVrEKLPTSG--VIMVTHqpgvwnLADDICD 556
Cdd:PRK13643 174 GLDPKARIEMMQLF-ESIHQSGqtVVLVTH------LMDDVAD 209
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
362-561 |
6.14e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 50.98 E-value: 6.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 362 NCQHaVQVANasirtpDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLShcwpwfkGDISSPAGSWYVSQT----- 436
Cdd:PRK13547 3 TADH-LHVAR------RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALA-------GDLTGGGAPRGARVTgdvtl 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 437 ---PLIK---------SGLLKEIICKALPLPVDD-KSLSEVLHQVGLGKLAarIHDHD----------------RWGDIL 487
Cdd:PRK13547 69 ngePLAAidaprlarlRAVLPQAAQPAFAFSAREiVLLGRYPHARRAGALT--HRDGEiawqalalagatalvgRDVTTL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 488 SSGEKQRIALARLI---------LRRPKWIFLDETTSHLEEQEAIRLLRLVRE--KLPTSGVIMVTHQPgvwNLADDICD 556
Cdd:PRK13547 147 SGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRlaRDWNLGVLAIVHDP---NLAARHAD 223
|
....*
gi 446551198 557 ISAVL 561
Cdd:PRK13547 224 RIAML 228
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
383-543 |
6.19e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.22 E-value: 6.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 383 LENLNFHVSPGKWLLLKGYSGAGKTTLLKTLShcwpwfkGDISSPAGSWYVSQTPL--------IKSGLLkeIICKALPL 454
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILS-------GNYQPDAGSILIDGQEMrfasttaaLAAGVA--IIYQELHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 455 pVDDKSLSEVL------HQVGL---GKLAARIHDH-DRWG-DI--------LSSGEKQRIALARLILRRPKWIFLDETTS 515
Cdd:PRK11288 91 -VPEMTVAENLylgqlpHKGGIvnrRLLNYEAREQlEHLGvDIdpdtplkyLSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180 190
....*....|....*....|....*....|
gi 446551198 516 HLEEQEAIRLLRLVREkLPTSG--VIMVTH 543
Cdd:PRK11288 170 SLSAREIEQLFRVIRE-LRAEGrvILYVSH 198
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
390-543 |
6.31e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.12 E-value: 6.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 390 VSPGKWLLLKGYSGAGKTTLLKTLS-HCWPWFkGDISSPAgSW-------------------------------YVSQTP 437
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSgELIPNL-GDYEEEP-SWdevlkrfrgtelqnyfkklyngeikvvhkpqYVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 438 LIKSGLLKEIICKalplpVDDKS-LSEVLHQVGLGKLAarihdhDRWGDILSSGEKQRIALARLILRRPKWIFLDETTSH 516
Cdd:PRK13409 174 KVFKGKVRELLKK-----VDERGkLDEVVERLGLENIL------DRDISELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
170 180
....*....|....*....|....*..
gi 446551198 517 LEEQEAIRLLRLVREKLPTSGVIMVTH 543
Cdd:PRK13409 243 LDIRQRLNVARLIRELAEGKYVLVVEH 269
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
382-554 |
6.82e-07 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 52.05 E-value: 6.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 382 ILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDISSPAGSW-------------YVSQTPLIKSG-LLKEI 447
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLkdidrhtlrqfinYLPQEPYIFSGsILENL 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 448 ICKALPLPVDDK-----SLSEV---LHQVGLGkLAARIHDHdrwGDILSSGEKQRIALARLILRRPKWIFLDETTSHLE- 518
Cdd:TIGR01193 569 LLGAKENVSQDEiwaacEIAEIkddIENMPLG-YQTELSEE---GSSISGGQKQRIALARALLTDSKVLILDESTSNLDt 644
|
170 180 190
....*....|....*....|....*....|....*...
