|
Name |
Accession |
Description |
Interval |
E-value |
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
1-567 |
0e+00 |
|
type I secretion system ATPase, LssB 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. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 791.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 1 MPKAWFFKVIWRFKKYYYQIILATFVINFLALVSSLYVMNVYDRVIPNKSYQTLWVLSIGVIIAILFEFTAKMLRGRLTD 80
Cdd:TIGR03375 133 RPKHWFWSTLKESWPLYRDVLIASLLINLLALASPLFVMNVYDRVVPNQAFETLWVLAIGVALAIVFDFVLKTLRSYFLD 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 81 IAGKKADLIISSALFRKVTNLKLQEKPISSGSYVNNLRDFESVRDFMTSASLLTLVDMPFLILFVSVIALVGGYLAFVPL 160
Cdd:TIGR03375 213 VAGKKADLILSAKLFERVLGLRMEARPASVGSFANQLREFESVRDFFTSATLTALIDLPFALLFLLVIAIIGGPLVWVPL 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 161 TIIPLVIIVGLLAQIPLSKYINESMKESSQRQGLAVEAIEGIETLKTNNAMNWAQKRWDYYTAKTASSSMKVKNISNFVI 240
Cdd:TIGR03375 293 VAIPLILLPGLLLQRPLSRLAEESMRESAQRNAVLVESLSGLETIKALNAEGRFQRRWEQTVAALARSGLKSRFLSNLAT 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 241 YFAVMMQQLNTIFLVIIGTYLIhsddPASKITMGALIATVILSGRALSPLGQIAGLAVRFQQAWVALKGVNGIVERPSER 320
Cdd:TIGR03375 373 NFAQFIQQLVSVAIVVVGVYLI----SDGELTMGGLIACVMLSGRALAPLGQLAGLLTRYQQAKTALQSLDELMQLPVER 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 321 ESARKYITLKQINGNIKFQNVSFAYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVD 400
Cdd:TIGR03375 449 PEGTRFLHRPRLQGEIEFRNVSFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVD 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 401 IRQIDPHYLRNQVLLLEQEPRLFLGSLRENLDLARmdGFSSDQDLIVALKRFGLDKVIKKHPRGLDMSLGENGLGLSGGQ 480
Cdd:TIGR03375 529 IRQIDPADLRRNIGYVPQDPRLFYGTLRDNIALGA--PYADDEEILRAAELAGVTEFVRRHPDGLDMQIGERGRSLSGGQ 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 481 KQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSKTLLVVTHRPQVLSIVNRIIVVDNGKVVMDGPRDAV 560
Cdd:TIGR03375 607 RQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVTHRTSLLDLVDRIIVMDNGRIVADGPKDQV 686
|
....*..
gi 1437745540 561 LQQLAKN 567
Cdd:TIGR03375 687 LEALRKG 693
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-563 |
0e+00 |
|
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: 618.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 2 PKAWFFKVIWRFKKYYYQIILATFVINFLALVSSLYVMNVYDRVIPNKSYQTLWVLSIGVIIAILFEFTAKMLRGRLTDI 81
Cdd:COG2274 143 GLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLR 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 82 AGKKADLIISSALFRKVTNLKLQEKPI-SSGSYVNNLRDFESVRDFMTSASLLTLVDMPFLILFVSVIALVGGYLAFVPL 160
Cdd:COG2274 223 LGQRIDLRLSSRFFRHLLRLPLSFFESrSVGDLASRFRDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 161 TIIPLVIIVGLLAQIPLSKYINESMKESSQRQGLAVEAIEGIETLKTNNAMNWAQKRWDYYTAKTASSSMKVKNISNFVI 240
Cdd:COG2274 303 LLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLS 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 241 YFAVMMQQLNTIFLVIIGTYLIHSDDpaskITMGALIATVILSGRALSPLGQIAGLAVRFQQAWVALKGVNGIVERPSER 320
Cdd:COG2274 383 TLSGLLQQLATVALLWLGAYLVIDGQ----LTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPER 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 321 ESARKYITLKQINGNIKFQNVSFAYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVD 400
Cdd:COG2274 459 EEGRSKLSLPRLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGID 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 401 IRQIDPHYLRNQVLLLEQEPRLFLGSLRENLDLARMDgfSSDQDLIVALKRFGLDKVIKKHPRGLDMSLGENGLGLSGGQ 480
Cdd:COG2274 539 LRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPD--ATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQ 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 481 KQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSKTLLVVTHRPQVLSIVNRIIVVDNGKVVMDGPRDAV 560
Cdd:COG2274 617 RQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEEL 696
|
...
gi 1437745540 561 LQQ 563
Cdd:COG2274 697 LAR 699
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
14-310 |
2.15e-150 |
|
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.
Pssm-ID: 350031 Cd Length: 293 Bit Score: 434.17 E-value: 2.15e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 14 KKYYYQIILATFVINFLALVSSLYVMNVYDRVIPNKSYQTLWVLSIGVIIAILFEFTAKMLRGRLTDIAGKKADLIISSA 93
Cdd:cd18587 1 RRIYRDVLLAALLINLFALASPLFVMNVYDRVVPNNAIETLWVLAIGVLIALLFDFILKLLRAYFIDVAGKRADVILSSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 94 LFRKVTNLKLQEKPISSGSYVNNLRDFESVRDFMTSASLLTLVDMPFLILFVSVIALVGGYLAFVPLTIIPLVIIVGLLA 173
Cdd:cd18587 81 LFERVLGLRLEARPASVGSFANNLREFESVRDFFTSATLTALIDLPFVLLFLAVIALIGGPLALVPLVAIPLVLLYGLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 174 QIPLSKYINESMKESSQRQGLAVEAIEGIETLKTNNAMNWAQKRWDYYTAKTASSSMKVKNISNFVIYFAVMMQQLNTIF 253
Cdd:cd18587 161 QKPLRRLVEESMRESAQKNALLVESLSGLETIKALGAEGRMQRRWEEAVAALARSSLKSRLLSSSATNFAQFVQQLVTVA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745540 254 LVIIGTYLIHSDDpaskITMGALIATVILSGRALSPLGQIAGLAVRFQQAWVALKGV 310
Cdd:cd18587 241 IVIVGVYLISDGE----LTMGGLIACVILSGRALAPLGQIAGLLTRYQQARTALKSL 293
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
5-563 |
2.25e-114 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 352.16 E-value: 2.25e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 5 WFFKVIWRFKKYYYQIILATFVINFLALVSSLYVMNVYDRVIPNKSYQTLWVLSIGVIIAILFEFTAKMLRGRLTDIAGK 84
Cdd:COG1132 11 RLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 85 KADLIISSALFRKVTNLKLQ--EKPiSSGSYVNNL-RDFESVRDFMTSaSLLTLVDMPFLILFVSVIALV-GGYLAFVPL 160
Cdd:COG1132 91 RVVADLRRDLFEHLLRLPLSffDRR-RTGDLLSRLtNDVDAVEQFLAH-GLPQLVRSVVTLIGALVVLFViDWRLALIVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 161 TIIPLVIIVGLLAQIPLSKYINESMKESSQRQGLAVEAIEGIETLKTNNAMNWAQKRWDYYTAKTASSSMKVKNISNFVI 240
Cdd:COG1132 169 LVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFF 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 241 YFAVMMQQLNTIFLVIIGTYLIHSDDpaskITMGALIATVILSGRALSPLGQIAGLAVRFQQAWVALKGVNGIVERPSER 320
Cdd:COG1132 249 PLMELLGNLGLALVLLVGGLLVLSGS----LTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 321 ESARKYITLKQINGNIKFQNVSFAYNqDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVD 400
Cdd:COG1132 325 PDPPGAVPLPPVRGEIEFENVSFSYP-GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 401 IRQIDPHYLRNQVLLLEQEPRLFLGSLRENLDLARMDgfSSDQDLIVALKRFGLDKVIKKHPRGLDMSLGENGLGLSGGQ 480
Cdd:COG1132 404 IRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPD--ATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQ 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 481 KQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSKTLLVVTHRPQVLSIVNRIIVVDNGKVVMDGPRDAV 560
Cdd:COG1132 482 RQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEEL 561
|
...
gi 1437745540 561 LQQ 563
Cdd:COG1132 562 LAR 564
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
8-570 |
4.56e-108 |
|
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: 335.18 E-value: 4.56e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 8 KVIWRFKKYYYQIILATFVINFLALVSSLYVMNVYDRVIPNKSYQTLWVLSIGVIIAILFEFTAKMLRGRLTDIAGKKAD 87
Cdd:COG4618 13 AALRACRRAFLSVGLFSFFINLLMLTPPLYMLQVYDRVLTSRSVDTLLMLTLLALGLYAVMGLLDAVRSRILVRVGARLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 88 LIISSALFRKVTNLKLQEkpiSSGSYVNNLRDFESVRDFMTSASLLTLVDMPFLILFVSVIALVG---GYLAFVPLTIIp 164
Cdd:COG4618 93 RRLGPRVFDAAFRAALRG---GGGAAAQALRDLDTLRQFLTGPGLFALFDLPWAPIFLAVLFLFHpllGLLALVGALVL- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 165 lvIIVGLLAQIPLSKYINESMKESSQRQGLAVEAIEGIETLktnNAM---NWAQKRWDYYTAKTASSSMKVKNISNF--- 238
Cdd:COG4618 169 --VALALLNERLTRKPLKEANEAAIRANAFAEAALRNAEVI---EAMgmlPALRRRWQRANARALALQARASDRAGGfsa 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 239 VIYFAVMMQQlntIFLVIIGTYL-IHSDdpaskITMGALIATVILSGRALSPLGQIAGLAVRFQQAWVALKGVNGIVErp 317
Cdd:COG4618 244 LSKFLRLLLQ---SAVLGLGAYLvIQGE-----ITPGAMIAASILMGRALAPIEQAIGGWKQFVSARQAYRRLNELLA-- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 318 sERESARKYITLKQINGNIKFQNVSFAYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLD 397
Cdd:COG4618 314 -AVPAEPERMPLPRPKGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 398 DVDIRQIDPHYLRNQVLLLEQEPRLFLGSLRENLdlARMDGfSSDQDLIVALKRFGLDKVIKKHPRGLDMSLGENGLGLS 477
Cdd:COG4618 393 GADLSQWDREELGRHIGYLPQDVELFDGTIAENI--ARFGD-ADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 478 GGQKQIVALARMTLRNPKIVLLDEPTTGLDQYSEiQALN-AISAW-CRSKTLLVVTHRPQVLSIVNRIIVVDNGKVVMDG 555
Cdd:COG4618 470 GGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGE-AALAaAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFG 548
|
570
....*....|....*
gi 1437745540 556 PRDAVLQQLAKNETE 570
Cdd:COG4618 549 PRDEVLARLARPAAA 563
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
13-564 |
3.13e-104 |
|
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: 324.69 E-value: 3.13e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 13 FKKYYYQIILATFVINFLALVSSLYVMNVYDRVIPNKSYQTLWVLSIGVIIAILFEFTAKMLRGRLTDIAGKKADLIISS 92
Cdd:TIGR01842 4 VKRTFIIVGLFSFVINILMLAPPLYMLQVYDRVLTSGSVPTLLMLTVLALGLYLFLGLLDALRSFVLVRIGEKLDGALNQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 93 ALFRKVTNLKLQEKPISSGsyvNNLRDFESVRDFMTSASLLTLVDMPFLILFVSVIALVGGYLAFvpLTIIPLVIIVGL- 171
Cdd:TIGR01842 84 PIFAASFSATLRRGSGDGL---QALRDLDQLRQFLTGPGLFAFFDAPWMPIYLLVCFLLHPWIGI--LALGGAVVLVGLa 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 172 -LAQIPLSKYINESMKESSQRQGLAVEAIEGIETLKTNNAMNWAQKRWDY----YTAKTASSSMKVKNISNFVIYFAVMM 246
Cdd:TIGR01842 159 lLNNRATKKPLKEATEASIRANNLADSALRNAEVIEAMGMMGNLTKRWGRfhskYLSAQSAASDRAGMLSNLSKYFRIVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 247 QQLntifLVIIGTYLIHSddpaSKITMGALIATVILSGRALSPLGQIAGLAVRFQQAWVALKGVNGIVERPSERESArky 326
Cdd:TIGR01842 239 QSL----VLGLGAYLAID----GEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELLANYPSRDPA--- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 327 ITLKQINGNIKFQNVSFAYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDP 406
Cdd:TIGR01842 308 MPLPEPEGHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDR 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 407 HYLRNQVLLLEQEPRLFLGSLRENLdlARMDGFSSDQDLIVALKRFGLDKVIKKHPRGLDMSLGENGLGLSGGQKQIVAL 486
Cdd:TIGR01842 388 ETFGKHIGYLPQDVELFPGTVAENI--ARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIAL 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745540 487 ARMTLRNPKIVLLDEPTTGLDQYSEIQALNAI-SAWCRSKTLLVVTHRPQVLSIVNRIIVVDNGKVVMDGPRDAVLQQL 564
Cdd:TIGR01842 466 ARALYGDPKLVVLDEPNSNLDEEGEQALANAIkALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAKL 544
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
334-555 |
3.33e-95 |
|
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: 290.26 E-value: 3.33e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 334 GNIKFQNVSFAYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQV 413
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 414 LLLEQEPRLFLGSLRENLDLArmDGFSSDQDLIVALKRFGLDKVIKKHPRGLDMSLGENGLGLSGGQKQIVALARMTLRN 493
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLG--APLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1437745540 494 PKIVLLDEPTTGLDQYSEIQALNAISAWCRSKTLLVVTHRPQVLSIVNRIIVVDNGKVVMDG 555
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
139-563 |
4.72e-87 |
|
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: 280.88 E-value: 4.72e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 139 PFLILFVSVIALVGGYLAFVP---LTIIPLVIIVGLLaqIP-----LSKYINESMKES-SQRQGLAVEAIEGIETLKTNN 209
Cdd:COG4987 135 PLLVALLVILAAVAFLAFFSPalaLVLALGLLLAGLL--LPllaarLGRRAGRRLAAArAALRARLTDLLQGAAELAAYG 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 210 AMNWAQKRWDYYTAKTASSSMKVKNISNFVIYFAVMMQQLNTIFLVIIGTYLIHSDDPAskitmGALIATVILSGRALS- 288
Cdd:COG4987 213 ALDRALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALS-----GPLLALLVLAALALFe 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 289 PLGQIAGLAVRFQQAWVALKGVNGIVERPSERESARKYITLKQiNGNIKFQNVSFAYNQDSSSVVKILSFEIKPGEKVGI 368
Cdd:COG4987 288 ALAPLPAAAQHLGRVRAAARRLNELLDAPPAVTEPAEPAPAPG-GPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAI 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 369 LGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLLLEQEPRLFLGSLRENLDLARMDgfSSDQDLIVA 448
Cdd:COG4987 367 VGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPD--ATDEELWAA 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 449 LKRFGLDKVIKKHPRGLDMSLGENGLGLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSKTLL 528
Cdd:COG4987 445 LERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVL 524
|
410 420 430
....*....|....*....|....*....|....*
gi 1437745540 529 VVTHRPQVLSIVNRIIVVDNGKVVMDGPRDAVLQQ 563
Cdd:COG4987 525 LITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQ 559
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-563 |
8.47e-83 |
|
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: 269.32 E-value: 8.47e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 3 KAWFFKVIWRFKKYYYQIILATFVINFLALVSSLYVMNVYDRVI-PNKSYQTLWVLSIGVIIAILFEFTAKMLRGRLTDI 81
Cdd:COG4988 5 DKRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIiGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 82 AGKKADLIISSALFRKVTNL---KLQEKpiSSGSYVNNLRD-FESVRDFMT---SASLLTLVdMPFLILFV-----SVIA 149
Cdd:COG4988 85 AAARVKRRLRRRLLEKLLALgpaWLRGK--STGELATLLTEgVEALDGYFArylPQLFLAAL-VPLLILVAvfpldWLSG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 150 LVggYLAFVPLtiIPL-VIIVGLLAQiplskyinesmkESSQRQ--------GLAVEAIEGIETLKTNNAMNWAQKRwdy 220
Cdd:COG4988 162 LI--LLVTAPL--IPLfMILVGKGAA------------KASRRQwralarlsGHFLDRLRGLTTLKLFGRAKAEAER--- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 221 yTAKTA----SSSMKVKNI---SNFVIYFAVMMqqlnTIFLVI--IGTYLIHSDdpaskITMGALIATVILSGRALSPLG 291
Cdd:COG4988 223 -IAEASedfrKRTMKVLRVaflSSAVLEFFASL----SIALVAvyIGFRLLGGS-----LTLFAALFVLLLAPEFFLPLR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 292 QiagLAVRF---QQAWVALKGVNGIVERPSERESARKYITLKQINGNIKFQNVSFAYNQDSSsVVKILSFEIKPGEKVGI 368
Cdd:COG4988 293 D---LGSFYharANGIAAAEKIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRP-ALDGLSLTIPPGERVAL 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 369 LGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLLLEQEPRLFLGSLRENLDLARMDgfSSDQDLIVA 448
Cdd:COG4988 369 VGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPD--ASDEELEAA 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 449 LKRFGLDKVIKKHPRGLDMSLGENGLGLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSKTLL 528
Cdd:COG4988 447 LEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVI 526
|
570 580 590
....*....|....*....|....*....|....*
gi 1437745540 529 VVTHRPQVLSIVNRIIVVDNGKVVMDGPRDAVLQQ 563
Cdd:COG4988 527 LITHRLALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
14-308 |
4.38e-76 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 243.26 E-value: 4.38e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 14 KKYYYQIILATFVINFLALVSSLYVMNVYDRVIPNKSYQTLWVLSIGVIIAILFEFTAKMLRGRLTDIAGKKADLIISSA 93
Cdd:cd18566 1 RPLLPQVLLASLFINILALATPLFILQVYDRVIPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 94 LFRKVTNLKLQE-KPISSGSYVNNLRDFESVRDFMTSASLLTLVDMPFLILFVSVIALVGGYLAFVPLTIIPLVIIVGLL 172
Cdd:cd18566 81 AFEHLLSLPLSFfEREPSGAHLERLNSLEQIREFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 173 AQIPLSKYINESMKESSQRQGLAVEAIEGIETLKTNNAMNWAQKRWDYYTAKTASSSMKVKNISNFVIYFAVMMQQLNTI 252
Cdd:cd18566 161 LGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745540 253 FLVIIGTYLIHSDDpaskITMGALIATVILSGRALSPLGQIAGLAVRFQQAWVALK 308
Cdd:cd18566 241 AVVAFGALLVINGD----LTVGALIACTMLSGRVLQPLQRAFGLWTRFQQVRVAVR 292
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
6-563 |
2.72e-67 |
|
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: 231.94 E-value: 2.72e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 6 FFKVIWRFKKYYYQIILATFVINFLALVSSLYVMNVYDRVIPNKSYQTLWVLSIGVIIAILFEFTAKMLRGRLTDIAGKK 85
Cdd:TIGR01193 147 FIPLITRQKKLIVNIVIAAIIVTLISIAGSYYLQKIIDTYIPHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQR 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 86 ADLIISSALFRKVTNLklqekPIS------SGSYVNNLRDFESVRDFMTSASLLTLVDMPFLILFVSVIALVGGYLAFVP 159
Cdd:TIGR01193 227 LSIDIILSYIKHLFEL-----PMSffstrrTGEIVSRFTDASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFLLS 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 160 LTIIPLVIIVGLLAQIPLSKYINESMKESSQRQGLAVEAIEGIETLKTNNAMNWAQKRWDYYTAKTASSSMKVKNISNFV 239
Cdd:TIGR01193 302 LLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKADQGQ 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 240 IYFAVMMQQLNTIFLVIIGTYLIHSddpaSKITMGALIATVILSGRALSPLGQIAGLAVRFQQAWVALKGVNGIVERPSE 319
Cdd:TIGR01193 382 QAIKAVTKLILNVVILWTGAYLVMR----GKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 320 RESARKYITLKQINGNIKFQNVSFAYNQdSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDV 399
Cdd:TIGR01193 458 FINKKKRTELNNLNGDIVINDVSYSYGY-GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGF 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 400 DIRQIDPHYLRNQVLLLEQEPRLFLGSLRENLDLARMDGFSSDqDLIVALKRFGLDKVIKKHPRGLDMSLGENGLGLSGG 479
Cdd:TIGR01193 537 SLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKENVSQD-EIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGG 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 480 QKQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAIsAWCRSKTLLVVTHRPQVLSIVNRIIVVDNGKVVMDGPRDA 559
Cdd:TIGR01193 616 QKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNL-LNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDE 694
|
....
gi 1437745540 560 VLQQ 563
Cdd:TIGR01193 695 LLDR 698
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
334-552 |
8.55e-66 |
|
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: 213.89 E-value: 8.55e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 334 GNIKFQNVSFAYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQV 413
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 414 LLLEQEPRLFLGSLRENLDLarmDGFSSDQDLIVALKRFGLDKVIKKHPRGLDMSLGENGLGLSGGQKQIVALARMTLRN 493
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDP---FGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745540 494 PKIVLLDEPTTGLDQYSEIQALNAISAWCRSKTLLVVTHRPQVLSIVNRIIVVDNGKVV 552
Cdd:cd03244 158 SKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVV 216
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
336-550 |
3.72e-63 |
|
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: 204.92 E-value: 3.72e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLL 415
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 416 LEQEPRLFLGSLRENLdlarmdgfssdqdlivalkrfgldkvikkhprgldmslgenglgLSGGQKQIVALARMTLRNPK 495
Cdd:cd03228 81 VPQDPFLFSGTIRENI--------------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1437745540 496 IVLLDEPTTGLDQYSEIQALNAISAWCRSKTLLVVTHRPQVLSIVNRIIVVDNGK 550
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
334-563 |
1.54e-60 |
|
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: 200.53 E-value: 1.54e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 334 GNIKFQNVSFAYNQDSSsVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQV 413
Cdd:cd03254 1 GEIEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 414 LLLEQEPRLFLGSLRENLDLARMDgfSSDQDLIVALKRFGLDKVIKKHPRGLDMSLGENGLGLSGGQKQIVALARMTLRN 493
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPN--ATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 494 PKIVLLDEPTTGLDQYSEIQALNAISAWCRSKTLLVVTHRPQVLSIVNRIIVVDNGKVVMDGPRDAVLQQ 563
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
274-563 |
9.29e-59 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 205.83 E-value: 9.29e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 274 GALIATVILSgrALSPLGQIAGLAVRFQ---QAWVALKGVNGIVERPSERESARKYiTLKQINGNIKFQNVSFAYNQDSS 350
Cdd:PRK11160 277 GALIALFVFA--ALAAFEALMPVAGAFQhlgQVIASARRINEITEQKPEVTFPTTS-TAAADQVSLTLNNVSFTYPDQPQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 351 SVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLLLEQEPRLFLGSLREN 430
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDN 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 431 LDLARMDgfSSDQDLIVALKRFGLDKVIKKhPRGLDMSLGENGLGLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYS 510
Cdd:PRK11160 434 LLLAAPN--ASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAET 510
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1437745540 511 EIQALNAISAWCRSKTLLVVTHRPQVLSIVNRIIVVDNGKVVMDGPRDAVLQQ 563
Cdd:PRK11160 511 ERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQ 563
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
23-546 |
3.74e-58 |
|
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: 203.29 E-value: 3.74e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 23 ATFVINFLALVSSLyvmnVYDRVIPNKSYQTLWVLSIGVIIAILFEFTAKMLRGRLTDIAGKKADLIISSALFRKVTNL- 101
Cdd:TIGR02857 16 ALLIIAQAWLLARV----VDGLISAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRERLLEAVAALg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 102 -KLQEKPiSSGSYVNN-LRDFESVRDF-------MTSASLLTLVdmpfLILFVSVIALVGGYLAFVPLTIIPL-VIIVGL 171
Cdd:TIGR02857 92 pRWLQGR-PSGELATLaLEGVEALDGYfarylpqLVLAVIVPLA----ILAAVFPQDWISGLILLLTAPLIPIfMILIGW 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 172 LAQiplsKYINESMKESSQRQGLAVEAIEGIETLKTNNAMNWAQKRWDYYTAKTASSSMKVKNI---SNFVIYFavmmqq 248
Cdd:TIGR02857 167 AAQ----AAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIaflSSAVLEL------ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 249 LNTIFL----VIIGTYLIHSDdpaskITMGALIATVILSGRALSPLGQiagLAVRF---QQAWVALKGVNGIVERPSERE 321
Cdd:TIGR02857 237 FATLSValvaVYIGFRLLAGD-----LDLATGLFVLLLAPEFYLPLRQ---LGAQYharADGVAAAEALFAVLDAAPRPL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 322 SARKYITLKQINGnIKFQNVSFAYNqDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDI 401
Cdd:TIGR02857 309 AGKAPVTAAPASS-LEFSGVSVAYP-GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 402 RQIDPHYLRNQVLLLEQEPRLFLGSLRENLDLARMDGfsSDQDLIVALKRFGLDKVIKKHPRGLDMSLGENGLGLSGGQK 481
Cdd:TIGR02857 387 ADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDA--SDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQA 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437745540 482 QIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSKTLLVVTHRPQVLSIVNRIIVV 546
Cdd:TIGR02857 465 QRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
336-563 |
5.37e-58 |
|
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: 193.91 E-value: 5.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAY-NQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVL 414
Cdd:cd03249 1 IEFKNVSFRYpSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 415 LLEQEPRLFLGSLRENLDLARMDGfsSDQDLIVALKRFGLDKVIKKHPRGLDMSLGENGLGLSGGQKQIVALARMTLRNP 494
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDA--TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745540 495 KIVLLDEPTTGLDQYSEIQALNAISAWCRSKTLLVVTHRPQVLSIVNRIIVVDNGKVVMDGPRDAVLQQ 563
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQ 227
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
336-567 |
8.37e-57 |
|
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: 190.90 E-value: 8.37e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNqDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLL 415
Cdd:cd03253 1 IEFENVTFAYD-PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 416 LEQEPRLFLGSLRENLDLARMDgfSSDQDLIVALKRFGLDKVIKKHPRGLDMSLGENGLGLSGGQKQIVALARMTLRNPK 495
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYGRPD--ATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1437745540 496 IVLLDEPTTGLDQYSEIQALNAISAWCRSKTLLVVTHRpqVLSIVN--RIIVVDNGKVVMDGPRDavlQQLAKN 567
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHR--LSTIVNadKIIVLKDGRIVERGTHE---ELLAKG 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
336-561 |
7.30e-56 |
|
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: 188.46 E-value: 7.30e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLL 415
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 416 LEQEPRLFLGSLRENLDLArmDGFSSDQDLIVALKRFGLDKVIKKHPRGLDMSLGENGLGLSGGQKQIVALARMTLRNPK 495
Cdd:cd03252 81 VLQENVLFNRSIRDNIALA--DPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745540 496 IVLLDEPTTGLDQYSEIQALNAISAWCRSKTLLVVTHRPQVLSIVNRIIVVDNGKVVMDGPRDAVL 561
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
52-563 |
1.59e-55 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 196.86 E-value: 1.59e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 52 QTLWVLSIGVIIAILFE----FTAKMLrgrLTDIAGKKAdLIISSALFRKVTNL---KLQEKPisSGSYVNNL-RDFESV 123
Cdd:TIGR02203 51 SVLWWVPLVVIGLAVLRgicsFVSTYL---LSWVSNKVV-RDIRVRMFEKLLGLpvsFFDRQP--TGTLLSRItFDSEQV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 124 RDFMTSAsLLTLVDMPFLILFVSVIALvggYLAFvPLTIIPLVI--IVGLLAQI------PLSKYINESMKESSQrqgLA 195
Cdd:TIGR02203 125 ASAATDA-FIVLVRETLTVIGLFIVLL---YYSW-QLTLIVVVMlpVLSILMRRvskrlrRISKEIQNSMGQVTT---VA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 196 VEAIEGIETLKTNNAMNWAQKRWDYYTAKTASSSMKVKN-------ISNFVIYFAVMMqqlnTIFLVIigtylihSDDPA 268
Cdd:TIGR02203 197 EETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSagsisspITQLIASLALAV----VLFIAL-------FQAQA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 269 SKITMGALIATVILSGRALSPLGQIAGLAVRFQQAWVALKGVNGIVERPSERESARKYItlKQINGNIKFQNVSFAYNQD 348
Cdd:TIGR02203 266 GSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKDTGTRAI--ERARGDVEFRNVTFRYPGR 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 349 SSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLLLEQEPRLFLGSLR 428
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIA 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 429 ENLDLARMDGFSsDQDLIVALKRFGLDKVIKKHPRGLDMSLGENGLGLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQ 508
Cdd:TIGR02203 424 NNIAYGRTEQAD-RAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDN 502
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1437745540 509 YSEIQALNAISAWCRSKTLLVVTHRPQVLSIVNRIIVVDNGKVVMDGPRDAVLQQ 563
Cdd:TIGR02203 503 ESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLAR 557
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
336-563 |
6.33e-54 |
|
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: 183.20 E-value: 6.33e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLL 415
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 416 LEQEPRLFLGSLRENLDLARMDgfSSDQDLIVALKRFGLDKVIKKHPRGLDMSLGENGLGLSGGQKQIVALARMTLRNPK 495
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPG--ATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1437745540 496 IVLLDEPTTGLDQYSEIQALNAISAWCRSKTLLVVTHRpqvLSIV---NRIIVVDNGKVVMDGPRDAVLQQ 563
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHR---LSTIenaDRIVVLEDGKIVERGTHEELLAQ 226
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
14-308 |
1.53e-51 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 178.85 E-value: 1.53e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 14 KKYYYQIILATFVINFLALVSSLYVMNVYDRVIPNKSYQTLWVLSIGVIIAILFEFTAKMLRGRLTDIAGKKADLIISSA 93
Cdd:cd18588 1 KKLLGEVLLASLFLQLFALVTPLFFQVIIDKVLVHRSLSTLDVLAIGLLVVALFEAVLSGLRTYLFSHTTNRIDAELGAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 94 LFRKVTNLklqekPIS------SGSYVNNLRDFESVRDFMTSASLLTLVDMPFLILFVSVIALVGGYLAFVPLTIIPLVI 167
Cdd:cd18588 81 LFRHLLRL-----PLSyfesrqVGDTVARVRELESIRQFLTGSALTLVLDLVFSVVFLAVMFYYSPTLTLIVLASLPLYA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 168 IVGLLAQIPLSKYINESMKESSQRQGLAVEAIEGIETLKTNNAMNWAQKRWDYYTAKTASSSMKVKNISNFVIYFAVMMQ 247
Cdd:cd18588 156 LLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQ 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1437745540 248 QLNTIFLVIIGTYLIHSDdpasKITMGALIATVILSGRALSPLGQIAGLAVRFQQAWVALK 308
Cdd:cd18588 236 KLTTLAILWFGAYLVMDG----ELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQAKVSVE 292
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
14-308 |
1.76e-51 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 178.57 E-value: 1.76e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 14 KKYYYQIILATFVINFLALVSSLYVMNVYDRVIPNKSYQTLWVLSIGVIIAILFEFTAKMLRGRLTDIAGKKADLIISSA 93
Cdd:cd18586 1 RRVFVEVGLFSFFINLLALAPPIFMLQVYDRVLPSGSLSTLLGLTLGMVVLLAFDGLLRQVRSRILQRVGLRLDVELGRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 94 LFRKVTNLKLQEKPisSGSYVNNLRDFESVRDFMTSASLLTLVDMPFLILFVSVIALVGGYLAFVPLTIIPLVIIVGLLA 173
Cdd:cd18586 81 VFRAVLELPLESRP--SGYWQQLLRDLDTLRNFLTGPSLFAFFDLPWAPLFLAVIFLIHPPLGWVALVGAPVLVGLAWLN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 174 QIPLSKYINESMKESSQRQGLAVEAIEGIETLKTNNAMNWAQKRWDYYTAKTASSSMKVKNISNFVIYFAVMMQQLNTIF 253
Cdd:cd18586 159 HRATRKPLGEANEAQAARDALAAETLRNAETIKALGMLGNLRRRWEARHAETLELQIRASDLAGAISAIGKTLRMALQSL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1437745540 254 LVIIGTYLIhsddPASKITMGALIATVILSGRALSPLGQIAGLAVRFQQAWVALK 308
Cdd:cd18586 239 ILGVGAYLV----IDGELTIGALIAASILSGRALAPIDQLVGAWKQLSAARQAYE 289
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
330-551 |
1.79e-51 |
|
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: 176.12 E-value: 1.79e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 330 KQINGNIKFQNVSFAY-NQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHY 408
Cdd:cd03248 6 DHLKGIVKFQNVTFAYpTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 409 LRNQVLLLEQEPRLFLGSLRENLDLARMDgfSSDQDLIVALKRFGLDKVIKKHPRGLDMSLGENGLGLSGGQKQIVALAR 488
Cdd:cd03248 86 LHSKVSLVGQEPVLFARSLQDNIAYGLQS--CSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1437745540 489 MTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSKTLLVVTHRPQVLSIVNRIIVVDNGKV 551
Cdd:cd03248 164 ALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
336-563 |
1.54e-50 |
|
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: 173.67 E-value: 1.54e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYnQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLL 415
Cdd:COG1122 1 IELENLSFSY-PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 416 LEQEPR--LFLGSLREnlDLA---RMDGFSSDQ-DLIV--ALKRFGLDKVIKKHPrgldmslgengLGLSGGQKQIVALA 487
Cdd:COG1122 80 VFQNPDdqLFAPTVEE--DVAfgpENLGLPREEiRERVeeALELVGLEHLADRPP-----------HELSGGQKQRVAIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745540 488 RMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRS-KTLLVVTHRPQ-VLSIVNRIIVVDNGKVVMDGPRDAVLQQ 563
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEgKTVIIVTHDLDlVAELADRVIVLDDGRIVADGTPREVFSD 224
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
9-569 |
3.16e-50 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 184.54 E-value: 3.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 9 VIWRFKKYY---YQIILATFVINFLALVSSLYVMNVYDRVIP----NKSYQTL----WVLSIGVIIAILFEFtakmLRGR 77
Cdd:TIGR00958 148 LLFRLLGLSgrdWPWLISAFVFLTLSSLGEMFIPFYTGRVIDtlggDKGPPALasaiFFMCLLSIASSVSAG----LRGG 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 78 LTDIAGKKADLIISSALFRKVTNLKL---QEKPisSGSYVNNL-RDFESVRDFMT-SASLLT--LVdmpflILFVSVIAL 150
Cdd:TIGR00958 224 SFNYTMARINLRIREDLFRSLLRQDLgffDENK--TGELTSRLsSDTQTMSRSLSlNVNVLLrnLV-----MLLGLLGFM 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 151 VGG--YLAFVPLTIIPLVI----IVGLLAQIpLSKYINESMKESSQrqgLAVEAIEGIETLKTNNAMNWAQKRwdYYTAK 224
Cdd:TIGR00958 297 LWLspRLTMVTLINLPLVFlaekVFGKRYQL-LSEELQEAVAKANQ---VAEEALSGMRTVRSFAAEEGEASR--FKEAL 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 225 TASSSMKVKNISNFVIYFAVM--MQQLNTIFLVIIGTYLIHsddpASKITMGALIATVILS---GRALSPLGQIAGlavR 299
Cdd:TIGR00958 371 EETLQLNKRKALAYAGYLWTTsvLGMLIQVLVLYYGGQLVL----TGKVSSGNLVSFLLYQeqlGEAVRVLSYVYS---G 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 300 FQQAWVALKGVNGIVERPSERESARKYiTLKQINGNIKFQNVSFAY-NQDSSSVVKILSFEIKPGEKVGILGRIGSGKST 378
Cdd:TIGR00958 444 MMQAVGASEKVFEYLDRKPNIPLTGTL-APLNLEGLIEFQDVSFSYpNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKST 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 379 TLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLLLEQEPRLFLGSLRENldLARMDGFSSDQDLIVALKRFGLDKVI 458
Cdd:TIGR00958 523 VAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVREN--IAYGLTDTPDEEIMAAAKAANAHDFI 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 459 KKHPRGLDMSLGENGLGLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYSEiQALNAISAWcRSKTLLVVTHRPQVLS 538
Cdd:TIGR00958 601 MEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECE-QLLQESRSR-ASRTVLLIAHRLSTVE 678
|
570 580 590
....*....|....*....|....*....|.
gi 1437745540 539 IVNRIIVVDNGKVVMDGPrdavLQQLAKNET 569
Cdd:TIGR00958 679 RADQILVLKKGSVVEMGT----HKQLMEDQG 705
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
336-551 |
2.16e-49 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 170.00 E-value: 2.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYnqDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLL 415
Cdd:COG4619 1 LELEGLSFRV--GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 416 LEQEPRLFLGSLRENLDLA---RMDGFsSDQDLIVALKRFGLDKVIkkhprgLDMSLGEnglgLSGGQKQIVALARMTLR 492
Cdd:COG4619 79 VPQEPALWGGTVRDNLPFPfqlRERKF-DRERALELLERLGLPPDI------LDKPVER----LSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1437745540 493 NPKIVLLDEPTTGLDQYSEIQALNAISAWCRSK--TLLVVTHRP-QVLSIVNRIIVVDNGKV 551
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYLAEEgrAVLWVSHDPeQIERVADRVLTLEAGRL 209
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
334-563 |
4.39e-47 |
|
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: 174.24 E-value: 4.39e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 334 GNIKFQNVSFAYNQDSssvvKIL---SFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLR 410
Cdd:COG5265 356 GEVRFENVSFGYDPER----PILkgvSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 411 NQVLLLEQEPRLFLGSLRENLDLARMDgfSSDQDLIVALKRFGLDKVIKKHPRGLDMSLGENGLGLSGGQKQIVALARMT 490
Cdd:COG5265 432 AAIGIVPQDTVLFNDTIAYNIAYGRPD--ASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTL 509
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745540 491 LRNPKIVLLDEPTTGLDQYSE--IQ-ALNAISawcRSKTLLVVTHRpqvLS-IVN--RIIVVDNGKVVMDGPRDAVLQQ 563
Cdd:COG5265 510 LKNPPILIFDEATSALDSRTEraIQaALREVA---RGRTTLVIAHR---LStIVDadEILVLEAGRIVERGTHAELLAQ 582
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
336-555 |
7.23e-47 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 162.10 E-value: 7.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIrQIDPHYLRNQVLL 415
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV-SDLEKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 416 LEQEPRLFLGSLRENLdlarmdgfssdqdlivalkrfgldkvikkhprgldmslgenGLGLSGGQKQIVALARMTLRNPK 495
Cdd:cd03247 80 LNQRPYLFDTTLRNNL-----------------------------------------GRRFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 496 IVLLDEPTTGLDQYSEIQALNAISAWCRSKTLLVVTHRPQVLSIVNRIIVVDNGKVVMDG 555
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
254-534 |
1.92e-46 |
|
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: 171.00 E-value: 1.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 254 LVIIGTYLIHSDDPASKITMGALIATVILSG----RALSPLGQIAGLAVRFQQAWVALKGV------NGIVERPSERESA 323
Cdd:TIGR02868 250 LAVLGALWAGGPAVADGRLAPVTLAVLVLLPlaafEAFAALPAAAQQLTRVRAAAERIVEVldaagpVAEGSAPAAGAVG 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 324 RKYITLKqingnikFQNVSFAYnQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQ 403
Cdd:TIGR02868 330 LGKPTLE-------LRDLSAGY-PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSS 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 404 IDPHYLRNQVLLLEQEPRLFLGSLRENLDLARMDGfsSDQDLIVALKRFGLDKVIKKHPRGLDMSLGENGLGLSGGQKQI 483
Cdd:TIGR02868 402 LDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDA--TDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQR 479
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1437745540 484 VALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSKTLLVVTHRP 534
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
336-571 |
1.30e-45 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 161.18 E-value: 1.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNqdSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRqIDPHYLRNQVLL 415
Cdd:COG4555 2 IEVENLSKKYG--KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR-KEPREARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 416 LEQEPRLFLG-SLRENLD----LARMDGFSSDQDLIVALKRFGLDKVikkhprgLDMSLGEnglgLSGGQKQIVALARMT 490
Cdd:COG4555 79 LPDERGLYDRlTVRENIRyfaeLYGLFDEELKKRIEELIELLGLEEF-------LDRRVGE----LSTGMKKKVALARAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 491 LRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRS-KTLLVVTHRPQVLS-IVNRIIVVDNGKVVMDGPRDAVLQQLAKNE 568
Cdd:COG4555 148 VHDPKVLLLDEPTNGLDVMARRLLREILRALKKEgKTVLFSSHIMQEVEaLCDRVVILHKGKVVAQGSLDELREEIGEEN 227
|
...
