|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-554 |
0e+00 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 1209.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 1 MAQYVYTMHRVGKIVPPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARPMPGINVGYLPQEPKL 80
Cdd:PRK11819 2 MAQYIYTMNRVSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 81 DPQATVRDIVEEAVGQIKQAQARLDEVYAAYAEPDADFDALAAEQAKLEAILQASDGHNLERQLEVAADALRLPPWDAKV 160
Cdd:PRK11819 82 DPEKTVRENVEEGVAEVKAALDRFNEIYAAYAEPDADFDALAAEQGELQEIIDAADAWDLDSQLEIAMDALRCPPWDAKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 161 EHLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPGTVVAITHDRYFLDNVAGWILELDRGHGIPF 240
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPW 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 241 EGNYSGWLESKAARLAQEAKQEASHAKAMKAELEWVRQGAKGRQAKSKARLQRFEELQSQEFQKRSETNEIYIPAGPRLG 320
Cdd:PRK11819 242 EGNYSSWLEQKAKRLAQEEKQEAARQKALKRELEWVRQSPKARQAKSKARLARYEELLSEEYQKRNETNEIFIPPGPRLG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 321 DKVIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETVQIASVDQSRDSLEG 400
Cdd:PRK11819 322 DKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRDALDP 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 401 NKTVWEQVSDGFEQIKIGNYEVPSRSYVGRFNFKGADQQKFVKDLSGGERGRLHLALTLKQGGNVLLLDEPSNDLDVETL 480
Cdd:PRK11819 402 NKTVWEEISGGLDIIKVGNREIPSRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETL 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599791 481 RALEEALLDFPGAAIVISHDRWFLDRIATHILSYEDDGKVTFFEGNYTEFEADRKKRLGDAASQPHRVRYKKLA 554
Cdd:PRK11819 482 RALEEALLEFPGCAVVISHDRWFLDRIATHILAFEGDSQVEWFEGNFQEYEEDKKRRLGADAARPHRIKYKKLT 555
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-553 |
0e+00 |
|
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: 1143.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 2 AQYVYTMHRVGKIVPPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARPMPGINVGYLPQEPKLD 81
Cdd:TIGR03719 1 AQYIYTMNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 82 PQATVRDIVEEAVGQIKQAQARLDEVYAAYAEPDADFDALAAEQAKLEAILQASDGHNLERQLEVAADALRLPPWDAKVE 161
Cdd:TIGR03719 81 PTKTVRENVEEGVAEIKDALDRFNEISAKYAEPDADFDKLAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPPWDADVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 162 HLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPGTVVAITHDRYFLDNVAGWILELDRGHGIPFE 241
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 242 GNYSGWLESKAARLAQEAKQEASHAKAMKAELEWVRQGAKGRQAKSKARLQRFEELQSQEFQKRSETNEIYIPAGPRLGD 321
Cdd:TIGR03719 241 GNYSSWLEQKQKRLEQEEKEESARQKTLKRELEWVRQSPKGRQAKSKARLARYEELLSQEFQKRNETAEIYIPPGPRLGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 322 KVIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETVQIASVDQSRDSLEGN 401
Cdd:TIGR03719 321 KVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDALDPN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 402 KTVWEQVSDGFEQIKIGNYEVPSRSYVGRFNFKGADQQKFVKDLSGGERGRLHLALTLKQGGNVLLLDEPSNDLDVETLR 481
Cdd:TIGR03719 401 KTVWEEISGGLDIIKLGKREIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLR 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599791 482 ALEEALLDFPGAAIVISHDRWFLDRIATHILSYEDDGKVTFFEGNYTEFEADRKKRLGDAASQPHRVRYKKL 553