gi 446551198 519 --EQEAIRLLRLVREKLptsgVIMVTHQPGVWNLADDI 554
Cdd:TIGR01193 645 itEKKIVNNLLNLQDKT----IIFVAHRLSVAKQSDKI 678
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
385-543 |
7.14e-07 |
|
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: 50.72 E-value: 7.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 385 NLNFHVSPGKWLLLKGYSGAGKTTLLKTLShcwpwfkGDISSPAGSWYVSQTPLIKS--GLLKEIICK------------ 450
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCIN-------RLIEPTSGKVLIDGQDIAAMsrKELRELRRKkismvfqsfall 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 451 ---------ALPLPVDDKSLS-------EVLHQVGLGKLAarihdhDRWGDILSSGEKQRIALARLILRRPKWIFLDETT 514
Cdd:cd03294 115 phrtvlenvAFGLEVQGVPRAereeraaEALELVGLEGWE------HKYPDELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190
....*....|....*....|....*....|....*
gi 446551198 515 SHL------EEQEaiRLLRLVREKLPTsgVIMVTH 543
Cdd:cd03294 189 SALdplirrEMQD--ELLRLQAELQKT--IVFITH 219
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
382-518 |
7.58e-07 |
|
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: 51.01 E-value: 7.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 382 ILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDISSPAGSWYVSQTPLIKSGLLKEIIckALPLPVDDKSL 461
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENI--IFGVSYDEYRY 129
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446551198 462 SEVLHQVGLGKLAARIHDHDRW-----GDILSSGEKQRIALARLILRRPKWIFLDETTSHLE 518
Cdd:cd03291 130 KSVVKACQLEEDITKFPEKDNTvlgegGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
355-543 |
7.71e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 51.37 E-value: 7.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 355 RPTNKP-KNCQHAVQVANASiRTPDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDISSPAGSwyV 433
Cdd:PRK11607 7 RPQAKTrKALTPLLEIRNLT-KSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD--L 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 434 SQTPLIKSGLLKEIICKAL-PLPVDDKSLSEVLHQVGL--GKLAARIHD-----H-----DRWGDILSSGEKQRIALARL 500
Cdd:PRK11607 84 SHVPPYQRPINMMFQSYALfPHMTVEQNIAFGLKQDKLpkAEIASRVNEmlglvHmqefaKRKPHQLSGGQRQRVALARS 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446551198 501 ILRRPKWIFLDETTSHLEEQEAIRLLRLVREKLPTSGV--IMVTH 543
Cdd:PRK11607 164 LAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVtcVMVTH 208
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
382-556 |
8.29e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 50.52 E-value: 8.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 382 ILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLS-----HCWPWFKGDISSPAGSWYVSQTPLIKS--------------- 441
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINlleqpEAGTIRVGDITIDTARSLSQQKGLIRQlrqhvgfvfqnfnlf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 442 ---GLLKEII-----CKALPLPVDDKSLSEVLHQVGL-GKlaarihdHDRWGDILSSGEKQRIALARLILRRPKWIFLDE 512
Cdd:PRK11264 98 phrTVLENIIegpviVKGEPKEEATARARELLAKVGLaGK-------ETSYPRRLSGGQQQRVAIARALAMRPEVILFDE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446551198 513 TTSHLEEQ---EAIRLLRLVREKLPTsgVIMVTHQPGvwnLADDICD 556
Cdd:PRK11264 171 PTSALDPElvgEVLNTIRQLAQEKRT--MVIVTHEMS---FARDVAD 212
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
379-543 |
8.71e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 50.86 E-value: 8.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 379 NKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTL---------------------SHCWpwfkgDISSPAGswYVSQTP 437
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMnallipsegkvyvdgldtsdeENLW-----DIRNKAG--MVFQNP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 438 --LIKSGLLKEIIC---KALPLPVDD--KSLSEVLHQVGLGKLAaRIHDHdrwgdILSSGEKQRIALARLILRRPKWIFL 510
Cdd:PRK13633 95 dnQIVATIVEEDVAfgpENLGIPPEEirERVDESLKKVGMYEYR-RHAPH-----LLSGGQKQRVAIAGILAMRPECIIF 168
|
170 180 190
....*....|....*....|....*....|....*
gi 446551198 511 DETTSHLEEQEAIRLLRLVREKLPTSG--VIMVTH 543
Cdd:PRK13633 169 DEPTAMLDPSGRREVVNTIKELNKKYGitIILITH 203
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
378-543 |
1.02e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 50.52 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 378 DNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLShcwpwfkgDISSPAGSWYVSQTPLIKSGLLKEI---------- 447
Cdd:PRK13648 20 DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMI--------GIEKVKSGEIFYNNQAITDDNFEKLrkhigivfqn 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 448 --------ICK---ALPL-----PVDD--KSLSEVLHQVGLGKLAarihDHDRwgDILSSGEKQRIALARLILRRPKWIF 509
Cdd:PRK13648 92 pdnqfvgsIVKydvAFGLenhavPYDEmhRRVSEALKQVDMLERA----DYEP--NALSGGQKQRVAIAGVLALNPSVII 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 446551198 510 LDETTSHLEEQEAIRLLRLVREKLPTSGV--IMVTH 543
Cdd:PRK13648 166 LDEATSMLDPDARQNLLDLVRKVKSEHNItiISITH 201
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
383-557 |
1.16e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.86 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 383 LENLNFHVSPGKWLLLKGYSGAGKTTLLKTLshcwpwfkgdisspagswyvsqtpLIKSGllKEIICKALPLPVDDKSLS 462
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG------------------------LYASG--KARLISFLPKFSRNKLIF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 463 ----EVLHQVGLGKLAArihdhDRWGDILSSGEKQRIALARLILRRPK--WIFLDETTSHLEEQEAIRLLRLVReKLPTS 536
Cdd:cd03238 65 idqlQFLIDVGLGYLTL-----GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIK-GLIDL 138
|
170 180
....*....|....*....|...