gi 1437745540 569 TEK 571
Cdd:COG4555 228 LED 230
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
215-563 |
2.73e-45 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 168.66 E-value: 2.73e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 215 QKRWDYYTAKTASSSMKV---KNISNFVIyfavmmQQLNTIFLVIIgTYLIHSDDPASKITMGALiaTVILSGR--ALSP 289
Cdd:PRK11176 227 TKRFDKVSNRMRQQGMKMvsaSSISDPII------QLIASLALAFV-LYAASFPSVMDTLTAGTI--TVVFSSMiaLMRP 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 290 LGQIAGLAVRFQQAWVALKGVNGIVERPSERESARKYItlKQINGNIKFQNVSFAYNQDSSSVVKILSFEIKPGEKVGIL 369
Cdd:PRK11176 298 LKSLTNVNAQFQRGMAACQTLFAILDLEQEKDEGKRVI--ERAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALV 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 370 GRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLLLEQEPRLFLGSLRENLDLARMDGFSSDQDLIVAL 449
Cdd:PRK11176 376 GRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQYSREQIEEAAR 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 450 KRFGLDkVIKKHPRGLDMSLGENGLGLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYSE--IQAlnAISAWCRSKTL 527
Cdd:PRK11176 456 MAYAMD-FINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESEraIQA--ALDELQKNRTS 532
|
330 340 350
....*....|....*....|....*....|....*.
gi 1437745540 528 LVVTHRPQVLSIVNRIIVVDNGKVVMDGPRDAVLQQ 563
Cdd:PRK11176 533 LVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQ 568
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
356-555 |
3.79e-44 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 165.79 E-value: 3.79e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 356 LSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAeQGSITLDDVDIRQIDPHYLRNQVLLLEQEPRLFLGSLRENLDLAR 435
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 436 MDgfSSDQDLIVALKRFGLDKVIKKHPRGLDMSLGENGLGLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYSE---I 512
Cdd:PRK11174 448 PD--ASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEqlvM 525
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1437745540 513 QALNAISawcRSKTLLVVTHRPQVLSIVNRIIVVDNGKVVMDG 555
Cdd:PRK11174 526 QALNAAS---RRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQG 565
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
336-564 |
8.34e-43 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 153.30 E-value: 8.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYnqDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQiDPHYLRNQVLL 415
Cdd:COG1131 1 IEVRGLTKRY--GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 416 LEQEPRLFLG-SLRENLDL-ARMDGFSSDQDLIVA---LKRFGLDKVIKKHPRgldmslgenglGLSGGQKQIVALARMT 490
Cdd:COG1131 78 VPQEPALYPDlTVRENLRFfARLYGLPRKEARERIdelLELFGLTDAADRKVG-----------TLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745540 491 LRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRS-KTLLVVTHrpqVLSIV----NRIIVVDNGKVVMDGPRDAVLQQL 564
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRELAAEgKTVLLSTH---YLEEAerlcDRVAIIDKGRIVADGTPDELKARL 222
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
14-308 |
8.94e-43 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 154.98 E-value: 8.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 14 KKYYYQIILATFVINFLALVSSLYVMNVYDRVIPNKSYQTLWVLSIGVIIAILFEFTAKMLRGRLTDIAGKKADLIISSA 93
Cdd:cd18783 1 KRLFRDVAIASLILHVLALAPPIFFQIVIDKVLVHQSYSTLYVLTIGVVIALLFEGILGYLRRYLLLVATTRIDARLALR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 94 LFRKVTNLKLQ--EKpISSGSYVNNLRDFESVRDFMTSASLLTLVDMPFLILFVSVIALVGGYLAFVPLTIIPLVIIVGL 171
Cdd:cd18783 81 TFDRLLSLPIDffER-TPAGVLTKHMQQIERIRQFLTGQLFGTLLDATSLLVFLPVLFFYSPTLALVVLAFSALIALIIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 172 LAQIPLSKYINESMKESSQRQGLAVEAIEGIETLKTnNAMNWAQKR-WDYYTAKTASSSMKVKNISNFVIYFAVMMQQLN 250
Cdd:cd18783 160 AFLPPFRRRLQALYRAEGERQAFLVETVHGIRTVKS-LALEPRQRReWDERVARAIRARFAVGRLSNWPQTLTGPLEKLM 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745540 251 TIFLVIIGTYLIHSDDpaskITMGALIATVILSGRALSPLGQIAGLAVRFQQAWVALK 308
Cdd:cd18783 239 TVGVIWVGAYLVFAGS----LTVGALIAFNMLAGRVAGPLVQLAGLVQEYQEARLSVR 292
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
337-550 |
9.96e-43 |
|
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: 152.24 E-value: 9.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 337 KFQNVSFAYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLLL 416
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 417 EQEPR--LFLGSLREnlDLA---RMDGFSSDQD---LIVALKRFGLDKVIKKHPRgldmslgenglGLSGGQKQIVALAR 488
Cdd:cd03225 81 FQNPDdqFFGPTVEE--EVAfglENLGLPEEEIeerVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1437745540 489 MTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRS-KTLLVVTHRPQ-VLSIVNRIIVVDNGK 550
Cdd:cd03225 148 VLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEgKTIIIVTHDLDlLLELADRVIVLEDGK 211
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
334-552 |
1.63e-42 |
|
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: 151.41 E-value: 1.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 334 GNIKFQNVSFAYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQV 413
Cdd:cd03369 5 GEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 414 LLLEQEPRLFLGSLRENLDlaRMDGFsSDQDLIVALKrfgldkvikkhprgldmsLGENGLGLSGGQKQIVALARMTLRN 493
Cdd:cd03369 85 TIIPQDPTLFSGTIRSNLD--PFDEY-SDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745540 494 PKIVLLDEPTTGLDQYSEIQALNAISAWCRSKTLLVVTHRPQVLSIVNRIIVVDNGKVV 552
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVK 202
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
336-551 |
3.59e-42 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 149.29 E-value: 3.59e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLL 415
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 416 LEQEPRLFLGSLRENLdlarmdgfssdqdlivalkrfgldkvikkhprgldmslgenglgLSGGQKQIVALARMTLRNPK 495
Cdd:cd03246 81 LPQDDELFSGSIAENI--------------------------------------------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745540 496 IVLLDEPTTGLDQYSEIQALNAISAW-CRSKTLLVVTHRPQVLSIVNRIIVVDNGKV 551
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
252-563 |
6.99e-42 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 159.36 E-value: 6.99e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 252 IFLviIGTYLIHSDdpasKITMGALIATVILSGRALSPLGQIAGL-------AVRFQQAWVALKGVNGIVERPSEREsar 324
Cdd:PRK13657 257 ILV--LGAALVQKG----QLRVGEVVAFVGFATLLIGRLDQVVAFinqvfmaAPKLEEFFEVEDAVPDVRDPPGAID--- 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 325 kyitLKQINGNIKFQNVSFAYNqDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQI 404
Cdd:PRK13657 328 ----LGRVKGAVEFDDVSFSYD-NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTV 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 405 DPHYLRNQVLLLEQEPRLFLGSLRENLDLARMDgfSSDQDLIVALKRFGLDKVIKKHPRGLDMSLGENGLGLSGGQKQIV 484
Cdd:PRK13657 403 TRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPD--ATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRL 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 485 ALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSKTLLVVTHRpqvLSIV---NRIIVVDNGKVVMDGPRDAVL 561
Cdd:PRK13657 481 AIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHR---LSTVrnaDRILVFDNGRVVESGSFDELV 557
|
..
gi 1437745540 562 QQ 563
Cdd:PRK13657 558 AR 559
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
334-568 |
3.55e-39 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 154.13 E-value: 3.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 334 GNIKFQNVSFAYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQV 413
Cdd:PLN03130 1236 GSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVL 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 414 LLLEQEPRLFLGSLRENLDlarmdGFS--SDQDLIVALKRFGLDKVIKKHPRGLDMSLGENGLGLSGGQKQIVALARMTL 491
Cdd:PLN03130 1316 GIIPQAPVLFSGTVRFNLD-----PFNehNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALL 1390
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745540 492 RNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSKTLLVVTHRPQVLSIVNRIIVVDNGKVV-MDGPrdavlQQLAKNE 568
Cdd:PLN03130 1391 RRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVeFDTP-----ENLLSNE 1463
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
353-504 |
3.68e-39 |
|
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: 140.48 E-value: 3.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 353 VKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLLLEQEPRLFLG-SLRENL 431
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745540 432 DLAR----MDGFSSDQDLIVALKRFGLDKVIKKHprgldmsLGENGLGLSGGQKQIVALARMTLRNPKIVLLDEPTT 504
Cdd:pfam00005 81 RLGLllkgLSKREKDARAEEALEKLGLGDLADRP-------VGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
336-563 |
4.03e-39 |
|
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: 150.05 E-value: 4.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAE---QGSITLDDVDIRQIDPHYLRNQ 412
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 413 VLLLEQEPRLFLGSLR------ENLDLARMDGFSSDQDLIVALKRFGLDKVIKKHPRgldmslgenglGLSGGQKQIVAL 486
Cdd:COG1123 85 IGMVFQDPMTQLNPVTvgdqiaEALENLGLSRAEARARVLELLEAVGLERRLDRYPH-----------QLSGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 487 ARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRS--KTLLVVTHRPQVLS-IVNRIIVVDNGKVVMDGPRDAVLQQ 563
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErgTTVLLITHDLGVVAeIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
336-561 |
4.13e-39 |
|
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: 143.65 E-value: 4.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYnqDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLL 415
Cdd:COG1120 2 LEAENLSVGY--GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 416 LEQEPRL-FLGSLRENLDLAR---MDGFS--SDQDL-IV--ALKRFGLDkvikkhprGL-DMSLGEnglgLSGGQKQIVA 485
Cdd:COG1120 80 VPQEPPApFGLTVRELVALGRyphLGLFGrpSAEDReAVeeALERTGLE--------HLaDRPVDE----LSGGERQRVL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745540 486 LARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRS--KTLLVVTHRP-QVLSIVNRIIVVDNGKVVMDGPRDAVL 561
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErgRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
336-551 |
2.02e-38 |
|
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: 140.70 E-value: 2.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSSSV--VKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDP----HYL 409
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEkelaAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 410 RNQVLLLEQEPRLfLGSL--REN----LDLARMDGFSSDQDLIVALKRFGLDKVIKKHPrgldmslGEnglgLSGGQKQI 483
Cdd:cd03255 81 RRHIGFVFQSFNL-LPDLtaLENvelpLLLAGVPKKERRERAEELLERVGLGDRLNHYP-------SE----LSGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 484 VALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRS--KTLLVVTHRPQVLSIVNRIIVVDNGKV 551
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEagTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
336-543 |
2.05e-38 |
|
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: 140.31 E-value: 2.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSssVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRnQVLL 415
Cdd:COG4133 3 LEAENLSCRRGERL--LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRR-RLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 416 LEQEPRLFLG-SLRENLDL-ARMDGFSSDQDLIV-ALKRFGLDKVIKKHPRGLdmslgenglglSGGQKQIVALARMTLR 492
Cdd:COG4133 80 LGHADGLKPElTVRENLRFwAALYGLRADREAIDeALEAVGLAGLADLPVRQL-----------SAGQKRRVALARLLLS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1437745540 493 NPKIVLLDEPTTGLDQYSEIQALNAISAWCRS-KTLLVVTHRPQVLSIVNRI 543
Cdd:COG4133 149 PAPLWLLDEPFTALDAAGVALLAELIAAHLARgGAVLLTTHQPLELAAARVL 200
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
339-555 |
2.40e-38 |
|
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: 139.11 E-value: 2.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 339 QNVSFAYNQdsSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLLLEQ 418
Cdd:cd03214 3 ENLSVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 419 eprlflgslrenldlarmdgfssdqdlivALKRFGLDKviKKHpRGLDMslgenglgLSGGQKQIVALARMTLRNPKIVL 498
Cdd:cd03214 81 -----------------------------ALELLGLAH--LAD-RPFNE--------LSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 499 LDEPTTGLDQYSEIQALNAISAWCRS--KTLLVVTHRP-QVLSIVNRIIVVDNGKVVMDG 555
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLARErgKTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
337-550 |
2.83e-38 |
|
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: 138.15 E-value: 2.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 337 KFQNVSFAYNqdSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLLL 416
Cdd:cd00267 1 EIENLSFRYG--GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 417 EQeprlflgslrenldlarmdgfssdqdlivalkrfgldkvikkhprgldmslgenglgLSGGQKQIVALARMTLRNPKI 496
Cdd:cd00267 79 PQ---------------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745540 497 VLLDEPTTGLDQYSEIQALNAISAWCRS-KTLLVVTHRPQVLS-IVNRIIVVDNGK 550
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAElAADRVIVLKDGK 157
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
14-308 |
3.19e-38 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 142.58 E-value: 3.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 14 KKYYYQIILATFVINFLALVSSLYVMNVYDRVIPNKSYQTLWVLSIGVIIAILFEFTAKMLRGRLTDIAGKKADLIISSA 93
Cdd:cd18570 1 KKLLILILLLSLLITLLGIAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 94 LFRKVTNLklqekPIS------SGSYVNNLRDFESVRDFMTSASLLTLVDMpFLILFVSVI-ALVGGYLAFVPLTIIPLV 166
Cdd:cd18570 81 YFKHLLKL-----PLSffetrkTGEIISRFNDANKIREAISSTTISLFLDL-LMVIISGIIlFFYNWKLFLITLLIIPLY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 167 IIVGLLAQIPLSKYINESMKESSQRQGLAVEAIEGIETLKTNNAMNWAQKRWDYYTAKTASSSMKVKNISNFVIYFAVMM 246
Cdd:cd18570 155 ILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLI 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1437745540 247 QQLNTIFLVIIGTYLIHSDdpasKITMGALIATVILSGRALSPLGQIAGLAVRFQQAWVALK 308
Cdd:cd18570 235 SLIGSLLILWIGSYLVIKG----QLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAAD 292
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
336-563 |
4.73e-38 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 147.36 E-value: 4.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSSSVVKIL---SFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQI---DPHYL 409
Cdd:COG1123 261 LEVRNLSKRYPVRGKGGVRAVddvSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLsrrSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 410 RNQVLLLEQEP------RLFLG-SLRENLDLARMDGFSSDQDLIV-ALKRFGLD-KVIKKHPRgldmslgenglGLSGGQ 480
Cdd:COG1123 341 RRRVQMVFQDPysslnpRMTVGdIIAEPLRLHGLLSRAERRERVAeLLERVGLPpDLADRYPH-----------ELSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 481 KQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRS--KTLLVVTHRpqvLSIV----NRIIVVDNGKVVMD 554
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElgLTYLFISHD---LAVVryiaDRVAVMYDGRIVED 486
|
....*....
gi 1437745540 555 GPRDAVLQQ 563
Cdd:COG1123 487 GPTEEVFAN 495
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
336-554 |
1.56e-37 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 138.64 E-value: 1.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSSSVV--KILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPH---YLR 410
Cdd:COG1136 5 LELRNLTKSYGTGEGEVTalRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERelaRLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 411 NQVL--------LLeqePRLflgSLRENLDLA-RMDGFSSDQD---LIVALKRFGLDKVIKKHPrgldmslGEnglgLSG 478
Cdd:COG1136 85 RRHIgfvfqffnLL---PEL---TALENVALPlLLAGVSRKERrerARELLERVGLGDRLDHRP-------SQ----LSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745540 479 GQKQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRS--KTLLVVTHRPQVLSIVNRIIVVDNGKVVMD 554
Cdd:COG1136 148 GQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElgTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
335-563 |
4.35e-37 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 137.58 E-value: 4.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 335 NIKFQNVSFAYNQDSSSvvkiLSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHylRNQVL 414
Cdd:COG3840 1 MLRLDDLTYRYGDFPLR----FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA--ERPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 415 LLEQEPRLF--LgSLRENLDLARMDG--FSSDQ--DLIVALKRFGLDKVIKKHPRGLdmslgenglglSGGQKQIVALAR 488
Cdd:COG3840 75 MLFQENNLFphL-TVAQNIGLGLRPGlkLTAEQraQVEQALERVGLAGLLDRLPGQL-----------SGGQRQRVALAR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745540 489 MTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSK--TLLVVTHRPQ-VLSIVNRIIVVDNGKVVMDGPRDAVLQQ 563
Cdd:COG3840 143 CLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERglTVLMVTHDPEdAARIADRVLLVADGRIAADGPTAALLDG 220
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
336-562 |
3.85e-36 |
|
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: 135.11 E-value: 3.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNqdSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPH---YLRNQ 412
Cdd:COG1127 6 IEVRNLTKSFG--DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 413 VLLLEQEPRLFlGS----------LRENLDLARmdgfsSDQDLIVALK--RFGLDKVIKKHPrgldmslGEnglgLSGGQ 480
Cdd:COG1127 84 IGMLFQGGALF-DSltvfenvafpLREHTDLSE-----AEIRELVLEKleLVGLPGAADKMP-------SE----LSGGM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 481 KQIVALARMTLRNPKIVLLDEPTTGLDQYS---------EIQ-ALNAisawcrskTLLVVTHR-PQVLSIVNRIIVVDNG 549
Cdd:COG1127 147 RKRVALARALALDPEILLYDEPTAGLDPITsavidelirELRdELGL--------TSVVVTHDlDSAFAIADRVAVLADG 218
|
250
....*....|...
gi 1437745540 550 KVVMDGPRDAVLQ 562
Cdd:COG1127 219 KIIAEGTPEELLA 231
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
334-563 |
8.46e-36 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 143.93 E-value: 8.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 334 GNIKFQNVSFAYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTtlkLAAGLY---PAEQGSITLDDVDIRQIDPHYLR 410
Cdd:TIGR00957 1283 GRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSS---LTLGLFrinESAEGEIIIDGLNIAKIGLHDLR 1359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 411 NQVLLLEQEPRLFLGSLRENLDlarmdGFS--SDQDLIVALKRFGLDKVIKKHPRGLDMSLGENGLGLSGGQKQIVALAR 488
Cdd:TIGR00957 1360 FKITIIPQDPVLFSGSLRMNLD-----PFSqySDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLAR 1434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745540 489 MTLRNPKIVLLDEPTTGLDqyseIQALNAISAWCRSK----TLLVVTHRPQVLSIVNRIIVVDNGKVVMDGPRDAVLQQ 563
Cdd:TIGR00957 1435 ALLRKTKILVLDEATAAVD----LETDNLIQSTIRTQfedcTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
340-562 |
1.02e-35 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 134.16 E-value: 1.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 340 NVSFAYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLLLEQE 419
Cdd:COG1124 8 SVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 420 PRLFL-------GSLRENLDLARMDGfsSDQDLIVALKRFGLDK-VIKKHPRgldmslgenglGLSGGQKQIVALARMTL 491
Cdd:COG1124 88 PYASLhprhtvdRILAEPLRIHGLPD--REERIAELLEQVGLPPsFLDRYPH-----------QLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1437745540 492 RNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSK--TLLVVTHRPQVLS-IVNRIIVVDNGKVVMDGPRDAVLQ 562
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAhLCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
336-563 |
1.16e-35 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 134.89 E-value: 1.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSSSVVKIL---SFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHY---L 409
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPFEKKALddvSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlkdL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 410 RNQVLLLEQEP--RLFLGSLREnlDLA---RMDGFSSDQ-DLIV--ALKRFGLDKVIK-KHPrgldmslgengLGLSGGQ 480
Cdd:TIGR04521 81 RKKVGLVFQFPehQLFEETVYK--DIAfgpKNLGLSEEEaEERVkeALELVGLDEEYLeRSP-----------FELSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 481 KQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRS--KTLLVVTHR-PQVLSIVNRIIVVDNGKVVMDGPR 557
Cdd:TIGR04521 148 MRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEkgLTVILVTHSmEDVAEYADRVIVMHKGKIVLDGTP 227
|
....*.
gi 1437745540 558 DAVLQQ 563
Cdd:TIGR04521 228 REVFSD 233
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
334-569 |
1.40e-35 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 143.19 E-value: 1.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 334 GNIKFQNVSFAYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQV 413
Cdd:PLN03232 1233 GSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVL 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 414 LLLEQEPRLFLGSLRENLdlarmDGFS--SDQDLIVALKRFGLDKVIKKHPRGLDMSLGENGLGLSGGQKQIVALARMTL 491
Cdd:PLN03232 1313 SIIPQSPVLFSGTVRFNI-----DPFSehNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALL 1387
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745540 492 RNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSKTLLVVTHRPQVLSIVNRIIVVDNGKVV-MDGPrdavlQQLAKNET 569
Cdd:PLN03232 1388 RRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLeYDSP-----QELLSRDT 1461
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
14-307 |
5.29e-35 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 133.45 E-value: 5.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 14 KKYYYQIILATFVINFLALVSSLYVMNVYDRVIPNKSYQTLWVLSIGVIIAILFEFTAKMLRGRLTDIAGKKADLIISSA 93
Cdd:cd18568 1 RKLLAEILLASLLLQLLGLALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 94 LFRKVTNLKLQE-KPISSGSYVNNLRDFESVRDFMTSASLLTLVDMPFLILFVSVIALVGGYLAFVPLTIIPLVIIVGLL 172
Cdd:cd18568 81 FYKHLLSLPLSFfASRKVGDIITRFQENQKIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 173 AQIPLSKYINESMKESSQRQGLAVEAIEGIETLKTNNAMNWAQKRWDYYTAKTASSSMKVKNISNFVIYFAVMMQQLNTI 252
Cdd:cd18568 161 SSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHLGTI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1437745540 253 FLVIIGTYLIHSDdpasKITMGALIATVILSGRALSPLGQIAGLAVRFQQAWVAL 307
Cdd:cd18568 241 AVLWYGAYLVISG----QLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISV 291
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
336-555 |
1.08e-34 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 130.33 E-value: 1.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYnqDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHyLRNqVLL 415
Cdd:cd03259 1 LELKGLSKTY--GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-RRN-IGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 416 LEQEPRLF--LgSLREN----LDLARMDGFSSDQDLIVALKRFGLDKVIKKHPRgldmslgenglGLSGGQKQIVALARM 489
Cdd:cd03259 77 VFQDYALFphL-TVAENiafgLKLRGVPKAEIRARVRELLELVGLEGLLNRYPH-----------ELSGGQQQRVALARA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745540 490 TLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRS--KTLLVVTHRPQ-VLSIVNRIIVVDNGKVVMDG 555
Cdd:cd03259 145 LAREPSLLLLDEPLSALDAKLREELREELKELQRElgITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
112-563 |
2.05e-34 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 137.54 E-value: 2.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 112 SYVNNlrDFESVRDfmtsaslltlvdmpfliLFVSVI-------ALVGGYL----------AFVPLTIIPLVIIVGLLAQ 174
Cdd:PRK10790 126 SRVTN--DTEVIRD-----------------LYVTVVatvlrsaALIGAMLvamfsldwrmALVAIMIFPAVLVVMVIYQ 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 175 ---IPLSKYI-----------NESMKESSQRQGLAVEAIEGIETLKTNnamnwaqkrWDYYTAKtasssMKVKNISNFvi 240
Cdd:PRK10790 187 rysTPIVRRVrayladindgfNEVINGMSVIQQFRQQARFGERMGEAS---------RSHYMAR-----MQTLRLDGF-- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 241 yfavMMQQLNTIF--LVIIGTYLIHSDDPASKITMGALIATVILSGRALSPLGQIAGLAVRFQQAWVALKGVNGIVERPS 318
Cdd:PRK10790 251 ----LLRPLLSLFsaLILCGLLMLFGFSASGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELMDGPR 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 319 ER--ESARkyiTLKQinGNIKFQNVSFAYNQDSSsVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITL 396
Cdd:PRK10790 327 QQygNDDR---PLQS--GRIDIDNVSFAYRDDNL-VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRL 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 397 DDVDIRQIDPHYLRNQVLLLEQEPRLFLGSLRENLDLARMdgfSSDQDLIVALKRFGLDKVIKKHPRGLDMSLGENGLGL 476
Cdd:PRK10790 401 DGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRD---ISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNL 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 477 SGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYSE--IQ-ALNAISawcRSKTLLVVTHRPQVLSIVNRIIVVDNGKVVM 553
Cdd:PRK10790 478 SVGQKQLLALARVLVQTPQILILDEATANIDSGTEqaIQqALAAVR---EHTTLVVIAHRLSTIVEADTILVLHRGQAVE 554
|
490
....*....|
gi 1437745540 554 DGPRDAVLQQ 563
Cdd:PRK10790 555 QGTHQQLLAA 564
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
340-555 |
2.39e-34 |
|
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: 129.93 E-value: 2.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 340 NVSFAYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPH---YLRNQVLLL 416
Cdd:cd03257 8 SVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlrkIRRKEIQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 417 EQEPRLFL-------GSLRENLDLARMDGFSSDQDLIVALKRFGL---DKVIKKHPRgldmslgenglGLSGGQKQIVAL 486
Cdd:cd03257 88 FQDPMSSLnprmtigEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPH-----------ELSGGQRQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1437745540 487 ARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSK--TLLVVTHRPQVLS-IVNRIIVVDNGKVVMDG 555
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAkIADRVAVMYAGKIVEEG 228
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
339-562 |
2.95e-34 |
|
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: 129.48 E-value: 2.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 339 QNVSFAYnqDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHY-LRNQVLLLE 417
Cdd:cd03224 4 ENLNAGY--GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 418 QEPRLFLG-SLRENLDLARMDGFSSDqdlivalKRFGLDKVIKKHPRGLDM--SLGENglgLSGGQKQIVALARMTLRNP 494
Cdd:cd03224 82 EGRRIFPElTVEENLLLGAYARRRAK-------RKARLERVYELFPRLKERrkQLAGT---LSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437745540 495 KIVLLDEPTTGL------DQYSEIQALNAisawcRSKTLLVVTHR-PQVLSIVNRIIVVDNGKVVMDGPRDAVLQ 562
Cdd:cd03224 152 KLLLLDEPSEGLapkiveEIFEAIRELRD-----EGVTILLVEQNaRFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
336-560 |
4.63e-34 |
|
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: 128.84 E-value: 4.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSssVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLY------PAEqGSITLDDVDIR--QIDPH 407
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgaPDE-GEVLLDGKDIYdlDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 408 YLRNQVLLLEQEPRLFLGSLRENLDLA-RMDGFSSDQDL--IV--ALKRFGLDKVIKKHPrgldmslgeNGLGLSGGQKQ 482
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlRLHGIKLKEELdeRVeeALRKAALWDEVKDRL---------HALGLSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 483 IVALARMTLRNPKIVLLDEPTTGLDQYS--EIQALnaISAWCRSKTLLVVTHRP-QVLSIVNRIIVVDNGKVVMDGPRDA 559
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPIStaKIEEL--IAELKKEYTIVIVTHNMqQAARVADRTAFLLNGRLVEFGPTEQ 226
|
.
gi 1437745540 560 V 560
Cdd:cd03260 227 I 227
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
336-560 |
1.02e-33 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 128.64 E-value: 1.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNqDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRN---Q 412
Cdd:COG3638 3 LELRNLSKRYP-GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRlrrR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 413 VLLLEQEPRLFlgslrENLD---------LARMDGFSS------DQDLIVA---LKRFGL-DKVIKKhprgLDMslgeng 473
Cdd:COG3638 82 IGMIFQQFNLV-----PRLSvltnvlagrLGRTSTWRSllglfpPEDRERAleaLERVGLaDKAYQR----ADQ------ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 474 lgLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSK--TLLVVTHRPQ-VLSIVNRIIVVDNGK 550
Cdd:COG3638 147 --LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDgiTVVVNLHQVDlARRYADRIIGLRDGR 224
|
250
....*....|
gi 1437745540 551 VVMDGPRDAV 560
Cdd:COG3638 225 VVFDGPPAEL 234
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
336-550 |
1.20e-33 |
|
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: 127.20 E-value: 1.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYN---QDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSItlddvdirqidphYLRNQ 412
Cdd:cd03250 1 ISVEDASFTWDsgeQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-------------SVPGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 413 VLLLEQEPRLFLGSLREN-LDLARMDgfssDQDLIVALKRFGLDKVIKKHPRGLDMSLGENGLGLSGGQKQIVALARMTL 491
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENiLFGKPFD----EERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1437745540 492 RNPKIVLLDEPTTGLDQYSEiQAL--NAI-SAWCRSKTLLVVTHRPQVLSIVNRIIVVDNGK 550
Cdd:cd03250 144 SDADIYLLDDPLSAVDAHVG-RHIfeNCIlGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
336-563 |
1.92e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 127.90 E-value: 1.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYnqDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPH--YL--RN 411
Cdd:COG1121 7 IELENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRigYVpqRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 412 QVllleqePRLF---------LGSLRENLDLARMDgfSSDQDLIV-ALKRFGLDKVIKKHprgldmsLGEnglgLSGGQK 481
Cdd:COG1121 85 EV------DWDFpitvrdvvlMGRYGRRGLFRRPS--RADREAVDeALERVGLEDLADRP-------IGE----LSGGQQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 482 QIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRS-KTLLVVTHRP-QVLSIVNRIIVVdNGKVVMDGPRDA 559
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREgKTILVVTHDLgAVREYFDRVLLL-NRGLVAHGPPEE 224
|
....
gi 1437745540 560 VLQQ 563
Cdd:COG1121 225 VLTP 228
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
337-555 |
7.02e-33 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 125.34 E-value: 7.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 337 KFQNVSFAYNQdsSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIdphylRNQVLLL 416
Cdd:cd03235 1 EVEDLTVSYGG--HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 417 EQE---PRLFLGSLRENLDLAR---MDGF-----SSDQDLIVALKRFGLDKVIKKHprgldmsLGEnglgLSGGQKQIVA 485
Cdd:cd03235 74 PQRrsiDRDFPISVRDVVLMGLyghKGLFrrlskADKAKVDEALERVGLSELADRQ-------IGE----LSGGQQQRVL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1437745540 486 LARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRS-KTLLVVTH-RPQVLSIVNRIIVVdNGKVVMDG 555
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHdLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
340-552 |
9.06e-33 |
|
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: 124.68 E-value: 9.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 340 NVSFAYNqDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDphyLRNQVLLLEQE 419
Cdd:cd03226 4 NISFSYK-KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE---RRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 420 PR--LFLGSLRENLDLARMDGFSSDQDLIVALKRFGLDKVIKKHPRGLdmslgenglglSGGQKQIVALARMTLRNPKIV 497
Cdd:cd03226 80 VDyqLFTDSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSL-----------SGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1437745540 498 LLDEPTTGLDQYSeiqaLNAISAWCRS-----KTLLVVTHRPQVLS-IVNRIIVVDNGKVV 552
Cdd:cd03226 149 IFDEPTSGLDYKN----MERVGELIRElaaqgKAVIVITHDYEFLAkVCDRVLLLANGAIV 205
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
336-562 |
1.07e-32 |
|
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: 125.31 E-value: 1.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYnqDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYL---RNQ 412
Cdd:cd03261 1 IELRGLTKSF--GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 413 VLLLEQEPRLFlGS----------LRENLDLARmdgfsSDQDLIVALK--RFGLDKVIKKHPrgldmslGEnglgLSGGQ 480
Cdd:cd03261 79 MGMLFQSGALF-DSltvfenvafpLREHTRLSE-----EEIREIVLEKleAVGLRGAEDLYP-------AE----LSGGM 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 481 KQIVALARMTLRNPKIVLLDEPTTGLDQYSE------IQALNAISAwcrsKTLLVVTHR-PQVLSIVNRIIVVDNGKVVM 553
Cdd:cd03261 142 KKRVALARALALDPELLLYDEPTAGLDPIASgviddlIRSLKKELG----LTSIMVTHDlDTAFAIADRIAVLYDGKIVA 217
|
....*....
gi 1437745540 554 DGPRDAVLQ 562
Cdd:cd03261 218 EGTPEELRA 226
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
336-557 |
1.43e-32 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 124.78 E-value: 1.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSSsVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPH---YLRNQ 412
Cdd:COG2884 2 IRFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReipYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 413 VLLLEQEPRLFLG-SLRENLDLA-RMDGFSSD---QDLIVALKRFGLDKVIKKHPRgldmslgEnglgLSGGQKQIVALA 487
Cdd:COG2884 81 IGVVFQDFRLLPDrTVYENVALPlRVTGKSRKeirRRVREVLDLVGLSDKAKALPH-------E----LSGGEQQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745540 488 RMTLRNPKIVLLDEPTTGLD-QYSE--IQALNAISAwcRSKTLLVVTHRpqvLSIVN----RIIVVDNGKVVMDGPR 557
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDpETSWeiMELLEEINR--RGTTVLIATHD---LELVDrmpkRVLELEDGRLVRDEAR 221
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
336-576 |
1.55e-32 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 125.59 E-value: 1.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSSS--VVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHylRNQV 413
Cdd:COG1116 8 LELRGVSKRFPTGGGGvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD--RGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 414 LlleQEPRLF--LgSLRENLDLA-RMDGFSSDQDLIVA---LKRFGLDKVIKKHPRgldmslgEnglgLSGGQKQIVALA 487
Cdd:COG1116 86 F---QEPALLpwL-TVLDNVALGlELRGVPKAERRERArelLELVGLAGFEDAYPH-------Q----LSGGMRQRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 488 RMTLRNPKIVLLDEPTTGLDQ------YSEIQALnaisaWCRS-KTLLVVTHRPQ---VLSivNRIIVVDN--GKVVMD- 554
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDAltrerlQDELLRL-----WQETgKTVLFVTHDVDeavFLA--DRVVVLSArpGRIVEEi 223
|
250 260
....*....|....*....|....*...
gi 1437745540 555 -----GPRDAVLQQLAK-NETEKQITAH 576
Cdd:COG1116 224 dvdlpRPRDRELRTSPEfAALRAEILDL 251
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
336-551 |
5.64e-32 |
|
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: 121.35 E-value: 5.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYnqDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQiDPHYLRNQVLL 415
Cdd:cd03230 1 IEVRNLSKRY--GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 416 LEQEPRLFLG-SLRENLDlarmdgfssdqdlivalkrfgldkvikkhprgldmslgenglgLSGGQKQIVALARMTLRNP 494
Cdd:cd03230 78 LPEEPSLYENlTVRENLK-------------------------------------------LSGGMKQRLALAQALLHDP 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745540 495 KIVLLDEPTTGLDQYSEIQALNAISAWCRS-KTLLVVTHRPQ-VLSIVNRIIVVDNGKV 551
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLRELKKEgKTILLSSHILEeAERLCDRVAILNNGRI 173
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
339-561 |
6.45e-32 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 123.17 E-value: 6.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 339 QNVSFAYNQdsSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYL-RNQVLLLE 417
Cdd:COG0410 7 ENLHAGYGG--IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 418 QEPRLFlGSL--RENLDLA---RMDGFSSDQDLIVALKRFgldkvikkhPRgldmsLGE--NGLG--LSGGQKQIVALAR 488
Cdd:COG0410 85 EGRRIF-PSLtvEENLLLGayaRRDRAEVRADLERVYELF---------PR-----LKErrRQRAgtLSGGEQQMLAIGR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 489 MTLRNPKIVLLDEPTTGL-----DQYSE-IQALNAisawcRSKTLLVVTHR-PQVLSIVNRIIVVDNGKVVMDGPRDAVL 561
Cdd:COG0410 150 ALMSRPKLLLLDEPSLGLaplivEEIFEiIRRLNR-----EGVTILLVEQNaRFALEIADRAYVLERGRIVLEGTAAELL 224
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
14-307 |
2.35e-31 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 123.47 E-value: 2.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 14 KKYYYQIILATFVINFLALVSSLYVMNVYDRVIPNKSYQTLWVLSIGVIIAILFEFTAKMLRGRLTDIAGKKADLIISSA 93
Cdd:cd18782 1 RRALIEVLALSFVVQLLGLANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 94 LFRKVTNLKL---QEKPIssGSYVNNLRDFESVRDFMTSASLLTLVDMPFLILFVSVIALVGGYLAFVPLTIIPLVIIVG 170
Cdd:cd18782 81 IIDHLLRLPLgffDKRPV--GELSTRISELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 171 LLAQIPLSKYINESMKESSQRQGLAVEAIEGIETLKTNNAMNWAQKRWDYYTAKTASSSMKVKNISNFVIYFAVMMQQLN 250
Cdd:cd18782 159 FLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLS 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745540 251 TIFLVIIGTYLIHSddpaSKITMGALIATVILSGRALSPLGQIAGLAVRFQQAWVAL 307
Cdd:cd18782 239 SLLVLWVGAYLVLR----GELTLGQLIAFRILSGYVTGPILRLSTLWQQFQELRVSL 291
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
356-555 |
6.30e-31 |
|
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: 119.91 E-value: 6.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 356 LSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHylRNQVLLLEQEPRLFLG-SLRENLDLA 434
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAHlTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 435 RMDGF---SSDQDLI-VALKRFGLDKVIKKHPRGLdmslgenglglSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYS 510
Cdd:cd03298 95 LSPGLkltAEDRQAIeVALARVGLAGLEKRLPGEL-----------SGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1437745540 511 EIQALNAISAWCRSK--TLLVVTHRPQ-VLSIVNRIIVVDNGKVVMDG 555
Cdd:cd03298 164 RAEMLDLVLDLHAETkmTVLMVTHQPEdAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
336-560 |
7.19e-31 |
|
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: 120.37 E-value: 7.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNqDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRN---Q 412
Cdd:cd03256 1 IEVENLSKTYP-NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrrQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 413 VLLLEQEPRLfLGSLR--ENLDLARMD---------GFSSDQDLIVA---LKRFGL-DKVIKKHPRgldmslgenglgLS 477
Cdd:cd03256 80 IGMIFQQFNL-IERLSvlENVLSGRLGrrstwrslfGLFPKEEKQRAlaaLERVGLlDKAYQRADQ------------LS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 478 GGQKQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSK--TLLVVTHRPQV-LSIVNRIIVVDNGKVVMD 554
Cdd:cd03256 147 GGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDLaREYADRIVGLKDGRIVFD 226
|
....*.