Cdd:TIGR03719 481 ALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGDSHVEWFEGNFSEYEEDKKRRLGEDADQPHRIKYKKL 552
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-533 |
0e+00 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 729.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 8 MHRVGKIVPpKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARPMPGINVGYLPQEPKLDPQATVR 87
Cdd:COG0488 1 LENLSKSFG-GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 88 DIVEEAVGQIKQAQARLDEVYAAYAEPDADFDALAAEQAKLEAIlqasDGHNLERQLEVAADALRLP--PWDAKVEHLSG 165
Cdd:COG0488 80 DTVLDGDAELRALEAELEELEAKLAEPDEDLERLAELQEEFEAL----GGWEAEARAEEILSGLGFPeeDLDRPVSELSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 166 GEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPGTVVAITHDRYFLDNVAGWILELDRGHGIPFEGNYS 245
Cdd:COG0488 156 GWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 246 GWLESKAARLAQEAKQEASHAKAMKAELEWVRQ-GAKGRQAK-SKARLQRFEELQSQEFQKRSETNEIYIPAGPRLGDKV 323
Cdd:COG0488 236 AYLEQRAERLEQEAAAYAKQQKKIAKEEEFIRRfRAKARKAKqAQSRIKALEKLEREEPPRRDKTVEIRFPPPERLGKKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETVQIASVDQSRDSLEGNKT 403
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELDPDKT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 404 VWEQVSDGFEqikiGNYEVPSRSYVGRFNFKGADQQKFVKDLSGGERGRLHLALTLKQGGNVLLLDEPSNDLDVETLRAL 483
Cdd:COG0488 396 VLDELRDGAP----GGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEAL 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 15599791 484 EEALLDFPGAAIVISHDRWFLDRIATHILSYEdDGKVTFFEGNYTEFEAD 533
Cdd:COG0488 472 EEALDDFPGTVLLVSHDRYFLDRVATRILEFE-DGGVREYPGGYDDYLEK 520
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
31-527 |
2.24e-110 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 342.70 E-value: 2.24e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 31 PGAKIGVLGLNGAGKSTLLRIMAGvdtEI---EGEARPMPGINVGYLPQEPKLDPQATVRDIVEEAVG----QIKQAQAR 103
Cdd:PRK11147 28 DNERVCLVGRNGAGKSTLMKILNG---EVlldDGRIIYEQDLIVARLQQDPPRNVEGTVYDFVAEGIEeqaeYLKRYHDI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 104 LDEVYAAYAEpdadfdALAAEQAKLEAILQASDGHNLERQLEVAADALRLPPwDAKVEHLSGGEKRRVALCRLLLSAPDM 183
Cdd:PRK11147 105 SHLVETDPSE------KNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDP-DAALSSLSGGWLRKAALGRALVSNPDV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 184 LLLDEPTNHLDADSVAWLEHFLHDFPGTVVAITHDRYFLDNVAGWILELDRGHGIPFEGNYSGWLESKAARLAQEAKQEA 263
Cdd:PRK11147 178 LLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYLLEKEEALRVEELQNA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 264 SHAKAMKAELEWVRQGAKGRQAKSKARLQRFEELQsQEFQKRSE---TNEIYIPAGPRLGDKVIELHNVTKGYGDRVLID 340
Cdd:PRK11147 258 EFDRKLAQEEVWIRQGIKARRTRNEGRVRALKALR-RERSERREvmgTAKMQVEEASRSGKIVFEMENVNYQIDGKQLVK 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 341 NLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETVQIASVDQSRDSLEGNKTVWEQVSDGFEQIKIGNY 420
Cdd:PRK11147 337 DFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELDPEKTVMDNLAEGKQEVMVNGR 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 421 EVPSRSYVGRFNFKGADQQKFVKDLSGGERGRLHLALTLKQGGNVLLLDEPSNDLDVETLRALEEALLDFPGAAIVISHD 500
Cdd:PRK11147 417 PRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHD 496
|
490 500
....*....|....*....|....*..