gi 446551198 537 G--VIMVTHQPGVWNLADDICDI 557
Cdd:cd03238 139 GntVILIEHNLDVLSSADWIIDF 161
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
361-543 |
1.17e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 50.37 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 361 KNCQHAVQVANASIR-TPDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDIS------SPAGSWY- 432
Cdd:PRK13632 2 KNKSVMIKVENVSFSyPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKidgitiSKENLKEi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 433 ------VSQTP--------------------LIKSGLLKEIIckalplpvddkslSEVLHQVGLGKLAarihdhDRWGDI 486
Cdd:PRK13632 82 rkkigiIFQNPdnqfigatveddiafglenkKVPPKKMKDII-------------DDLAKKVGMEDYL------DKEPQN 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 487 LSSGEKQRIALARLILRRPKWIFLDETTSHLE---EQEAIRLLRLVREKlPTSGVIMVTH 543
Cdd:PRK13632 143 LSGGQKQRVAIASVLALNPEIIIFDESTSMLDpkgKREIKKIMVDLRKT-RKKTLISITH 201
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
378-547 |
1.47e-06 |
|
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: 50.96 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 378 DNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTL-----------------SHC----W---PWFKGDISSPAGS--- 430
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgmdqyeptsgriiyhvALCekcgYverPSKVGEPCPVCGGtle 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 431 ------WYVSQTplIKSGLLKEI---ICKALPLPVDDKSLSEV---LHQVGLG---------KLAARIHDHDRWGDI--- 486
Cdd:TIGR03269 91 peevdfWNLSDK--LRRRIRKRIaimLQRTFALYGDDTVLDNVleaLEEIGYEgkeavgravDLIEMVQLSHRITHIard 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446551198 487 LSSGEKQRIALARLILRRPKWIFLDETTSHLEEQEAIRLLRLVREKLPTSGVIMV--THQPGV 547
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVltSHWPEV 231
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
383-561 |
1.75e-06 |
|
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: 50.57 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 383 LENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDISSPAGSWYVSQT---PLIKS------GLL--------- 444
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTkpgPDGRGrakryiGILhqeydlyph 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 445 -------KEIICKALPLPVDDKSLSEVLHQVGLGKLAARiHDHDRWGDILSSGEKQRIALARLILRRPKWIFLDETTSHL 517
Cdd:TIGR03269 380 rtvldnlTEAIGLELPDELARMKAVITLKMVGFDEEKAE-EILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTM 458
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446551198 518 EEQEAIRLLRLV---REKLPTSGVImVTHQpgvWNLADDICDISAVL 561
Cdd:TIGR03269 459 DPITKVDVTHSIlkaREEMEQTFII-VSHD---MDFVLDVCDRAALM 501
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
463-546 |
1.92e-06 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 49.32 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 463 EVLHQVGLgklAARIHdHdrWGDILSSGEKQRIALARLILRRPKWIFLDETTSHLEEQEAIRLLRLVREkLPTSGVIM-- 540
Cdd:PRK09493 119 ELLAKVGL---AERAH-H--YPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQD-LAEEGMTMvi 191
|
....*.
gi 446551198 541 VTHQPG 546
Cdd:PRK09493 192 VTHEIG 197
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
383-555 |
2.09e-06 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 50.15 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 383 LENLNFHVSPGKWLLLKGYSGAGKTTLLKtlshC-----WP-----WFKG---DISSPA-----GswYVSQTPL------ 438
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLR----IiagleTPdsgriVLNGrdlFTNLPPrerrvG--FVFQHYAlfphmt 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 439 ----IKSGLlkeiicKALPLPVDD--KSLSEVLHQVGLGKLAarihdhDRWGDILSSGEKQRIALARLILRRPKWIFLDE 512
Cdd:COG1118 92 vaenIAFGL------RVRPPSKAEirARVEELLELVQLEGLA------DRYPSQLSGGQRQRVALARALAVEPEVLLLDE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446551198 513 TTSHL-----EEQEaiRLLRLVREKLPTSgVIMVTHQPG-VWNLADDIC 555
Cdd:COG1118 160 PFGALdakvrKELR--RWLRRLHDELGGT-TVFVTHDQEeALELADRVV 205
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
378-550 |
2.11e-06 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 49.18 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 378 DNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHcWP---------WFKG-DIS--SP-----AGSWYVSQTPLIK 440
Cdd:TIGR01978 11 EDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAG-HPsyevtsgtiLFKGqDLLelEPderarAGLFLAFQYPEEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 441 SGL-LKEIICKAL----------PLPVDD--KSLSEVLHQVGL-GKLAARIHDhdrwgDILSSGEKQRIALARLILRRPK 506
Cdd:TIGR01978 90 PGVsNLEFLRSALnarrsargeePLDLLDfeKLLKEKLALLDMdEEFLNRSVN-----EGFSGGEKKRNEILQMALLEPK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446551198 507 WIFLDETTSHLEeqeaIRLLRLVRE-----KLPTSGVIMVTHQPGVWNL 550
Cdd:TIGR01978 165 LAILDEIDSGLD----IDALKIVAEginrlREPDRSFLIITHYQRLLNY 209
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
348-518 |
2.18e-06 |
|
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: 50.68 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 348 FHQLTEQRPTNKPKNCQHAVQVANASIR-TPdnkiILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDISS 426
Cdd:TIGR01271 410 FEKIKQNNKARKQPNGDDGLFFSNFSLYvTP----VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKH 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 427 PAGSWYVSQTPLIKSGLLKEIICkaLPLPVDDKSLSEVLHQVGLGKLAARIHDHDR-----WGDILSSGEKQRIALARLI 501
Cdd:TIGR01271 486 SGRISFSPQTSWIMPGTIKDNII--FGLSYDEYRYTSVIKACQLEEDIALFPEKDKtvlgeGGITLSGGQRARISLARAV 563
|
170
....*....|....*..