gi 1437745540 555 GPRDAV 560
Cdd:cd03256 227 GPPAEL 232
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
336-555 |
1.07e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 120.87 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLL 415
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 416 LEQEP-RLFLGSLRENlDLA-----RMDGFSSDQDLIVAL-KRFGLDKVIKKHPrgldmslgengLGLSGGQKQIVALAR 488
Cdd:PRK13632 88 IFQNPdNQFIGATVED-DIAfglenKKVPPKKMKDIIDDLaKKVGMEDYLDKEP-----------QNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 489 MTLRNPKIVLLDEPTTGLD---QYSEIQALNAISAwCRSKTLLVVTHRPQVLSIVNRIIVVDNGKVVMDG 555
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDpkgKREIKKIMVDLRK-TRKKTLISITHDMDEAILADKVIVFSEGKLIAQG 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
336-550 |
5.40e-30 |
|
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: 116.13 E-value: 5.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQdsSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHY--LRNQV 413
Cdd:cd03229 1 LELKNVSKRYGQ--KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 414 LLLEQEPRLFlgslrenldlarmdgfssdqdlivalkrfgldkvikkhPRgldMSLGEN-GLGLSGGQKQIVALARMTLR 492
Cdd:cd03229 79 GMVFQDFALF--------------------------------------PH---LTVLENiALGLSGGQQQRVALARALAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1437745540 493 NPKIVLLDEPTTGLDQYS--EIQALnaISAWCRS--KTLLVVTHRP-QVLSIVNRIIVVDNGK 550
Cdd:cd03229 118 DPDVLLLDEPTSALDPITrrEVRAL--LKSLQAQlgITVVLVTHDLdEAARLADRVVVLRDGK 178
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
332-563 |
6.61e-30 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 118.47 E-value: 6.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 332 INGNIKFQNVSFAYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTtLKLAA-GLYPAEQGSITLDDVDIRQIDPHYLR 410
Cdd:cd03288 16 LGGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSS-LSLAFfRMVDIFDGKIVIDGIDISKLPLHTLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 411 NQVLLLEQEPRLFLGSLRENLDLARMdgfSSDQDLIVALKRFGLDKVIKKHPRGLDMSLGENGLGLSGGQKQIVALARMT 490
Cdd:cd03288 95 SRLSIILQDPILFSGSIRFNLDPECK---CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAF 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1437745540 491 LRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSKTLLVVTHRPQVLSIVNRIIVVDNGKVV-MDGPRDAVLQQ 563
Cdd:cd03288 172 VRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVeCDTPENLLAQE 245
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
357-565 |
2.58e-29 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 115.83 E-value: 2.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 357 SFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHylRNQVLLLEQEPRLF--LgSLRENLDLA 434
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFshL-TVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 435 RMDG--FSSDQDLIVA--LKRFGLDKVIKKHPrgldmslGEnglgLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYS 510
Cdd:PRK10771 96 LNPGlkLNAAQREKLHaiARQMGIEDLLARLP-------GQ----LSGGQRQRVALARCLVREQPILLLDEPFSALDPAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745540 511 EIQALNAISAWCRSK--TLLVVTHR-PQVLSIVNRIIVVDNGKVVMDGPRDAVLQQLA 565
Cdd:PRK10771 165 RQEMLTLVSQVCQERqlTLLMVSHSlEDAARIAPRSLVVADGRIAWDGPTDELLSGKA 222
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
336-558 |
2.90e-29 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 116.76 E-value: 2.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRqiDPHYL---RNQ 412
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTL--DEENLweiRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 413 VLLLEQEP-RLFLGSLRENlDLArmdgFSS-----DQDLIV-----ALKRFGLDKVIKKHPRgldmslgenglGLSGGQK 481
Cdd:TIGR04520 79 VGMVFQNPdNQFVGATVED-DVA----FGLenlgvPREEMRkrvdeALKLVGMEDFRDREPH-----------LLSGGQK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 482 QIVALARMTLRNPKIVLLDEPTTGLDQY------SEIQALNAIsawcRSKTLLVVTHRPQVLSIVNRIIVVDNGKVVMDG 555
Cdd:TIGR04520 143 QRVAIAGVLAMRPDIIILDEATSMLDPKgrkevlETIRKLNKE----EGITVISITHDMEEAVLADRVIVMNKGKIVAEG 218
|
....
gi 1437745540 556 -PRD 558
Cdd:TIGR04520 219 tPRE 222
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
342-563 |
6.40e-29 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 120.97 E-value: 6.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 342 SFAYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLLLEQEPR 421
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 422 LFLGSLRENLDLARMDGFSSDQDLIVALKRFGLDkvIKKHPRGLDMSLGENGLGLSGGQKQIVALARMTLRNPKIVLLDE 501
Cdd:PRK10789 400 LFSDTVANNIALGRPDATQQEIEHVARLASVHDD--ILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDD 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1437745540 502 PTTGLDQYSEIQALNAISAWCRSKTLLVVTHRPQVLSIVNRIIVVDNGKVVMDGPRDAVLQQ 563
Cdd:PRK10789 478 ALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQ 539
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
336-532 |
9.76e-29 |
|
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: 113.72 E-value: 9.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYnQDSSSVVKIL---SFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHylrnq 412
Cdd:cd03293 1 LEVRNVSKTY-GGGGGAVTALediSLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 413 VLLLEQEPRLF--LgSLREN----LDLARMDGFSSDQDLIVALKRFGLDKVIKKHPRgldmslgenglGLSGGQKQIVAL 486
Cdd:cd03293 75 RGYVFQQDALLpwL-TVLDNvalgLELQGVPKAEARERAEELLELVGLSGFENAYPH-----------QLSGGMRQRVAL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1437745540 487 ARMTLRNPKIVLLDEPTTGLDQ------YSEIQALnaisaWCRS-KTLLVVTH 532
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDAltreqlQEELLDI-----WRETgKTVLLVTH 190
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
336-558 |
1.34e-28 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 117.12 E-value: 1.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYnqDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHyLRNqVLL 415
Cdd:COG3842 6 LELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE-KRN-VGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 416 LEQEPRLF--LgSLREN----LdlaRMDGFS-SDQDLIV--ALKRFGLDKVIKKHPRgldmslgEnglgLSGGQKQIVAL 486
Cdd:COG3842 82 VFQDYALFphL-TVAENvafgL---RMRGVPkAEIRARVaeLLELVGLEGLADRYPH-------Q----LSGGQQQRVAL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 487 ARmTL-RNPKIVLLDEPTTGLDQ------YSEI----QALNAisawcrskTLLVVTHRPQ-VLSIVNRIIVVDNGKVVMD 554
Cdd:COG3842 147 AR-ALaPEPRVLLLDEPLSALDAklreemREELrrlqRELGI--------TFIYVTHDQEeALALADRIAVMNDGRIEQV 217
|
....*
gi 1437745540 555 G-PRD 558
Cdd:COG3842 218 GtPEE 222
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
352-561 |
3.79e-28 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 112.53 E-value: 3.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 352 VVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHylrnQVLLLE-----QEPRLFLG- 425
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH----EIARLGigrtfQIPRLFPEl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 426 SLRENLDLA---------RMDGFSSDQDLIVA-----LKRFGLDKVikkhprgLDMSLGEnglgLSGGQKQIVALARMTL 491
Cdd:cd03219 91 TVLENVMVAaqartgsglLLARARREEREAREraeelLERVGLADL-------ADRPAGE----LSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1437745540 492 RNPKIVLLDEPTTGLDQySEIQALNAI--SAWCRSKTLLVVTHR-PQVLSIVNRIIVVDNGKVVMDGPRDAVL 561
Cdd:cd03219 160 TDPKLLLLDEPAAGLNP-EETEELAELirELRERGITVLLVEHDmDVVMSLADRVTVLDQGRVIAEGTPDEVR 231
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
334-551 |
4.12e-28 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 113.80 E-value: 4.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 334 GNIKFQNVSFAYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEqGSITLDDVDIRQIDPHYLRNQV 413
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 414 LLLEQEPRLFLGSLRENLDlarMDGFSSDQDLIVALKRFGLDKVIKKHPRGLDMSLGENGLGLSGGQKQIVALARMTLRN 493
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLD---PYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1437745540 494 PKIVLLDEPTTGLD--QYSEI-QALNAISAWCrskTLLVVTHRPQVLSIVNRIIVVDNGKV 551
Cdd:cd03289 157 AKILLLDEPSAHLDpiTYQVIrKTLKQAFADC---TVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
336-555 |
4.46e-28 |
|
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: 112.08 E-value: 4.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSSSV--VKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQiDPHYLRNQV 413
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 414 LLLEQE----PRLflgSLRENLD-LARMDGFSSDQdlivALKRfgLDKVIKKhprgLDMS--LGENGLGLSGGQKQIVAL 486
Cdd:cd03266 81 GFVSDStglyDRL---TARENLEyFAGLYGLKGDE----LTAR--LEELADR----LGMEelLDRRVGGFSTGMRQKVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1437745540 487 ARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRS-KTLLVVTHRPQ-VLSIVNRIIVVDNGKVVMDG 555
Cdd:cd03266 148 ARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQeVERLCDRVVVLHRGRVVYEG 218
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
336-561 |
4.99e-28 |
|
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: 112.87 E-value: 4.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNqdSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAG-LYPAEQGSITL-----DDVDIRQIDPH-- 407
Cdd:COG1119 4 LELRNVTVRRG--GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLfgerrGGEDVWELRKRig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 408 ---------YLRN----QVLL--------LEQEPrlflgslrenldlarmdgfsSDQDLIVA---LKRFGLDKVIkkhpr 463
Cdd:COG1119 82 lvspalqlrFPRDetvlDVVLsgffdsigLYREP--------------------TDEQRERArelLELLGLAHLA----- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 464 glDMSLGEnglgLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRS--KTLLVVTHRPQ-VLSIV 540
Cdd:COG1119 137 --DRPFGT----LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHVEeIPPGI 210
|
250 260
....*....|....*....|.
gi 1437745540 541 NRIIVVDNGKVVMDGPRDAVL 561
Cdd:COG1119 211 THVLLLKDGRVVAAGPKEEVL 231
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
336-568 |
5.62e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 113.60 E-value: 5.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSSSVVKIL---SFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDI--RQIDPHYLR 410
Cdd:PRK13637 3 IKIENLTHIYMEGTPFEKKALdnvNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 411 NQVLLLEQEP--RLFLGSLREnlDLA---RMDGFSSDQ---DLIVALKRFGLDKVIKKhprglDMSLGEnglgLSGGQKQ 482
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEK--DIAfgpINLGLSEEEienRVKRAMNIVGLDYEDYK-----DKSPFE----LSGGQKR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 483 IVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSK--TLLVVTHRPQ-VLSIVNRIIVVDNGKVVMDGPRDA 559
Cdd:PRK13637 152 RVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEdVAKLADRIIVMNKGKCELQGTPRE 231
|
....*....
gi 1437745540 560 VLQQLAKNE 568
Cdd:PRK13637 232 VFKEVETLE 240
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
247-534 |
6.96e-28 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 117.99 E-value: 6.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 247 QQLNTIFLVIIGT--YLihsddpASKITMGALIATVILSGR---ALS-PLGQIAGLAvrfqqAWVA----LKGVNGIVER 316
Cdd:COG4178 276 GQLAVIFPILVAAprYF------AGEITLGGLMQAASAFGQvqgALSwFVDNYQSLA-----EWRAtvdrLAGFEEALEA 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 317 PSERESARKYITLKQiNGNIKFQNVSFaYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITL 396
Cdd:COG4178 345 ADALPEAASRIETSE-DGALALEDLTL-RTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 397 DDVDirqidphylrnQVLLLEQEPRLFLGSLRENLDLARMDGFSSDQDLIVALKRFGLDKVIKKhprgLDMSlgEN-GLG 475
Cdd:COG4178 423 PAGA-----------RVLFLPQRPYLPLGTLREALLYPATAEAFSDAELREALEAVGLGHLAER----LDEE--ADwDQV 485
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745540 476 LSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSKTLLVVTHRP 534
Cdd:COG4178 486 LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRS 544
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
336-552 |
1.14e-27 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 114.40 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSssVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYlRN--QV 413
Cdd:COG3839 4 LELENVSKSYGGVE--ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-RNiaMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 414 LlleQEPRLF--LgSLREN----LDLARMDGfsSDQDLIV--ALKRFGLDKVIKKHPRgldmslgenglGLSGGQKQIVA 485
Cdd:COG3839 81 F---QSYALYphM-TVYENiafpLKLRKVPK--AEIDRRVreAAELLGLEDLLDRKPK-----------QLSGGQRQRVA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745540 486 LARMTLRNPKIVLLDEPTTGLDQY------SEIQALNAisawcRSK-TLLVVTHRpQV--LSIVNRIIVVDNGKVV 552
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDAKlrvemrAEIKRLHR-----RLGtTTIYVTHD-QVeaMTLADRIAVMNDGRIQ 213
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
336-555 |
1.66e-27 |
|
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: 109.98 E-value: 1.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYnqDSSSVVKILSFEIKPGeKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRqIDPHYLRNQVLL 415
Cdd:cd03264 1 LQLENLTKRY--GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL-KQPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 416 LEQEPRLFLG-SLRENLD-LARMDGFSS---DQDLIVALKRFGLDKVIKKHPRGLdmslgenglglSGGQKQIVALARMT 490
Cdd:cd03264 77 LPQEFGVYPNfTVREFLDyIAWLKGIPSkevKARVDEVLELVNLGDRAKKKIGSL-----------SGGMRRRVGIAQAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745540 491 LRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSKTLLVVTHRPQ-VLSIVNRIIVVDNGKVVMDG 555
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEdVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
336-558 |
6.74e-27 |
|
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: 108.86 E-value: 6.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYnqDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHylRNQVLL 415
Cdd:cd03300 1 IELENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 416 LEQEPRLFLG-SLREN----LDLARMDGFSSDQDLIVALKRFGLDKVIKKHPRgldmslgenglGLSGGQKQIVALARMT 490
Cdd:cd03300 77 VFQNYALFPHlTVFENiafgLRLKKLPKAEIKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745540 491 LRNPKIVLLDEPTTGLD---------QYSEIQALNAIsawcrskTLLVVTH-RPQVLSIVNRIIVVDNGKVV-MDGPRD 558
Cdd:cd03300 146 VNEPKVLLLDEPLGALDlklrkdmqlELKRLQKELGI-------TFVFVTHdQEEALTMSDRIAVMNKGKIQqIGTPEE 217
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
357-551 |
1.29e-26 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 107.64 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 357 SFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHylRNQVLLLEQEPRLFLG-SLRENLDLAR 435
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPY--QRPVSMLFQENNLFAHlTVRQNIGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 436 MDGF---SSDQDLIVALKR-FGLDKVIKKHPRGLdmslgenglglSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYSE 511
Cdd:TIGR01277 96 HPGLklnAEQQEKVVDAAQqVGIADYLDRLPEQL-----------SGGQRQRVALARCLVRPNPILLLDEPFSALDPLLR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1437745540 512 IQALNAISAWC--RSKTLLVVTHRPQ-VLSIVNRIIVVDNGKV 551
Cdd:TIGR01277 165 EEMLALVKQLCseRQRTLLMVTHHLSdARAIASQIAVVSQGKI 207
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
336-555 |
1.35e-26 |
|
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: 107.59 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQiDPHYLRNQVLL 415
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 416 LEQEPRLFLG-SLRENLDL-ARMDGFS-SDQDLIVA--LKRFGLDKVIKKHPRgldmslgenglGLSGGQKQIVALARMT 490
Cdd:cd03263 80 CPQFDALFDElTVREHLRFyARLKGLPkSEIKEEVEllLRVLGLTDKANKRAR-----------TLSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745540 491 LRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSKTLLVVTHRPQVLSIV-NRIIVVDNGKVVMDG 555
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALcDRIAIMSDGKLRCIG 214
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
14-308 |
2.41e-26 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 109.14 E-value: 2.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 14 KKYYYQIILATFVINFLALVSSLYVMNVYDRVIPNKSYQTLWVLSIGVIIAILFEFTAKMLRGRLTDIAGKKADLIISSA 93
Cdd:cd18555 1 KKLLISILLLSLLLQLLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 94 LFRKVtnLKLqekPI------SSGSYVNNLRDFESVRDFMTSASLLTLVDMPFLILFVSVIALVGGYLAFVPLTIIPLVI 167
Cdd:cd18555 81 FFEHL--LKL---PYsffenrSSGDLLFRANSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 168 IVGLLAQIPLSKYINESMKESSQRQGLAVEAIEGIETLKTNNAMNWAQKRWDYYTAKTASSSMKVKNISNFVIYFAVMMQ 247
Cdd:cd18555 156 LLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQ 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1437745540 248 QLNTIFLVIIGTYLIHSddpaSKITMGALIATVILSGRALSPLGQIAGLAVRFQQAWVALK 308
Cdd:cd18555 236 FIAPLLILWIGAYLVIN----GELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLE 292
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
140-581 |
3.20e-26 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 114.36 E-value: 3.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 140 FLILFVSVIALVGGY---------LAFVPLTIIPLVIIVGLLAQIPLSKYINESMKESSQRQGLAVEAIEGIETLKTN-- 208
Cdd:PTZ00265 175 FITIFTYASAFLGLYiwslfknarLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYcg 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 209 -----NAMNWAQKRWDYYTAKTA-SSSMKVKNISNFVIyfavmmqqLNTIFLVIIGTYLIHSD----DPASKITMGALIA 278
Cdd:PTZ00265 255 ektilKKFNLSEKLYSKYILKANfMESLHIGMINGFIL--------ASYAFGFWYGTRIIISDlsnqQPNNDFHGGSVIS 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 279 tvILSGRALSP--LGQIAGLAVRFQQAWVALKGVNGIVERPSERESARKYITLKQINgNIKFQNVSFAYN-QDSSSVVKI 355
Cdd:PTZ00265 327 --ILLGVLISMfmLTIILPNITEYMKSLEATNSLYEIINRKPLVENNDDGKKLKDIK-KIQFKNVRFHYDtRKDVEIYKD 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 356 LSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDV-DIRQIDPHYLRNQVLLLEQEPRLFLGSLRENL--- 431
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIkys 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 432 -----DLARM------DGFSS-----------------------------------------DQDLIVALKRFGLDKVIK 459
Cdd:PTZ00265 484 lyslkDLEALsnyyneDGNDSqenknkrnscrakcagdlndmsnttdsneliemrknyqtikDSEVVDVSKKVLIHDFVS 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 460 KHPRGLDMSLGENGLGLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAW--CRSKTLLVVTHRPQVL 537
Cdd:PTZ00265 564 ALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkgNENRITIIIAHRLSTI 643
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1437745540 538 SIVNRIIVVDNGKVVMDGPRDAVLQQLAKNETEKQITAHSKNQN 581
Cdd:PTZ00265 644 RYANTIFVLSNRERGSTVDVDIIGEDPTKDNKENNNKNNKDDNN 687
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
338-582 |
4.92e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 112.08 E-value: 4.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 338 FQNVSFAYNQDsssvvKIL---SFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDvDIRqidphylrnqVL 414
Cdd:COG0488 1 LENLSKSFGGR-----PLLddvSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR----------IG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 415 LLEQEPRLF---------------LGSLRENLD----------------------LARMDGFSSDQDLIVALKRFGLDkv 457
Cdd:COG0488 65 YLPQEPPLDddltvldtvldgdaeLRALEAELEeleaklaepdedlerlaelqeeFEALGGWEAEARAEEILSGLGFP-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 458 ikkhPRGLDMSLGEnglgLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDqyseiqaLNAIsAWC------RSKTLLVVT 531
Cdd:COG0488 143 ----EEDLDRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLD-------LESI-EWLeeflknYPGTVLVVS 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745540 532 H------RpqvlsIVNRIIVVDNGKVVM-DGPRDAVLQQLAKNEtEKQITAHSKNQNR 582
Cdd:COG0488 207 HdryfldR-----VATRILELDRGKLTLyPGNYSAYLEQRAERL-EQEAAAYAKQQKK 258
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
336-548 |
5.35e-26 |
|
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: 104.54 E-value: 5.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAyNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLddvdirqidphYLRNQVLL 415
Cdd:cd03223 1 IELENLSLA-TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM-----------PEGEDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 416 LEQEPRLFLGSLRENLdlarmdgfssdqdlivalkRFGLDKVikkhprgldmslgenglgLSGGQKQIVALARMTLRNPK 495
Cdd:cd03223 69 LPQRPYLPLGTLREQL-------------------IYPWDDV------------------LSGGEQQRLAFARLLLHKPK 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1437745540 496 IVLLDEPTTGLDQYSEIQALNAISAwcRSKTLLVVTHRPQVLSIVNRIIVVDN 548
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQLLKE--LGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
336-559 |
7.34e-26 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 105.98 E-value: 7.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYnQDSSSVVKIL---SFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDphylRNQ 412
Cdd:COG4181 9 IELRGLTKTV-GTGAGELTILkgiSLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALD----EDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 413 VLLLE--------QEPRLfLGSL--REN----LDLARM-DGFSSDQDLivaLKRFGLDKVIKKHPRgldmslgenglGLS 477
Cdd:COG4181 84 RARLRarhvgfvfQSFQL-LPTLtaLENvmlpLELAGRrDARARARAL---LERVGLGHRLDHYPA-----------QLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 478 GGQKQIVALARMTLRNPKIVLLDEPTTGLDQYS--EIQ----ALNAISAwcrsKTLLVVTHRPQVLSIVNRIIVVDNGKV 551
Cdd:COG4181 149 GGEQQRVALARAFATEPAILFADEPTGNLDAATgeQIIdllfELNRERG----TTLVLVTHDPALAARCDRVLRLRAGRL 224
|
....*...
gi 1437745540 552 VMDGPRDA 559
Cdd:COG4181 225 VEDTAATA 232
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
352-573 |
1.00e-25 |
|
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: 105.70 E-value: 1.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 352 VVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQiDPHYLRNQVLL--LEQEPRLFLG-SLR 428
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITK-LPMHKRARLGIgyLPQEASIFRKlTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 429 ENLDLA-RMDGFSSDQDLIVA---LKRFGLDKVIKKhprgldmslgeNGLGLSGGQKQIVALARMTLRNPKIVLLDEPTT 504
Cdd:cd03218 94 ENILAVlEIRGLSKKEREEKLeelLEEFHITHLRKS-----------KASSLSGGERRRVEIARALATNPKFLLLDEPFA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437745540 505 GLDQYS--EIQALNAIsawCRSKTL--LVVTH--RpQVLSIVNRIIVVDNGKVVMDGPRDavlqQLAKNETEKQI 573
Cdd:cd03218 163 GVDPIAvqDIQKIIKI---LKDRGIgvLITDHnvR-ETLSITDRAYIIYEGKVLAEGTPE----EIAANELVRKV 229
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
334-561 |
1.17e-25 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 112.56 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 334 GNIKFQNVSFAYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQV 413
Cdd:PTZ00243 1307 GSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQF 1386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 414 LLLEQEPRLFLGSLRENLdlarmDGFS--SDQDLIVALKRFGLDKVIKKHPRGLDMSLGENGLGLSGGQKQIVALARMTL 491
Cdd:PTZ00243 1387 SMIPQDPVLFDGTVRQNV-----DPFLeaSSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALL 1461
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745540 492 -RNPKIVLLDEPTTGLDQY--SEIQA--LNAISAWcrskTLLVVTHRPQVLSIVNRIIVVDNGKVV-MDGPRDAVL 561
Cdd:PTZ00243 1462 kKGSGFILMDEATANIDPAldRQIQAtvMSAFSAY----TVITIAHRLHTVAQYDKIIVMDHGAVAeMGSPRELVM 1533
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
356-562 |
1.18e-25 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 106.28 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 356 LSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHylrnqvlllE----------QEPRLFLG 425
Cdd:COG0411 23 VSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPH---------RiarlgiartfQNPRLFPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 426 -SLRENLDLA--------------RMDGFSSDQDLIVA-----LKRFGLDKVIKKHPRGLdmslgenglglSGGQKQIVA 485
Cdd:COG0411 94 lTVLENVLVAaharlgrgllaallRLPRARREEREAREraeelLERVGLADRADEPAGNL-----------SYGQQRRLE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 486 LAR--MTlrNPKIVLLDEPTTGLDQySEIQALNA----ISAWcRSKTLLVVTHR-PQVLSIVNRIIVVDNGKVVMDGPRD 558
Cdd:COG0411 163 IARalAT--EPKLLLLDEPAAGLNP-EETEELAElirrLRDE-RGITILLIEHDmDLVMGLADRIVVLDFGRVIAEGTPA 238
|
....
gi 1437745540 559 AVLQ 562
Cdd:COG0411 239 EVRA 242
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
356-555 |
2.96e-25 |
|
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: 103.91 E-value: 2.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 356 LSFEIkPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDV---DIRQ---IDPHylRNQVLLLEQEPRLFLG-SLR 428
Cdd:cd03297 17 IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRKkinLPPQ--QRKIGLVFQQYALFPHlNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 429 ENLDLArMDGFSSDQDLIVA---LKRFGLDKVIKKHPrgldmslgengLGLSGGQKQIVALARMTLRNPKIVLLDEPTTG 505
Cdd:cd03297 94 ENLAFG-LKRKRNREDRISVdelLDLLGLDHLLNRYP-----------AQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1437745540 506 LDQYSEIQALNAISAwcRSKTL----LVVTHRP-QVLSIVNRIIVVDNGKVVMDG 555
Cdd:cd03297 162 LDRALRLQLLPELKQ--IKKNLnipvIFVTHDLsEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
336-556 |
4.10e-25 |
|
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: 103.81 E-value: 4.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVS--FAYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRN-- 411
Cdd:cd03258 2 IELKNVSkvFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 412 -QVLLLEQEPRLFLG-SLREN----LDLARMDGFSSDQDLIVALKRFGLDKVIKKHPRGLdmslgenglglSGGQKQIVA 485
Cdd:cd03258 82 rRIGMIFQHFNLLSSrTVFENvalpLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQL-----------SGGQKQRVG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1437745540 486 LARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSK--TLLVVTHRPQVL-SIVNRIIVVDNGKVVMDGP 556
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVkRICDRVAVMEKGEVVEEGT 224
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
336-554 |
4.98e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 104.40 E-value: 4.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSSSVVKIL---SFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIdPHYLRNQ 412
Cdd:COG1101 2 LELKNLSKTFNPGTVNEKRALdglNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKL-PEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 413 VLlleqePRLF----LG-----SLRENLDLARMDGfssdqdlivalKRFGLDKVIKKHPRG--------LDMSLgENGLG 475
Cdd:COG1101 81 YI-----GRVFqdpmMGtapsmTIEENLALAYRRG-----------KRRGLRRGLTKKRRElfrellatLGLGL-ENRLD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 476 -----LSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSK--TLLVVTHR-PQVLSIVNRIIVVD 547
Cdd:COG1101 144 tkvglLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENnlTTLMVTHNmEQALDYGNRLIMMH 223
|
....*..
gi 1437745540 548 NGKVVMD 554
Cdd:COG1101 224 EGRIILD 230
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
336-550 |
1.35e-24 |
|
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: 99.45 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYnqDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDvdirqidphylRNQVLL 415
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 416 LEQeprlflgslrenldlarmdgfssdqdlivalkrfgldkvikkhprgldmslgenglgLSGGQKQIVALARMTLRNPK 495
Cdd:cd03221 68 FEQ---------------------------------------------------------LSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745540 496 IVLLDEPTTGLDQYSeIQAL-NAISAWcrSKTLLVVTHRPQVLS-IVNRIIVVDNGK 550
Cdd:cd03221 91 LLLLDEPTNHLDLES-IEALeEALKEY--PGTVILVSHDRYFLDqVATKIIELEDGK 144
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
334-577 |
1.97e-24 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 108.84 E-value: 1.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 334 GNIKFQNVSFAYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEqGSITLDDVDIRQIDPHYLRNQV 413
Cdd:TIGR01271 1216 GQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAF 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 414 LLLEQEPRLFLGSLRENLD-LARMdgfsSDQDLIVALKRFGLDKVIKKHPRGLDMSLGENGLGLSGGQKQIVALARMTLR 492
Cdd:TIGR01271 1295 GVIPQKVFIFSGTFRKNLDpYEQW----SDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILS 1370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 493 NPKIVLLDEPTTGLD--QYSEI-QALNAISAWCrskTLLVVTHRPQVLSIVNRIIVVDNGKVVMdgpRDAVLQQLAKNET 569
Cdd:TIGR01271 1371 KAKILLLDEPSAHLDpvTLQIIrKTLKQSFSNC---TVILSEHRVEALLECQQFLVIEGSSVKQ---YDSIQKLLNETSL 1444
|
....*...
gi 1437745540 570 EKQITAHS 577
Cdd:TIGR01271 1445 FKQAMSAA 1452
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
336-552 |
2.46e-24 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 101.25 E-value: 2.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDS--SSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSIT-----LDDVDIRQIDPhy 408
Cdd:TIGR02982 2 ISIRNLNHYYGHGSlrKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKvlgqeLHGASKKQLVQ-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 409 LRNQVLLLEQEPRLfLGSL--REN----LDLArmDGFSSDQDLIVA---LKRFGLDKVIKKHPRGLdmslgenglglSGG 479
Cdd:TIGR02982 80 LRRRIGYIFQAHNL-LGFLtaRQNvqmaLELQ--PNLSYQEARERAramLEAVGLGDHLNYYPHNL-----------SGG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437745540 480 QKQIVALARMTLRNPKIVLLDEPTTGLDQYS--EIQALNAISAWCRSKTLLVVTHRPQVLSIVNRIIVVDNGKVV 552
Cdd:TIGR02982 146 QKQRVAIARALVHHPKLVLADEPTAALDSKSgrDVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDGKLL 220
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
336-564 |
3.33e-24 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 101.61 E-value: 3.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSSsVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYL---RNQ 412
Cdd:TIGR02315 2 LEVENLSKVYPNGKQ-ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLrklRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 413 VLLLEQE----PRLflgSLRENLDLAR---------MDGFSSDQDLIVA---LKRFGLDKvikKHPRGLDMslgenglgL 476
Cdd:TIGR02315 81 IGMIFQHynliERL---TVLENVLHGRlgykptwrsLLGRFSEEDKERAlsaLERVGLAD---KAYQRADQ--------L 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 477 SGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSKTLLVVTHRPQV---LSIVNRIIVVDNGKVVM 553
Cdd:TIGR02315 147 SGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVdlaKKYADRIVGLKAGEIVF 226
|
250
....*....|....*
gi 1437745540 554 DGP----RDAVLQQL 564
Cdd:TIGR02315 227 DGApselDDEVLRHI 241
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
336-551 |
3.73e-24 |
|
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: 100.68 E-value: 3.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNqdSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDI--RQIDPHYLRNQV 413
Cdd:cd03262 1 IEIKNLHKSFG--DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 414 LLLEQEPRLF--LGSLrENLDLARMD--GFSSDQDLIVA---LKRFGLDKVIKKHPRgldmslgenglGLSGGQKQIVAL 486
Cdd:cd03262 79 GMVFQQFNLFphLTVL-ENITLAPIKvkGMSKAEAEERAlelLEKVGLADKADAYPA-----------QLSGGQQQRVAI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745540 487 ARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSK-TLLVVTHRPQ-VLSIVNRIIVVDNGKV 551
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGmTMVVVTHEMGfAREVADRVIFMDDGRI 213
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
336-561 |
4.37e-24 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 101.22 E-value: 4.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNV--SFAYNQdsssVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDI--RQIDPHYLRN 411
Cdd:COG1126 2 IEIENLhkSFGDLE----VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 412 QVLLLEQEPRLF--LgSLRENLDLA--RMDGFSSDQDLIVA---LKRFGLDKVIKKHPRGLdmslgenglglSGGQKQIV 484
Cdd:COG1126 78 KVGMVFQQFNLFphL-TVLENVTLApiKVKKMSKAEAEERAmelLERVGLADKADAYPAQL-----------SGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 485 ALAR---MtlrNPKIVLLDEPTTGLD--QYSEIqaLNAISAWCRSK-TLLVVTH-----RpqvlSIVNRIIVVDNGKVVM 553
Cdd:COG1126 146 AIARalaM---EPKVMLFDEPTSALDpeLVGEV--LDVMRDLAKEGmTMVVVTHemgfaR----EVADRVVFMDGGRIVE 216
|
....*...
gi 1437745540 554 DGPRDAVL 561
Cdd:COG1126 217 EGPPEEFF 224
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
336-561 |
4.69e-24 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 101.22 E-value: 4.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNqDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLL 415
Cdd:cd03295 1 IEFENVTKRYG-GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 416 LEQEPRLFLG-SLRENLdlarmdgfssdqDLIVALKRFGLDKvIKKHPRGL--DMSLGENGLG------LSGGQKQIVAL 486
Cdd:cd03295 80 VIQQIGLFPHmTVEENI------------ALVPKLLKWPKEK-IRERADELlaLVGLDPAEFAdrypheLSGGQQQRVGV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 487 ARMTLRNPKIVLLDEPTTGLD---------QYSEIQALnaisawcRSKTLLVVTHRPQ-VLSIVNRIIVVDNGKVVMDGP 556
Cdd:cd03295 147 ARALAADPPLLLMDEPFGALDpitrdqlqeEFKRLQQE-------LGKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGT 219
|
....*
gi 1437745540 557 RDAVL 561
Cdd:cd03295 220 PDEIL 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
336-565 |
4.70e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 101.99 E-value: 4.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYnQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDirQIDPHYLrnqvll 415
Cdd:PRK13644 2 IRLENVSYSY-PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID--TGDFSKL------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 416 leQEPRLFLGSLRENLDlARMDGFSSDQDLIVALKRFGLDKV-IKKHprgLDMSLGENGLG---------LSGGQKQIVA 485
Cdd:PRK13644 73 --QGIRKLVGIVFQNPE-TQFVGRTVEEDLAFGPENLCLPPIeIRKR---VDRALAEIGLEkyrhrspktLSGGQGQCVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 486 LARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRS-KTLLVVTHRPQVLSIVNRIIVVDNGKVVMDGPRDAVLQQL 564
Cdd:PRK13644 147 LAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
.
gi 1437745540 565 A 565
Cdd:PRK13644 227 S 227
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
7-548 |
4.98e-24 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 107.42 E-value: 4.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 7 FKVIWRFKK----YYYQIILATFVINFLALVSSLYVMNVYD--RVIPNKSYQTLWVLSIGVIIailfeFTAKMLRGRLTD 80
Cdd:PTZ00265 817 YREIFSYKKdvtiIALSILVAGGLYPVFALLYAKYVSTLFDfaNLEANSNKYSLYILVIAIAM-----FISETLKNYYNN 891
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 81 IAGKKADLIISSALFRkvtNLKLQE---------KPISSGSYVNnlRDFESVRD-------FMTSASLLTLVDMPFLILF 144
Cdd:PTZ00265 892 VIGEKVEKTMKRRLFE---NILYQEisffdqdkhAPGLLSAHIN--RDVHLLKTglvnnivIFTHFIVLFLVSMVMSFYF 966
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 145 VSVIALVGGYLAFVPLTIIplviivGLLAQIPLSKYINEsmKESSQRQG----------------LAVEAIEGIETLKT- 207
Cdd:PTZ00265 967 CPIVAAVLTGTYFIFMRVF------AIRARLTANKDVEK--KEINQPGTvfaynsddeifkdpsfLIQEAFYNMNTVIIy 1038
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 208 ---NNAMNWAQKRWDYytaktASSSMKVKNISNFVIY-FAVMMQQLNTIFLVIIGTYLIHSDDPASKITMGALIaTVILS 283
Cdd:PTZ00265 1039 gleDYFCNLIEKAIDY-----SNKGQKRKTLVNSMLWgFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLF-TFLFT 1112
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 284 GralSPLGQIAGLAVRFQQAWVALKGVNGIVERPSE---RESARKYITLKQ-INGNIKFQNVSFAY-NQDSSSVVKILSF 358
Cdd:PTZ00265 1113 G---SYAGKLMSLKGDSENAKLSFEKYYPLIIRKSNidvRDNGGIRIKNKNdIKGKIEIMDVNFRYiSRPNVPIYKDLTF 1189
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 359 EIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQ----------------------------------------------- 391
Cdd:PTZ00265 1190 SCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNdhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsged 1269
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 392 -------GSITLDDVDIRQIDPHYLRNQVLLLEQEPRLFLGSLRENLDLARMDgfSSDQDLIVALKRFGLDKVIKKHPRG 464
Cdd:PTZ00265 1270 stvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKED--ATREDVKRACKFAAIDEFIESLPNK 1347
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 465 LDMSLGENGLGLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYSE--IQALNAISAWCRSKTLLVVTHRPQVLSIVNR 542
Cdd:PTZ00265 1348 YDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEklIEKTIVDIKDKADKTIITIAHRIASIKRSDK 1427
|
....*.
gi 1437745540 543 IIVVDN 548
Cdd:PTZ00265 1428 IVVFNN 1433
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
357-565 |
8.63e-24 |
|
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: 102.87 E-value: 8.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 357 SFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDD---VDIRQ-ID--PHylRNQVLLLEQEPRLF--LgSLR 428
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARgIFlpPH--RRRIGYVFQEARLFphL-SVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 429 ENLDLAR------MDGFSSDQdlIVALkrFGLDKVIKKHPRGLdmslgenglglSGGQKQIVALARMTLRNPKIVLLDEP 502
Cdd:COG4148 96 GNLLYGRkrapraERRISFDE--VVEL--LGIGHLLDRRPATL-----------SGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745540 503 TTGLDQYS--EIqaLNAISAWCRSKTL--LVVTHRPQ-VLSIVNRIIVVDNGKVVMDGPRDAVLQQLA 565
Cdd:COG4148 161 LAALDLARkaEI--LPYLERLRDELDIpiLYVSHSLDeVARLADHVVLLEQGRVVASGPLAEVLSRPD 226
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
339-560 |
1.04e-23 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 99.91 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 339 QNVSFAYNQdsSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYL-RNQVLLLE 417
Cdd:TIGR03410 4 SNLNVYYGQ--SHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 418 QE----PRLflgSLRENLDLArMDGFSSDQDLIVALKrFGLDKVIK--KHPRGLDmslgenglgLSGGQKQIVALARMTL 491
Cdd:TIGR03410 82 QGreifPRL---TVEENLLTG-LAALPRRSRKIPDEI-YELFPVLKemLGRRGGD---------LSGGQQQQLAIARALV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1437745540 492 RNPKIVLLDEPTTGLdQYSEIQ----ALNAISAWCRSKTLLVVTHRPQVLSIVNRIIVVDNGKVVMDGPRDAV 560
Cdd:TIGR03410 148 TRPKLLLLDEPTEGI-QPSIIKdigrVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
317-552 |
2.05e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 103.99 E-value: 2.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 317 PSERESARKYITLKqingnikfqNVSFAYnqDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITL 396
Cdd:COG0488 306 PPPERLGKKVLELE---------GLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 397 -DDVDI-------RQIDPH-----YLRN-QVLLLEQEPRLFLGSLrenldlarmdGFSSDQdlivalkrfgLDKVIKKhp 462
Cdd:COG0488 375 gETVKIgyfdqhqEELDPDktvldELRDgAPGGTEQEVRGYLGRF----------LFSGDD----------AFKPVGV-- 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 463 rgldmslgenglgLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYSeIQALN-AISAWcrSKTLLVVTHRPQVL-SIV 540
Cdd:COG0488 433 -------------LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIET-LEALEeALDDF--PGTVLLVSHDRYFLdRVA 496
|
250
....*....|..
gi 1437745540 541 NRIIVVDNGKVV 552
Cdd:COG0488 497 TRILEFEDGGVR 508
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
352-555 |
2.20e-23 |
|
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: 98.44 E-value: 2.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 352 VVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIrqIDPHYLRNQVLLLEQEPRLFLG-SLREN 430
Cdd:cd03268 15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY--QKNIEALRRIGALIEAPGFYPNlTAREN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 431 LDL-ARMDGFsSDQDLIVALKRFGLDKVIKKHPRgldmslgenglGLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQY 509
Cdd:cd03268 93 LRLlARLLGI-RKKRIDEVLDVVGLKDSAKKKVK-----------GFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1437745540 510 --SEIQALnaISAWCRS-KTLLVVTHrpqVLS----IVNRIIVVDNGKVVMDG 555
Cdd:cd03268 161 giKELREL--ILSLRDQgITVLISSH---LLSeiqkVADRIGIINKGKLIEEG 208
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
336-563 |
3.44e-23 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 100.99 E-value: 3.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSssVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIR-QIDPHylRNQVL 414
Cdd:COG1118 3 IEVRNISKRFGSFT--LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPR--ERRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 415 LLEQEPRLF--LgSLRENldlarmdgfssdqdliVAlkrFGLDkvIKKHPRG---------LDMsLGENGLG------LS 477
Cdd:COG1118 79 FVFQHYALFphM-TVAEN----------------IA---FGLR--VRPPSKAeirarveelLEL-VQLEGLAdrypsqLS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 478 GGQKQIVALARMTLRNPKIVLLDEPTTGLDqyseIQALNAISAWCRS------KTLLVVTHRPQ-VLSIVNRIIVVDNGK 550
Cdd:COG1118 136 GGQRQRVALARALAVEPEVLLLDEPFGALD----AKVRKELRRWLRRlhdelgGTTVFVTHDQEeALELADRVVVMNQGR 211
|
250
....*....|...
gi 1437745540 551 VVMDGPRDAVLQQ 563
Cdd:COG1118 212 IEQVGTPDEVYDR 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
336-552 |
5.02e-23 |
|
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: 97.33 E-value: 5.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYnqDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPhYLRNQVLL 415
Cdd:cd03301 1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPP-KDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 416 LEQ---EPRLflgSLREN----LDLARMDGFSSDQDLIVALKRFGLDKVIKKHPRgldmslgenglGLSGGQKQIVALAR 488
Cdd:cd03301 78 FQNyalYPHM---TVYDNiafgLKLRKVPKDEIDERVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745540 489 MTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCR--SKTLLVVTHrPQV--LSIVNRIIVVDNGKVV 552
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTH-DQVeaMTMADRIAVMNDGQIQ 210
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
352-568 |
5.86e-23 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 97.79 E-value: 5.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 352 VVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHylRNQVLLLEQEPRLFlgslrenl 431
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALF-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 432 dlARMDGFssdQDLIVALKRFGLDKV-IKKHPR------GLDMSLGENGLGLSGGQKQIVALARMTLRNPKIVLLDEPTT 504
Cdd:cd03299 84 --PHMTVY---KNIAYGLKKRKVDKKeIERKVLeiaemlGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745540 505 GLDQYSEIQALNAISAWCRSK--TLLVVTHR-PQVLSIVNRIIVVDNGKVVMDGPRDAVLQQlAKNE 568
Cdd:cd03299 159 ALDVRTKEKLREELKKIRKEFgvTVLHVTHDfEEAWALADKVAIMLNGKLIQVGKPEEVFKK-PKNE 224
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
356-534 |
8.60e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 96.48 E-value: 8.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 356 LSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDP----HYL--RNQVllleqEPRLflgSLRE 429
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVaeacHYLghRNAM-----KPAL---TVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 430 NLDL-ARMDGfSSDQDLIVALKRFGLDKVikkhprgLDMSLGEnglgLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQ 508
Cdd:PRK13539 93 NLEFwAAFLG-GEELDIAAALEAVGLAPL-------AHLPFGY----LSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
170 180
....*....|....*....|....*..
gi 1437745540 509 YSEIQALNAISAWCRSK-TLLVVTHRP 534
Cdd:PRK13539 161 AAVALFAELIRAHLAQGgIVIAATHIP 187
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
20-308 |
9.48e-23 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 98.78 E-value: 9.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 20 IILATFVINFLALVSSLYVMNVYDRVIPNKSYQTLWVLSIGVIIAILFEFTAKMLRGRLTDIAGKKADLIISSALFRKVT 99
Cdd:cd07346 4 ALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 100 NLKL---QEKPisSGSYVNNL-RDFESVRDFMTSASLLTLVDMPFLILFVSVIALVGGYLAFVPLTIIPLVIIVGLLAQI 175
Cdd:cd07346 84 RLSLsffDRNR--TGDLMSRLtSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 176 PLSKYINESMKESSQRQGLAVEAIEGIETLKTNNAMNWAQKRWDYYTAKTASSSMKVKNISNFVIYFAVMMQQLNTIFLV 255
Cdd:cd07346 162 RIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVL 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1437745540 256 IIGTYLIHSDDpaskITMGALIATVILSGRALSPLGQIAGLAVRFQQAWVALK 308
Cdd:cd07346 242 LYGGYLVLQGS----LTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLE 290
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
336-558 |
1.15e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 98.24 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSSS----VVKILSFEIKPGEKVGILGRIGSGKSTTLK-LAAGLYPAEqGSITLDDVDIRQIDPHY-L 409
Cdd:PRK13633 5 IKCKNVSYKYESNEESteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKhMNALLIPSE-GKVYVDGLDTSDEENLWdI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 410 RNQVLLLEQEPR-----------LFLGSlrENLDL------ARMDGfssdqdlivALKRFGLDKViKKHPRGLdmslgen 472
Cdd:PRK13633 84 RNKAGMVFQNPDnqivativeedVAFGP--ENLGIppeeirERVDE---------SLKKVGMYEY-RRHAPHL------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 473 glgLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSK--TLLVVTHRPQVLSIVNRIIVVDNGK 550
Cdd:PRK13633 145 ---LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGK 221
|
....*....
gi 1437745540 551 VVMDG-PRD 558
Cdd:PRK13633 222 VVMEGtPKE 230
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
336-556 |
1.53e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 97.78 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLL 415
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 416 LEQEP-RLFLGSL--------RENLDLARMDGFSSDQDlivALKRFGLDKVIKKHPRgldmslgenglGLSGGQKQIVAL 486
Cdd:PRK13635 86 VFQNPdNQFVGATvqddvafgLENIGVPREEMVERVDQ---ALRQVGMEDFLNREPH-----------RLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1437745540 487 ARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSK--TLLVVTHRPQVLSIVNRIIVVDNGKVVMDGP 556
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEILEEGT 223
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
356-507 |
2.68e-22 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 94.87 E-value: 2.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 356 LSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNqvLlleqeprLFLGSL-------- 427
Cdd:PRK13538 20 LSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQD--L-------LYLGHQpgiktelt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 428 -RENLD-LARMDGFSSDQDLIVALKRFGLDKVikkhprgLDMSLGEnglgLSGGQKQIVALARMTLRNPKIVLLDEPTTG 505
Cdd:PRK13538 91 aLENLRfYQRLHGPGDDEALWEALAQVGLAGF-------EDVPVRQ----LSAGQQRRVALARLWLTRAPLWILDEPFTA 159
|
..
gi 1437745540 506 LD 507
Cdd:PRK13538 160 ID 161
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
352-562 |
3.57e-22 |
|
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: 94.52 E-value: 3.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 352 VVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGL--YPAEQGSITLDDVDIRQIDPH-YLRNQVLLLEQEPrlflgslr 428
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEeRARLGIFLAFQYP-------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 429 enldlARMDGfssdqdliVALKRFgldkvikkhPRGLDMslgenglGLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDq 508
Cdd:cd03217 87 -----PEIPG--------VKNADF---------LRYVNE-------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD- 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1437745540 509 yseIQAL----NAISAWCRSKT-LLVVTHRPQVLSIV--NRIIVVDNGKVVMDGPRDAVLQ 562
Cdd:cd03217 137 ---IDALrlvaEVINKLREEGKsVLIITHYQRLLDYIkpDRVHVLYDGRIVKSGDKELALE 194
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
339-563 |
4.38e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 95.99 E-value: 4.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 339 QNVSFAYNQdsSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLLLEQ 418
Cdd:PRK13548 6 RNLSVRLGG--RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 419 EPRL-FLGSLRENLDLARMDGFSS---DQDLIV-ALKRFGLDkvikkHPRGLDMslgengLGLSGGQKQIVALAR----- 488
Cdd:PRK13548 84 HSSLsFPFTVEEVVAMGRAPHGLSraeDDALVAaALAQVDLA-----HLAGRDY------PQLSGGEQQRVQLARvlaql 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 489 -MTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSKTLLVVThrpqVLSIVN-------RIIVVDNGKVVMDGPRDAV 560
Cdd:PRK13548 153 wEPDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIV----VLHDLNlaaryadRIVLLHQGRLVADGTPAEV 228
|
...
gi 1437745540 561 LQQ 563
Cdd:PRK13548 229 LTP 231
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
336-564 |
7.77e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 96.41 E-value: 7.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYnqDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHyLRNQVLL 415
Cdd:PRK13537 8 IDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH-ARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 416 LEQEPRL---FlgSLRENLDL-ARMDGFSSDQ--DLIVALKRFGldkvikKHPRGLDMSLGEnglgLSGGQKQIVALARM 489
Cdd:PRK13537 85 VPQFDNLdpdF--TVRENLLVfGRYFGLSAAAarALVPPLLEFA------KLENKADAKVGE----LSGGMKRRLTLARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 490 TLRNPKIVLLDEPTTGLDQyseiQALNAI-----SAWCRSKTLLVVTH-RPQVLSIVNRIIVVDNGKVVMDG-PRDAVLQ 562
Cdd:PRK13537 153 LVNDPDVLVLDEPTTGLDP----QARHLMwerlrSLLARGKTILLTTHfMEEAERLCDRLCVIEEGRKIAEGaPHALIES 228
|
..
gi 1437745540 563 QL 564
Cdd:PRK13537 229 EI 230
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
339-563 |
1.16e-21 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 94.80 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 339 QNVSFAYNQdsSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLLLEQ 418
Cdd:COG4559 5 ENLSVRLGG--RTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 419 EPRL-FLGSLRENLDLARMDGFSS---DQDLIV-ALKRFGLDkvikkhprGLdmsLGENGLGLSGGQKQIVALAR----- 488
Cdd:COG4559 83 HSSLaFPFTVEEVVALGRAPHGSSaaqDRQIVReALALVGLA--------HL---AGRSYQTLSGGEQQRVQLARvlaql 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 489 --MTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSKTLLVVthrpqVLSIVN-------RIIVVDNGKVVMDGPRDA 559
Cdd:COG4559 152 wePVDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVA-----VLHDLNlaaqyadRILLLHQGRLVAQGTPEE 226
|
....
gi 1437745540 560 VLQQ 563
Cdd:COG4559 227 VLTD 230
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
356-562 |
1.34e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 93.98 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 356 LSFEIKPGEKVGILGRIGSGKSTTLKLAAGL--YPAEQGSITLDDVDIRQIDPH------------------------YL 409
Cdd:COG0396 19 VNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDeraragiflafqypveipgvsvsnFL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 410 R---NQVLLLEQEPRLFLGSLRENLDLARMDgfssdQDLivaLKRfgldkvikkhprgldmSLGEnglGLSGGQKQIVAL 486
Cdd:COG0396 99 RtalNARRGEELSAREFLKLLKEKMKELGLD-----EDF---LDR----------------YVNE---GFSGGEKKRNEI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 487 ARMTLRNPKIVLLDEPTTGLDqyseIQALNAISAWCRS-----KTLLVVTHRPQVLSIVN--RIIVVDNGKVVMDGPRDA 559
Cdd:COG0396 152 LQMLLLEPKLAILDETDSGLD----IDALRIVAEGVNKlrspdRGILIITHYQRILDYIKpdFVHVLVDGRIVKSGGKEL 227
|
...
gi 1437745540 560 VLQ 562
Cdd:COG0396 228 ALE 230
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
357-560 |
1.79e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 97.78 E-value: 1.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 357 SFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPH-YLRNQVLLLEQEPRLFLG-SLRENLDLA 434
Cdd:COG1129 24 SLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRdAQAAGIAIIHQELNLVPNlSVAENIFLG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 435 RMD---GFSSDQDLIV----ALKRFGLDkvIKkhprgLDMSLGEnglgLSGGQKQIVALARMTLRNPKIVLLDEPTTGLD 507
Cdd:COG1129 104 REPrrgGLIDWRAMRRrareLLARLGLD--ID-----PDTPVGD----LSVAQQQLVEIARALSRDARVLILDEPTASLT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745540 508 QySEIQALNAI----SAwcRSKTLLVVTHR-PQVLSIVNRIIVVDNGKVVMDGPRDAV 560
Cdd:COG1129 173 E-REVERLFRIirrlKA--QGVAIIYISHRlDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
336-574 |
2.05e-21 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 93.95 E-value: 2.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYnqDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLK----LAAgLYP---AEqGSITLDDVDI--RQIDP 406
Cdd:COG1117 12 IEVRNLNVYY--GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrMND-LIPgarVE-GEILLDGEDIydPDVDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 407 HYLRNQVLLLEQEPRLFLGSLRENLDLA-RMDGFSSDQDL--IV--ALKRFGL-DKVikKHprgldmSLGENGLGLSGGQ 480
Cdd:COG1117 88 VELRRRVGMVFQKPNPFPKSIYDNVAYGlRLHGIKSKSELdeIVeeSLRKAALwDEV--KD------RLKKSALGLSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 481 KQIVALARMTLRNPKIVLLDEPTTGLDQYS----E--IQALnaisawcRSK-TLLVVTHRP-QVLSIVNRIIVVDNGKVV 552
Cdd:COG1117 160 QQRLCIARALAVEPEVLLMDEPTSALDPIStakiEelILEL-------KKDyTIVIVTHNMqQAARVSDYTAFFYLGELV 232
|
250 260
....*....|....*....|..
gi 1437745540 553 MDGPRDAVLQQLAKNETEKQIT 574
Cdd:COG1117 233 EFGPTEQIFTNPKDKRTEDYIT 254
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
336-560 |
2.13e-21 |
|
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: 93.56 E-value: 2.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSSsvVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHylRNQVLL 415
Cdd:cd03296 3 IEVRNVSKRFGDFVA--LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 416 LEQEPRLFLG-SLRENLDL---ARMDGFSSDQDLIVA-----LKRFGLDKVIKKHPRgldmslgenglGLSGGQKQIVAL 486
Cdd:cd03296 79 VFQHYALFRHmTVFDNVAFglrVKPRSERPPEAEIRAkvhelLKLVQLDWLADRYPA-----------QLSGGQRQRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 487 ARMTLRNPKIVLLDEPTTGLDQyseiQALNAISAWCR------SKTLLVVTH-RPQVLSIVNRIIVVDNGKVVMDGPRDA 559
Cdd:cd03296 148 ARALAVEPKVLLLDEPFGALDA----KVRKELRRWLRrlhdelHVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDE 223
|
.
gi 1437745540 560 V 560
Cdd:cd03296 224 V 224
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
352-562 |
2.20e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 93.17 E-value: 2.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 352 VVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIdPHYLRNQVLL--LEQEPRLFLG-SLR 428
Cdd:COG1137 18 VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHL-PMHKRARLGIgyLPQEASIFRKlTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 429 EN----LDLARMDgfSSDQDLIVA--LKRFGLDKvIKKHPrgldmslgenGLGLSGGQKQIVALARMTLRNPKIVLLDEP 502
Cdd:COG1137 97 DNilavLELRKLS--KKEREERLEelLEEFGITH-LRKSK----------AYSLSGGERRRVEIARALATNPKFILLDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1437745540 503 TTGLDQYS--EIQALnaIsawcrsKTL-------LVVTHrpQV---LSIVNRIIVVDNGKVVMDGPRDAVLQ 562
Cdd:COG1137 164 FAGVDPIAvaDIQKI--I------RHLkergigvLITDH--NVretLGICDRAYIISEGKVLAEGTPEEILN 225
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
19-303 |
2.76e-21 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 94.54 E-value: 2.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 19 QIILATFVINFLALVSSLYVMNVYDRVIPNKSYQTLWVLSIGVIIAILFEFTAKMLRGRLTDIAGKKADLIISSALFRKV 98
Cdd:cd18779 6 QILLASLLLQLLGLALPLLTGVLVDRVIPRGDRDLLGVLGLGLAALVLTQLLAGLLRSHLLLRLRTRLDTQLTLGFLEHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 99 TNLKL---QEKpiSSGSYVNNLRDFESVRDFMTSASLLTLVDMPFLILFVSVIALVGGYLAFVPLTIIPLVIIVGLLAQI 175
Cdd:cd18779 86 LRLPYrffQQR--STGDLLMRLSSNATIRELLTSQTLSALLDGTLVLGYLALLFAQSPLLGLVVLGLAALQVALLLATRR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 176 PLSKYINESMKESSQRQGLAVEAIEGIETLKTNNAMNWAQKRW-DYYTAKTASSSMKvKNISNFVIYFAVMMQQLNTIFL 254
Cdd:cd18779 164 RVRELMARELAAQAEAQSYLVEALSGIETLKASGAEDRALDRWsNLFVDQLNASLRR-GRLDALVDALLATLRLAAPLVL 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1437745540 255 VIIGTYLIHSDdpasKITMGALIATVILSGRALSPLGQIAGLAVRFQQA 303
Cdd:cd18779 243 LWVGAWQVLDG----QLSLGTMLALNALAGAFLAPLASLVGTAQQLQLL 287
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
345-532 |
2.95e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 92.47 E-value: 2.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 345 YNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLLLEQEPRLFL 424
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 425 GSLRENLDLA-RMDGFSSDQDLIVA-LKRFGLDKVIkkhprgLDMSLGEnglgLSGGQKQIVALARMTLRNPKIVLLDEP 502
Cdd:PRK10247 95 DTVYDNLIFPwQIRNQQPDPAIFLDdLERFALPDTI------LTKNIAE----LSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
170 180 190
....*....|....*....|....*....|..
gi 1437745540 503 TTGLDQYSEIQALNAISAWCRSKTLLV--VTH 532
Cdd:PRK10247 165 TSALDESNKHNVNEIIHRYVREQNIAVlwVTH 196
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
352-551 |
3.03e-21 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 91.34 E-value: 3.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 352 VVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLLLEQEPRlflgslrenl 431
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYVPEDR---------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 432 dlarmdgfssdqdlivalKRFGLdkvikkhprGLDMSLGEN---GLGLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQ 508
Cdd:cd03215 85 ------------------KREGL---------VLDLSVAENialSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDV 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1437745540 509 ------YSEIQALNAisawcRSKT-LLVVTHRPQVLSIVNRIIVVDNGKV 551
Cdd:cd03215 138 gakaeiYRLIRELAD-----AGKAvLLISSELDELLGLCDRILVMYEGRI 182
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
336-558 |
3.56e-21 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 95.40 E-value: 3.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYnqDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHylRNQVLL 415
Cdd:PRK09452 15 VELRGISKSF--DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 416 LEQEPRLFLG-SLRENLDLA-RMDGFSSDQ---DLIVALKRFGLDKVIKKHPRgldmslgenglGLSGGQKQIVALARMT 490
Cdd:PRK09452 91 VFQSYALFPHmTVFENVAFGlRMQKTPAAEitpRVMEALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 491 LRNPKIVLLDEPTTGLDqY-------SEIQALN---AIsawcrskTLLVVTH-RPQVLSIVNRIIVVDNGKVVMDG-PRD 558
Cdd:PRK09452 160 VNKPKVLLLDESLSALD-YklrkqmqNELKALQrklGI-------TFVFVTHdQEEALTMSDRIVVMRDGRIEQDGtPRE 231
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
357-554 |
3.89e-21 |
|
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: 90.57 E-value: 3.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 357 SFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRqidphylrnqvllleqeprlflgslrenldlarm 436
Cdd:cd03216 20 SLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS---------------------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 437 dgFSSDQDlivALKRfgldkvikkhprgldmslgenGLG----LSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQySEI 512
Cdd:cd03216 66 --FASPRD---ARRA---------------------GIAmvyqLSVGERQMVEIARALARNARLLILDEPTAALTP-AEV 118
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1437745540 513 QALNAISAWCRS--KTLLVVTHR-PQVLSIVNRIIVVDNGKVVMD 554
Cdd:cd03216 119 ERLFKVIRRLRAqgVAVIFISHRlDEVFEIADRVTVLRDGRVVGT 163
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
336-555 |
4.98e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 94.00 E-value: 4.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSSSVVKIL---SFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRqIDPHYLRNQ 412
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELKALdnvSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEK-NKKKTKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 413 VLLLE---QEPRL----FLGSLRENL----DLARMDGFSS--DQDLIVALKRFGLDKV-IKKHPR------GLDMS-LGE 471
Cdd:PRK13651 82 KVLEKlviQKTRFkkikKIKEIRRRVgvvfQFAEYQLFEQtiEKDIIFGPVSMGVSKEeAKKRAAkyielvGLDESyLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 472 NGLGLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRS-KTLLVVTHR-PQVLSIVNRIIVVDNG 549
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDlDNVLEWTKRTIFFKDG 241
|
....*.
gi 1437745540 550 KVVMDG 555
Cdd:PRK13651 242 KIIKDG 247
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
352-552 |
1.01e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 95.47 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 352 VVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPH--------YL----RNQVLLLEQe 419
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRdairagiaYVpedrKGEGLVLDL- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 420 prlflgSLRENLDLARMDGFSsdqdlivalkRFGL----------DKVIKK---HPRGLDMSLGEnglgLSGGQKQIVAL 486
Cdd:COG1129 346 ------SIRENITLASLDRLS----------RGGLldrrreralaEEYIKRlriKTPSPEQPVGN----LSGGNQQKVVL 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 487 ARMTLRNPKIVLLDEPTTGLD--QYSEIQAL-NAISAwcRSKTLLVVTHR-PQVLSIVNRIIVVDNGKVV 552
Cdd:COG1129 406 AKWLATDPKVLILDEPTRGIDvgAKAEIYRLiRELAA--EGKAVIVISSElPELLGLSDRILVMREGRIV 473
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
339-562 |
1.02e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 91.49 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 339 QNVSFAYNqdSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPH-YLRNQVLLLE 417
Cdd:PRK10895 7 KNLAKAYK--GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaRARRGIGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 418 QEPRLFLG-SLRENLdlarMDGFSSDQDLIVALKRFGLDKVIKK-HPRGLDMSLGENglgLSGGQKQIVALARMTLRNPK 495
Cdd:PRK10895 85 QEASIFRRlSVYDNL----MAVLQIRDDLSAEQREDRANELMEEfHIEHLRDSMGQS---LSGGERRRVEIARALAANPK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 496 IVLLDEPTTGLDQYSEIQaLNAISAWCRSKTL--LVVTHR-PQVLSIVNRIIVVDNGKVVMDGPRDAVLQ 562
Cdd:PRK10895 158 FILLDEPFAGVDPISVID-IKRIIEHLRDSGLgvLITDHNvRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
337-548 |
1.51e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 90.23 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 337 KFQNVSFAYNQdsSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAE---QGSITLDDVDIRQIDPHylRNQV 413
Cdd:COG4136 3 SLENLTITLGG--RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAE--QRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 414 LLLEQEPRLF--LgSLRENL--DLARMDGFSSDQDLIV-ALKRFGLDKVIKKHPRGLdmslgenglglSGGQKQIVALAR 488
Cdd:COG4136 79 GILFQDDLLFphL-SVGENLafALPPTIGRAQRRARVEqALEEAGLAGFADRDPATL-----------SGGQRARVALLR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745540 489 MTLRNPKIVLLDEPTTGLDqyseiQALNA-ISAWCRSK-------TLLvVTHRPQVLSIVNRIIVVDN 548
Cdd:COG4136 147 ALLAEPRALLLDEPFSKLD-----AALRAqFREFVFEQirqrgipALL-VTHDEEDAPAAGRVLDLGN 208
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
352-568 |
1.89e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 92.09 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 352 VVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPH-----------YLRNQVllLEQep 420
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRrigylpeerglYPKMKV--GEQ-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 421 RLFLGSLReNLDLARmdgfsSDQDLIVALKRFGL----DKVIKKhprgldmslgenglgLSGGQKQ----IVALarmtLR 492
Cdd:COG4152 92 LVYLARLK-GLSKAE-----AKRRADEWLERLGLgdraNKKVEE---------------LSKGNQQkvqlIAAL----LH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 493 NPKIVLLDEPTTGLDQYS------EIQALNAisawcRSKTLLVVTHR-PQVLSIVNRIIVVDNGKVVMDGPRDAVLQQLA 565
Cdd:COG4152 147 DPELLILDEPFSGLDPVNvellkdVIRELAA-----KGTTVIFSSHQmELVEELCDRIVIINKGRKVLSGSVDEIRRQFG 221
|
...
gi 1437745540 566 KNE 568
Cdd:COG4152 222 RNT 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
356-563 |
1.95e-20 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 92.42 E-value: 1.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 356 LSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPA---EQGSITLDDVDIRQIDPHYLR----NQVLLLEQEPrlfLGSL- 427
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRkirgREIQMIFQDP---MTSLn 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 428 ---------RENLDLAR-MDGFSSDQDLIVALKRFGLD---KVIKKHPrgldmslGEnglgLSGGQKQIVALARMTLRNP 494
Cdd:COG0444 101 pvmtvgdqiAEPLRIHGgLSKAEARERAIELLERVGLPdpeRRLDRYP-------HE----LSGGMRQRVMIARALALEP 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745540 495 KIVLLDEPTTGLDqySEIQA--LNAISAWCRSK--TLLVVTHRpqvLSIV----NRIIVVDNGKVVMDGPRDAVLQQ 563
Cdd:COG0444 170 KLLIADEPTTALD--VTIQAqiLNLLKDLQRELglAILFITHD---LGVVaeiaDRVAVMYAGRIVEEGPVEELFEN 241
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
338-555 |
3.02e-20 |
|
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: 88.76 E-value: 3.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 338 FQNVSFAYNQDSSSVVKIL----SFEIKPGEKVGILGRIGSGKSTTLKLAAGL--YPAEQGSITLDDvdiRQIDPHYLRN 411
Cdd:cd03213 6 FRNLTVTVKSSPSKSGKQLlknvSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLING---RPLDKRSFRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 412 QVLLLEQEpRLFLGSL--RENLDLArmdgfssdqdliVALKrfgldkvikkhprgldmslgenglGLSGGQKQIVALARM 489
Cdd:cd03213 83 IIGYVPQD-DILHPTLtvRETLMFA------------AKLR------------------------GLSGGERKRVSIALE 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745540 490 TLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRS-KTLLVVTHRP--QVLSIVNRIIVVDNGKVVMDG 555
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTgRTIICSIHQPssEIFELFDKLLLLSQGRVIYFG 194
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
328-568 |
5.25e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 89.84 E-value: 5.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 328 TLKQINGNIKFQNVSFAYNqdSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKL---AAGLYPA--EQGSITLDDVDI- 401
Cdd:PRK14243 3 TLNGTETVLRTENLNVYYG--SFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGfrVEGKVTFHGKNLy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 402 -RQIDPHYLRNQVLLLEQEPRLFLGSLRENLDL-ARMDGFSSDQDLIV--ALKRFGL-DKVIKKhprgldmsLGENGLGL 476
Cdd:PRK14243 81 aPDVDPVEVRRRIGMVFQKPNPFPKSIYDNIAYgARINGYKGDMDELVerSLRQAALwDEVKDK--------LKQSGLSL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 477 SGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSKTLLVVTHRPQVLSIVNRIIVVDNGKVVMDGP 556
Cdd:PRK14243 153 SGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGG 232
|
250
....*....|..
gi 1437745540 557 RDAVLQQLAKNE 568
Cdd:PRK14243 233 RYGYLVEFDRTE 244
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
356-561 |
5.50e-20 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 91.71 E-value: 5.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 356 LSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDV---DIRQ---IDPHylRNQVLLLEQEPRLFLG-SLR 428
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfDSRKgifLPPE--KRRIGYVFQEARLFPHlSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 429 ENLDLARMDGFSSDQ----DLIVALkrFGLDKVIKKHPRGLdmslgenglglSGGQKQIVALARMTLRNPKIVLLDEPTT 504
Cdd:TIGR02142 94 GNLRYGMKRARPSERrisfERVIEL--LGIGHLLGRLPGRL-----------SGGEKQRVAIGRALLSSPRLLLMDEPLA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1437745540 505 GLD---QYSEIQALNAISAWCRSKTLLvVTHRPQ-VLSIVNRIIVVDNGKVVMDGPRDAVL 561
Cdd:TIGR02142 161 ALDdprKYEILPYLERLHAEFGIPILY-VSHSLQeVLRLADRVVVLEDGRVAAAGPIAEVW 220
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
353-574 |
6.00e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 90.92 E-value: 6.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 353 VKILSFEIKPGEKVGILGRIGSGKSTTLKLAAG-LYPAEqGSITLDDVDIRQIDPHYLRNQVLLLEQEPRLFlgslrenL 431
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGiLVPTS-GEVRVLGYVPFKRRKEFARRIGVVFGQRSQLW-------W 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 432 DLARMDGFS--------SDQDLIVALKRF----GLDKVIKKHPRGLdmSLGEnglglsggqkqivalaRMT-------LR 492
Cdd:COG4586 110 DLPAIDSFRllkaiyriPDAEYKKRLDELvellDLGELLDTPVRQL--SLGQ----------------RMRcelaaalLH 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 493 NPKIVLLDEPTTGLDQYSEIQALNAISAWCRSK--TLLVVTHRPQ-VLSIVNRIIVVDNGKVVMDGPRDAVLQQLAKnet 569
Cdd:COG4586 172 RPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMDdIEALCDRVIVIDHGRIIYDGSLEELKERFGP--- 248
|
....*
gi 1437745540 570 EKQIT 574
Cdd:COG4586 249 YKTIV 253
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
134-552 |
2.99e-19 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 91.40 E-value: 2.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 134 TLVDMPFLILFVSVIALVGGYLAFVP---LTIIPLVIIVGLLAQIPLSKYINESMKESSQRQGLAVEA----IEGIETLK 206
Cdd:COG4615 121 AFVRLPELLQSVALVLGCLAYLAWLSpplFLLTLVLLGLGVAGYRLLVRRARRHLRRAREAEDRLFKHfralLEGFKELK 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 207 TNnamnwAQKRWDYYTA--KTASSSMKVKNISNFVIY-FAVMMqqLNTIFLVIIGT--YLIHSDDPASKITMGALIATVI 281
Cdd:COG4615 201 LN-----RRRRRAFFDEdlQPTAERYRDLRIRADTIFaLANNW--GNLLFFALIGLilFLLPALGWADPAVLSGFVLVLL 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 282 -LSGralsPLGQIAGLAVRFQQAWVALKGVNGIVERPSERESARKYITLKQINGN---IKFQNVSFAY---NQDSSSVVK 354
Cdd:COG4615 274 fLRG----PLSQLVGALPTLSRANVALRKIEELELALAAAEPAAADAAAPPAPADfqtLELRGVTYRYpgeDGDEGFTLG 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 355 ILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQ---VLlleQEPRLFlgslRENL 431
Cdd:COG4615 350 PIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLfsaVF---SDFHLF----DRLL 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 432 DLarmDGFSSDQDLIVALKRFGLD-KVikkhprgldmSLgENG----LGLSGGQKQIVALARMTLRNPKIVLLDEPTTgl 506
Cdd:COG4615 423 GL---DGEADPARARELLERLELDhKV----------SV-EDGrfstTDLSQGQRKRLALLVALLEDRPILVFDEWAA-- 486
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1437745540 507 DQ--------YSEI-QALNAisawcRSKTLLVVTHRPQVLSIVNRIIVVDNGKVV 552
Cdd:COG4615 487 DQdpefrrvfYTELlPELKA-----RGKTVIAISHDDRYFDLADRVLKMDYGKLV 536
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
336-562 |
3.03e-19 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 87.07 E-value: 3.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQdsSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIR--QIDPHYLRNQV 413
Cdd:PRK09493 2 IEFKNVSKHFGP--TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 414 LLLEQEPRLF--LGSLrENLDLA--RMDGFSSDQ--DLIVALkrfgLDKVikkhprGLDMSLGENGLGLSGGQKQIVALA 487
Cdd:PRK09493 80 GMVFQQFYLFphLTAL-ENVMFGplRVRGASKEEaeKQAREL----LAKV------GLAERAHHYPSELSGGQQQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745540 488 RMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWC-RSKTLLVVTHRPQVLSIV-NRIIVVDNGKVVMDGPRDAVLQ 562
Cdd:PRK09493 149 RALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAeEGMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIK 225
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
344-507 |
3.50e-19 |
|
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: 85.87 E-value: 3.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 344 AYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLLLEQ---EP 420
Cdd:TIGR01189 7 ACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLpglKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 421 RLflgSLRENLDLARMDGFSSDQDLIVALKRFGLdkvikkhpRGL-DMSLGEnglgLSGGQKQIVALARMTLRNPKIVLL 499
Cdd:TIGR01189 87 EL---SALENLHFWAAIHGGAQRTIEDALAAVGL--------TGFeDLPAAQ----LSAGQQRRLALARLWLSRRPLWIL 151
|
....*...
gi 1437745540 500 DEPTTGLD 507
Cdd:TIGR01189 152 DEPTTALD 159
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
336-551 |
3.81e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 87.86 E-value: 3.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSSS-VVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVL 414
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 415 LLEQEP-RLFLGSLRENlDLA-RMDGFSSDQDLIV-----ALKRFGLDKVIKKHPRgldmslgenglGLSGGQKQIVALA 487
Cdd:PRK13650 85 MVFQNPdNQFVGATVED-DVAfGLENKGIPHEEMKervneALELVGMQDFKEREPA-----------RLSGGQKQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745540 488 RMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAwCRSK---TLLVVTHRPQVLSIVNRIIVVDNGKV 551
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRLELIKTIKG-IRDDyqmTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
336-555 |
3.83e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 87.87 E-value: 3.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYnQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLL 415
Cdd:PRK13647 5 IEVEDLHFRY-KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 416 LEQEP--RLFLGSLRE-------NLDLARMDGFSSDQDlivALKRFGLDKVIKKHPRgldmslgenglGLSGGQKQIVAL 486
Cdd:PRK13647 84 VFQDPddQVFSSTVWDdvafgpvNMGLDKDEVERRVEE---ALKAVRMWDFRDKPPY-----------HLSYGQKKRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1437745540 487 ARMTLRNPKIVLLDEPTTGLD---QYSEIQALNAISAwcRSKTLLVVTHRPQ-VLSIVNRIIVVDNGKVVMDG 555
Cdd:PRK13647 150 AGVLAMDPDVIVLDEPMAYLDprgQETLMEILDRLHN--QGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEG 220
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
310-564 |
5.79e-19 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 90.25 E-value: 5.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 310 VNGIVERPSERESARKYITLKQIngnIKFQNVSFAYNQDSSSVVKI---LSFEIKPGEKVGILGRIGSGKSTTLKLAAGL 386
Cdd:TIGR03269 257 VAVFMEGVSEVEKECEVEVGEPI---IKVRNVSKRYISVDRGVVKAvdnVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGV 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 387 YPAEQGSITL---DD-VDIRQIDPHyLRNQVL----LLEQEPRLF-----LGSLRENLDLARMDGFSSDQDLIVaLKRFG 453
Cdd:TIGR03269 334 LEPTSGEVNVrvgDEwVDMTKPGPD-GRGRAKryigILHQEYDLYphrtvLDNLTEAIGLELPDELARMKAVIT-LKMVG 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 454 LDKviKKHPRGLDMSLGEnglgLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAI--SAWCRSKTLLVVT 531
Cdd:TIGR03269 412 FDE--EKAEEILDKYPDE----LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkAREEMEQTFIIVS 485
|
250 260 270
....*....|....*....|....*....|....
gi 1437745540 532 HRPQ-VLSIVNRIIVVDNGKVVMDGPRDAVLQQL 564
Cdd:TIGR03269 486 HDMDfVLDVCDRAALMRDGKIVKIGDPEEIVEEL 519
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
356-555 |
9.06e-19 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 85.40 E-value: 9.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 356 LSFEIKPGEKVGILGRIGSGKSTTLKLAAGLypAEQGSITLDDVDI--RQIDPHYLRNQVLLLEQEPRlFLGSL--RENL 431
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGR--VEGGGTTSGQILFngQPRKPDQFQKCVAYVRQDDI-LLPGLtvRETL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 432 DLArmdgfssdqdLIVALKRFGLDKVIKKhpRGLDMSLGENGL---------GLSGGQKQIVALARMTLRNPKIVLLDEP 502
Cdd:cd03234 103 TYT----------AILRLPRKSSDAIRKK--RVEDVLLRDLALtriggnlvkGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745540 503 TTGLDQYSEIQALNAISAWCRSKTLLVVT-H--RPQVLSIVNRIIVVDNGKVVMDG 555
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLARRNRIVILTiHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
341-563 |
1.01e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 89.29 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 341 VSFAYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHY-LRNQVLLLeQE 419
Cdd:PRK10762 256 VRLKVDNLSGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANGIVYI-SE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 420 PR----LFLG-SLRENLDLARMDGFSSD------QDLIVALKRFgldkvIK----KHPrGLDMSLGEnglgLSGGQKQIV 484
Cdd:PRK10762 335 DRkrdgLVLGmSVKENMSLTALRYFSRAggslkhADEQQAVSDF-----IRlfniKTP-SMEQAIGL----LSGGNQQKV 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 485 ALARMTLRNPKIVLLDEPTTGLD--QYSEI-QALNAISAWCRSkTLLVVTHRPQVLSIVNRIIVVDNGKVVMDGPRDAVL 561
Cdd:PRK10762 405 AIARGLMTRPKVLILDEPTRGVDvgAKKEIyQLINQFKAEGLS-IILVSSEMPEVLGMSDRILVMHEGRISGEFTREQAT 483
|
..