gi 446551198 502 LRRPKWIFLDETTSHLE 518
Cdd:TIGR01271 564 YKDADLYLLDSPFTHLD 580
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
462-561 |
2.60e-06 |
|
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: 49.03 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 462 SEVLHQVGLgklaaRIHDHDRWGDILSSGEKQRIALARLILRRPKWIFLDETTSHLE---EQEAIRLLRLVREKLPTSgV 538
Cdd:TIGR02769 131 AELLDMVGL-----RSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDmvlQAVILELLRKLQQAFGTA-Y 204
|
90 100
....*....|....*....|...
gi 446551198 539 IMVTHQpgvWNLADDICDISAVL 561
Cdd:TIGR02769 205 LFITHD---LRLVQSFCQRVAVM 224
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
376-543 |
3.60e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 48.54 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 376 TPDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLShcwpwfkGDISSPAGS----------W-------YVS---Q 435
Cdd:COG1101 15 TVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIA-------GSLPPDSGSilidgkdvtkLpeykrakYIGrvfQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 436 TPLI------------------------KSGLLKEiickalplpvDDKSLSEVLHQVGLGkLAARIhdHDRWGdILSSGE 491
Cdd:COG1101 88 DPMMgtapsmtieenlalayrrgkrrglRRGLTKK----------RRELFRELLATLGLG-LENRL--DTKVG-LLSGGQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446551198 492 KQRIALARLILRRPKWIFLDETTSHLEEQEAIRLL----RLVRE-KLPTsgvIMVTH 543
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLelteKIVEEnNLTT---LMVTH 207
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
483-518 |
4.96e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.64 E-value: 4.96e-06
10 20 30
....*....|....*....|....*....|....*.
gi 446551198 483 WGDILSSGEKQRIALARLILRRPKWIFLDETTSHLE 518
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
461-543 |
9.86e-06 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 47.37 E-value: 9.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 461 LSEVLHQVGLgklaaRIHDHDRWGDILSSGEKQRIALARLILRRPKWIFLDETTSHLE---EQEAIRLLRLVREKLPTsG 537
Cdd:PRK10419 131 ASEMLRAVDL-----DDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDlvlQAGVIRLLKKLQQQFGT-A 204
|
....*.
gi 446551198 538 VIMVTH 543
Cdd:PRK10419 205 CLFITH 210
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
487-543 |
1.02e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 47.77 E-value: 1.02e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 446551198 487 LSSGEKQRIALARLILRRPKWIFLDETTSHLEEQEAIRLLRLVrEKLPTSG--VIMVTH 543
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIF-DNLNKQGktIILVTH 223
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
383-544 |
1.04e-05 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 47.31 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 383 LENLNFHVSPGKWLLLKGYSGAGKTTLLKTLS--------------------HCWPWFKGDI-SSPAGSWYV-SQTPLI- 439
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSglitgdksagshiellgrtvQREGRLARDIrKSRANTGYIfQQFNLVn 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 440 KSGLLKEIICKAL---PL---------PVDDKSLSEVLHQVGLGKLAarihdHDRWgDILSSGEKQRIALARLILRRPKW 507
Cdd:PRK09984 100 RLSVLENVLIGALgstPFwrtcfswftREQKQRALQALTRVGMVHFA-----HQRV-STLSGGQQQRVAIARALMQQAKV 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 446551198 508 IFLDETTSHLEEQEAIRLLRLVREKLPTSGVIMVT--HQ 544
Cdd:PRK09984 174 ILADEPIASLDPESARIVMDTLRDINQNDGITVVVtlHQ 212
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
383-561 |
1.12e-05 |
|
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: 46.59 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 383 LENLNFHVSPGKWLLLKGYSGAGKTTLLKTLShcwpwfkGDISSPAGS-----WYVSQTPL---IKSGLL--KEIICKAL 452
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLA-------GLLEPDAGFatvdgFDVVKEPAearRRLGFVsdSTGLYDRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 453 plpvddkSLSEV------LHQVGLGKLAARIHD----------HDRWGDILSSGEKQRIALARLILRRPKWIFLDETTSH 516
Cdd:cd03266 94 -------TARENleyfagLYGLKGDELTARLEEladrlgmeelLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446551198 517 LEEQeAIRLLRLVREKLPTSG--VIMVTHqpgVWNLADDICDISAVL 561
Cdd:cd03266 167 LDVM-ATRALREFIRQLRALGkcILFSTH---IMQEVERLCDRVVVL 209
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
380-556 |
1.16e-05 |
|
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: 46.50 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 380 KIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLShcwpwfkgDISSPagswyvsqtpliKSGllkEIICKALPLPVDDK 459
Cdd:cd03269 13 VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMIL--------GIILP------------DSG---EVLFDGKPLDIAAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 460 S----LSE---------VLHQV-------GLGKLAARiHDHDRW-------------GDILSSGEKQRIALARLILRRPK 506
Cdd:cd03269 70 NrigyLPEerglypkmkVIDQLvylaqlkGLKKEEAR-RRIDEWlerlelseyankrVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446551198 507 WIFLDETTSHLEEQEAIRLLRLVREkLPTSG--VIMVTHQpgvWNLADDICD 556
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRE-LARAGktVILSTHQ---MELVEELCD 196
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
378-545 |
1.17e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.57 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 378 DNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLS-----------------HcwpwfKGDISSPAGSWYVSQTPL-I 439
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAervttgvitggdrlvngR-----PLDSSFQRSIGYVQQQDLhL 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 440 KSGLLKEII--------CKALPLPVDDKSLSEVLHQVGLGKLAARIHDHDrwGDILSSGEKQRIALARLILRRPK-WIFL 510
Cdd:TIGR00956 849 PTSTVRESLrfsaylrqPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVP--GEGLNVEQRKRLTIGVELVAKPKlLLFL 926
|
170 180 190
....*....|....*....|....*....|....*..