gi 1437745540 562 QQ 563
Cdd:PRK10762 484 QE 485
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
336-555 |
1.17e-18 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 84.64 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQdsSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPH-------- 407
Cdd:cd03269 1 LEVENVTKRFGR--VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNrigylpee 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 408 ---YLRNQVllleQEPRLFLGSLRenlDLARMDGFSSDQDLivaLKRFGL----DKVIKKhprgldmslgenglgLSGGQ 480
Cdd:cd03269 79 rglYPKMKV----IDQLVYLAQLK---GLKKEEARRRIDEW---LERLELseyaNKRVEE---------------LSKGN 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745540 481 KQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRS-KTLLVVTHR-PQVLSIVNRIIVVDNGKVVMDG 555
Cdd:cd03269 134 QQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAgKTVILSTHQmELVEELCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
336-558 |
1.42e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 86.42 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSSSVVKIL---SFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDvdiRQIDPHY---- 408
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKGLdniSFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAG---YHITPETgnkn 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 409 ---LRNQVLLLEQ--EPRLFLGSLRENLDLARMD-GFSSDQDLIVA---LKRFGL-DKVIKKHPrgldmslgengLGLSG 478
Cdd:PRK13641 80 lkkLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfGFSEDEAKEKAlkwLKKVGLsEDLISKSP-----------FELSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 479 GQKQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRS-KTLLVVTHR-PQVLSIVNRIIVVDNGKVVM-DG 555
Cdd:PRK13641 149 GQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAgHTVILVTHNmDDVAEYADDVLVLEHGKLIKhAS 228
|
...
gi 1437745540 556 PRD 558
Cdd:PRK13641 229 PKE 231
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
336-558 |
2.21e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 85.51 E-value: 2.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNqDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYL--RNQV 413
Cdd:PRK13639 2 LETRDLKYSYP-DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 414 LLLEQEP--RLFLGSLRENLDLARMD-GFSSDQ---DLIVALKRFGLDKVIKKHPRGLdmslgenglglSGGQKQIVALA 487
Cdd:PRK13639 81 GIVFQNPddQLFAPTVEEDVAFGPLNlGLSKEEvekRVKEALKAVGMEGFENKPPHHL-----------SGGQKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1437745540 488 RMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSK-TLLVVTHRPQVLSI-VNRIIVVDNGKVVMDG-PRD 558
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGiTIIISTHDVDLVPVyADKVYVMSDGKIIKEGtPKE 223
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
336-573 |
2.90e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 85.18 E-value: 2.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSSSVVKIL---SFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQI----DPHY 408
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEGRALfdvNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 409 LRNQVLLLEQ--EPRLFLGSLRENLDLARMDgFSSDQDLIVALKRFGLDKVikkhprGLDMSL-GENGLGLSGGQKQIVA 485
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQN-FGVSQEEAEALAREKLALV------GISESLfEKNPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 486 LARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRS-KTLLVVTH-RPQVLSIVNRIIVVDNGKVVMDGPRDAVLQQ 563
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSgMTIVLVTHlMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
250
....*....|
gi 1437745540 564 LAKNEtEKQI 573
Cdd:PRK13649 236 VDFLE-EKQL 244
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
352-561 |
2.96e-18 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 84.42 E-value: 2.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 352 VVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPhyLRNQVLLLEQeprlflgsLRENL 431
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARS--LSQQKGLIRQ--------LRQHV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 432 dlarmdGFSSdQDLIVALKRFGLDKVI------KKHPRGLDMSLGENGLG--------------LSGGQKQIVALARMTL 491
Cdd:PRK11264 88 ------GFVF-QNFNLFPHRTVLENIIegpvivKGEPKEEATARARELLAkvglagketsyprrLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1437745540 492 RNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSK-TLLVVTHRPQVL-SIVNRIIVVDNGKVVMDGPRDAVL 561
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKALF 232
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
336-551 |
3.11e-18 |
|
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: 83.61 E-value: 3.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSSSVVKIlSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDI-----RQIDphYLR 410
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGI-NISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlrgRAIP--YLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 411 NQVLLLEQEPRLFLG-SLRENLDLARMDGFSSDQD----LIVALKRFGLDKVIKKHPRGLdmslgenglglSGGQKQIVA 485
Cdd:cd03292 78 RKIGVVFQDFRLLPDrNVYENVAFALEVTGVPPREirkrVPAALELVGLSHKHRALPAEL-----------SGGEQQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1437745540 486 LARMTLRNPKIVLLDEPTTGLD-QYS-EI-QALNAISAwcRSKTLLVVTHRPqvlSIVN----RIIVVDNGKV 551
Cdd:cd03292 147 IARAIVNSPTILIADEPTGNLDpDTTwEImNLLKKINK--AGTTVVVATHAK---ELVDttrhRVIALERGKL 214
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
336-574 |
3.47e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 84.44 E-value: 3.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSSsvVKILSFEIKPGEKVGILGRIGSGKSTTLKL---AAGLYP--AEQGSITLDDVDI--RQIDPHY 408
Cdd:PRK14239 6 LQVSDLSVYYNKKKA--LNSVSLDFYPNEITALIGPSGSGKSTLLRSinrMNDLNPevTITGSIVYNGHNIysPRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 409 LRNQVLLLEQEPRLFLGSLRENLDLA-RMDGFSSDQDLivalkrfglDKVIKKHPRGLDM------SLGENGLGLSGGQK 481
Cdd:PRK14239 84 LRKEIGMVFQQPNPFPMSIYENVVYGlRLKGIKDKQVL---------DEAVEKSLKGASIwdevkdRLHDSALGLSGGQQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 482 QIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSKTLLVVTHRPQVLS-IVNRIIVVDNGKVVMDGPRDAV 560
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASrISDRTGFFLDGDLIEYNDTKQM 234
|
250
....*....|....
gi 1437745540 561 LQQLAKNETEKQIT 574
Cdd:PRK14239 235 FMNPKHKETEDYIS 248
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
333-555 |
3.73e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 85.06 E-value: 3.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 333 NGNIKFQNVSFAYNQDSSSVVKIL---SFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDD----VDIRQI- 404
Cdd:PRK13645 4 SKDIILDNVSYTYAKKTPFEFKALnntSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 405 DPHYLRNQVLLLEQEP--RLFLGSLrenldlarmdgfssDQDLIVALKRFGLDK--VIKKHPRGLDM-SLGEN-----GL 474
Cdd:PRK13645 84 EVKRLRKEIGLVFQFPeyQLFQETI--------------EKDIAFGPVNLGENKqeAYKKVPELLKLvQLPEDyvkrsPF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 475 GLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRS--KTLLVVTHR-PQVLSIVNRIIVVDNGKV 551
Cdd:PRK13645 150 ELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNmDQVLRIADEVIVMHEGKV 229
|
....
gi 1437745540 552 VMDG 555
Cdd:PRK13645 230 ISIG 233
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
347-564 |
4.48e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.45 E-value: 4.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 347 QDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTlKLAAGLYPAEQGSITLDDVDIRQIDPHYL---RNQVLLLEQEPRlf 423
Cdd:PRK15134 296 VDHNVVVKNISFTLRPGETLGLVGESGSGKSTT-GLALLRLINSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPN-- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 424 lGSLRENLDLAR------------MDGFSSDQDLIVALKRFGLDKVIK-KHPrgldmslGEnglgLSGGQKQIVALARMT 490
Cdd:PRK15134 373 -SSLNPRLNVLQiieeglrvhqptLSAAQREQQVIAVMEEVGLDPETRhRYP-------AE----FSGGQRQRIAIARAL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 491 LRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSKTL--LVVTHRPQVL-SIVNRIIVVDNGKVVMDG--------PRDA 559
Cdd:PRK15134 441 ILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVrALCHQVIVLRQGEVVEQGdcervfaaPQQE 520
|
....*
gi 1437745540 560 VLQQL 564
Cdd:PRK15134 521 YTRQL 525
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
352-552 |
4.83e-18 |
|
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: 84.09 E-value: 4.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 352 VVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDP---HYLRNQVLLLEQE------PRL 422
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRkqrRAFRRDVQLVFQDspsavnPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 423 FLG-SLRENL-DLARMDGFSSDQDLIVALKRFGL-DKVIKKHPRGLdmslgenglglSGGQKQIVALARMTLRNPKIVLL 499
Cdd:TIGR02769 106 TVRqIIGEPLrHLTSLDESEQKARIAELLDMVGLrSEDADKLPRQL-----------SGGQLQRINIARALAVKPKLIVL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745540 500 DEPTTGLD---QYSEIQALNAISAwcRSKT-LLVVTHRPQ-VLSIVNRIIVVDNGKVV 552
Cdd:TIGR02769 175 DEAVSNLDmvlQAVILELLRKLQQ--AFGTaYLFITHDLRlVQSFCQRVAVMDKGQIV 230
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
352-558 |
5.50e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 83.96 E-value: 5.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 352 VVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIdphylRNQVLLLEQEPRLF-LGSLREN 430
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-----REDTRLMFQDARLLpWKKVIDN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 431 LDLarmdGFSSD--QDLIVALKRFGLDKVIKKHPRGLdmslgenglglSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQ 508
Cdd:PRK11247 102 VGL----GLKGQwrDAALQALAAVGLADRANEWPAAL-----------SGGQKQRVALARALIHRPGLLLLDEPLGALDA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1437745540 509 YSEIQALNAI-SAWCRSK-TLLVVTHR-PQVLSIVNRIIVVDNGKVVMDGPRD 558
Cdd:PRK11247 167 LTRIEMQDLIeSLWQQHGfTVLLVTHDvSEAVAMADRVLLIEEGKIGLDLTVD 219
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
336-563 |
6.15e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 83.91 E-value: 6.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSssVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLL 415
Cdd:PRK11231 3 LRTENLTVGYGTKR--ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 416 LEQEPRLFLG-SLRENLDLARMDGFS-------SDQDLI-VALKRFGLDKVIKKhpRGLDmslgenglgLSGGQKQIVAL 486
Cdd:PRK11231 81 LPQHHLTPEGiTVRELVAYGRSPWLSlwgrlsaEDNARVnQAMEQTRINHLADR--RLTD---------LSGGQRQRAFL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 487 ArMTL-RNPKIVLLDEPTTGLD---Q---YSEIQALNAisawcRSKTLLVVTHR-PQVLSIVNRIIVVDNGKVVMDGPRD 558
Cdd:PRK11231 150 A-MVLaQDTPVVLLDEPTTYLDinhQvelMRLMRELNT-----QGKTVVTVLHDlNQASRYCDHLVVLANGHVMAQGTPE 223
|
....*
gi 1437745540 559 AVLQQ 563
Cdd:PRK11231 224 EVMTP 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
353-563 |
8.06e-18 |
|
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: 86.66 E-value: 8.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 353 VKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEqGSITLDDVDIRQIDPHYLRN-----QVLLleQEPrlfLGSL 427
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-GEIRFDGQDLDGLSRRALRPlrrrmQVVF--QDP---FGSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 428 ----------RENLDLARMDGFSSDQDLIV--ALKRFGLDK-VIKKHPRgldmslgEnglgLSGGQKQIVALAR-MTLRn 493
Cdd:COG4172 376 sprmtvgqiiAEGLRVHGPGLSAAERRARVaeALEEVGLDPaARHRYPH-------E----FSGGQRQRIAIARaLILE- 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437745540 494 PKIVLLDEPTTGLDQysEIQA--LNAISAWCRSKTL--LVVTHRPQVL-SIVNRIIVVDNGKVVMDGPRDAVLQQ 563
Cdd:COG4172 444 PKLLVLDEPTSALDV--SVQAqiLDLLRDLQREHGLayLFISHDLAVVrALAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
356-534 |
8.30e-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: 82.16 E-value: 8.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 356 LSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLLLEQEPRLFLGSLRENLDLAR 435
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFWH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 436 MDGfsSDQDLIVALKRFGLdkvikkhpRGL-DMSLGEnglgLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQA 514
Cdd:cd03231 99 ADH--SDEQVEEALARVGL--------NGFeDRPVAQ----LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170 180
....*....|....*....|.
gi 1437745540 515 LNAISAWC-RSKTLLVVTHRP 534
Cdd:cd03231 165 AEAMAGHCaRGGMVVLTTHQD 185
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
353-555 |
8.36e-18 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 82.42 E-value: 8.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 353 VKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQiDPHYLRNQVLLLEQEPRLFLG-SLRENL 431
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDElTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 432 DL-ARMDGFSSD---QDLIVALKRFGL----DKVIKKHprgldmslgenglglSGGQKQIVALARMTLRNPKIVLLDEPT 503
Cdd:cd03265 95 YIhARLYGVPGAerrERIDELLDFVGLleaaDRLVKTY---------------SGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1437745540 504 TGLDQYSEIQALNAISAWCRSK--TLLVVTH-RPQVLSIVNRIIVVDNGKVVMDG 555
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEEFgmTILLTTHyMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
336-563 |
1.01e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 84.88 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNqdSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIrqidPHYLRNQVLL 415
Cdd:PRK13536 42 IDLAGVSKSYG--DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV----PARARLARAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 416 LEQEPRLflgslrENLDLArmdgFSSDQDLIVALKRFGL-----DKVIkkhPRGLDMSLGENGLG-----LSGGQKQIVA 485
Cdd:PRK13536 116 IGVVPQF------DNLDLE----FTVRENLLVFGRYFGMstreiEAVI---PSLLEFARLESKADarvsdLSGGMKRRLT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 486 LARMTLRNPKIVLLDEPTTGLDQYSE---IQALNAISAwcRSKTLLVVTH-RPQVLSIVNRIIVVDNGKVVMDGPRDAVL 561
Cdd:PRK13536 183 LARALINDPQLLILDEPTTGLDPHARhliWERLRSLLA--RGKTILLTTHfMEEAERLCDRLCVLEAGRKIAEGRPHALI 260
|
..
gi 1437745540 562 QQ 563
Cdd:PRK13536 261 DE 262
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
81-563 |
1.16e-17 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 87.31 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 81 IAGKKADLIISSALFRKVTNLKLQEKPISSGSYVNNLRDFESVRdFMTSASLLTLV-DMPF-LILFVSVIALVGGYLAFV 158
Cdd:TIGR00957 384 VSGMRIKTAVMGAVYRKALVITNSARKSSTVGEIVNLMSVDAQR-FMDLATYINMIwSAPLqVILALYFLWLNLGPSVLA 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 159 PLTIIPLVIIVGLLAQIPLSKYINESMKESSQRQGLAVEAIEGIETLKTnnaMNWAQKRWDYYTAkTASSSMKVKNISNF 238
Cdd:TIGR00957 463 GVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKL---YAWELAFLDKVEG-IRQEELKVLKKSAY 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 239 vIYFAVMMQQLNTIFLVIIGTYLIH-SDDPASKITMGALIATVILSGRALSPLGQIAGLAVRFQQAWVALKGVNGIVERP 317
Cdd:TIGR00957 539 -LHAVGTFTWVCTPFLVALITFAVYvTVDENNILDAEKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHE 617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 318 SERESARKYITLKQINGN-IKFQNVSFAYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITL 396
Cdd:TIGR00957 618 ELEPDSIERRTIKPGEGNsITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM 697
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 397 DDVDIRQIDPHYLRNQVLlleQEPRLFLGSLRENLDLARMDGFSSDQDLIVAlkrfgldkvikkhPRGLDMSLGENGLGL 476
Cdd:TIGR00957 698 KGSVAYVPQQAWIQNDSL---RENILFGKALNEKYYQQVLEACALLPDLEIL-------------PSGDRTEIGEKGVNL 761
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 477 SGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAI---SAWCRSKTLLVVTHRPQVLSIVNRIIVVDNGKVVM 553
Cdd:TIGR00957 762 SGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISE 841
|
490
....*....|
gi 1437745540 554 DGPRDAVLQQ 563
Cdd:TIGR00957 842 MGSYQELLQR 851
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
368-555 |
1.29e-17 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 84.08 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 368 ILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHylRNQVLLLEQEPRLFlgslrenldlARMdgfSSDQDLIV 447
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH--LRHINMVFQSYALF----------PHM---TVEENVAF 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 448 ALKRFGLDKVIKKhPRGLDM----SLGENG----LGLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAIS 519
Cdd:TIGR01187 66 GLKMRKVPRAEIK-PRVLEAlrlvQLEEFAdrkpHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELK 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 1437745540 520 AWCRS--KTLLVVTH-RPQVLSIVNRIIVVDNGKVVMDG 555
Cdd:TIGR01187 145 TIQEQlgITFVFVTHdQEEAMTMSDRIAIMRKGKIAQIG 183
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
336-556 |
1.81e-17 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 83.97 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSSSV--VKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRN-- 411
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 412 --------QVLLLEQepRlflgSLREN----LDLARMDGfsSDQDLIVA--LKRFGLDKVIKKHPRgldmslgenglGLS 477
Cdd:COG1135 82 rkigmifqHFNLLSS--R----TVAENvalpLEIAGVPK--AEIRKRVAelLELVGLSDKADAYPS-----------QLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 478 GGQKQIVALARMTLRNPKIVLLDEPTTGLDQYS--EIQAL----NA---IsawcrskTLLVVTHRPQVL-SIVNRIIVVD 547
Cdd:COG1135 143 GGQKQRVGIARALANNPKVLLCDEATSALDPETtrSILDLlkdiNRelgL-------TIVLITHEMDVVrRICDRVAVLE 215
|
....*....
gi 1437745540 548 NGKVVMDGP 556
Cdd:COG1135 216 NGRIVEQGP 224
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
336-555 |
1.90e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 82.49 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLL 415
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 416 LEQEP-RLFLGSLREnLDLArmdgfssdqdlivalkrFGL-------DKVIKKHPRGL---DMSLGENG--LGLSGGQKQ 482
Cdd:PRK13648 88 VFQNPdNQFVGSIVK-YDVA-----------------FGLenhavpyDEMHRRVSEALkqvDMLERADYepNALSGGQKQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437745540 483 IVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSK--TLLVVTHRPQVLSIVNRIIVVDNGKVVMDG 555
Cdd:PRK13648 150 RVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEG 224
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
357-560 |
2.09e-17 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 83.63 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 357 SFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYL---RNQVLLLEQEP------RLFLG-S 426
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplRRRMQMVFQDPyaslnpRMTVGdI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 427 LRENLDLARMDGFSSDQDLIVALkrfgLDKVikkhprGLD---------MslgenglgLSGGQKQIVALARMTLRNPKIV 497
Cdd:COG4608 118 IAEPLRIHGLASKAERRERVAEL----LELV------GLRpehadryphE--------FSGGQRQRIGIARALALNPKLI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 498 LLDEPTTGLDqYSeIQA--------------LnaisawcrskTLLVVTHRpqvLSIV----NRIIVVDNGKVVMDGPRDA 559
Cdd:COG4608 180 VCDEPVSALD-VS-IQAqvlnlledlqdelgL----------TYLFISHD---LSVVrhisDRVAVMYLGKIVEIAPRDE 244
|
.
gi 1437745540 560 V 560
Cdd:COG4608 245 L 245
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
353-555 |
2.79e-17 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 82.82 E-value: 2.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 353 VKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQiDPHYLRNQVLLLEQEPRLFLG-SLRENL 431
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVR-EPRKVRRSIGIVPQYASVDEDlTGRENL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 432 DL-ARMDGFSSD---QDLIVALKRFGLDKVIKKHPRGLdmslgenglglSGGQKQIVALARMTLRNPKIVLLDEPTTGLD 507
Cdd:TIGR01188 88 EMmGRLYGLPKDeaeERAEELLELFELGEAADRPVGTY-----------SGGMRRRLDIAASLIHQPDVLFLDEPTTGLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1437745540 508 Q------YSEIQALNAisawcRSKTLLVVTHR-PQVLSIVNRIIVVDNGKVVMDG 555
Cdd:TIGR01188 157 PrtrraiWDYIRALKE-----EGVTILLTTHYmEEADKLCDRIAIIDHGRIIAEG 206
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
336-563 |
2.83e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 81.67 E-value: 2.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSSS--------------------VVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSIT 395
Cdd:COG1134 5 IEVENVSKSYRLYHEPsrslkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 396 LDDvdirQIDPhylrnqvlLLEqeprlfLG-------SLRENLDL-ARMDGFSSDQ-----DLIVA---LKRFgldkvik 459
Cdd:COG1134 85 VNG----RVSA--------LLE------LGagfhpelTGRENIYLnGRLLGLSRKEidekfDEIVEfaeLGDF------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 460 khprgLDMSLGenglGLSGGQKQIVALARMTLRNPKIVLLDEPT-TGlDQYSEIQALNAISA-WCRSKTLLVVTH-RPQV 536
Cdd:COG1134 140 -----IDQPVK----TYSSGMRARLAFAVATAVDPDILLVDEVLaVG-DAAFQKKCLARIRElRESGRTVIFVSHsMGAV 209
|
250 260
....*....|....*....|....*..
gi 1437745540 537 LSIVNRIIVVDNGKVVMDGPRDAVLQQ 563
Cdd:COG1134 210 RRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
347-562 |
3.45e-17 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 81.80 E-value: 3.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 347 QDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAE--------QGSITLDDVDIRQIDPHYL-RNQVLLLE 417
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLaRLRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 418 QEPRLFLGSLRENLDL-----ARMDGFSSDQDLIVALKRFGLdkvikkhpRGLDMSLGENGLGLSGGQKQIVALARM--- 489
Cdd:PRK13547 91 AAQPAFAFSAREIVLLgryphARRAGALTHRDGEIAWQALAL--------AGATALVGRDVTTLSGGELARVQFARVlaq 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 490 ------TLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSKTL--LVVTHRPQVLS-IVNRIIVVDNGKVVMDGPRDAV 560
Cdd:PRK13547 163 lwpphdAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgvLAIVHDPNLAArHADRIAMLADGAIVAHGAPADV 242
|
..
gi 1437745540 561 LQ 562
Cdd:PRK13547 243 LT 244
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
310-555 |
3.66e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 83.35 E-value: 3.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 310 VNGIVERPSEResARKYIT-LKQIngnikfQNVSFAYnqDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYP 388
Cdd:PRK11607 1 MNDAIPRPQAK--TRKALTpLLEI------RNLTKSF--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 389 AEQGSITLDDVDIRQIDPhYLRNQVLLLEQ---------EPRLFLGSLRENLDLARMDGFSSDQDLIVALKRFGldkviK 459
Cdd:PRK11607 71 PTAGQIMLDGVDLSHVPP-YQRPINMMFQSyalfphmtvEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFA-----K 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 460 KHPRGLdmslgenglglSGGQKQIVALARMTLRNPKIVLLDEPTTGLD-------QYSEIQALNAISAWCrsktlLVVTH 532
Cdd:PRK11607 145 RKPHQL-----------SGGQRQRVALARSLAKRPKLLLLDEPMGALDkklrdrmQLEVVDILERVGVTC-----VMVTH 208
|
250 260
....*....|....*....|....
gi 1437745540 533 -RPQVLSIVNRIIVVDNGKVVMDG 555
Cdd:PRK11607 209 dQEEAMTMAGRIAIMNRGKFVQIG 232
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
339-565 |
3.69e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 81.08 E-value: 3.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 339 QNVSFAYNQDSSSVVKI-----LSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQID-PHYLRNQ 412
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIqalheVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQtAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 413 VLLLEQEPRLFLG-SLRENLdlaRMDGFSSDQDLIvaLKRfgLDKVIKKHPRGLDMSLGENGLgLSGGQKQIVALARMTL 491
Cdd:PRK11614 82 VAIVPEGRRVFSRmTVEENL---AMGGFFAERDQF--QER--IKWVYELFPRLHERRIQRAGT-MSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745540 492 RNPKIVLLDEPTTGLDQYSEIQALNAISAwCRSKTL---LVVTHRPQVLSIVNRIIVVDNGKVVMDGPRDAVLQQLA 565
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQ-LREQGMtifLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEA 229
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
333-558 |
3.77e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 82.16 E-value: 3.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 333 NGNIKFQNVSFAYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLY---PAEQGSITLDDVDIRQIDPHYL 409
Cdd:PRK13640 3 DNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 410 RNQVLLLEQEP-RLFLGSL--------RENLDLARMDGFSSDQDlivALKRFGLDKVIKKHPRgldmslgenglGLSGGQ 480
Cdd:PRK13640 83 REKVGIVFQNPdNQFVGATvgddvafgLENRAVPRPEMIKIVRD---VLADVGMLDYIDSEPA-----------NLSGGQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 481 KQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSKTLLVV--THRPQVLSIVNRIIVVDNGKVV-MDGPR 557
Cdd:PRK13640 149 KQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVIsiTHDIDEANMADQVLVLDDGKLLaQGSPV 228
|
.
gi 1437745540 558 D 558
Cdd:PRK13640 229 E 229
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
348-538 |
5.07e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 79.59 E-value: 5.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 348 DSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDdvdiRQIDPHYLRNQVLLleqePRLF---- 423
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRA----GGARVAYVPQRSEV----PDSLpltv 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 424 -----LGSLRENLDLARMDGfsSDQDLIV-ALKRFGLDKVIKKhprgldmSLGEnglgLSGGQKQIVALARMTLRNPKIV 497
Cdd:NF040873 75 rdlvaMGRWARRGLWRRLTR--DDRAAVDdALERVGLADLAGR-------QLGE----LSGGQRQRALLAQGLAQEADLL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1437745540 498 LLDEPTTGLDQYSEIQALNAISAWC-RSKTLLVVTHRPQVLS 538
Cdd:NF040873 142 LLDEPTTGLDAESRERIIALLAEEHaRGATVVVVTHDLELVR 183
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
336-539 |
7.35e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 80.85 E-value: 7.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYnqDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAE-----QGSITLDDVDI--RQIDPHY 408
Cdd:PRK14258 8 IKVNNLSFYY--DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIyeRRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 409 LRNQVLLLEQEPRLFLGSLRENLdlarmdgfSSDQDLIVALKRFGLDKVIKKHPRGLDM------SLGENGLGLSGGQKQ 482
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVYDNV--------AYGVKIVGWRPKLEIDDIVESALKDADLwdeikhKIHKSALDLSGGQQQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 483 IVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAI-SAWCRSK-TLLVVTHR-PQVLSI 539
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIqSLRLRSElTMVIVSHNlHQVSRL 217
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
339-555 |
1.14e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 81.05 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 339 QNVSFAYNQDSSSVVKIL---SFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDI-------RQIDPHY 408
Cdd:PRK13631 25 KNLYCVFDEKQENELVALnniSYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIgdkknnhELITNPY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 409 ---------LRNQVLLLEQEP--RLFLGSLRENLdlarMDGfssdqdlIVALKRFGLD--KVIKKH--PRGLDMS-LGEN 472
Cdd:PRK13631 105 skkiknfkeLRRRVSMVFQFPeyQLFKDTIEKDI----MFG-------PVALGVKKSEakKLAKFYlnKMGLDDSyLERS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 473 GLGLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAI-SAWCRSKTLLVVTHR-PQVLSIVNRIIVVDNGK 550
Cdd:PRK13631 174 PFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLIlDAKANNKTVFVITHTmEHVLEVADEVIVMDKGK 253
|
....*
gi 1437745540 551 VVMDG 555
Cdd:PRK13631 254 ILKTG 258
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
357-556 |
1.32e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 83.17 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 357 SFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAE---QGSITLDDvdiRQIDPHYLRnQVLLLEQEPRLFLGSLRENLDL 433
Cdd:TIGR00955 45 SGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNG---MPIDAKEMR-AISAYVQQDDLFIPTLTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 434 ARMDGFSSDQDLIVALKRFGLDKVIkkhprgLDMSL--------GENGL--GLSGGQKQIVALARMTLRNPKIVLLDEPT 503
Cdd:TIGR00955 121 MFQAHLRMPRRVTKKEKRERVDEVL------QALGLrkcantriGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745540 504 TGLDQYSE---IQALNAISAwcRSKTLLVVTHRP--QVLSIVNRIIVVDNGKVVMDGP 556
Cdd:TIGR00955 195 SGLDSFMAysvVQVLKGLAQ--KGKTIICTIHQPssELFELFDKIILMAEGRVAYLGS 250
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
336-564 |
1.49e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 80.55 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSSSVVKIL---SFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDI------RQIDP 406
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASRALfdiDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstskqKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 407 HYLRNQVLLLEQEPRLFLGSLRENLDLARMD-GFSSDQDLIVA---LKRFGLDKVI-KKHPrgldmslgengLGLSGGQK 481
Cdd:PRK13643 82 VRKKVGVVFQFPESQLFEETVLKDVAFGPQNfGIPKEKAEKIAaekLEMVGLADEFwEKSP-----------FELSGGQM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 482 QIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRS-KTLLVVTH-RPQVLSIVNRIIVVDNGKVVMDGPRDA 559
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHlMDDVADYADYVYLLEKGHIISCGTPSD 230
|
....*
gi 1437745540 560 VLQQL 564
Cdd:PRK13643 231 VFQEV 235
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
352-555 |
1.55e-16 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 79.30 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 352 VVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLLLEQEPRLFlgslrenL 431
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTQLW-------W 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 432 DLARMDGFSSDQDlIVALKRFGLDKVIKKHPRGLDMS--LGENGLGLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQY 509
Cdd:cd03267 109 DLPVIDSFYLLAA-IYDLPPARFKKRLDELSELLDLEelLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1437745540 510 SEIQALNAISAWCRSK--TLLVVTHRPQ-VLSIVNRIIVVDNGKVVMDG 555
Cdd:cd03267 188 AQENIRNFLKEYNRERgtTVLLTSHYMKdIEALARRVLVIDKGRLLYDG 236
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
336-532 |
1.59e-16 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 79.52 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSSSVVKI--LSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQidPHYLR--- 410
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQPALqdVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG--PGADRgvv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 411 --NQVLLleqePRLflgSLRENLDLA-RMDGFSSDQDLIVA---LKRFGLDKVIKKHPrgldmslgengLGLSGGQKQIV 484
Cdd:COG4525 82 fqKDALL----PWL---NVLDNVAFGlRLRGVPKAERRARAeelLALVGLADFARRRI-----------WQLSGGMRQRV 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1437745540 485 ALARMTLRNPKIVLLDEPTTGLDQYS--EIQALnAISAWCRS-KTLLVVTH 532
Cdd:COG4525 144 GIARALAADPRFLLMDEPFGALDALTreQMQEL-LLDVWQRTgKGVFLITH 193
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
336-573 |
1.94e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 82.16 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYnqDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGL--YPAEQGSI------------------- 394
Cdd:TIGR03269 1 IEVKNLTKKF--DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpskv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 395 -----------TLDDVDIRQIDPHY---LRNQVLLLEQEPRLFLGSLR--ENLDLARMD-GFSSDQDLIVALKRfgLDKV 457
Cdd:TIGR03269 79 gepcpvcggtlEPEEVDFWNLSDKLrrrIRKRIAIMLQRTFALYGDDTvlDNVLEALEEiGYEGKEAVGRAVDL--IEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 458 IKKHPRgldMSLGENglgLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSK--TLLVVTHRPQ 535
Cdd:TIGR03269 157 QLSHRI---THIARD---LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPE 230
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1437745540 536 VLS-IVNRIIVVDNGKVVMDGPRDAV----LQQLAKNETEKQI 573
Cdd:TIGR03269 231 VIEdLSDKAIWLENGEIKEEGTPDEVvavfMEGVSEVEKECEV 273
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
129-569 |
2.87e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 82.72 E-value: 2.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 129 SASLLTLVDMPFLILFVSVIALVGGYLAFVpltIIPLVIIvgLLAQipLSKYINESMKESSQRQGLAVEAIEGIETLKtn 208
Cdd:PLN03232 423 SAPFRIIVSMVLLYQQLGVASLFGSLILFL---LIPLQTL--IVRK--MRKLTKEGLQWTDKRVGIINEILASMDTVK-- 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 209 nAMNWaQKRWDYYTAKTASSSMKVKNISNFVIYFAVMMqqLNTIFLVI----IGTYLIHSDD--PASKITMGALIATVil 282
Cdd:PLN03232 494 -CYAW-EKSFESRIQGIRNEELSWFRKAQLLSAFNSFI--LNSIPVVVtlvsFGVFVLLGGDltPARAFTSLSLFAVL-- 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 283 sgraLSPLGQIAGLAVRFQQAWVALKGVNGIVErpSERESARKYITLKQINGNIKFQNVSFAYNQDSSS-VVKILSFEIK 361
Cdd:PLN03232 568 ----RSPLNMLPNLLSQVVNANVSLQRIEELLL--SEERILAQNPPLQPGAPAISIKNGYFSWDSKTSKpTLSDINLEIP 641
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 362 PGEKVGILGRIGSGKSTTLKLAAG-LYPAEQGSITLddvdirqidphylRNQVLLLEQEPRLFLGSLRENLDlarmdgFS 440
Cdd:PLN03232 642 VGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVI-------------RGSVAYVPQVSWIFNATVRENIL------FG 702
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 441 SDQDLivalKRFG--LDKVIKKHP----RGLDMS-LGENGLGLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQ 513
Cdd:PLN03232 703 SDFES----ERYWraIDVTALQHDldllPGRDLTeIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQ 778
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745540 514 ALNA-ISAWCRSKTLLVVTHRPQVLSIVNRIIVVDNGKVVMDGprdaVLQQLAKNET 569
Cdd:PLN03232 779 VFDScMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEG----TFAELSKSGS 831
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
336-558 |
3.30e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 79.44 E-value: 3.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSS---SVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDI--RQIDPH--Y 408
Cdd:PRK13646 3 IRFDNVSYTYQKGTPyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthKTKDKYirP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 409 LRNQVLLLEQ--EPRLFLGSLrenldlarmdgfssDQDLIVALKRFGLD-KVIKKHPRGLDMSLG-------ENGLGLSG 478
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTV--------------EREIIFGPKNFKMNlDEVKNYAHRLLMDLGfsrdvmsQSPFQMSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 479 GQKQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWC--RSKTLLVVTHR-PQVLSIVNRIIVVDNGKVVMDG 555
Cdd:PRK13646 149 GQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDmNEVARYADEVIVMKEGSIVSQT 228
|
....
gi 1437745540 556 -PRD 558
Cdd:PRK13646 229 sPKE 232
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
353-563 |
4.91e-16 |
|
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: 81.02 E-value: 4.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 353 VKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAE-QGSITLD--DVDIRQIDPHYLRNQVLLLEQEPR-------- 421
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINgkPVDIRNPAQAIRAGIAMVPEDRKRhgivpilg 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 422 ----LFLGSLRENLDLARMDGFSSDQDLIVALKRFgldKVIKKHPrglDMSLGenglGLSGGQKQIVALARMTLRNPKIV 497
Cdd:TIGR02633 356 vgknITLSVLKSFCFKMRIDAAAELQIIGSAIQRL---KVKTASP---FLPIG----RLSGGNQQKAVLAKMLLTNPRVL 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 498 LLDEPTTGLD---QYSEIQALNAISAwcRSKTLLVVTHR-PQVLSIVNRIIVVDNGKVVMDGPRDAVLQQ 563
Cdd:TIGR02633 426 ILDEPTRGVDvgaKYEIYKLINQLAQ--EGVAIIVVSSElAEVLGLSDRVLVIGEGKLKGDFVNHALTQE 493
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
353-576 |
9.13e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 77.43 E-value: 9.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 353 VKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPA----EQGSITLDDVdirQIDPHYLRNQ-VLLLEQEPRLFLGSL 427
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGK---PVAPCALRGRkIATIMQNPRSAFNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 428 RENLDLAR-----MDGFSSDQDLIVALKRFGLD---KVIKKHPrgldmslgengLGLSGG--QKQIVALARMTlRNPKIV 497
Cdd:PRK10418 96 HTMHTHARetclaLGKPADDATLTAALEAVGLEnaaRVLKLYP-----------FEMSGGmlQRMMIALALLC-EAPFII 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 498 LlDEPTTGLDQYSEIQALNAISAWCRSKTL--LVVTHRPQVLS-IVNRIIVVDNGKVVMDGPRDAVLQQLAKNETEKQIT 574
Cdd:PRK10418 164 A-DEPTTDLDVVAQARILDLLESIVQKRALgmLLVTHDMGVVArLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVS 242
|
..
gi 1437745540 575 AH 576
Cdd:PRK10418 243 AH 244
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
338-556 |
1.30e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 77.03 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 338 FQNVSFAYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQID---PHYLRNQVL 414
Cdd:PRK10419 13 YAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 415 LLEQE------PRLFLGS-----LRENLDLARMDGFSSDQDLivaLKRFGLD-KVIKKHPRGLdmslgenglglSGGQKQ 482
Cdd:PRK10419 93 MVFQDsisavnPRKTVREiirepLRHLLSLDKAERLARASEM---LRAVDLDdSVLDKRPPQL-----------SGGQLQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 483 IVALARMTLRNPKIVLLDEPTTGLD---QYSEIQALNAISAwcRSKT-LLVVTHRpqvLSIV----NRIIVVDNGKVVMD 554
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDlvlQAGVIRLLKKLQQ--QFGTaCLFITHD---LRLVerfcQRVMVMDNGQIVET 233
|
..
gi 1437745540 555 GP 556
Cdd:PRK10419 234 QP 235
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
335-555 |
1.52e-15 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 76.59 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 335 NIKFQNVSFAYNqdSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITL--------DDVDIRQIdp 406
Cdd:COG4161 2 SIQLKNINCFYG--SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIaghqfdfsQKPSEKAI-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 407 HYLRNQVLLLEQE----PRLflgSLRENLDLA--RMDGFSSDQDLIVA---LKRFGLDKVIKKHPrgldmslgengLGLS 477
Cdd:COG4161 78 RLLRQKVGMVFQQynlwPHL---TVMENLIEApcKVLGLSKEQAREKAmklLARLRLTDKADRFP-----------LHLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 478 GGQKQIVALARMTLRNPKIVLLDEPTTGLDqySEI--QALNAISAWCRSK-TLLVVTHRPQVL-SIVNRIIVVDNGKVVM 553
Cdd:COG4161 144 GGQQQRVAIARALMMEPQVLLFDEPTAALD--PEItaQVVEIIRELSQTGiTQVIVTHEVEFArKVASQVVYMEKGRIIE 221
|
..
gi 1437745540 554 DG 555
Cdd:COG4161 222 QG 223
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
330-549 |
2.46e-15 |
|
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: 76.43 E-value: 2.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 330 KQINGNIKFQN----VSFA-YNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITlddvdirqi 404
Cdd:cd03291 25 KQENNDRKHSSddnnLFFSnLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK--------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 405 dpHYLRnqVLLLEQEPRLFLGSLRENLdlarMDGFSSDQ-DLIVALKRFGLDKVIKKHPRGLDMSLGENGLGLSGGQKQI 483
Cdd:cd03291 96 --HSGR--ISFSSQFSWIMPGTIKENI----IFGVSYDEyRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRAR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745540 484 VALARMTLRNPKIVLLDEPTTGLDQYSEIQALNaiSAWCR---SKTLLVVTHRPQVLSIVNRIIVVDNG 549
Cdd:cd03291 168 ISLARAVYKDADLYLLDSPFGYLDVFTEKEIFE--SCVCKlmaNKTRILVTSKMEHLKKADKILILHEG 234
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
19-278 |
2.66e-15 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 76.73 E-value: 2.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 19 QIILATFVINFLALVSSLYVMNVYDRVIPNKSYQTLWVLSIGVIIAILFEFTAKMLRGRLTDIAGKKADLIISSALFRKV 98
Cdd:cd18567 6 QILLLSLALELFALASPLYLQLVIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 99 TNLklqekPIS------SGSYVNNLRDFESVRDFMTSASLLTLVDMPFLILFVSVIALVGGYLAFVPLTIIPLVIIVGLL 172
Cdd:cd18567 86 LRL-----PLSyfekrhLGDIVSRFGSLDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALIVLAAVALYALLRLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 173 AQIPLSKYINESMKESSQRQGLAVEAIEGIETLKTNNAMNWAQKRWDYYTAKTASSSMKVKNISnfvIYFAVMMQ---QL 249
Cdd:cd18567 161 LYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQ---ILFSAANGllfGL 237
|
250 260
....*....|....*....|....*....
gi 1437745540 250 NTIFLVIIGTYLIHSddpaSKITMGALIA 278
Cdd:cd18567 238 ENILVIYLGALLVLD----GEFTVGMLFA 262
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
356-532 |
3.31e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 75.89 E-value: 3.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 356 LSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRqiDPHYLRNQVLllEQEPRLFLGSLRENLDLA- 434
Cdd:PRK11248 20 INLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE--GPGAERGVVF--QNEGLLPWRNVQDNVAFGl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 435 RMDGFSSDQDLIVA---LKRFGLDKVIKKHPrgldmslgengLGLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYS- 510
Cdd:PRK11248 96 QLAGVEKMQRLEIAhqmLKKVGLEGAEKRYI-----------WQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTr 164
|
170 180
....*....|....*....|....
gi 1437745540 511 -EIQALnAISAWCRS-KTLLVVTH 532
Cdd:PRK11248 165 eQMQTL-LLKLWQETgKQVLLITH 187
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
347-532 |
3.37e-15 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 74.00 E-value: 3.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 347 QDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLD--DVDIRQIDPHYLRNQVLLLEQEP--RL 422
Cdd:TIGR01166 2 PGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDgePLDYSRKGLLERRQRVGLVFQDPddQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 423 FLGSLRENLDLARMD-GFSSDQdlIVALKRFGLDKVIKKHPRGLDMSLgenglgLSGGQKQIVALARMTLRNPKIVLLDE 501
Cdd:TIGR01166 82 FAADVDQDVAFGPLNlGLSEAE--VERRVREALTAVGASGLRERPTHC------LSGGEKKRVAIAGAVAMRPDVLLLDE 153
|
170 180 190
....*....|....*....|....*....|....
gi 1437745540 502 PTTGLD---QYSEIQALNAISAwcRSKTLLVVTH 532
Cdd:TIGR01166 154 PTAGLDpagREQMLAILRRLRA--EGMTVVISTH 185
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
20-284 |
3.90e-15 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 75.76 E-value: 3.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 20 IILATFVINFLALVSSLYVMNVYDRVIPNKS--YQTLWVLSIGVIIAILFEFTAKMLRGRLTDIAGKKADLIISSALFRK 97
Cdd:pfam00664 4 AILLAILSGAISPAFPLVLGRILDVLLPDGDpeTQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 98 VTNLklqekPIS------SGSYVNNL-RDFESVRDFMTSASLLTLVDMPFLILFVSVIALVGGYLAFVPLTIIPLVIIVG 170
Cdd:pfam00664 84 ILRQ-----PMSffdtnsVGELLSRLtNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 171 LLAQIPLSKYINESMKESSQRQGLAVEAIEGIETLKTNNAMNWAQKRWDYYTAKTASSSMKVKNISNFVIYFAVMMQQLN 250
Cdd:pfam00664 159 AVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLS 238
|
250 260 270
....*....|....*....|....*....|....
gi 1437745540 251 TIFLVIIGTYLIHSDDpaskITMGALIATVILSG 284
Cdd:pfam00664 239 YALALWFGAYLVISGE----LSVGDLVAFLSLFA 268
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
336-556 |
4.48e-15 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 76.76 E-value: 4.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSSSV--VKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYL---R 410
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 411 NQVLLLEQEprlF-LGSLR---ENLDLA-RMDGFSSDQdlIVA-----LKRFGLDKVIKKHPRGLdmslgenglglSGGQ 480
Cdd:PRK11153 82 RQIGMIFQH---FnLLSSRtvfDNVALPlELAGTPKAE--IKArvtelLELVGLSDKADRYPAQL-----------SGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 481 KQIVALARMTLRNPKIVLLDEPTTGLDQ---------YSEIQALNAIsawcrskTLLVVTHRPQVL-SIVNRIIVVDNGK 550
Cdd:PRK11153 146 KQRVAIARALASNPKVLLCDEATSALDPattrsilelLKDINRELGL-------TIVLITHEMDVVkRICDRVAVIDAGR 218
|
....*.
gi 1437745540 551 VVMDGP 556
Cdd:PRK11153 219 LVEQGT 224
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
356-561 |
5.15e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 74.97 E-value: 5.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 356 LSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEqGSITLDDVDIRQIDPHYL-RNQVLLLEQEPRLFLGSLRENLDLA 434
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS-GSIQFAGQPLEAWSAAELaRHRAYLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 435 RMDGFSSDQDLIValkrfgLDKVIKKhpRGLDMSLGENGLGLSGGQKQIVALARMTLR-----NP--KIVLLDEPTTGLD 507
Cdd:PRK03695 94 QPDKTRTEAVASA------LNEVAEA--LGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPMNSLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745540 508 --QYSEIQALnaISAWCRS-KTLLVVTHR-PQVLSIVNRIIVVDNGKVVMDGPRDAVL 561
Cdd:PRK03695 166 vaQQAALDRL--LSELCQQgIAVVMSSHDlNHTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
353-565 |
6.29e-15 |
|
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: 74.99 E-value: 6.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 353 VKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRN----QVLLLEQEPRLFLG-SL 427
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLPHrTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 428 REN----LDLARMDGFSSDQDLIVALKRFGLDKVIKKHPRGLdmslgenglglSGGQKQIVALARMTLRNPKIVLLDEPT 503
Cdd:cd03294 120 LENvafgLEVQGVPRAEREERAAEALELVGLEGWEHKYPDEL-----------SGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 504 TGLD-------QySEIQALNAIsawcRSKTLLVVTHRP-QVLSIVNRIIVVDNGKVVMDGPRDAVLQQLA 565
Cdd:cd03294 189 SALDplirremQ-DELLRLQAE----LQKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEILTNPA 253
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
271-534 |
6.54e-15 |
|
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: 77.87 E-value: 6.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 271 ITMGALIATVILSGRALSplgQIAGLAVRFQQAWVALKGVNG------IVERPSERESARKYITLKQINGN-------IK 337
Cdd:TIGR00954 377 LKAADALGRLMLAGRDMT---RLAGFTARVDTLLQVLDDVKSgnfkrpRVEEIESGREGGRNSNLVPGRGIveyqdngIK 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 338 FQNVSFAyNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDvdirqidphylRNQVLLLE 417
Cdd:TIGR00954 454 FENIPLV-TPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-----------KGKLFYVP 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 418 QEPRLFLGSLRENL------DLARMDGFSsDQDLIVALKRFGLDKVIKkhpRGLDMSLGENGLG-LSGGQKQIVALARMT 490
Cdd:TIGR00954 522 QRPYMTLGTLRDQIiypdssEDMKRRGLS-DKDLEQILDNVQLTHILE---REGGWSAVQDWMDvLSGGEKQRIAMARLF 597
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1437745540 491 LRNPKIVLLDEPTTGLdqysEIQALNAISAWCRSK--TLLVVTHRP 534
Cdd:TIGR00954 598 YHKPQFAILDECTSAV----SVDVEGYMYRLCREFgiTLFSVSHRK 639
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
336-552 |
8.00e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 73.76 E-value: 8.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYnQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPH---YLRNQ 412
Cdd:PRK10908 2 IRFEHVSKAY-LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 413 VLLLEQEPRLFLG-SLRENLDLARMDGFSSDQDL----IVALKRFGLDKVIKKHPrgldmslgengLGLSGGQKQIVALA 487
Cdd:PRK10908 81 IGMIFQDHHLLMDrTVYDNVAIPLIIAGASGDDIrrrvSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745540 488 RMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCR-SKTLLVVTHRPQVLSIVN-RIIVVDNGKVV 552
Cdd:PRK10908 150 RAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATHDIGLISRRSyRMLTLSDGHLH 216
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
349-563 |
9.37e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 75.91 E-value: 9.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 349 SSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLD--DVDIRQIDphylRNQVLLLEQEPRLFLG- 425
Cdd:PRK11432 18 SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDgeDVTHRSIQ----QRDICMVFQSYALFPHm 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 426 SLRENLDLA-RMDGFSSD---QDLIVALKRFGLDKVikkHPRGLDMslgenglgLSGGQKQIVALARMTLRNPKIVLLDE 501
Cdd:PRK11432 94 SLGENVGYGlKMLGVPKEerkQRVKEALELVDLAGF---EDRYVDQ--------ISGGQQQRVALARALILKPKVLLFDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1437745540 502 PTTGLD---------QYSEIQALNAIsawcrskTLLVVTH-RPQVLSIVNRIIVVDNGKVVMDGPRDAVLQQ 563
Cdd:PRK11432 163 PLSNLDanlrrsmreKIRELQQQFNI-------TSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
332-555 |
9.40e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 74.74 E-value: 9.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 332 INGNIKFQNVSFAYNQDSS-SVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLR 410
Cdd:PRK13642 1 MNKILEVENLVFKYEKESDvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 411 NQVLLLEQEP-RLFLGSLRENldlarmdgfssdqDLIVALKRFGL--DKVIKKHPRGLdmsLGENGLG--------LSGG 479
Cdd:PRK13642 81 RKIGMVFQNPdNQFVGATVED-------------DVAFGMENQGIprEEMIKRVDEAL---LAVNMLDfktreparLSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745540 480 QKQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAwCRSK---TLLVVTHRPQVLSIVNRIIVVDNGKVVMDG 555
Cdd:PRK13642 145 QKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHE-IKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEA 222
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
340-563 |
1.01e-14 |
|
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: 77.03 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 340 NVSFAYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTT----LKLAAGLYPAEQGSITLDDVDIRQIDPHYLR----N 411
Cdd:COG4172 13 SVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSERELRrirgN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 412 QVLLLEQEPrlfLGSL----------RENLDLARmdGFSSDQ--DLIVALkrfgLDKVIKKHPrgldmslgENGLG---- 475
Cdd:COG4172 93 RIAMIFQEP---MTSLnplhtigkqiAEVLRLHR--GLSGAAarARALEL----LERVGIPDP--------ERRLDayph 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 476 -LSGGQKQIVALArMTLRN-PKIVLLDEPTTGLD---Q------YSEIQALNAISawcrsktLLVVTHRpqvLSIV---- 540
Cdd:COG4172 156 qLSGGQRQRVMIA-MALANePDLLIADEPTTALDvtvQaqildlLKDLQRELGMA-------LLLITHD---LGVVrrfa 224
|
250 260
....*....|....*....|...
gi 1437745540 541 NRIIVVDNGKVVMDGPRDAVLQQ 563
Cdd:COG4172 225 DRVAVMRQGEIVEQGPTAELFAA 247
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
349-574 |
1.11e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 74.18 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 349 SSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKL---AAGLYPAEQ--GSITLDDVDIRQIDPHYLRNQVLLLEQEPRLF 423
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYPEARvsGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 424 LG-SLRENLDLA-RMDGFSSDQDLIVALKRFGLDKV-----IKKHprgLDMSLGEnglgLSGGQKQIVALARMTLRNPKI 496
Cdd:PRK14247 95 PNlSIFENVALGlKLNRLVKSKKELQERVRWALEKAqlwdeVKDR---LDAPAGK----LSGGQQQRLCIARALAFQPEV 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745540 497 VLLDEPTTGLDQYSEIQALNAISAWCRSKTLLVVTHRP-QVLSIVNRIIVVDNGKVVMDGPRDAVLQQLAKNETEKQIT 574
Cdd:PRK14247 168 LLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPqQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTEKYVT 246
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
352-555 |
1.47e-14 |
|
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: 72.95 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 352 VVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDdvdiRQIDPhylrnqvlLLEQ----EPRLflgSL 427
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVR----GRVSS--------LLGLgggfNPEL---TG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 428 RENLDL-ARMDGFSsdQDLIVALKRF-----GLDKVIKKHPRgldmslgenglGLSGGQKQIVALARMTLRNPKIVLLDE 501
Cdd:cd03220 102 RENIYLnGRLLGLS--RKEIDEKIDEiiefsELGDFIDLPVK-----------TYSSGMKARLAFAIATALEPDILLIDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745540 502 PTTGLDQYSEIQALNAISAWC-RSKTLLVVTHRP-QVLSIVNRIIVVDNGKVVMDG 555
Cdd:cd03220 169 VLAVGDAAFQEKCQRRLRELLkQGKTVILVSHDPsSIKRLCDRALVLEKGKIRFDG 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
357-566 |
1.57e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 76.22 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 357 SFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDD--VDIRqiDPHY-LRNQVLLLEQEPRLFlGSL--RENL 431
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIR--SPRDaIALGIGMVHQHFMLV-PNLtvAENI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 432 DLARMDGFSSDQDL------IVAL-KRFGL----DKVIKkhprglDMSLGEnglglsggqKQIVALARMTLRNPKIVLLD 500
Cdd:COG3845 102 VLGLEPTKGGRLDRkaararIRELsERYGLdvdpDAKVE------DLSVGE---------QQRVEILKALYRGARILILD 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437745540 501 EPTTGL-DQysEIQALNAIsawCRS-----KTLLVVTHR-PQVLSIVNRIIVVDNGKVV--MDgPRDAVLQQLAK 566
Cdd:COG3845 167 EPTAVLtPQ--EADELFEI---LRRlaaegKSIIFITHKlREVMAIADRVTVLRRGKVVgtVD-TAETSEEELAE 235
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
336-559 |
1.90e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 73.12 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNqdSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITL-----------DDVDIRQi 404
Cdd:PRK11124 3 IQLNGINCFYG--AHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfdfsktpSDKAIRE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 405 dphyLRNQVLLLEQE----PRLflgSLRENLDLA--RMDGFSSDQDLIVA---LKRFGLDKVIKKHPrgldmslgengLG 475
Cdd:PRK11124 80 ----LRRNVGMVFQQynlwPHL---TVQQNLIEApcRVLGLSKDQALARAeklLERLRLKPYADRFP-----------LH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 476 LSGGQKQIVALARMTLRNPKIVLLDEPTTGLDqySEI--QALNAISAWCRSK-TLLVVTHRPQVL-SIVNRIIVVDNGKV 551
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALD--PEItaQIVSIIRELAETGiTQVIVTHEVEVArKTASRVVYMENGHI 219
|
....*...
gi 1437745540 552 VMDGPRDA 559
Cdd:PRK11124 220 VEQGDASC 227
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
341-561 |
2.81e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 74.88 E-value: 2.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 341 VSFAynqdSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLLLEQEP 420
Cdd:PRK09536 11 VEFG----DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 421 RL-FLGSLRENLD------LARMDGFSSDQDLIV--ALKRFGLDKVIkkhprglDMSLGEnglgLSGGQKQIVALARMTL 491
Cdd:PRK09536 87 SLsFEFDVRQVVEmgrtphRSRFDTWTETDRAAVerAMERTGVAQFA-------DRPVTS----LSGGERQRVLLARALA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437745540 492 RNPKIVLLDEPTTGLDQYSEIQALNAISAWCRS-KTLLVVTHRpqvLSIVNR----IIVVDNGKVVMDGPRDAVL 561
Cdd:PRK09536 156 QATPVLLLDEPTASLDINHQVRTLELVRRLVDDgKTAVAAIHD---LDLAARycdeLVLLADGRVRAAGPPADVL 227
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
352-549 |
3.10e-14 |
|
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: 72.08 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 352 VVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDD----VDIRQIDPHylrnQVLLLEQE-------- 419
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHdggwVDLAQASPR----EILALRRRtigyvsqf 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 420 ----PRLflgslrENLDL----ARMDGFSSDQDLIVA---LKRFGLdkvikkhPRGLdmslgengLGL-----SGGQKQI 483
Cdd:COG4778 102 lrviPRV------SALDVvaepLLERGVDREEARARArelLARLNL-------PERL--------WDLppatfSGGEQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1437745540 484 VALARMTLRNPKIVLLDEPTTGLDQYSE------IQALNAisawcRSKTLLVVTHRPQVLSIV-NRIIVVDNG 549
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRavvvelIEEAKA-----RGTAIIGIFHDEEVREAVaDRVVDVTPF 228
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
342-556 |
3.71e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 75.53 E-value: 3.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 342 SFAYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTL-------KLAAGLYP-AEQGSITLDDVDIRQ--------ID 405
Cdd:PRK10535 13 SYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMnilgcldKPTSGTYRvAGQDVATLDADALAQlrrehfgfIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 406 PHYLRNQVLLLEQE---PRLFLGSLR-ENLDLARMdgfssdqdlivALKRFGLDKVIKKHPRGLdmslgenglglSGGQK 481
Cdd:PRK10535 93 QRYHLLSHLTAAQNvevPAVYAGLERkQRLLRAQE-----------LLQRLGLEDRVEYQPSQL-----------SGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745540 482 QIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWC-RSKTLLVVTHRPQVLSIVNRIIVVDNGKVVMDGP 556
Cdd:PRK10535 151 QRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPP 226
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
353-549 |
3.97e-14 |
|
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: 72.11 E-value: 3.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 353 VKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYL---RNQVLLleqePRLflgSLRE 429
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMvvfQNYSLL----PWL---TVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 430 NLDLA----RMDGFSSDQDLIVA--LKRFGLDKVIKKHPrgldmslGEnglgLSGGQKQIVALARMTLRNPKIVLLDEPT 503
Cdd:TIGR01184 74 NIALAvdrvLPDLSKSERRAIVEehIALVGLTEAADKRP-------GQ----LSGGMKQRVAIARALSIRPKVLLLDEPF 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1437745540 504 TGLDQY--SEIQAlNAISAWCRSK-TLLVVTHR-PQVLSIVNRIIVVDNG 549
Cdd:TIGR01184 143 GALDALtrGNLQE-ELMQIWEEHRvTVLMVTHDvDEALLLSDRVVMLTNG 191
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
360-566 |
6.95e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 75.15 E-value: 6.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 360 IKPGEKVGILGRIGSGKSTTLKLAA----GLYPAEQGSITLDDVDIRQIDPHYLRNQVLLLEQEPRLFLGSLRENLDLA- 434
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFPHLTVGETLDFAa 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 435 -------RMDGFSSDQ------DLIVALkrFGLDkvikkHPRglDMSLGENGL-GLSGGQKQIVALARMTLRNPKIVLLD 500
Cdd:TIGR00956 164 rcktpqnRPDGVSREEyakhiaDVYMAT--YGLS-----HTR--NTKVGNDFVrGVSGGERKRVSIAEASLGGAKIQCWD 234
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 501 EPTTGLDQYSEIQALNAI--SAWCRSKTLLVVTHR--PQVLSIVNRIIVVDNGKVVMDGPRDAVLQQLAK 566
Cdd:TIGR00956 235 NATRGLDSATALEFIRALktSANILDTTPLVAIYQcsQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEK 304
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
349-563 |
7.22e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 71.39 E-value: 7.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 349 SSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHY---LRNQVL-LLEQEPRLF- 423
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQKLgFIYQFHHLLp 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 424 ----LGSLRENLDLARMDGFSSDQDLIVALKRFGLDKVIKKHPRGLdmslgenglglSGGQKQIVALARMTLRNPKIVLL 499
Cdd:PRK11629 101 dftaLENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSEL-----------SGGERQRVAIARALVNNPRLVLA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745540 500 DEPTTGLDQY---SEIQALNAISAwcRSKT-LLVVTHRPQVLSIVNRiivvdngKVVMdgpRDAVLQQ 563
Cdd:PRK11629 170 DEPTGNLDARnadSIFQLLGELNR--LQGTaFLVVTHDLQLAKRMSR-------QLEM---RDGRLTA 225
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
335-551 |
7.39e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 73.14 E-value: 7.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 335 NIKFQNVSFAYnqDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHylRNQVL 414
Cdd:PRK11000 3 SVTLRNVTKAY--GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 415 LLEQE----PRLflgSLREN----LDLARMDGFSSDQDLIVALKRFGLDKVIKKHPRgldmslgenglGLSGGQKQIVAL 486
Cdd:PRK11000 79 MVFQSyalyPHL---SVAENmsfgLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPK-----------ALSGGQRQRVAI 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745540 487 ARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCR--SKTLLVVTHrPQV--LSIVNRIIVVDNGKV 551
Cdd:PRK11000 145 GRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTH-DQVeaMTLADKIVVLDAGRV 212
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
360-551 |
7.99e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 70.96 E-value: 7.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 360 IKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPH---YLRNQ-VLLLEQEPRLF--LGSLrENLDL 433
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRAKhVGFVFQSFMLIptLNAL-ENVEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 434 -ARMDGFS---SDQDLIVALKRFGLDKVIKKHPRGLdmslgenglglSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQY 509
Cdd:PRK10584 112 pALLRGESsrqSRNGAKALLEQLGLGKRLDHLPAQL-----------SGGEQQRVALARAFNGRPDVLFADEPTGNLDRQ 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1437745540 510 SEIQALNAISAWCR--SKTLLVVTHRPQVLSIVNRIIVVDNGKV 551
Cdd:PRK10584 181 TGDKIADLLFSLNRehGTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
335-551 |
8.65e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 72.81 E-value: 8.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 335 NIKFQNVSFAYNQdsSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIdpHYLRNQVL 414
Cdd:PRK10851 2 SIEIANIKKSFGR--TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL--HARDRKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 415 LLEQEPRLFLG-SLRENLDLA--------RMDGFSSDQDLIVALKRFGLDKVIKKHPRGLdmslgenglglSGGQKQIVA 485
Cdd:PRK10851 78 FVFQHYALFRHmTVFDNIAFGltvlprreRPNAAAIKAKVTQLLEMVQLAHLADRYPAQL-----------SGGQKQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1437745540 486 LARMTLRNPKIVLLDEPTTGLDQyseiQALNAISAWCRSK------TLLVVTH-RPQVLSIVNRIIVVDNGKV 551
Cdd:PRK10851 147 LARALAVEPQILLLDEPFGALDA----QVRKELRRWLRQLheelkfTSVFVTHdQEEAMEVADRVVVMSQGNI 215
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
348-555 |
9.92e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 71.21 E-value: 9.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 348 DSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGlYPAEQ---GSITLDDVDIRQIDPHyLRNQ--VLLLEQEP-- 420
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG-HPAYKileGDILFKGESILDLEPE-ERAHlgIFLAFQYPie 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 421 ----------RLFLGSLRENLDLARMDGFSSDQDLIVALKRFGLDkvikkhPRGLDMSLGEnglGLSGGQKQIVALARMT 490
Cdd:CHL00131 96 ipgvsnadflRLAYNSKRKFQGLPELDPLEFLEIINEKLKLVGMD------PSFLSRNVNE---GFSGGEKKRNEILQMA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1437745540 491 LRNPKIVLLDEPTTGLDqyseIQALNAISAWC-----RSKTLLVVTHRPQVLSIV--NRIIVVDNGKVVMDG 555
Cdd:CHL00131 167 LLDSELAILDETDSGLD----IDALKIIAEGInklmtSENSIILITHYQRLLDYIkpDYVHVMQNGKIIKTG 234
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
353-576 |
1.01e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 71.36 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 353 VKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLLLEQEPRLFLG------- 425
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPSTSLNprqrisq 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 426 ----SLRENLDLarmDGFSSDQDLIVALKRFGL--DKViKKHPRgldmslgenglGLSGGQKQIVALARMTLRNPKIVLL 499
Cdd:PRK15112 109 ildfPLRLNTDL---EPEQREKQIIETLRQVGLlpDHA-SYYPH-----------MLAPGQKQRLGLARALILRPKVIIA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 500 DEPTTGLDQYS---------EIQALNAISawcrskTLLVVTHRPQVLSIVNRIIVVDNGKVVMDGPRDAVLQQLAKNETE 570
Cdd:PRK15112 174 DEALASLDMSMrsqlinlmlELQEKQGIS------YIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTK 247
|
....*.
gi 1437745540 571 KQITAH 576
Cdd:PRK15112 248 RLIAGH 253
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
353-555 |
1.11e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 73.67 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 353 VKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHY-LRNQVLLLEQEPRLFLG-SLREN 430
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLaAQLGIGIIYQELSVIDElTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 431 LDLARMdgfssdqdliVALKRFGLDKVIKKHPR----------GLDMSLGENGLGLSGGQKQIVALARMTLRNPKIVLLD 500
Cdd:PRK09700 101 LYIGRH----------LTKKVCGVNIIDWREMRvraammllrvGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745540 501 EPTTGLDQySEIQALNAISAWCRS--KTLLVVTHR-PQVLSIVNRIIVVDNGKVVMDG 555
Cdd:PRK09700 171 EPTSSLTN-KEVDYLFLIMNQLRKegTAIVYISHKlAEIRRICDRYTVMKDGSSVCSG 227
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
352-578 |
1.24e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.55 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 352 VVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDP---HYLrnQVLLLEQEPRLFLG-SL 427
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPakaHQL--GIYLVPQEPLLFPNlSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 428 RENLDL---ARMDGFSSDQDLIVALKrFGLDkvikkhprgLDMSLGEnglgLSGGQKQIVALARMTLRNPKIVLLDEPTT 504
Cdd:PRK15439 104 KENILFglpKRQASMQKMKQLLAALG-CQLD---------LDSSAGS----LEVADRQIVEILRGLMRDSRILILDEPTA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 505 GLDQ------YSEIQALNAisawcRSKTLLVVTHR-PQVLSIVNRIIVVDNGKVVMDGP-----RDAVLQQLAKNETEKQ 572
Cdd:PRK15439 170 SLTPaeterlFSRIRELLA-----QGVGIVFISHKlPEIRQLADRISVMRDGTIALSGKtadlsTDDIIQAITPAAREKS 244
|
....*.
gi 1437745540 573 ITAHSK 578
Cdd:PRK15439 245 LSASQK 250
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
348-573 |
1.72e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 70.85 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 348 DSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDV------DIRQIDPHYLRNQVLLLEQEPR 421
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 422 LFLG-SLRENLDLA-RMDGFSSDQDL--IV--ALKRFGLDKVIkkHPRgldmsLGENGLGLSGGQKQIVALARMTLRNPK 495
Cdd:PRK14246 101 PFPHlSIYDNIAYPlKSHGIKEKREIkkIVeeCLRKVGLWKEV--YDR-----LNSPASQLSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745540 496 IVLLDEPTTGLDQYSEIQALNAISAWCRSKTLLVVTHRP-QVLSIVNRIIVVDNGKVVMDGPRDAVLQQLAKNETEKQI 573
Cdd:PRK14246 174 VLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPqQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
336-555 |
2.13e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 71.03 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYnQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDD--VDIRQIDPHYLRNQV 413
Cdd:PRK13636 6 LKVEELNYNY-SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 414 LLLEQEP--RLFLGSLRENLDLARMD-GFSSDQ---DLIVALKRFGLDKVIKKHPRGLdmslgenglglSGGQKQIVALA 487
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYQDVSFGAVNlKLPEDEvrkRVDNALKRTGIEHLKDKPTHCL-----------SFGQKKRVAIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1437745540 488 RMTLRNPKIVLLDEPTTGLDQY--SEIQALNAISAWCRSKTLLVVTHRPQVLSI-VNRIIVVDNGKVVMDG 555
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDPMgvSEIMKLLVEMQKELGLTIIIATHDIDIVPLyCDNVFVMKEGRVILQG 224
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
352-563 |
2.49e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 70.38 E-value: 2.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 352 VVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQI----------DPH---YLRNQVLLLEQ 418
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvaDKNqlrLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 419 EPRLF-LGSLRENLDLARMD--GFSSDQDLIVALKRfgLDKVikkhprGLD-MSLGENGLGLSGGQKQIVALARMTLRNP 494
Cdd:PRK10619 100 HFNLWsHMTVLENVMEAPIQvlGLSKQEARERAVKY--LAKV------GIDeRAQGKYPVHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1437745540 495 KIVLLDEPTTGLDQYSEIQALNAISAWCRS-KTLLVVTHRPQVLSIV-NRIIVVDNGKVVMDGPRDAVLQQ 563
Cdd:PRK10619 172 EVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
357-561 |
2.72e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 69.95 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 357 SFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRnqvlllEQEPRLFL----GSLREN-L 431
Cdd:PRK11701 26 SFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALS------EAERRRLLrtewGFVHQHpR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 432 DLARMD----GFSSDQDLIVALKRFG---------LDKV------IKKHPRgldmslgenglGLSGGQKQIVALARMTLR 492
Cdd:PRK11701 100 DGLRMQvsagGNIGERLMAVGARHYGdiratagdwLERVeidaarIDDLPT-----------TFSGGMQQRLQIARNLVT 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1437745540 493 NPKIVLLDEPTTGLDqySEIQA--LNAISAWCRSKTL--LVVTHRPQVLSIV-NRIIVVDNGKVVMDGPRDAVL 561
Cdd:PRK11701 169 HPRLVFMDEPTGGLD--VSVQArlLDLLRGLVRELGLavVIVTHDLAVARLLaHRLLVMKQGRVVESGLTDQVL 240
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
340-560 |
2.99e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 69.76 E-value: 2.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 340 NVSFaynqDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHylrnqvlllE-- 417
Cdd:COG4674 17 TVSF----DGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEH---------Eia 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 418 --------QEPRLFLG-SLRENLDLArmdgFSSDQDLIVALkRFGLDKVIKKHprgLDMSLGENGLG---------LSGG 479
Cdd:COG4674 84 rlgigrkfQKPTVFEElTVFENLELA----LKGDRGVFASL-FARLTAEERDR---IEEVLETIGLTdkadrlaglLSHG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 480 QKQIVALARMTLRNPKIVLLDEPTTGL-----DQYSEIqaLNAISawcRSKTLLVVTHRPQ-VLSIVNRIIVVDNGKVVM 553
Cdd:COG4674 156 QKQWLEIGMLLAQDPKLLLLDEPVAGMtdaetERTAEL--LKSLA---GKHSVVVVEHDMEfVRQIARKVTVLHQGSVLA 230
|
....*..
gi 1437745540 554 DGPRDAV 560
Cdd:COG4674 231 EGSLDEV 237
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
339-575 |
3.39e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.05 E-value: 3.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 339 QNVSFAYNQDSS--SVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAE-----QGSITLDDVDIRQIDPHYLR- 410
Cdd:PRK15134 9 ENLSVAFRQQQTvrTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASEQTLRg 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 411 ---NQVLLLEQEPRLFLGSLR-------ENLDLAR-MDGFSSDQDLIVALKRFGLDKVIKKhprgldmsLGENGLGLSGG 479
Cdd:PRK15134 89 vrgNKIAMIFQEPMVSLNPLHtlekqlyEVLSLHRgMRREAARGEILNCLDRVGIRQAAKR--------LTDYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 480 QKQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCR--SKTLLVVTHRpqvLSIV----NRIIVVDNGKVVM 553
Cdd:PRK15134 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHN---LSIVrklaDRVAVMQNGRCVE 237
|
250 260
....*....|....*....|..
gi 1437745540 554 DGPRDAVLQQLAKNETEKQITA 575
Cdd:PRK15134 238 QNRAATLFSAPTHPYTQKLLNS 259
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
336-558 |
3.81e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 70.05 E-value: 3.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDS---SSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDI----RQIDPHY 408
Cdd:PRK13634 3 ITFQKVEHRYQYKTpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 409 LRNQVLLLEQ--EPRLFLGSLRENLDLARMD-GFSSDQDLIVA---LKRFGLD-KVIKKHPrgldmslgengLGLSGGQK 481
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNfGVSEEDAKQKAremIELVGLPeELLARSP-----------FELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 482 QIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSK--TLLVVTHRPQ-VLSIVNRIIVVDNGKVVMDG-PR 557
Cdd:PRK13634 152 RRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSMEdAARYADQIVVMHKGTVFLQGtPR 231
|
.
gi 1437745540 558 D 558
Cdd:PRK13634 232 E 232
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
352-563 |
4.68e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.50 E-value: 4.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 352 VVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYP-AEQGSITLDD--VDIRqiDP-HYLRNQVLLLEQE-------P 420
Cdd:PRK13549 277 RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGkpVKIR--NPqQAIAQGIAMVPEDrkrdgivP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 421 RLFLGslrENLDLARMDGFSSDQDLIVALKRFGLDKVIKK------HPrglDMSLGenglGLSGGQKQIVALARMTLRNP 494
Cdd:PRK13549 355 VMGVG---KNITLAALDRFTGGSRIDDAAELKTILESIQRlkvktaSP---ELAIA----RLSGGNQQKAVLAKCLLLNP 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1437745540 495 KIVLLDEPTTGLD---QYsEIQAL-NAISAwcRSKTLLVVTHR-PQVLSIVNRIIVVDNGKVVMDGPRDAVLQQ 563
Cdd:PRK13549 425 KILILDEPTRGIDvgaKY-EIYKLiNQLVQ--QGVAIIVISSElPEVLGLSDRVLVMHEGKLKGDLINHNLTQE 495
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
345-552 |
5.06e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.45 E-value: 5.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 345 YNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITlDDVDIRQIDPhylrnQVLLLEQEPRLfl 424
Cdd:COG2401 38 LRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGC-VDVPDNQFGR-----EASLIDAIGRK-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 425 GSLRENLDLARMDGFSsdqDLIVALKRFgldkvikKHprgldmslgenglgLSGGQKQIVALARMTLRNPKIVLLDEPTT 504
Cdd:COG2401 110 GDFKDAVELLNAVGLS---DAVLWLRRF-------KE--------------LSTGQKFRFRLALLLAERPKLLVIDEFCS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1437745540 505 GLD-QYSEIQALNAISAWCRS-KTLLVVTHRPQVLS--IVNRIIVVDNGKVV 552
Cdd:COG2401 166 HLDrQTAKRVARNLQKLARRAgITLVVATHHYDVIDdlQPDLLIFVGYGGVP 217
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
353-567 |
5.73e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 70.83 E-value: 5.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 353 VKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYL----RNQVLLLEQEPRLF----- 423
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSFALMphmtv 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 424 LGSLRENLDLARMDGFSSDQDLIVALKRFGLDKVIKKHPRgldmslgenglGLSGGQKQIVALARMTLRNPKIVLLDEPT 503
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745540 504 TGLDQY--SEIQALNAISAWCRSKTLLVVTHR-PQVLSIVNRIIVVDNGKVVMDGPRDAVLQQLAKN 567
Cdd:PRK10070 193 SALDPLirTEMQDELVKLQAKHQRTIVFISHDlDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAND 259
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
368-560 |
6.84e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 70.29 E-value: 6.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 368 ILGRIGSGKSTTLKLAAGLYPAEQGSITLDD---VDIRQ---IDPHylRNQVLLLEQEPRLFLG-SLRENLdLARMDGFS 440
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKgicLPPE--KRRIGYVFQDARLFPHyKVRGNL-RYGMAKSM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 441 SDQ-DLIVALkrFGLDKVIKKHPrgldmslgengLGLSGGQKQIVALARMTLRNPKIVLLDEPTTGLD--------QYse 511
Cdd:PRK11144 106 VAQfDKIVAL--LGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlprkrellPY-- 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1437745540 512 IQALnaisawcrSKTL----LVVTHRPQ-VLSIVNRIIVVDNGKVVMDGPRDAV 560
Cdd:PRK11144 171 LERL--------AREInipiLYVSHSLDeILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
336-549 |
9.16e-13 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 67.74 E-value: 9.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSSSVVKIlSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSI----TLDDVDIRQIDPHYLRN 411
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNI-NIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 412 QVLLLEQEPRLFLGSLRENLDlarmdgFSS---DQDLIVALKRFGLDKVIKKHPRGLDMSLGENGLGLSGGQKQIVALAR 488
Cdd:cd03290 80 SVAYAAQKPWLLNATVEENIT------FGSpfnKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1437745540 489 MTLRNPKIVLLDEPTTGLD-QYSEIQALNAISAWCR--SKTLLVVTHRPQVLSIVNRIIVVDNG 549
Cdd:cd03290 154 ALYQNTNIVFLDDPFSALDiHLSDHLMQEGILKFLQddKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
308-549 |
1.47e-12 |
|
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: 70.71 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 308 KGVNGIVERPSERESARKyitlkQINGN--IKFQNVSFAynqdSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAG 385
Cdd:TIGR01271 404 EGIGELFEKIKQNNKARK-----QPNGDdgLFFSNFSLY----VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMG 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 386 -LYPAEqGSITlddvdirqidpHYLRnqVLLLEQEPRLFLGSLRENLdlarMDGFSSDQ-DLIVALKRFGLDKVIKKHPR 463
Cdd:TIGR01271 475 eLEPSE-GKIK-----------HSGR--ISFSPQTSWIMPGTIKDNI----IFGLSYDEyRYTSVIKACQLEEDIALFPE 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 464 GLDMSLGENGLGLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNaiSAWCR---SKTLLVVTHRPQVLSIV 540
Cdd:TIGR01271 537 KDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFE--SCLCKlmsNKTRILVTSKLEHLKKA 614
|
....*....
gi 1437745540 541 NRIIVVDNG 549
Cdd:TIGR01271 615 DKILLLHEG 623
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
357-558 |
1.57e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.94 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 357 SFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLLLEQEPRLFLG-----SLRENL 431
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLCPEDRKAEGiipvhSVADNI 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 432 DLARMDGFSsdqdlivalkRFGL-----------DKVIKK------HPRGLDMSlgenglgLSGGQKQIVALARMTLRNP 494
Cdd:PRK11288 353 NISARRHHL----------RAGClinnrweaenaDRFIRSlniktpSREQLIMN-------LSGGNQQKAILGRWLSEDM 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745540 495 KIVLLDEPTTGLD--QYSEI-QALNAISAwcRSKTLLVVTHR-PQVLSIVNRIIVVDNGKVVMDGPRD 558
Cdd:PRK11288 416 KVILLDEPTRGIDvgAKHEIyNVIYELAA--QGVAVLFVSSDlPEVLGVADRIVVMREGRIAGELARE 481
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
336-501 |
2.32e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 69.62 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYnQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLL 415
Cdd:PRK10522 323 LELRNVTFAY-QDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 416 LEQEPRLF---LGSlrenldlarmDGFSSDQDLIVA-LKRFGL-DKVIKKHPRGLDmslgengLGLSGGQKQIVALARMT 490
Cdd:PRK10522 402 VFTDFHLFdqlLGP----------EGKPANPALVEKwLERLKMaHKLELEDGRISN-------LKLSKGQKKRLALLLAL 464
|
170
....*....|.