gi 446551198 511 DETTSHLEEQEAIRLLRLVReKLPTSG-VIMVT-HQP 545
Cdd:TIGR00956 927 DEPTSGLDSQTAWSICKLMR-KLADHGqAILCTiHQP 962
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
377-543 |
1.26e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.81 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 377 PDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGD-ISSPA---GswYVSQTPL----------IKSG 442
Cdd:PRK11819 17 PPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEaRPAPGikvG--YLPQEPQldpektvrenVEEG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 443 L---------LKEIICK-ALPLPVDDKSLSEvlhqvgLGKLAARIHDHDRW-----------------GD----ILSSGE 491
Cdd:PRK11819 95 VaevkaaldrFNEIYAAyAEPDADFDALAAE------QGELQEIIDAADAWdldsqleiamdalrcppWDakvtKLSGGE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446551198 492 KQRIALARLILRRPKWIFLDETTSHLEEQEAIRLLRLVREKLPTsgVIMVTH 543
Cdd:PRK11819 169 RRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGT--VVAVTH 218
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
392-543 |
2.20e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 47.09 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 392 PGKWLLLKGYSGAGKTTLLKTLS-HCWPWFkGDISSPAgSW-------------------------------YVSQTPLI 439
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSgELKPNL-GDYDEEP-SWdevlkrfrgtelqdyfkklangeikvahkpqYVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 440 KSGLLKEIICKalplpVDDK-SLSEVLHQVGLGKLAarihdhDRWGDILSSGEKQRIALARLILRRPKWIFLDETTSHLE 518
Cdd:COG1245 176 FKGTVRELLEK-----VDERgKLDELAEKLGLENIL------DRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
170 180
....*....|....*....|....*..
gi 446551198 519 EQEAIRLLRLVREkLPTSG--VIMVTH 543
Cdd:COG1245 245 IYQRLNVARLIRE-LAEEGkyVLVVEH 270
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
364-546 |
2.46e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 46.03 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 364 QHAVQVANASIRTPDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDIS---SPAGSW-------YV 433
Cdd:PRK15056 4 QAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISilgQPTRQAlqknlvaYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 434 SQTPLIKSG---LLKEIICKA---------LPLPVDDKSLSEVLHQVGLGKlaariHDHDRWGDiLSSGEKQRIALARLI 501
Cdd:PRK15056 84 PQSEEVDWSfpvLVEDVVMMGryghmgwlrRAKKRDRQIVTAALARVDMVE-----FRHRQIGE-LSGGQKKRVFLARAI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446551198 502 LRRPKWIFLDETTSHLEEQEAIRLLRLVREkLPTSGVIMV--THQPG 546
Cdd:PRK15056 158 AQQGQVILLDEPFTGVDVKTEARIISLLRE-LRDEGKTMLvsTHNLG 203
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
382-546 |
2.91e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 45.67 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 382 ILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGdiSSPAGSWYVSQTPLIKSGLLK-----EIICKaLPLPV 456
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPE--ARVSGEVYLDGQDIFKMDVIElrrrvQMVFQ-IPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 457 DDKSLSEvlhQVGLGKLAARIHDHDR---------------WGDI----------LSSGEKQRIALARLILRRPKWIFLD 511
Cdd:PRK14247 95 PNLSIFE---NVALGLKLNRLVKSKKelqervrwalekaqlWDEVkdrldapagkLSGGQQQRLCIARALAFQPEVLLAD 171
|
170 180 190
....*....|....*....|....*....|....*
gi 446551198 512 ETTSHLEEQEAIRLLRLVREKLPTSGVIMVTHQPG 546
Cdd:PRK14247 172 EPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQ 206
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
378-556 |
3.13e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 45.87 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 378 DNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLShcwpwfkgDISSP-AGSWYVSQTPLIKS------------GLL 444
Cdd:COG4152 12 GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIIL--------GILAPdSGEVLWDGEPLDPEdrrrigylpeerGLY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 445 K-----EIIC-----KALPLPVDDKSLSEVLHQVGLGklaarihdhDRWGD-I--LSSGEKQRIALARLILRRPKWIFLD 511
Cdd:COG4152 84 PkmkvgEQLVylarlKGLSKAEAKRRADEWLERLGLG---------DRANKkVeeLSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446551198 512 ETTSHL--EEQEAIR--LLRLVREKLPtsgVIMVTHQpgvWNLADDICD 556
Cdd:COG4152 155 EPFSGLdpVNVELLKdvIRELAAKGTT---VIFSSHQ---MELVEELCD 197
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
347-561 |