gi 1437745540 491 LRNPKIVLLDE 501
Cdd:PRK10522 465 AEERDILLLDE 475
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
326-555 |
2.81e-12 |
|
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: 66.13 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 326 YITLKQINGNIKFQnvsfaYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGL---YPAEQGSITLDDVDIR 402
Cdd:cd03233 1 ASTLSWRNISFTTG-----KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegNVSVEGDIHYNGIPYK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 403 QIDPHYlRNQVLLLEQE----PRLflgSLRENLDLA-RMDGfssdqdlivalkrfglDKVIKkhprgldmslgenglGLS 477
Cdd:cd03233 76 EFAEKY-PGEIIYVSEEdvhfPTL---TVRETLDFAlRCKG----------------NEFVR---------------GIS 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 478 GGQKQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRS--KTLLVVTHRP--QVLSIVNRIIVVDNGKVVM 553
Cdd:cd03233 121 GGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVlkTTTFVSLYQAsdEIYDLFDKVLVLYEGRQIY 200
|
..
gi 1437745540 554 DG 555
Cdd:cd03233 201 YG 202
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
352-507 |
3.28e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 68.90 E-value: 3.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 352 VVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLLLEQEPRLFLG-----S 426
Cdd:COG3845 273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAYIPEDRLGRGlvpdmS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 427 LRENLDLARMD--GFSS----DQDLIVALKRfgldKVIKKH---PRGLDMSLGenglGLSGGQKQIVALARMTLRNPKIV 497
Cdd:COG3845 353 VAENLILGRYRrpPFSRggflDRKAIRAFAE----ELIEEFdvrTPGPDTPAR----SLSGGNQQKVILARELSRDPKLL 424
|
170
....*....|
gi 1437745540 498 LLDEPTTGLD 507
Cdd:COG3845 425 IAAQPTRGLD 434
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
353-552 |
3.68e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.78 E-value: 3.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 353 VKIL---SFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVdirqidPHYLRNQ-------VLLLEQE--- 419
Cdd:PRK11288 17 VKALddiSFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ------EMRFASTtaalaagVAIIYQElhl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 420 -PRLflgSLRENLDLARMD---GFSSDQDLIV----ALKRFGLDkvikkhprgLD--MSLGEnglgLSGGQKQIVALARM 489
Cdd:PRK11288 91 vPEM---TVAENLYLGQLPhkgGIVNRRLLNYeareQLEHLGVD---------IDpdTPLKY----LSIGQRQMVEIAKA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745540 490 TLRNPKIVLLDEPTTGLDQySEIQALNAISAWCRS--KTLLVVTHR-PQVLSIVNRIIVVDNGKVV 552
Cdd:PRK11288 155 LARNARVIAFDEPTSSLSA-REIEQLFRVIRELRAegRVILYVSHRmEEIFALCDAITVFKDGRYV 219
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
339-564 |
3.90e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 66.93 E-value: 3.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 339 QNVSFAYNqdSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLLLEQ 418
Cdd:PRK10253 11 EQLTLGYG--KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 419 EPRLfLGSLRENLDLARmdGFSSDQDLIVALKRFGLDKVIKK-HPRGLDMSLGENGLGLSGGQKQIVALARMTLRNPKIV 497
Cdd:PRK10253 89 NATT-PGDITVQELVAR--GRYPHQPLFTRWRKEDEEAVTKAmQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIM 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1437745540 498 LLDEPTTGLDQYSEIQALNAISAWCRSK--TLLVVTHR-PQVLSIVNRIIVVDNGKVVMDG-PRDAVLQQL 564
Cdd:PRK10253 166 LLDEPTTWLDISHQIDLLELLSELNREKgyTLAAVLHDlNQACRYASHLIALREGKIVAQGaPKEIVTAEL 236
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
358-552 |
4.84e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.82 E-value: 4.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 358 FEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLD-DVDIR--QIDP--------------------------HY 408
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEqDLIVArlQQDPprnvegtvydfvaegieeqaeylkryHD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 409 LRNQVlllEQEP--RLF--LGSLRENLDLArmDGFSSDQDLIVALKRFGLDKvikkhprglDMSLGEnglgLSGGQKQIV 484
Cdd:PRK11147 104 ISHLV---ETDPseKNLneLAKLQEQLDHH--NLWQLENRINEVLAQLGLDP---------DAALSS----LSGGWLRKA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1437745540 485 ALARMTLRNPKIVLLDEPTTGLDqyseIQALNAISAWCRS--KTLLVVTH-RPQVLSIVNRIIVVDNGKVV 552
Cdd:PRK11147 166 ALGRALVSNPDVLLLDEPTNHLD----IETIEWLEGFLKTfqGSIIFISHdRSFIRNMATRIVDLDRGKLV 232
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
336-555 |
5.40e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 69.00 E-value: 5.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYnqDSSSVVKILS---FEIKPGEKVGILGRIGSGKSTTLKLAAG-LYPAEQGSITLddvdirqidphylRN 411
Cdd:PLN03130 615 ISIKNGYFSW--DSKAERPTLSninLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVI-------------RG 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 412 QVLLLEQEPRLFLGSLRENLdlarMDGFSSDQDLI-VALKRFGLDKVIKKHPRGLDMSLGENGLGLSGGQKQIVALARMT 490
Cdd:PLN03130 680 TVAYVPQVSWIFNATVRDNI----LFGSPFDPERYeRAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAV 755
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745540 491 LRNPKIVLLDEPTTGLDQYSEIQALNA-ISAWCRSKTLLVVTHRPQVLSIVNRIIVVDNGKVVMDG 555
Cdd:PLN03130 756 YSNSDVYIFDDPLSALDAHVGRQVFDKcIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEG 821
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
353-575 |
5.87e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 68.34 E-value: 5.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 353 VKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSIT-----LDDVDIRQIDPhyLRNQVLLLEQ------EPR 421
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIfngqrIDTLSPGKLQA--LRRDIQFIFQdpyaslDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 422 LFLG-SLRENLDLARM-DGFSSDQDLIVALKRFGL-DKVIKKHPRgldmslgenglGLSGGQKQIVALARMTLRNPKIVL 498
Cdd:PRK10261 418 QTVGdSIMEPLRVHGLlPGKAAAARVAWLLERVGLlPEHAWRYPH-----------EFSGGQRQRICIARALALNPKVII 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 499 LDEPTTGLDQYSEIQALNAISAWCRSK--TLLVVTHRPQVLS-IVNRIIVVDNGKVVMDGPRDAVLQQLAKNETEKQITA 575
Cdd:PRK10261 487 ADEAVSALDVSIRGQIINLLLDLQRDFgiAYLFISHDMAVVErISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAA 566
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
357-507 |
6.23e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 68.61 E-value: 6.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 357 SFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDvdiRQIDPHYL--RNQVLLLEQEprlFlgSL------R 428
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFG---QPVDAGDIatRRRVGYMSQA---F--SLygeltvR 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 429 ENLDL-ARMdgFSSDQDLIVA-----LKRFGLDKVIKKHPRGLDMslgenglglsgGQKQIVALARMTLRNPKIVLLDEP 502
Cdd:NF033858 358 QNLELhARL--FHLPAAEIAArvaemLERFDLADVADALPDSLPL-----------GIRQRLSLAVAVIHKPELLILDEP 424
|
....*
gi 1437745540 503 TTGLD 507
Cdd:NF033858 425 TSGVD 429
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
339-562 |
9.77e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 65.58 E-value: 9.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 339 QNVSFAYNQDSSSV-----VKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQV 413
Cdd:PRK10575 8 SDTTFALRNVSFRVpgrtlLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 414 LLLEQE-PRLFLGSLRENLDLARMDGFSsdqdlivALKRFGLDKVIKkhprgLDMSLGENGL---------GLSGGQKQI 483
Cdd:PRK10575 88 AYLPQQlPAAEGMTVRELVAIGRYPWHG-------ALGRFGAADREK-----VEEAISLVGLkplahrlvdSLSGGERQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 484 VALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSKTLLVVThrpqVLSIVN-------RIIVVDNGKVVMDGP 556
Cdd:PRK10575 156 AWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA----VLHDINmaarycdYLVALRGGEMIAQGT 231
|
....*.
gi 1437745540 557 RDAVLQ 562
Cdd:PRK10575 232 PAELMR 237
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
344-551 |
1.38e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.06 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 344 AYNQDSssvVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLLLEQEPRLF 423
Cdd:PRK10982 258 SLRQPS---IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFALVTEERRS 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 424 LGsLRENLDLarmdGFSSdqdLIVALKR----FGL--DKVIKKHPRGLDMSLG------ENGLG-LSGGQKQIVALARMT 490
Cdd:PRK10982 335 TG-IYAYLDI----GFNS---LISNIRNyknkVGLldNSRMKSDTQWVIDSMRvktpghRTQIGsLSGGNQQKVIIGRWL 406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1437745540 491 LRNPKIVLLDEPTTGLDQYS--EIQALNAISAWCRSKTLLVVTHRPQVLSIVNRIIVVDNGKV 551
Cdd:PRK10982 407 LTQPEILMLDEPTRGIDVGAkfEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
368-577 |
2.16e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 64.73 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 368 ILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDI--RQI----DPHYLRNQVLLLEQEPRLFLGSLRENLdlarMDGFSS 441
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLggRSIfnyrDVLEFRRRVGMLFQRPNPFPMSIMDNV----LAGVRA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 442 DQdlIVALKRF-----------GLDKVIKKHprgldmsLGENGLGLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYS 510
Cdd:PRK14271 128 HK--LVPRKEFrgvaqarltevGLWDAVKDR-------LSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTT 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745540 511 EIQALNAISAWCRSKTLLVVTHR-PQVLSIVNRIIVVDNGKVVMDGPRDAVLQQLAKNETEKQITAHS 577
Cdd:PRK14271 199 TEKIEEFIRSLADRLTVIIVTHNlAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAGLS 266
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
356-532 |
2.44e-11 |
|
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: 66.50 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 356 LSFeiKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDdvdirqidPHYlrnQVLLLEQEPRLFLG-SLRENLdla 434
Cdd:TIGR03719 26 LSF--FPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ--------PGI---KVGYLPQEPQLDPTkTVRENV--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 435 rMDGFSSDQDlivALKRFG------------LDKVIKK---------------HPRGLDMSL-------GENGLG-LSGG 479
Cdd:TIGR03719 90 -EEGVAEIKD---ALDRFNeisakyaepdadFDKLAAEqaelqeiidaadawdLDSQLEIAMdalrcppWDADVTkLSGG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745540 480 QKQIVALARMTLRNPKIVLLDEPTTGLDQYSeiqalnaiSAWCR------SKTLLVVTH 532
Cdd:TIGR03719 166 ERRRVALCRLLLSKPDMLLLDEPTNHLDAES--------VAWLErhlqeyPGTVVAVTH 216
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
360-532 |
2.45e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 66.37 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 360 IKPGEKVGILGRIGSGKSTTLKLAAG-LYP-----AEQGSItlDDV-------------------DIRQI-DPHYLrnqv 413
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGeLIPnlgdyEEEPSW--DEVlkrfrgtelqnyfkklyngEIKVVhKPQYV---- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 414 lllEQEPRLFLGSLRENLDlaRMDGFSSDQDLIvalKRFGLDKVikkhprgLDMSLGEnglgLSGGQKQIVALARMTLRN 493
Cdd:PRK13409 170 ---DLIPKVFKGKVRELLK--KVDERGKLDEVV---ERLGLENI-------LDRDISE----LSGGELQRVAIAAALLRD 230
|
170 180 190
....*....|....*....|....*....|....*....
gi 1437745540 494 PKIVLLDEPTTGLDQYSEIQALNAISAWCRSKTLLVVTH 532
Cdd:PRK13409 231 ADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEH 269
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
357-560 |
2.85e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 63.86 E-value: 2.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 357 SFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYL-RNQVLLLEQEPRLFLG-SLRENLDLA 434
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIaRMGVVRTFQHVRLFREmTVIENLLVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 435 --------------RMDGF-SSDQDlivALKR--FGLDKVikkhprGL-DMSLGENGlGLSGGQKQIVALARMTLRNPKI 496
Cdd:PRK11300 105 qhqqlktglfsgllKTPAFrRAESE---ALDRaaTWLERV------GLlEHANRQAG-NLAYGQQRRLEIARCMVTQPEI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745540 497 VLLDEPTTGLDQySEIQALNAISAWCRSK---TLLVVTH-RPQVLSIVNRIIVVDNGKVVMDGPRDAV 560
Cdd:PRK11300 175 LMLDEPAAGLNP-KETKELDELIAELRNEhnvTVLLIEHdMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
356-507 |
3.87e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 65.53 E-value: 3.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 356 LSFeiKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDdvdirqidPHYlrnQVLLLEQEPRLFLG-SLRENLdla 434
Cdd:PRK11819 28 LSF--FPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPA--------PGI---KVGYLPQEPQLDPEkTVRENV--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 435 rMDGFssdQDLIVALKRF------------GLDKVIKKHPR-----------GLDMSL-----------GENGLG-LSGG 479
Cdd:PRK11819 92 -EEGV---AEVKAALDRFneiyaayaepdaDFDALAAEQGElqeiidaadawDLDSQLeiamdalrcppWDAKVTkLSGG 167
|
170 180
....*....|....*....|....*...
gi 1437745540 480 QKQIVALARMTLRNPKIVLLDEPTTGLD 507
Cdd:PRK11819 168 ERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
359-547 |
3.97e-11 |
|
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: 65.58 E-value: 3.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 359 EIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLdDVDIrQIDPHYLRNqvlllEQEprlflGSLRENLDLARMDG 438
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE-DLKI-SYKPQYISP-----DYD-----GTVEEFLRSANTDD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 439 FSSD--QDLIValKRFGLDKVikkhprgLDMSLGEnglgLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALN 516
Cdd:COG1245 430 FGSSyyKTEII--KPLGLEKL-------LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAK 496
|
170 180 190
....*....|....*....|....*....|....
gi 1437745540 517 AIS--AWCRSKTLLVVTHRPQVLS-IVNRIIVVD 547
Cdd:COG1245 497 AIRrfAENRGKTAMVVDHDIYLIDyISDRLMVFE 530
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
359-547 |
4.35e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.60 E-value: 4.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 359 EIKPGEKVGILGRIGSGKSTTLKLAAG-LYPAEqGSITLdDVDIrQIDPHYLRNQVlllEQEPRLFLGSLRENLDlarmd 437
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGvLKPDE-GEVDP-ELKI-SYKPQYIKPDY---DGTVEDLLRSITDDLG----- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 438 gfSS--DQDLIvalKRFGLDKVikkhprgLDMSLGEnglgLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQAL 515
Cdd:PRK13409 430 --SSyyKSEII---KPLQLERL-------LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVA 493
|
170 180 190
....*....|....*....|....*....|....*
gi 1437745540 516 NAIS--AWCRSKTLLVVTHRPQVLS-IVNRIIVVD 547
Cdd:PRK13409 494 KAIRriAEEREATALVVDHDIYMIDyISDRLMVFE 528
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
310-551 |
5.93e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.81 E-value: 5.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 310 VNGIVERPSERESARKYITLKQINGNIKFQNVSFAYNQDSSSV--VKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLY 387
Cdd:PRK09700 234 NDDIVRLMVGRELQNRFNAMKENVSNLAHETVFEVRNVTSRDRkkVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVD 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 388 PAEQGSITLDDVDIRQIDPHYLRNQVLLLEQEPRLFLG-----SLRENLDLAR----------MDGFSSDQDLIVALKRF 452
Cdd:PRK09700 314 KRAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRDNGffpnfSIAQNMAISRslkdggykgaMGLFHEVDEQRTAENQR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 453 GLDKvIKKHprgldmSLGENGLGLSGGQKQIVALARMTLRNPKIVLLDEPTTGLD--QYSEIQALNAISAWCRSKTLLVV 530
Cdd:PRK09700 394 ELLA-LKCH------SVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDvgAKAEIYKVMRQLADDGKVILMVS 466
|
250 260
....*....|....*....|.
gi 1437745540 531 THRPQVLSIVNRIIVVDNGKV 551
Cdd:PRK09700 467 SELPEIITVCDRIAVFCEGRL 487
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
21-308 |
6.56e-11 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 63.60 E-value: 6.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 21 ILATFVINFLALVSSLYVMNVYDRVIPNKSYQTLWVLSIGVIIAILFEFTAKMLRGRLTDIAGKKADLIISSALFRKVTN 100
Cdd:cd18542 5 ILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 101 LklqekpisSGSYVNNLR----------DFESVRDFMtSASLLTLVDMPFLILFVSVIAL-VGGYLAFVPLTIIPLVIIV 169
Cdd:cd18542 85 L--------SFSFHDKARtgdlmsrctsDVDTIRRFL-AFGLVELVRAVLLFIGALIIMFsINWKLTLISLAIIPFIALF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 170 GLLaqipLSKYINESMKESSQRQG----LAVEAIEGIETLKtnnamnwAQKRWDYYTAKTASSSMK-----VKNISNFVI 240
Cdd:cd18542 156 SYV----FFKKVRPAFEEIREQEGelntVLQENLTGVRVVK-------AFAREDYEIEKFDKENEEyrdlnIKLAKLLAK 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 241 YFAVM--MQQLNTIFLVIIGTYLIHSDdpasKITMGALIATVILSGRALSPLGQIAGLAVRFQQAWVALK 308
Cdd:cd18542 225 YWPLMdfLSGLQIVLVLWVGGYLVING----EITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAE 290
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
340-520 |
1.18e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.12 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 340 NVSFAYnQDSSsVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYlrnqvllleQE 419
Cdd:PRK13540 6 ELDFDY-HDQP-LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTY---------QK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 420 PRLFLG---------SLREN--LDLArmdgFSSDQDLIVALKR-FGLDKVIKkHPRGLdmslgenglgLSGGQKQIVALA 487
Cdd:PRK13540 75 QLCFVGhrsginpylTLRENclYDIH----FSPGAVGITELCRlFSLEHLID-YPCGL----------LSSGQKRQVALL 139
|
170 180 190
....*....|....*....|....*....|...
gi 1437745540 488 RMTLRNPKIVLLDEPTTGLDQYSEIQALNAISA 520
Cdd:PRK13540 140 RLWMSKAKLWLLDEPLVALDELSLLTIITKIQE 172
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
335-551 |
1.26e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 63.32 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 335 NIKFQNVSFAYNQDSSsVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPH------Y 408
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQ-VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAdrdiamV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 409 LRNQVLLleqePRLflgSLREN----LDLARMDGFSSDQDLIVALKRFGLDKVIKKHPRGLdmslgenglglSGGQKQIV 484
Cdd:PRK11650 82 FQNYALY----PHM---SVRENmaygLKIRGMPKAEIEERVAEAARILELEPLLDRKPREL-----------SGGQRQRV 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745540 485 ALARMTLRNPKIVLLDEPTTGLD-----QY-SEIQALNAisawcRSKTL-LVVTHrPQV--LSIVNRIIVVDNGKV 551
Cdd:PRK11650 144 AMGRAIVREPAVFLFDEPLSNLDaklrvQMrLEIQRLHR-----RLKTTsLYVTH-DQVeaMTLADRVVVMNGGVA 213
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
300-531 |
1.49e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 64.65 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 300 FQQAWVALKGVNGIVERPSERESARKYITlkqINGN----IKFQNVSFAYNQDSSSVVKILSFEIKPGEKVGILGRIGSG 375
Cdd:TIGR01257 1901 FLSRWIAEPAKEPIFDEDDDVAEERQRII---SGGNktdiLRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAG 1977
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 376 KSTTLKLAAGLYPAEQGSITLDDVDIRQ--IDPHYLRNQVLLLEQEPRLFLGslRENLDL-ARMDGFSSDQdlivalkrf 452
Cdd:TIGR01257 1978 KTTTFKMLTGDTTVTSGDATVAGKSILTniSDVHQNMGYCPQFDAIDDLLTG--REHLYLyARLRGVPAEE--------- 2046
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 453 gLDKVIKKHPRGLDMSLGENGLG--LSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSKTLLVV 530
Cdd:TIGR01257 2047 -IEKVANWSIQSLGLSLYADRLAgtYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVL 2125
|
.
gi 1437745540 531 T 531
Cdd:TIGR01257 2126 T 2126
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
315-555 |
1.65e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 64.41 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 315 ERPSERESARKyitlKQINGNIKFQNVSFAYNQDsssvvkiLSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSI 394
Cdd:PTZ00243 649 ATPTSERSAKT----PKMKTDDFFELEPKVLLRD-------VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 395 tlddvdirqidphYLRNQVLLLEQEPRLFLGSLRENL------DLARMdgfssdQDlivALKRFGLDKVIKKHPRGLDMS 468
Cdd:PTZ00243 718 -------------WAERSIAYVPQQAWIMNATVRGNIlffdeeDAARL------AD---AVRVSQLEADLAQLGGGLETE 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 469 LGENGLGLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQY-SEIQALNAISAWCRSKTLLVVTHRPQVLSIVNRIIVVD 547
Cdd:PTZ00243 776 IGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALG 855
|
....*...
gi 1437745540 548 NGKVVMDG 555
Cdd:PTZ00243 856 DGRVEFSG 863
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
349-574 |
1.70e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 61.78 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 349 SSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQ-----GSITLDDVDI--RQIDPHYLRNQVLLLEQEPR 421
Cdd:PRK14267 16 SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIysPDVDPIEVRREVGMVFQYPN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 422 LFLG-SLRENLDLA-RMDGFSSDQDLI-----VALKRFGLDKVIKKHprgldmsLGENGLGLSGGQKQIVALARMTLRNP 494
Cdd:PRK14267 96 PFPHlTIYDNVAIGvKLNGLVKSKKELderveWALKKAALWDEVKDR-------LNDYPSNLSGGQRQRLVIARALAMKP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 495 KIVLLDEPTTGLDQYSEIQALNAISAWCRSKTLLVVTHRP-QVLSIVNRIIVVDNGKVVMDGPRDAVLQQLAKNETEKQI 573
Cdd:PRK14267 169 KILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPaQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYV 248
|
.
gi 1437745540 574 T 574
Cdd:PRK14267 249 T 249
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
359-532 |
1.72e-10 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 61.66 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 359 EIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIrQIDPHYLrnqvllleqEPRlFLGSLRENLdLARMDG 438
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQYI---------KAD-YEGTVRDLL-SSITKD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 439 FSSDQDLIValkrfgldKVIKkhPRGLDMSLGENGLGLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAI 518
Cdd:cd03237 89 FYTHPYFKT--------EIAK--PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVI 158
|
170
....*....|....*.
gi 1437745540 519 S--AWCRSKTLLVVTH 532
Cdd:cd03237 159 RrfAENNEKTAFVVEH 174
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
369-555 |
1.78e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 64.26 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 369 LGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIrQIDPHYLRNQVLLLEQEPRLF--LGSLRENLDLARMDGFSSDQdli 446
Cdd:TIGR01257 962 LGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFhhLTVAEHILFYAQLKGRSWEE--- 1037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 447 valKRFGLDKVIKKhpRGLDMSLGENGLGLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSKT 526
Cdd:TIGR01257 1038 ---AQLEMEAMLED--TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRT 1112
|
170 180 190
....*....|....*....|....*....|
gi 1437745540 527 LLVVTHRPQVLSIV-NRIIVVDNGKVVMDG 555
Cdd:TIGR01257 1113 IIMSTHHMDEADLLgDRIAIISQGRLYCSG 1142
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
336-551 |
2.61e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 63.34 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYnQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAG-LYPAEQGSITLDDVDIRQIDPHYLRNqvL 414
Cdd:PLN03073 509 ISFSDASFGY-PGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGeLQPSSGTVFRSAKVRMAVFSQHHVDG--L 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 415 LLEQEPRLFLgslrenldlARMDGFSSDQDLIVALKRFGLDKVIKKHPRgldmslgengLGLSGGQKQIVALARMTLRNP 494
Cdd:PLN03073 586 DLSSNPLLYM---------MRCFPGVPEQKLRAHLGSFGVTGNLALQPM----------YTLSGGQKSRVAFAKITFKKP 646
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1437745540 495 KIVLLDEPTTGLDqyseiqaLNAISAWCRSKTL-----LVVTHRPQVLS-IVNRIIVVDNGKV 551
Cdd:PLN03073 647 HILLLDEPSNHLD-------LDAVEALIQGLVLfqggvLMVSHDEHLISgSVDELWVVSEGKV 702
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
14-303 |
3.06e-10 |
|
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and similar proteins; This group includes the 6-TMD of an uncharacterized peptidase-containing ABC transporter of T1SS (type 1 secretion systems), similar to heterocyst differentiation protein HetC. HetC is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350015 [Multi-domain] Cd Length: 294 Bit Score: 61.30 E-value: 3.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 14 KKYYYQIILATFVINFLALVSSLYVMNVYDRVIPNKSYQTLWVLSIGVIIAILFEFTAKMLRGRLTDIAGKKADLIISSA 93
Cdd:cd18571 1 KKLILQLLLGLLLGSLLQLIFPFLTQSIVDKGINNKDLNFIYLILIAQLVLFLGSTSIEFIRSWILLHISSRINISIISD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 94 LFRKVTNLklqekPIS------SGSYVNNLRDFESVRDFMTSASLLTLVDMPFLILFVSVIALVGGY--LAFVPLTIIPL 165
Cdd:cd18571 81 FLIKLMRL-----PISffdtkmTGDILQRINDHSRIESFLTSSSLSILFSLLNLIVFSIVLAYYNLTifLIFLIGSVLYI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 166 VIIVGLLAQIplsKYIN-ESMKESSQRQGLAVEAIEGIETLKTNNAMNwaQKRWDY--YTAKTASSSMKVKNISNFVIYF 242
Cdd:cd18571 156 LWILLFLKKR---KKLDyKRFDLSSENQSKLIELINGMQEIKLNNSER--QKRWEWerIQAKLFKINIKSLKLDQYQQIG 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1437745540 243 AVMMQQL-NTIFLVIIGTYLIHSDdpaskITMGALIATVILSGRALSPLGQIAGLAVRFQQA 303
Cdd:cd18571 231 ALFINQLkNILITFLAAKLVIDGE-----ITLGMMLAIQYIIGQLNSPIEQLIGFIQSLQDA 287
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
339-552 |
3.78e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.60 E-value: 3.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 339 QNVSFAYnqDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITL-DDVDI---RQIDPHYLRNQVL 414
Cdd:PRK15064 323 ENLTKGF--DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWsENANIgyyAQDHAYDFENDLT 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 415 LL------------EQEPRLFLGSLRenldlarmdgFSSDQdlivalkrfgldkvIKKHPRGLdmslgenglglSGGQKQ 482
Cdd:PRK15064 401 LFdwmsqwrqegddEQAVRGTLGRLL----------FSQDD--------------IKKSVKVL-----------SGGEKG 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1437745540 483 IVALARMTLRNPKIVLLDEPTTGLDQYSeIQALN-AISAWcrSKTLLVVTH-RPQVLSIVNRIIVVDNGKVV 552
Cdd:PRK15064 446 RMLFGKLMMQKPNVLVMDEPTNHMDMES-IESLNmALEKY--EGTLIFVSHdREFVSSLATRIIEITPDGVV 514
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
353-560 |
6.13e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 60.75 E-value: 6.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 353 VKIL---SFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHY---LRNQVLLLEQEP------ 420
Cdd:PRK11308 28 VKALdgvSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqklLRQKIQIVFQNPygslnp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 421 RLFLGSLRE-----NLDLARMDGFSSDQDLivaLKRFGLD-KVIKKHPRgldMslgenglgLSGGQKQIVALARMTLRNP 494
Cdd:PRK11308 108 RKKVGQILEeplliNTSLSAAERREKALAM---MAKVGLRpEHYDRYPH---M--------FSGGQRQRIAIARALMLDP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437745540 495 KIVLLDEPTTGLDQYSEIQALN---------AISAWCRSKTLLVVTHrpqvlsIVNRIIVVDNGKVVMDGPRDAV 560
Cdd:PRK11308 174 DVVVADEPVSALDVSVQAQVLNlmmdlqqelGLSYVFISHDLSVVEH------IADEVMVMYLGRCVEKGTKEQI 242
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
336-582 |
6.32e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 62.11 E-value: 6.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQdsSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDvDIR-----QIDPHYLR 410
Cdd:PRK10636 313 LKMEKVSAGYGD--RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAK-GIKlgyfaQHQLEFLR 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 411 NQVLLLEQeprlflgslrenldLARMDGFSSDQDLIVALKRFGL--DKVIKKHPRgldmslgenglgLSGGQKQIVALAR 488
Cdd:PRK10636 390 ADESPLQH--------------LARLAPQELEQKLRDYLGGFGFqgDKVTEETRR------------FSGGEKARLVLAL 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 489 MTLRNPKIVLLDEPTTGLDqYSEIQALN-AISAWcrSKTLLVVTH-RPQVLSIVNRIIVVDNGKV-VMDGP--------R 557
Cdd:PRK10636 444 IVWQRPNLLLLDEPTNHLD-LDMRQALTeALIDF--EGALVVVSHdRHLLRSTTDDLYLVHDGKVePFDGDledyqqwlS 520
|
250 260
....*....|....*....|....*....
gi 1437745540 558 DAVLQQLAKNETEKQITAHS----KNQNR 582
Cdd:PRK10636 521 DVQKQENQTDEAPKENNANSaqarKDQKR 549
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
336-507 |
8.55e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 59.74 E-value: 8.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQdsSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSItlddvdirqidphylrnqvll 415
Cdd:PRK09544 5 VSLENVSVSFGQ--RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 416 lEQEPRLFLGSLRENLDL-----------ARMDGFSSDQDLIVALKRFG----LDKVIKKhprgldmslgenglgLSGGQ 480
Cdd:PRK09544 62 -KRNGKLRIGYVPQKLYLdttlpltvnrfLRLRPGTKKEDILPALKRVQaghlIDAPMQK---------------LSGGE 125
|
170 180
....*....|....*....|....*..
gi 1437745540 481 KQIVALARMTLRNPKIVLLDEPTTGLD 507
Cdd:PRK09544 126 TQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
356-507 |
9.47e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.22 E-value: 9.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 356 LSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDP--HYLRNQVLLLE--QEPRLFL-GSLREN 430
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTaqRLARGLVYLPEdrQSSGLYLdAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 431 ---LDLARMDGFSSDQDLIVALKRFgldkvikKHPRGLDMSLGENGL-GLSGGQKQIVALARMTLRNPKIVLLDEPTTGL 506
Cdd:PRK15439 362 vcaLTHNRRGFWIKPARENAVLERY-------RRALNIKFNHAEQAArTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
.
gi 1437745540 507 D 507
Cdd:PRK15439 435 D 435
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
335-555 |
9.60e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 59.42 E-value: 9.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 335 NIKFQNVSFAYNQdsssVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGL--YPAEQGSITLDDVDIRQIDPHYLRNQ 412
Cdd:PRK09580 3 SIKDLHVSVEDKA----ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 413 -VLLLEQEP--------RLFLGSLRENLDLARmdgfssDQDlivALKRFGLDKVIKKHPRGLDMSlgENGL------GLS 477
Cdd:PRK09580 79 gIFMAFQYPveipgvsnQFFLQTALNAVRSYR------GQE---PLDRFDFQDLMEEKIALLKMP--EDLLtrsvnvGFS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 478 GGQKQIVALARMTLRNPKIVLLDEPTTGLDqyseIQALNAISAWCRS-----KTLLVVTHRPQVLSIV--NRIIVVDNGK 550
Cdd:PRK09580 148 GGEKKRNDILQMAVLEPELCILDESDSGLD----IDALKIVADGVNSlrdgkRSFIIVTHYQRILDYIkpDYVHVLYQGR 223
|
....*
gi 1437745540 551 VVMDG 555
Cdd:PRK09580 224 IVKSG 228
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
336-555 |
1.17e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 59.26 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQDSSsvVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDV-------------DIR 402
Cdd:PRK09984 5 IRVEKLAKTFNQHQA--LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELlgrtvqregrlarDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 403 QIDPHY--------LRNQVLLLEQEPRLFLGSLRENLDLARMDGFSSDQDLIVALKRFGLDKVikKHPRgldMSLgengl 474
Cdd:PRK09984 83 KSRANTgyifqqfnLVNRLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQALTRVGMVHF--AHQR---VST----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 475 gLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSKTLLVVTHRPQV---LSIVNRIIVVDNGKV 551
Cdd:PRK09984 153 -LSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVdyaLRYCERIVALRQGHV 231
|
....
gi 1437745540 552 VMDG 555
Cdd:PRK09984 232 FYDG 235
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
360-555 |
1.17e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.05 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 360 IKPGEKVGILGRIGSGKSTTLKLAAGLY---------------PAEQ-----GSITLDDVdirqIDPHylrnqvlLLEQE 419
Cdd:PLN03211 91 ASPGEILAVLGPSGSGKSTLLNALAGRIqgnnftgtilannrkPTKQilkrtGFVTQDDI----LYPH-------LTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 420 PRLFLGSLRENLDLARMDGFSSDQDLIVALkrfGLDKVikkhprgldmslgENGL-------GLSGGQKQIVALARMTLR 492
Cdd:PLN03211 160 TLVFCSLLRLPKSLTKQEKILVAESVISEL---GLTKC-------------ENTIignsfirGISGGERKRVSIAHEMLI 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745540 493 NPKIVLLDEPTTGLDQYSEIQALNAISAWC-RSKTLLVVTHRP--QVLSIVNRIIVVDNGKVVMDG 555
Cdd:PLN03211 224 NPSLLILDEPTSGLDATAAYRLVLTLGSLAqKGKTIVTSMHQPssRVYQMFDSVLVLSEGRCLFFG 289
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
352-561 |
2.20e-09 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 58.27 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 352 VVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDD---------------VDIRQIDphYLRNQVLLL 416
Cdd:COG4598 23 VLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGeeirlkpdrdgelvpADRRQLQ--RIRTRLGMV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 417 EQEprlF-LGS---LRENLDLA--RMDGFSSDQDLIVA---LKRFGLDKVIKKHPRGLdmslgenglglSGGQKQIVALA 487
Cdd:COG4598 101 FQS---FnLWShmtVLENVIEApvHVLGRPKAEAIERAealLAKVGLADKRDAYPAHL-----------SGGQQQRAAIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 488 RMTLRNPKIVLLDEPTTGLDqySE--------IQALNAisawcRSKTLLVVTH-----RpqvlSIVNRIIVVDNGKVVMD 554
Cdd:COG4598 167 RALAMEPEVMLFDEPTSALD--PElvgevlkvMRDLAE-----EGRTMLVVTHemgfaR----DVSSHVVFLHQGRIEEQ 235
|
....*..
gi 1437745540 555 GPRDAVL 561
Cdd:COG4598 236 GPPAEVF 242
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
344-532 |
2.49e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.55 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 344 AYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSItlddvdirQIDPHYLRN-----QVLLLEQ 418
Cdd:PRK13543 18 AFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQI--------QIDGKTATRgdrsrFMAYLGH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 419 EPRLF--LGSLrENLD-LARMDGFSSDQDLIVALKRFGL----DKVIKKhprgldmslgenglgLSGGQKQIVALARMTL 491
Cdd:PRK13543 90 LPGLKadLSTL-ENLHfLCGLHGRRAKQMPGSALAIVGLagyeDTLVRQ---------------LSAGQKKRLALARLWL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1437745540 492 RNPKIVLLDEPTTGLDqYSEIQALN-AISAWCRSK-TLLVVTH 532
Cdd:PRK13543 154 SPAPLWLLDEPYANLD-LEGITLVNrMISAHLRGGgAALVTTH 195
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
361-550 |
3.09e-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: 57.76 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 361 KPGEKVGILGRIGSGKSTTLKLAAG-LYP---AEQGSITLDDV-------------------DIRQI-DPHYLrnqvlll 416
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGkLKPnlgKFDDPPDWDEIldefrgselqnyftkllegDVKVIvKPQYV------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 417 EQEPRLFLGSLRENLDLARMDGFssdQDLIValKRFGLDKVIKKHprgLDmslgenglGLSGGQKQIVALARMTLRNPKI 496
Cdd:cd03236 97 DLIPKAVKGKVGELLKKKDERGK---LDELV--DQLELRHVLDRN---ID--------QLSGGELQRVAIAAALARDADF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1437745540 497 VLLDEPTTGLDQYSEIQALNAISAWCR-SKTLLVVTHRPQVLSIVNRIIVVDNGK 550
Cdd:cd03236 161 YFFDEPSSYLDIKQRLNAARLIRELAEdDNYVLVVEHDLAVLDYLSDYIHCLYGE 215
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
357-573 |
9.25e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 56.81 E-value: 9.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 357 SFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIdphYLRNQVLLLEQEprlflgslrENLDLArm 436
Cdd:PRK15056 27 SFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA---LQKNLVAYVPQS---------EEVDWS-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 437 dgFSSDQDLIVALKRFG---LDKVIKKHPRG--------LDMS------LGEnglgLSGGQKQIVALARMTLRNPKIVLL 499
Cdd:PRK15056 93 --FPVLVEDVVMMGRYGhmgWLRRAKKRDRQivtaalarVDMVefrhrqIGE----LSGGQKKRVFLARAIAQQGQVILL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 500 DEPTTGLDQYSE---IQALNAISAwcRSKTLLVVTHRPQVLSIVNRIIVVDNGKVVMDGPRD-------------AVLQQ 563
Cdd:PRK15056 167 DEPFTGVDVKTEariISLLRELRD--EGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTEttftaenlelafsGVLRH 244
|
250
....*....|
gi 1437745540 564 LAKNETEKQI 573
Cdd:PRK15056 245 VALNGSEESI 254
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
353-560 |
1.22e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 57.02 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 353 VKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSIT--------LDDVDIRQIdphylRNQVLLLEQEPrlfL 424
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwlgkdllgMKDDEWRAV-----RSDIQMIFQDP---L 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 425 GSLRENLDLA------------RMDGFSSDQDLIVALKRFGL-DKVIKKHPRGLdmslgenglglSGGQKQIVALARMTL 491
Cdd:PRK15079 109 ASLNPRMTIGeiiaeplrtyhpKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEF-----------SGGQCQRIGIARALI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745540 492 RNPKIVLLDEPTTGLDQYSEIQALNAISAWCR---------SKTLLVVTHrpqvlsIVNRIIVVDNGKVVMDGPRDAV 560
Cdd:PRK15079 178 LEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemglslifiAHDLAVVKH------ISDRVLVMYLGHAVELGTYDEV 249
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
336-563 |
1.99e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 55.96 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYnQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLL 415
Cdd:PRK13652 4 IETRDLCYSY-SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 416 LEQEPRLFLGSLRENLDLA------RMDGFSSDQDLIVALKRFGLDKVIKKHPRGLdmslgenglglSGGQKQIVALARM 489
Cdd:PRK13652 83 VFQNPDDQIFSPTVEQDIAfgpinlGLDEETVAHRVSSALHMLGLEELRDRVPHHL-----------SGGEKKRVAIAGV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745540 490 TLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSKTLLVV--THRPQ-VLSIVNRIIVVDNGKVVMDGPRDAVLQQ 563
Cdd:PRK13652 152 IAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIfsTHQLDlVPEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
361-532 |
2.82e-08 |
|
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: 56.72 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 361 KPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITlDDVDIRQIDPHY-----------LRNQVL-------LLEQEPRL 422
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYD-EEPSWDEVLKRFrgtelqdyfkkLANGEIkvahkpqYVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 423 FLGSLRENLDlaRMDGFSSDQDLIvalKRFGLDKVikkhprgLDMSLGEnglgLSGGQKQIVALARMTLRNPKIVLLDEP 502
Cdd:COG1245 176 FKGTVRELLE--KVDERGKLDELA---EKLGLENI-------LDRDISE----LSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|.