3.53e-05 |
|
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: 45.22 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 347 EFHQLTEQRPTNKPKNCQHAVQVANASIRTPDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDISS 426
Cdd:cd03220 2 ELENVSKSYPTYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 427 pAGSwyVSqtPLIK--SGLLKE------IICKALPLPVDDKSLSEVLHQV----GLGKlaaRIHDHDRwgdILSSGEKQR 494
Cdd:cd03220 82 -RGR--VS--SLLGlgGGFNPEltgrenIYLNGRLLGLSRKEIDEKIDEIiefsELGD---FIDLPVK---TYSSGMKAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446551198 495 IALARLILRRPKWIFLDETTSHLEEQEAIRLLRLVREKL-PTSGVIMVTHQPgvwNLADDICDISAVL 561
Cdd:cd03220 151 LAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLkQGKTVILVSHDP---SSIKRLCDRALVL 215
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
366-543 |
3.55e-05 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 45.46 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 366 AVQVANASIRTPdNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDI-------SSP-AGSWYVSQtp 437
Cdd:PRK11248 1 MLQISHLYADYG-GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSItldgkpvEGPgAERGVVFQ-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 438 liKSGLL-----KEIICKALPLPVDDKS-----LSEVLHQVGLgklaARIHDHDRWGdiLSSGEKQRIALARLILRRPKW 507
Cdd:PRK11248 78 --NEGLLpwrnvQDNVAFGLQLAGVEKMqrleiAHQMLKKVGL----EGAEKRYIWQ--LSGGQRQRVGIARALAANPQL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446551198 508 IFLDETTSHLE----EQEAIRLLRLVREKlpTSGVIMVTH 543
Cdd:PRK11248 150 LLLDEPFGALDaftrEQMQTLLLKLWQET--GKQVLLITH 187
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
379-512 |
4.16e-05 |
|
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: 45.23 E-value: 4.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 379 NKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTL------SHCWPWFKG-DIS-------SPAGSWYVSQTPLIKSGL- 443
Cdd:cd03218 12 KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIvglvkpDSGKILLDGqDITklpmhkrARLGIGYLPQEASIFRKLt 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446551198 444 LKEIICKALPLPVDDKS-----LSEVLHQVGLGKLAarihdhDRWGDILSSGEKQRIALARLILRRPKWIFLDE 512
Cdd:cd03218 92 VEENILAVLEIRGLSKKereekLEELLEEFHITHLR------KSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
375-517 |
5.77e-05 |
|
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: 45.83 E-value: 5.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 375 RTPDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWP-----WFKG-DISS-------------------PAG 429
Cdd:COG4172 294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPsegeiRFDGqDLDGlsrralrplrrrmqvvfqdPFG 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 430 S----WYVSQtpliksgllkeIIckALPLPVDDKSLS---------EVLHQVGLGKlAARihdhDRWGDILSSGEKQRIA 496
Cdd:COG4172 374 SlsprMTVGQ-----------II--AEGLRVHGPGLSaaerrarvaEALEEVGLDP-AAR----HRYPHEFSGGQRQRIA 435
|
170 180
....*....|....*....|..
gi 446551198 497 LAR-LILrRPKWIFLDETTSHL 517
Cdd:COG4172 436 IARaLIL-EPKLLVLDEPTSAL 456
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
382-554 |
6.75e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.47 E-value: 6.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 382 ILENLNFHVSPGKWLLLKGYSGAGKTT-------LLKTLSHCWPwfKGDISSPAGSWYVSQTPLIK-------SGLLKEI 447
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSVtalsilrLLPSPPVVYP--SGDIRFHGESLLHASEQTLRgvrgnkiAMIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 448 ICKALPLPVDDKSLSEVL--HQvGLGKLAAR---IHDHDRWG---------DI---LSSGEKQRIALARLILRRPKWIFL 510
Cdd:PRK15134 102 MVSLNPLHTLEKQLYEVLslHR-GMRREAARgeiLNCLDRVGirqaakrltDYphqLSGGERQRVMIAMALLTRPELLIA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446551198 511 DETTSHLE---EQEAIRLLRLVREKLpTSGVIMVTHQPG-VWNLADDI 554
Cdd:PRK15134 181 DEPTTALDvsvQAQILQLLRELQQEL-NMGLLFITHNLSiVRKLADRV 227
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
463-557 |
8.03e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 45.49 E-value: 8.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 463 EVLHQVGLGKlaaRIHDHDrwgDILSSGEKQRIALARLILRRPKWIFLDETTSHLEEQ---EAIRLLRLVREKLPTsgVI 539
Cdd:PRK10535 127 ELLQRLGLED---RVEYQP---SQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHsgeEVMAILHQLRDRGHT--VI 198
|
90
....*....|....*...
gi 446551198 540 MVTHQPGVWNLADDICDI 557
Cdd:PRK10535 199 IVTHDPQVAAQAERVIEI 216
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
487-560 |
8.92e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.12 E-value: 8.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 487 LSSGEKQRIALA-----RLILRRPkWIFLDETTSHLEEQEAIRLLRLVREKL-PTSGVIMVTHQPGVWNLADDICDISAV 560
Cdd:cd03227 78 LSGGEKELSALAlilalASLKPRP-LYILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAELADKLIHIKKV 156
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
368-552 |
1.30e-04 |
|
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: 44.82 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 368 QVANASIRTPDNKII--LENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPwfkgdiSSPAGSWYVSQTPLIKSGLLK 445
Cdd:TIGR02633 259 EARNLTCWDVINPHRkrVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYP------GKFEGNVFINGKPVDIRNPAQ 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 446 EIICKALPLPVDDKSlSEVLHQVGLGK---LAA--------RIHDHDRWGDI--------------------LSSGEKQR 494
Cdd:TIGR02633 333 AIRAGIAMVPEDRKR-HGIVPILGVGKnitLSVlksfcfkmRIDAAAELQIIgsaiqrlkvktaspflpigrLSGGNQQK 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446551198 495 IALARLILRRPKWIFLDETTSHLE---EQEAIRLL-RLVREKLptsGVIMVTHQ-PGVWNLAD 552
Cdd:TIGR02633 412 AVLAKMLLTNPRVLILDEPTRGVDvgaKYEIYKLInQLAQEGV---AIIVVSSElAEVLGLSD 471
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
371-555 |
1.80e-04 |
|
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: 43.02 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 371 NASIRTP---DNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWF---KGDIS------------SPAGSWY 432
Cdd:cd03233 8 NISFTTGkgrSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHyngipykefaekYPGEIIY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 433 VSQTPL-IKSGLLKEIIckalplpvdDKSLSEVLHQVGLGklaarihdhdrwgdiLSSGEKQRIALARLILRRPKWIFLD 511
Cdd:cd03233 88 VSEEDVhFPTLTVRETL---------DFALRCKGNEFVRG---------------ISGGERKRVSIAEALVSRASVLCWD 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446551198 512 ETTSHLEEQEAIRLLRLVREKLPTSG--VIMVTHQPG--VWNLADDIC 555
Cdd:cd03233 144 NSTRGLDSSTALEILKCIRTMADVLKttTFVSLYQASdeIYDLFDKVL 191
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
487-545 |
2.81e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 42.91 E-value: 2.81e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 446551198 487 LSSGEKQRIALARLILRRPKWIFLDETTSHLEEQEAIRLLRLVREKLPTSGVIMVTHQP 545
Cdd:PRK14267 150 LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSP 208
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
484-523 |
5.07e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 42.70 E-value: 5.07e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 446551198 484 GDILSSGEKQRIALARLILRRPKWIFLDETTSHL--EEQEAI 523
Cdd:PRK11176 478 GVLLSGGQRQRIAIARALLRDSPILILDEATSALdtESERAI 519
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
378-554 |
6.12e-04 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 42.32 E-value: 6.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 378 DNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLShcwpwfkG--DISSpaGSWY-----VSQTPLIKSGLLKEIICK 450
Cdd:PRK11000 14 GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIA-------GleDITS--GDLFigekrMNDVPPAERGVGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 451 AL-P-LPVDDkSLSEVLHQVGLGKL--------AARI----HDHDRWGDILSSGEKQRIALARLILRRPKWIFLDETTSH 516
Cdd:PRK11000 85 ALyPhLSVAE-NMSFGLKLAGAKKEeinqrvnqVAEVlqlaHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446551198 517 LEE----QEAIRLLRLvrEKLPTSGVIMVTH-QPGVWNLADDI 554
Cdd:PRK11000 164 LDAalrvQMRIEISRL--HKRLGRTMIYVTHdQVEAMTLADKI 204
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
367-518 |
6.23e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 41.68 E-value: 6.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 367 VQVANASIRTPDNKIiLENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPW-----FKGDISSPAGSWYVSQTPLIKs 441
Cdd:PRK14239 6 LQVSDLSVYYNKKKA-LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLnpevtITGSIVYNGHNIYSPRTDTVD- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 442 gLLKEI---ICKALPLP---------------VDDKslsEVLHQVGLGKL-AARIHDH--DRWGDI---LSSGEKQRIAL 497
Cdd:PRK14239 84 -LRKEIgmvFQQPNPFPmsiyenvvyglrlkgIKDK---QVLDEAVEKSLkGASIWDEvkDRLHDSalgLSGGQQQRVCI 159
|
170 180
....*....|....*....|.