gi 1437745540 503 TTGLDQYSEIQALNAISAWCRS-KTLLVVTH 532
Cdd:COG1245 240 SSYLDIYQRLNVARLIRELAEEgKYVLVVEH 270
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
340-555 |
3.07e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.40 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 340 NVSFAYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDD----------VDIRQIDPHYL 409
Cdd:PRK10261 19 NIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 410 RN----QVLLLEQEPRLFLG-------SLRENLDLARmdGFSSDQDLIVAlKRFgLDKVikKHPRGLDMsLGENGLGLSG 478
Cdd:PRK10261 99 RHvrgaDMAMIFQEPMTSLNpvftvgeQIAESIRLHQ--GASREEAMVEA-KRM-LDQV--RIPEAQTI-LSRYPHQLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 479 GQKQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCR--SKTLLVVTHRPQVLS-IVNRIIVVDNGKVVMDG 555
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKemSMGVIFITHDMGVVAeIADRVLVMYQGEAVETG 251
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
158-303 |
3.56e-08 |
|
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350013 [Multi-domain] Cd Length: 294 Bit Score: 55.17 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 158 VPLTiipLVIIVGLLAQIPLSKYINESMKESSQRQ--------GLAVEAIEGIETLKTNNAMNWAQKRWDYYTAKTASSS 229
Cdd:cd18569 141 VPLT---LIGIAIALLNLLVLRLVSRKRVDLNRRLlqdsgkltGTTMSGLQMIETLKASGAESDFFSRWAGYQAKVLNAQ 217
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1437745540 230 MKVKNISNFVIYFAVMMQQLNTIFLVIIGTYLIHSddpaSKITMGALIATVILSGRALSPLGQIAGLAVRFQQA 303
Cdd:cd18569 218 QELGRTNQLLGALPTLLSALTNAAILGLGGLLVMD----GALTIGMLVAFQSLMASFLAPVNSLVGLGGTLQEM 287
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
336-568 |
4.58e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 54.77 E-value: 4.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAynQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYL---RNQ 412
Cdd:PRK11831 8 VDMRGVSFT--RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 413 VLLLEQEPRLFLG---------SLRENLDLARMDGFSSdqdLIVALKRFGLDKVIKKHPRGLdmslgenglglSGGQKQI 483
Cdd:PRK11831 86 MSMLFQSGALFTDmnvfdnvayPLREHTQLPAPLLHST---VMMKLEAVGLRGAAKLMPSEL-----------SGGMARR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 484 VALARMTLRNPKIVLLDEPTTGLDQYSE------IQALN-AISAWCrsktlLVVTHR-PQVLSIVNRIIVVDNGKVVMDG 555
Cdd:PRK11831 152 AALARAIALEPDLIMFDEPFVGQDPITMgvlvklISELNsALGVTC-----VVVSHDvPEVLSIADHAYIVADKKIVAHG 226
|
250
....*....|...
gi 1437745540 556 PRdavlQQLAKNE 568
Cdd:PRK11831 227 SA----QALQANP 235
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
351-562 |
5.01e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 56.39 E-value: 5.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 351 SVVKILSFEIKPGEKVGILGRIGSGKSTTL-KLAAGLYPAEQ--GSITLDDVDIRQIDPHylRNQVLLLEQEPRLFLGSL 427
Cdd:PLN03140 179 TILKDASGIIKPSRMTLLLGPPSSGKTTLLlALAGKLDPSLKvsGEITYNGYRLNEFVPR--KTSAYISQNDVHVGVMTV 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 428 RENLDL-ARMDGFSSDQDLIVALKRFGLDKVIKKHP-----------RGLDMSL-------------------GENGL-G 475
Cdd:PLN03140 257 KETLDFsARCQGVGTRYDLLSELARREKDAGIFPEAevdlfmkatamEGVKSSLitdytlkilgldickdtivGDEMIrG 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 476 LSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQ---YSEIQALNAISAWCRSKTLL-VVTHRPQVLSIVNRIIVVDNGKV 551
Cdd:PLN03140 337 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSsttYQIVKCLQQIVHLTEATVLMsLLQPAPETFDLFDDIILLSEGQI 416
|
250
....*....|.
gi 1437745540 552 VMDGPRDAVLQ 562
Cdd:PLN03140 417 VYQGPRDHILE 427
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
431-582 |
7.95e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 54.36 E-value: 7.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 431 LDLARMDGFSSDQDLivaLKRFGLDKvikkhprgldmSLGENGLGLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYS 510
Cdd:NF000106 114 LDLSRKDARARADEL---LERFSLTE-----------AAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRT 179
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1437745540 511 EIQALNAISAWCR--SKTLLVVTHRPQVLSIVNRIIVVDNGKVVMDGPRDAvLQQLAKNETEKQITAHSKNQNR 582
Cdd:NF000106 180 RNEVWDEVRSMVRdgATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDE-LKTKVGGRTLQIRPAHAAELDR 252
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
353-575 |
1.77e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.78 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 353 VKIL---SFEIKPGEKVGILGRIGSGKSTTLKLAAGLYP--AEQGSITLDDVDIRqidPHYLRN----------QVLLLE 417
Cdd:PRK13549 18 VKALdnvSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELQ---ASNIRDteragiaiihQELALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 418 QE----PRLFLGslRENLDLARMDgfssDQDLIVALKRFgLDKVikkhprGLDMSLGENGLGLSGGQKQIVALARMTLRN 493
Cdd:PRK13549 95 KElsvlENIFLG--NEITPGGIMD----YDAMYLRAQKL-LAQL------KLDINPATPVGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 494 PKIVLLDEPTTGLDQySEIQALNAISAWCRSK--TLLVVTHR-PQVLSIVNRIIVVDNGKVVMDGPrdavlqqlAKNETE 570
Cdd:PRK13549 162 ARLLILDEPTASLTE-SETAVLLDIIRDLKAHgiACIYISHKlNEVKAISDTICVIRDGRHIGTRP--------AAGMTE 232
|
....*
gi 1437745540 571 KQITA 575
Cdd:PRK13549 233 DDIIT 237
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
336-507 |
2.85e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 53.40 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYnqDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITL-DDVDIRQIDphylrnqvl 414
Cdd:TIGR03719 323 IEAENLTKAF--GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKLAYVD--------- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 415 lleQEprlflgslRENLDLAR--MDGFSSDQDLIVA----------LKRFGLdkvikkhpRGLDMS--LGEnglgLSGGQ 480
Cdd:TIGR03719 392 ---QS--------RDALDPNKtvWEEISGGLDIIKLgkreipsrayVGRFNF--------KGSDQQkkVGQ----LSGGE 448
|
170 180
....*....|....*....|....*..
gi 1437745540 481 KQIVALARMTLRNPKIVLLDEPTTGLD 507
Cdd:TIGR03719 449 RNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
360-506 |
3.63e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.81 E-value: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 360 IKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIR-QIDPHYLRNQVLLLEQEPRLFLG-SLRENLDLAR-- 435
Cdd:PRK10982 21 VRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQELNLVLQrSVMDNMWLGRyp 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1437745540 436 MDGFSSDQDlivalKRFGLDKVIKKHpRGLDMSLGENGLGLSGGQKQIVALARMTLRNPKIVLLDEPTTGL 506
Cdd:PRK10982 101 TKGMFVDQD-----KMYRDTKAIFDE-LDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
359-550 |
4.06e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 50.26 E-value: 4.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 359 EIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIrQIDPHYLRnqvllleqeprlflgslrenldlarmdg 438
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP-VYKPQYID---------------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 439 fssdqdlivalkrfgldkvikkhprgldmslgenglgLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAI 518
Cdd:cd03222 72 -------------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAI 114
|
170 180 190
....*....|....*....|....*....|....
gi 1437745540 519 SAWCR--SKTLLVVTHRPQVLSIVNRIIVVDNGK 550
Cdd:cd03222 115 RRLSEegKKTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
353-556 |
4.90e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 52.05 E-value: 4.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 353 VKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGL--YP----AEQgsITLDDVDIRQIDPHYLRN----QVLLLEQEPRl 422
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidYPgrvmAEK--LEFNGQDLQRISEKERRNlvgaEVAMIFQDPM- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 423 flgslrENLDLARMDGFSsdqdLIVALKRFGLDKVIKKHPRGLDMsLGENGL------------GLSGGQKQIVALARMT 490
Cdd:PRK11022 100 ------TSLNPCYTVGFQ----IMEAIKVHQGGNKKTRRQRAIDL-LNQVGIpdpasrldvyphQLSGGMSQRVMIAMAI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745540 491 LRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSK--TLLVVTHR-PQVLSIVNRIIVVDNGKVVMDGP 556
Cdd:PRK11022 169 ACRPKLLIADEPTTALDVTIQAQIIELLLELQQKEnmALVLITHDlALVAEAAHKIIVMYAGQVVETGK 237
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
29-303 |
6.63e-07 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 51.28 E-value: 6.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 29 FLALVSSLYVMNVYDRVIPNKS-YQTLWVLSIGVIIAILFEFTAKMLRGRltdiAGKKADLIISSALFRKVTNLKLQE-K 106
Cdd:cd18551 13 AASLAQPLLVKNLIDALSAGGSsGGLLALLVALFLLQAVLSALSSYLLGR----TGERVVLDLRRRLWRRLLRLPVSFfD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 107 PISSG---SYVNNlrDFESVRDFMTSasllTLVDmpfliLFVSVIALVGG-YLAFV---PLTIIPLVII-VGLLAQIPLS 178
Cdd:cd18551 89 RRRSGdlvSRVTN--DTTLLRELITS----GLPQ-----LVTGVLTVVGAvVLMFLldwVLTLVTLAVVpLAFLIILPLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 179 KYINesmKESSQRQ-------GLAVEAIEGIETLKTNNAMNWAQKRWDYYTAKTASSSMKVKNISNFVIYFAVMMQQLNT 251
Cdd:cd18551 158 RRIR---KASKRAQdalgelsAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLAL 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1437745540 252 IFLVIIGTYLIHSDDpaskITMGALIATVILSGRALSPLGQIAGLAVRFQQA 303
Cdd:cd18551 235 LVVLGVGGARVASGA----LTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKA 282
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
140-303 |
7.46e-07 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 51.32 E-value: 7.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 140 FLILFVS--VIALVGGY-LAFVPLTIIPLVIIVGLLAQIPLSKYINESMKESSQRQGLAVEAIEGIETLKTNNAMNWAQK 216
Cdd:cd18577 131 SLSTFIAgfIIAFIYSWkLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIK 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 217 RWDYYTAKTASSSMKVKNISNF---VIYFAVMmqqLNTIFLVIIGTYLIHSDdpasKITMGALIATV--ILSGrALSpLG 291
Cdd:cd18577 211 RYSKALEKARKAGIKKGLVSGLglgLLFFIIF---AMYALAFWYGSRLVRDG----EISPGDVLTVFfaVLIG-AFS-LG 281
|
170
....*....|..
gi 1437745540 292 QIAGLAVRFQQA 303
Cdd:cd18577 282 QIAPNLQAFAKA 293
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
21-306 |
2.46e-06 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 49.31 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 21 ILATFVINFLALVSSLYVMNVYDRVI--PNKSYQTLWVLSIGVIIAILFEFTAKMLRGRLTDIAGKKADLIISSALFRKV 98
Cdd:cd18544 5 LLLLLLATALELLGPLLIKRAIDDYIvpGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 99 TNLKLQ---EKPIssGSYVNNL-RDFESVRDFMTSASLLTLVDMPFLILFVSVIALVGGYLAFVPLTIIPLVIIVGLLAQ 174
Cdd:cd18544 85 QRLPLSffdRTPV--GRLVTRVtNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 175 iplsKYINESMKESsqRQGLAV------EAIEGIETLKTNNAMNWAQKRWD-----YYTAKtasssmkVKNISNFVIYFA 243
Cdd:cd18544 163 ----KKSRKAYREV--REKLSRlnaflqESISGMSVIQLFNREKREFEEFDeinqeYRKAN-------LKSIKLFALFRP 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437745540 244 VM--MQQLNTIFLVIIGTYLIHSDDpaskITMGALIATVILSGRALSPLGQIAGLAVRFQQAWVA 306
Cdd:cd18544 230 LVelLSSLALALVLWYGGGQVLSGA----VTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMAS 290
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
356-559 |
2.91e-06 |
|
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: 50.21 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 356 LSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYP--AEQGSITLDDVD-----IRQIDphylRNQVLLLEQEPRLFLG-SL 427
Cdd:TIGR02633 20 IDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPlkasnIRDTE----RAGIVIIHQELTLVPElSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 428 RENLDLAR---MDGFSSDQDLIVaLKRFGLDKVIKKHPRGLDMSLGENGlglsGGQKQIVALARMTLRNPKIVLLDEPTT 504
Cdd:TIGR02633 96 AENIFLGNeitLPGGRMAYNAMY-LRAKNLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745540 505 GLDQySEIQALNAISAWCRSKTL--LVVTHR-PQVLSIVNRIIVVDNGKVVmdGPRDA 559
Cdd:TIGR02633 171 SLTE-KETEILLDIIRDLKAHGVacVYISHKlNEVKAVCDTICVIRDGQHV--ATKDM 225
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
363-552 |
3.64e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.86 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 363 GEKVGILGRIGSGKSTTLKLAA-----------GLYPAEQgSITLDDVDIRQ--IDPHYLRNQVL-----LLEQEPRLFL 424
Cdd:PLN03073 203 GRHYGLVGRNGTGKTTFLRYMAmhaidgipkncQILHVEQ-EVVGDDTTALQcvLNTDIERTQLLeeeaqLVAQQRELEF 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 425 GSLRENLDLARMDGFSSD---QDLIVALKRFGLDKVIKKHPR------GL----DMSLGENGLgLSGGQKQIVALARMTL 491
Cdd:PLN03073 282 ETETGKGKGANKDGVDKDavsQRLEEIYKRLELIDAYTAEARaasilaGLsftpEMQVKATKT-FSGGWRMRIALARALF 360
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1437745540 492 RNPKIVLLDEPTTGLDQYSEIQALNAISAWcrSKTLLVVTHRPQVL-SIVNRIIVVDNGKVV 552
Cdd:PLN03073 361 IEPDLLLLDEPTNHLDLHAVLWLETYLLKW--PKTFIVVSHAREFLnTVVTDILHLHGQKLV 420
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
360-552 |
4.75e-06 |
|
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: 47.62 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 360 IKPGEKVGILGRIGSGKSTTLKLAAGlyPAEQGSITLD-DVDIRQIDPHYLRnQVLLLEQEPrLFLGSL--RENLDlarm 436
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVITGEiLINGRPLDKNFQR-STGYVEQQD-VHSPNLtvREALR---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 437 dgFSsdqdlivALKRfgldkvikkhprgldmslgenglGLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQ---YSEIQ 513
Cdd:cd03232 102 --FS-------ALLR-----------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSqaaYNIVR 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1437745540 514 ALNAISAwcRSKTLLVVTHRP--QVLSIVNRIIVVD-NGKVV 552
Cdd:cd03232 150 FLKKLAD--SGQAILCTIHQPsaSIFEKFDRLLLLKrGGKTV 189
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
362-549 |
5.30e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 46.60 E-value: 5.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 362 PGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLRNQVLlleqeprlflgslrenldlarmdgfss 441
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 442 dqdlivalkrfgldkvikkhprgldmsLGENGLGLSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAW 521
Cdd:smart00382 54 ---------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELR 106
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1437745540 522 -------CRSKTLLVVTHRPQVL------SIVNRIIVVDNG 549
Cdd:smart00382 107 lllllksEKNLTVILTTNDEKDLgpallrRRFDRRIVLLLI 147
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
353-555 |
5.55e-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: 46.93 E-value: 5.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 353 VKILSFEIKPGEKVGILGRIGSGKSTTLKlaAGLYPAEQGSITLDDvdirqidPHYLRNQVLlleqeprlFLGSLRENLD 432
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYASGKARLISFL-------PKFSRNKLI--------FIDQLQFLID 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 433 LarmdgfssdqdlivalkrfgldkvikkhprGLD-MSLGENGLGLSGGQKQIVALARMTLRNPK--IVLLDEPTTGLDQY 509
Cdd:cd03238 74 V------------------------------GLGyLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQ 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1437745540 510 SEIQALNAISAWCRSK-TLLVVTHRPQVLSIVNRIIVV------DNGKVVMDG 555
Cdd:cd03238 124 DINQLLEVIKGLIDLGnTVILIEHNLDVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
476-569 |
8.55e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.47 E-value: 8.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 476 LSGGQKQIVALARMTLRNPKIVLLDEPTTGLDQYSEIQALNAISAWCRSK-TLLVVTHR-PQVLSIVNRIIVVDNGKVVM 553
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGiTLVLVLNRfDEIPDFVQFAGVLADCTLAE 215
|
90 100
....*....|....*....|.
gi 1437745540 554 DGPRDAVLQ-----QLAKNET 569
Cdd:PRK10938 216 TGEREEILQqalvaQLAHSEQ 236
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
356-507 |
9.82e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.47 E-value: 9.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 356 LSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPaeQG---SITL------DDVDIRQIDPH--YLRNQvllLEQEPRLFL 424
Cdd:PRK10938 279 LSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHP--QGysnDLTLfgrrrgSGETIWDIKKHigYVSSS---LHLDYRVST 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 425 gSLReNLDLArmdGF---------SSDQDLIVA---LKRFGLDKVIKKHPRGldmslgenglGLSGGQKQIVALARMTLR 492
Cdd:PRK10938 354 -SVR-NVILS---GFfdsigiyqaVSDRQQKLAqqwLDILGIDKRTADAPFH----------SLSWGQQRLALIVRALVK 418
|
170
....*....|....*
gi 1437745540 493 NPKIVLLDEPTTGLD 507
Cdd:PRK10938 419 HPTLLILDEPLQGLD 433
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
352-562 |
1.20e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.86 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 352 VVKILSFEIKPGEKVGILGRIGSGKSttlKLAAGLY-----PAEQGSITLDDVDIRQIDPHYLRNQVLLLEQEPRLFLG- 425
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRT---ELAMSVFgrsygRNISGTVFKDGKEVDVSTVSDAIDAGLAYVTEDRKGYGl 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 426 ----SLRENLDLARMDGFSS------DQDLIVAlKRFGLDKVIKKHprgldmSLGENGLGLSGGQKQIVALARMTLRNPK 495
Cdd:NF040905 352 nlidDIKRNITLANLGKVSRrgvideNEEIKVA-EEYRKKMNIKTP------SVFQKVGNLSGGNQQKVVLSKWLFTDPD 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1437745540 496 IVLLDEPTTGLDQ------YSEIQALNAisawcRSKTLLVVTHR-PQVLSIVNRIIVVDNGKVVMDGPRDAVLQ 562
Cdd:NF040905 425 VLILDEPTRGIDVgakyeiYTIINELAA-----EGKGVIVISSElPELLGMCDRIYVMNEGRITGELPREEASQ 493
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
14-304 |
1.21e-05 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 47.44 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 14 KKYYYQIILATFVINFLALVSSLYVMNVYDRVIPNKSYQTLWVLSIGVIIAILFEFTAKMLRGRLTDIAGKK--ADLiiS 91
Cdd:cd18549 1 KKLFFLDLFCAVLIAALDLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARieTDM--R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 92 SALFRKVTNLklqekpisSGSYVNNLRdfesvrdfmtSASLLT-LVDMPFLI----------LFVSVIALVG--GYLAF- 157
Cdd:cd18549 79 RDLFEHLQKL--------SFSFFDNNK----------TGQLMSrITNDLFDIselahhgpedLFISIITIIGsfIILLTi 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 158 -VPLTIIPLVIIVGLLAqipLSKYINESMKESSQRQGLAV--------EAIEGIETLKTNNAMNWAQKRWD-----YYTA 223
Cdd:cd18549 141 nVPLTLIVFALLPLMII---FTIYFNKKMKKAFRRVREKIgeinaqleDSLSGIRVVKAFANEEYEIEKFDegndrFLES 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 224 KTASssmkVKNISNF--VIYFavmMQQLNTIFLVIIGTYLIHSDdpasKITMGALIATVILSGRALSPLGQIAGLAVRFQ 301
Cdd:cd18549 218 KKKA----YKAMAYFfsGMNF---FTNLLNLVVLVAGGYFIIKG----EITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQ 286
|
...
gi 1437745540 302 QAW 304
Cdd:cd18549 287 KGM 289
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
21-303 |
1.55e-05 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 47.09 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 21 ILATFVINFLALVSSLYVMNVYDRVIPNKSYQTLwvLSIGVIIAILFEFTA--KMLRGRLTDIAGKKADLIISSALFRKv 98
Cdd:cd18576 2 LILLLLSSAIGLVFPLLAGQLIDAALGGGDTASL--NQIALLLLGLFLLQAvfSFFRIYLFARVGERVVADLRKDLYRH- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 99 tnlkLQEKPISsgsYVNNLR----------DFESVRDFMTSASLLTLVDMPFLILFVSVIALVGGYLAFVPLTIIPLVII 168
Cdd:cd18576 79 ----LQRLPLS---FFHERRvgeltsrlsnDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 169 VGLL--AQI-PLSKYINESMKESSqrqGLAVEAIEGIETLKTNNAMNWAQKRWDYYTAKTASSSMKVKNISNFVIYFAVM 245
Cdd:cd18576 152 VAVLfgRRIrKLSKKVQDELAEAN---TIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIF 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745540 246 MQQLNTIFLVIIGTYLIHSDDpaskITMGALIATVILSGRALSPLGQIAGLAVRFQQA 303
Cdd:cd18576 229 LLFGAIVAVLWYGGRLVLAGE----LTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKA 282
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
20-303 |
2.00e-05 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 46.63 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 20 IILATFVINFLALVSSLYVMNVYDRVIPNKS------YQTLWVLSIGVIIAILFEFTAKMLRGRLTDIAGKKADLIISSA 93
Cdd:cd18547 4 VIILAIISTLLSVLGPYLLGKAIDLIIEGLGggggvdFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 94 LFRKVTNLklqekPIS------SG---SYVNNlrDFESVRDFMTSA------SLLTLVDMPFLILFVSVI-ALVGgyLAF 157
Cdd:cd18547 84 LFEKLQRL-----PLSyfdthsHGdimSRVTN--DVDNISQALSQSltqlisSILTIVGTLIMMLYISPLlTLIV--LVT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 158 VPLTIIpLVIIVGLLAQiplsKYINESMKESSQRQGLAVEAIEGIETLKTNNAMNWAQKRWDYYTAKTASSSMKVKNISN 237
Cdd:cd18547 155 VPLSLL-VTKFIAKRSQ----KYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSG 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745540 238 FVIYFAVMMQQLNTIFLVIIGTYLIHSDdpasKITMGALIATVILSGRALSPLGQIAGLAVRFQQA 303
Cdd:cd18547 230 LLMPIMNFINNLGYVLVAVVGGLLVING----ALTVGVIQAFLQYSRQFSQPINQISQQINSLQSA 291
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
474-544 |
2.40e-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: 45.04 E-value: 2.40e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745540 474 LGLSGGQKQIVALA-RMTLRNPK---IVLLDEPTTGLDQYSEIQALNAISA-WCRSKTLLVVTHRPQVLSIVNRII 544
Cdd:cd03227 76 LQLSGGEKELSALAlILALASLKprpLYILDEIDRGLDPRDGQALAEAILEhLVKGAQVIVITHLPELAELADKLI 151
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
360-544 |
3.53e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.70 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 360 IKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDD-------------VDIRQIDphylrnQVLLLEQEPRlflgS 426
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnqetpaLPQPALE------YVIDGDREYR----Q 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 427 LRENLDLA--RMDGFSsdqdliVALKRFGLDKVIKKHPRGLDMSLgENGLG------------LSGGQKQIVALARMTLR 492
Cdd:PRK10636 94 LEAQLHDAneRNDGHA------IATIHGKLDAIDAWTIRSRAASL-LHGLGfsneqlerpvsdFSGGWRMRLNLAQALIC 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1437745540 493 NPKIVLLDEPTTGLDqyseIQALNAISAWCRS--KTLLVVTHRPQVLS-IVNRII 544
Cdd:PRK10636 167 RSDLLLLDEPTNHLD----LDAVIWLEKWLKSyqGTLILISHDRDFLDpIVDKII 217
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
47-308 |
4.66e-05 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 45.55 E-value: 4.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 47 PNKSYQTLWVLSIGVIIAILFEFTAKMLRGRLTDIAGKKADLIISSALFRKVTNLKLQEKPISSGSYVNNL--RDFESVR 124
Cdd:cd18579 31 PDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRKALRLSSSARQETSTGEIVNLmsVDVQRIE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 125 DFMTSasLLTLVDMPFLILFVSVI--ALVGgYLAFVPLtiipLVIIVGLLAQIPLSKYI----NESMKESSQRQGLAVEA 198
Cdd:cd18579 111 DFFLF--LHYLWSAPLQIIVALYLlyRLLG-WAALAGL----GVLLLLIPLQAFLAKLIsklrKKLMKATDERVKLTNEI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 199 IEGIETLKTNNamnwaqkrW-DYYTAKTASSSMK-VKNISNFVIYFAVMMQQLNTI-FLVIIGTYLIHSddpaskITMGA 275
Cdd:cd18579 184 LSGIKVIKLYA--------WeKPFLKRIEELRKKeLKALRKFGYLRALNSFLFFSTpVLVSLATFATYV------LLGNP 249
|
250 260 270
....*....|....*....|....*....|....*...
gi 1437745540 276 LIATVILSGRAL-----SPLGQIAGLAVRFQQAWVALK 308
Cdd:cd18579 250 LTAAKVFTALSLfnllrFPLLMLPQAISSLIEALVSLK 287
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
336-507 |
7.77e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.49 E-value: 7.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYnqDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITL-DDVDIRQIDPHylrnqvl 414
Cdd:PRK11819 325 IEAENLSKSF--GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgETVKLAYVDQS------- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 415 lleqeprlflgslRENLDLARM--DGFSSDQDLIVALK----------RFGLdkvikkhpRGLDMS--LGEnglgLSGGQ 480
Cdd:PRK11819 396 -------------RDALDPNKTvwEEISGGLDIIKVGNreipsrayvgRFNF--------KGGDQQkkVGV----LSGGE 450
|
170 180
....*....|....*....|....*..
gi 1437745540 481 KQIVALARMTLRNPKIVLLDEPTTGLD 507
Cdd:PRK11819 451 RNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
306-582 |
9.87e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.33 E-value: 9.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 306 ALKGVNgiVERPSERE---SARKYITLKQINGNIKF--QNVSfaYNQDSSSVVKILSFEIKPGEKVGILGRIGSGKSTTL 380
Cdd:PRK11147 287 ALKALR--RERSERREvmgTAKMQVEEASRSGKIVFemENVN--YQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 381 KLAAGLYPAEQGSITL-DDVDIRQIDPHylrnqvllleqeprlflgslRENLDLAR--MDGFSS-DQDLIValkrfgldk 456
Cdd:PRK11147 363 KLMLGQLQADSGRIHCgTKLEVAYFDQH--------------------RAELDPEKtvMDNLAEgKQEVMV--------- 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 457 vikkhprgldmslgeNG-----LG------------------LSGGQKQIVALARMTLRNPKIVLLDEPTTGLDqyseIQ 513
Cdd:PRK11147 414 ---------------NGrprhvLGylqdflfhpkramtpvkaLSGGERNRLLLARLFLKPSNLLILDEPTNDLD----VE 474
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437745540 514 ALNAISAWCRS--KTLLVVTHRPQVL--SIVNRIIVVDNGKV--VMDGPRDAVlQQLAKNETEKQITAHSKNQNR 582
Cdd:PRK11147 475 TLELLEELLDSyqGTVLLVSHDRQFVdnTVTECWIFEGNGKIgrYVGGYHDAR-QQQAQYLALKQPAVKKKEEAA 548
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
21-310 |
1.04e-04 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 44.33 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 21 ILATFVINFL----ALVSSLYVMNVYDRVIPN-------KSYQTLWVLSIGVIIAILFEFTAKMLRGRLTDIAGKKADLI 89
Cdd:cd18554 1 IIITIVIGLVrfgiPLLLPLILKYIVDDVIQGssltldeKVYKLFTIIGIMFFIFLILRPPVEYYRQYFAQWIANKILYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 90 ISSALFRKVTNLKLQ----EKPISSGSYVNNlrDFESVRDFMTSASLLTLVDMPFLILFVSVIALVGGYLAFVPLTIIPL 165
Cdd:cd18554 81 IRKDLFDHLQKLSLRyyanNRSGEIISRVIN--DVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 166 VIIVGLLAQIPLSKYINESMKESSQRQGLAVEAIEGIETLKTNNAMNWAQKRWDYYTAKTASSSMKVKNISNFVIYFAVM 245
Cdd:cd18554 159 YILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVNT 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437745540 246 MQQLNTIFLVIIGTYLIHSddpaSKITMGALIATVILSGRALSPLGQIAGLAVRFQQAWVALKGV 310
Cdd:cd18554 239 ITDLAPLLVIGFAAYLVIE----GNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
119-306 |
3.51e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 42.88 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 119 DFESVRDFMTSASLLTLVDMPFLILFVSVIALVGGYLAFVPLTIIPLViivgLLAQIPLSKYINESMKESSQRQG----L 194
Cdd:cd18564 120 DVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIALAVAPLL----LLAARRFSRRIKEASREQRRREGalasV 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 195 AVEAIEGIETLKTNNAMNWAQKRWDYYTAKTASSSMKVKNISN---------------FVIYFAVMmqqlntifLVIIGT 259
Cdd:cd18564 196 AQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQAllspvvdvlvavgtaLVLWFGAW--------LVLAGR 267
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1437745540 260 ylihsddpaskITMGALIATVILSGRALSPLGQIAGLAVRFQQAWVA 306
Cdd:cd18564 268 -----------LTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASAS 303
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
21-307 |
5.13e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 42.48 E-value: 5.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 21 ILATFVINFLALVSSLYVMNVYDRVIPNKSYQTLWVLSIGVIIAILFEFTAKMLRGRLTDIAGKKADLIISSALFRKVTN 100
Cdd:cd18546 5 LLLVVVDTAASLAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 101 LKLQ----EKpisSGSYVNNL-RDFESVRDFMTSaSLLTLVDMPFLILFVSVIALV-GGYLAFVPLTIIPLVIIVGLLAQ 174
Cdd:cd18546 85 LSLDfherET---SGRIMTRMtSDIDALSELLQT-GLVQLVVSLLTLVGIAVVLLVlDPRLALVALAALPPLALATRWFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 175 IPLSKYINESMKESSQRQGLAVEAIEGIETLKTNNAMNWAQKR-----WDYYTAKTASssmkVKNISnfvIYFAVMM--Q 247
Cdd:cd18546 161 RRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERfaelsDDYRDARLRA----QRLVA---IYFPGVEllG 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 248 QLNTIFLVIIGTYLIHSDDpaskITMGALIATVILSGRALSPLGQIAGLAVRFQQAWVAL 307
Cdd:cd18546 234 NLATAAVLLVGAWRVAAGT----LTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAAL 289
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
464-515 |
6.34e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 41.83 E-value: 6.34e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745540 464 GLD-MSLGENGLGLSGGQKQIVALARMTLR---NPKIVLLDEPTTGLdQYSEIQAL 515
Cdd:cd03271 157 GLGyIKLGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGL-HFHDVKKL 211
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
360-507 |
8.94e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.40 E-value: 8.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 360 IKPGEKVGILGRIGSGKSTTLKLAAGlyPAEQGSITLDD--VDIRQIDPHYLRNQVLLLEQEPRLFLGSLRENLDL-ARM 436
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVITGGDrlVNGRPLDSSFQRSIGYVQQQDLHLPTSTVRESLRFsAYL 863
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745540 437 dgfSSDQDLIVALKRFGLDKVIKKhprgLDMS------LGENGLGLSGGQKQIVALARMTLRNPK-IVLLDEPTTGLD 507
Cdd:TIGR00956 864 ---RQPKSVSKSEKMEYVEEVIKL----LEMEsyadavVGVPGEGLNVEQRKRLTIGVELVAKPKlLLFLDEPTSGLD 934
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
28-303 |
1.23e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 41.01 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 28 NFLALVSSL-------YVMNVYDRVIPNKSYQTLWVLSIGVIIAILFEFTAKMLRGRLTDIAGKKADLIISSALFRKVTN 100
Cdd:cd18557 2 LLFLLISSAaqlllpyLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 101 lklqeKPIS------SGSYVNNL-RDFESVRDFMTSA------SLLTLVDMPFLILFVSVIalvggyLAFVPLTIIPLVI 167
Cdd:cd18557 82 -----QEIAffdkhkTGELTSRLsSDTSVLQSAVTDNlsqllrNILQVIGGLIILFILSWK------LTLVLLLVIPLLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 168 IVGLL--AQI-PLSKYINESMKESSQrqgLAVEAIEGIETLKTNNAMNWAQKRWDYYTAKTASSSMK-------VKNISN 237
Cdd:cd18557 151 IASKIygRYIrKLSKEVQDALAKAGQ---VAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKkalanalFQGITS 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745540 238 FVIYFAvmmqqlntIFLVI-IGTYLIHSddpaSKITMGALIATVILSGRALSPLGQIAGLAVRFQQA 303
Cdd:cd18557 228 LLIYLS--------LLLVLwYGGYLVLS----GQLTVGELTSFILYTIMVASSVGGLSSLLADIMKA 282
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
336-508 |
1.40e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 40.24 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 336 IKFQNVSFAYNQdssSVVKILSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGSITLDDVDIRQIDPHYLR--NQV 413
Cdd:PRK13541 2 LSLHQLQFNIEQ---KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTyiGHN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 414 LLLEQEPRLFlgslrENLDLARmDGFSSDQDLIVALKRFGLDKVikkhprgldmsLGENGLGLSGGQKQIVALARMTLRN 493
Cdd:PRK13541 79 LGLKLEMTVF-----ENLKFWS-EIYNSAETLYAAIHYFKLHDL-----------LDEKCYSLSSGMQKIVAIARLIACQ 141
|
170
....*....|....*
gi 1437745540 494 PKIVLLDEPTTGLDQ 508
Cdd:PRK13541 142 SDLWLLDEVETNLSK 156
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
109-319 |
1.61e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 40.90 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 109 SSGSYVNNL-RDFESVRDfMTSASLLTLVDMPFLILFVSVIALVGGY-LAFVPLTIIPLVIIVGLLAQIPLSKY---INE 183
Cdd:cd18578 109 STGALTSRLsTDASDVRG-LVGDRLGLILQAIVTLVAGLIIAFVYGWkLALVGLATVPLLLLAGYLRMRLLSGFeekNKK 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 184 SMKESSQrqgLAVEAIEGIETLKTNNAMNWAQKRWDYYTAKTASSSMKVKNISNFVIYFAVMMQQLNTIFLVIIGTYLIH 263
Cdd:cd18578 188 AYEESSK---IASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVA 264
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745540 264 SDdpasKITMGALIAT---VILSGRAlspLGQIAGLAVRFQQAWVALKGVNGIVERPSE 319
Cdd:cd18578 265 NG----EYTFEQFFIVfmaLIFGAQS---AGQAFSFAPDIAKAKAAAARIFRLLDRKPE 316
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
354-544 |
2.32e-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: 39.93 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 354 KILSFEIKPGEKVGILGRIGSGKSTtlkLAAGLYPAEQGSITLDDVD--IRQIDPHYLRNQVLLLE-------------- 417
Cdd:cd03270 12 KNVDVDIPRNKLVVITGVSGSGKSS---LAFDTIYAEGQRRYVESLSayARQFLGQMDKPDVDSIEglspaiaidqktts 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 418 QEPRLFLGSLRENLDLARM----DGfssdqdlIVALKRFGLDKvikkhprGLD-MSLGENGLGLSGGQKQIVALARMTLR 492
Cdd:cd03270 89 RNPRSTVGTVTEIYDYLRLlfarVG-------IRERLGFLVDV-------GLGyLTLSRSAPTLSGGEAQRIRLATQIGS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745540 493 NPKIVL--LDEPTTGLDQySEIQALNAISAWCRSK--TLLVVTHRPQVLSIVNRII 544
Cdd:cd03270 155 GLTGVLyvLDEPSIGLHP-RDNDRLIETLKRLRDLgnTVLVVEHDEDTIRAADHVI 209
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
467-506 |
2.41e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.77 E-value: 2.41e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1437745540 467 MSLGENGLGLSGGQKQIVALARMTLR---NPKIVLLDEPTTGL 506
Cdd:TIGR00630 821 IRLGQPATTLSGGEAQRIKLAKELSKrstGRTLYILDEPTTGL 863
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
114-303 |
2.61e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 40.24 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 114 VNNLRDF--ESVRDFMTSASLLTLVdmpFLILFvsviaLVGGYLAFVPLTIIPLVIIVGLLAQIPLS-KYinESMKESSQ 190
Cdd:cd18565 121 VNQLERFldDGANSIIRVVVTVLGI---GAILF-----YLNWQLALVALLPVPLIIAGTYWFQRRIEpRY--RAVREAVG 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 191 RQGLAVE-AIEGIETLKTNNAMNWAQKR-----WDYYTAKTASSsmKVKNISNFVIYFAVMmqqLNTIFLVIIGTYLIHS 264
Cdd:cd18565 191 DLNARLEnNLSGIAVIKAFTAEDFERERvadasEEYRDANWRAI--RLRAAFFPVIRLVAG---AGFVATFVVGGYWVLD 265
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1437745540 265 DDPA--SKITMGALIATVILSGRALSPLGQIAGLAVRFQQA 303
Cdd:cd18565 266 GPPLftGTLTVGTLVTFLFYTQRLLWPLTRLGDLIDQYQRA 306
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
332-394 |
4.79e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 39.87 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745540 332 INGNIKFQNVSFAYNQDSSSVVKI------------------LSFEIKPGEKVGILGRIGSGKSTTLKLAAGLYPAEQGS 393
Cdd:PRK13545 1 MNYKVKFEHVTKKYKMYNKPFDKLkdlffrskdgeyhyalnnISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGT 80
|
.
gi 1437745540 394 I 394
Cdd:PRK13545 81 V 81
|
|
| |