gi 446551198 498 ARLILRRPKWIFLDETTSHLE 518
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALD 180
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
487-554 |
6.26e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 42.14 E-value: 6.26e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446551198 487 LSSGEKQRIALARLILRRPKWIFLDETTSHLE---EQEAIRLLRLVREKLPTsgVIMVTHQ-PGVWNLADDI 554
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDpkgEHEMMQLILDAKANNKT--VFVITHTmEHVLEVADEV 246
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
378-542 |
1.16e-03 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 41.33 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 378 DNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLShcwpwfkgDISSP-AGSWYVSQTPLIKSGLLKEIICKALPL-- 454
Cdd:PRK13537 18 GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLL--------GLTHPdAGSISLCGEPVPSRARHARQRVGVVPQfd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 455 PVD-DKSLSEVLHQVG--LGKLAARIHD---------------HDRWGDiLSSGEKQRIALARLILRRPKWIFLDETTSH 516
Cdd:PRK13537 90 NLDpDFTVRENLLVFGryFGLSAAAARAlvppllefaklenkaDAKVGE-LSGGMKRRLTLARALVNDPDVLVLDEPTTG 168
|
170 180
....*....|....*....|....*.
gi 446551198 517 LEEQEAIRLLRLVREKLPTSGVIMVT 542
Cdd:PRK13537 169 LDPQARHLMWERLRSLLARGKTILLT 194
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
382-512 |
1.18e-03 |
|
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: 40.74 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 382 ILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWP------WFKG-DIS--SP-----AGSWYVSQTPLIKSGL---- 443
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPprsgsiRFDGeDITglPPhriarLGIGYVPEGRRIFPSLtvee 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446551198 444 -LkEIickALPLPVDDKSLSEVLHQVgLG---KLAARIHdhdRWGDILSSGEKQRIALARLILRRPKWIFLDE 512
Cdd:COG0410 98 nL-LL---GAYARRDRAEVRADLERV-YElfpRLKERRR---QRAGTLSGGEQQMLAIGRALMSRPKLLLLDE 162
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
463-518 |
1.32e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 41.10 E-value: 1.32e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 446551198 463 EVLHQVGLgklaaRIHDHDRWGDILSSGEKQRIALARLILRRPKWIFLDETTSHLE 518
Cdd:PRK11308 136 AMMAKVGL-----RPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
463-557 |
1.36e-03 |
|
ATP-binding cassette domain I 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: 213237 [Multi-domain] Cd Length: 226 Bit Score: 40.32 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 463 EVLHQVGLGKLAArihdhDRWGDILSSGEKQRIALARLI---LRRPKWIfLDETTSHLEEQEAIRLLRLVReKLPTSG-- 537
Cdd:cd03270 119 GFLVDVGLGYLTL-----SRSAPTLSGGEAQRIRLATQIgsgLTGVLYV-LDEPSIGLHPRDNDRLIETLK-RLRDLGnt 191
|
90 100
....*....|....*....|
gi 446551198 538 VIMVTHQPGVWNLADDICDI 557
Cdd:cd03270 192 VLVVEHDEDTIRAADHVIDI 211
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
487-544 |
1.56e-03 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 40.72 E-value: 1.56e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 487 LSSGEKQRIALARLILRRPKWIFLDETTSHLEEQEAIRLLRLVrEKLPTSG--VIMVTHQ 544
Cdd:PRK10619 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIM-QQLAEEGktMVVVTHE 211
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
485-552 |
1.56e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.50 E-value: 1.56e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446551198 485 DILSSGEKQRIALArLIL----RRPKWIF-LDETTSHLEEQEAIRLLRLVREKLPTSGVIMVTHQPGVWNLAD 552
Cdd:pfam02463 1076 DLLSGGEKTLVALA-LIFaiqkYKPAPFYlLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKAD 1147
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
484-543 |
1.70e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 40.54 E-value: 1.70e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 484 GDILSSGEKQRIALARLILRRPKWIFLDETTSHLEEQEAIRLLRLVREKLPTSGVIMVTH 543
Cdd:PRK14243 149 GLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTH 208
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
488-556 |
1.82e-03 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 40.86 E-value: 1.82e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446551198 488 SSGEKQRIALARLILRRPKWIFLDETTSHLE---EQEAIRLLRLVREKLPTSgVIMVTHQPGVwnlADDICD 556
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDvtvQAQIMTLLNELKREFNTA-IIMITHDLGV---VAGICD 230
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
382-543 |
2.24e-03 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 39.88 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 382 ILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKG-------DIS-------SPAGSWYVSQTPLIKSGLlkEI 447
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGniiiddeDISllplharARRGIGYLPQEASIFRRL--SV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 448 ICKALPLPVDDKSLSEVLHQVGLGKLAARIH-DH--DRWGDILSSGEKQRIALARLILRRPKWIFLDETTSHLEEQEAIR 524
Cdd:PRK10895 96 YDNLMAVLQIRDDLSAEQREDRANELMEEFHiEHlrDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVID 175
|
170 180
....*....|....*....|.
gi 446551198 525 LLRLVrEKLPTS--GVIMVTH 543
Cdd:PRK10895 176 IKRII-EHLRDSglGVLITDH 195
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
487-552 |
2.34e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 39.37 E-value: 2.34e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551198 487 LSSGEKQRIALARL--ILR-RPK-WIFLDETTSHLEEQEAIRLLRLVREKLPTSGVIMVTHQPGVWNLAD 552
Cdd:cd03278 114 LSGGEKALTALALLfaIFRvRPSpFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAAD 183
|
|
| |