gi 15599791 501 RWFLDRIATHILSYEDDGKVTFFEGNY 527
Cdd:PRK11147 497 RQFVDNTVTECWIFEGNGKIGRYVGGY 523
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
25-534 |
1.47e-84 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 272.15 E-value: 1.47e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 25 ISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARPMPGINVGYLPQEPKLDPQATVRDIV---EEAVGQIKQAQ 101
Cdd:PRK15064 20 ISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFTVLDTVimgHTELWEVKQER 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 102 ARLdevyaaYAEPDA-DFDALAAeqAKLEAILQASDGHNLERQlevaADALRLPPWDAKVEH------LSGGEKRRVALC 174
Cdd:PRK15064 100 DRI------YALPEMsEEDGMKV--ADLEVKFAEMDGYTAEAR----AGELLLGVGIPEEQHyglmseVAPGWKLRVLLA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 175 RLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPGTVVAITHDRYFLDNVAGWILELDRGHGIPFEGNYSGWLEskAAR 254
Cdd:PRK15064 168 QALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEYMT--AAT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 255 LAQEaKQEASHAK--AMKAEL-EWVRQ----GAKGRQAKSKARlqRFEELQSQEFQKRSETNE-IYIPAGPRLGDKVIEL 326
Cdd:PRK15064 246 QARE-RLLADNAKkkAQIAELqSFVSRfsanASKAKQATSRAK--QIDKIKLEEVKPSSRQNPfIRFEQDKKLHRNALEV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 327 HNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETVQIASVDQ-SRDSLEGNKTV- 404
Cdd:PRK15064 323 ENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQdHAYDFENDLTLf 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 405 -----WEQVSDGfEQIkignyevpSRSYVGRFNFKGADQQKFVKDLSGGERGRLHLALTLKQGGNVLLLDEPSNDLDVET 479
Cdd:PRK15064 403 dwmsqWRQEGDD-EQA--------VRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMES 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 15599791 480 LRALEEALLDFPGAAIVISHDRWFLDRIATHILSYEDDGkVTFFEGNYTEFEADR 534
Cdd:PRK15064 474 IESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDG-VVDFSGTYEEYLRSQ 527
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-545 |
2.66e-74 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 248.16 E-value: 2.66e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGvDTEIEGEARPMPGI-NVGYLPQE-PKLDPQATvrDIVEEAVGQ 96
Cdd:PRK10636 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKN-EISADGGSYTFPGNwQLAWVNQEtPALPQPAL--EYVIDGDRE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 97 IKQAQARLDEvyaayAEPDADFDALAAEQAKLEAIlQA----SDGHNLERQLEVAADALRLPpwdakVEHLSGGEKRRVA 172
Cdd:PRK10636 91 YRQLEAQLHD-----ANERNDGHAIATIHGKLDAI-DAwtirSRAASLLHGLGFSNEQLERP-----VSDFSGGWRMRLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 173 LCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPGTVVAITHDRYFLDNVAGWILELDRGHGIPFEGNYSGWLESKA 252
Cdd:PRK10636 160 LAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 253 ARLAQ-----EAKQE-----ASHAKAMKAelewvrQGAKGRQAKSKAR-LQRFEELQSQ------EFQKRSETNeiyipa 315
Cdd:PRK10636 240 TRLAQqqamyESQQErvahlQSYIDRFRA------KATKAKQAQSRIKmLERMELIAPAhvdnpfHFSFRAPES------ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 316 gprLGDKVIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETVQIASVDQSR 395
Cdd:PRK10636 308 ---LPNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 396 -DSLEGNKTVWEQVSdgfeQIKIGNYEVPSRSYVGRFNFKGADQQKFVKDLSGGERGRLHLALTLKQGGNVLLLDEPSND 474
Cdd:PRK10636 385 lEFLRADESPLQHLA----RLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNH 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599791 475 LDVETLRALEEALLDFPGAAIVISHDRWFLdRIATHILSYEDDGKVTFFEG---NYTEFEADRKKRLGDAASQP 545
Cdd:PRK10636 461 LDLDMRQALTEALIDFEGALVVVSHDRHLL-RSTTDDLYLVHDGKVEPFDGdleDYQQWLSDVQKQENQTDEAP 533
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
326-538 |
6.50e-64 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 217.63 E-value: 6.50e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 326 LHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETVQIASVDQSrDSLEGNKTVW 405
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQE-PPLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 406 EQVSDGFEQIK--------------------------------IGNYEVPSR--SYVGRFNFKGADQQKFVKDLSGGERG 451
Cdd:COG0488 80 DTVLDGDAELRaleaeleeleaklaepdedlerlaelqeefeaLGGWEAEARaeEILSGLGFPEEDLDRPVSELSGGWRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 452 RLHLALTLKQGGNVLLLDEPSNDLDVETLRALEEALLDFPGAAIVISHDRWFLDRIATHILsyE-DDGKVTFFEGNYTEF 530
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRIL--ElDRGKLTLYPGNYSAY 237
|
....*...
gi 15599791 531 EADRKKRL 538
Cdd:COG0488 238 LEQRAERL 245
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
324-518 |
7.90e-55 |
|
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: 181.49 E-value: 7.90e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETVQIASVDQsrdslegnkt 403
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 404 vweqvsdgfeqikignyevpsrsyvgrfnfkgadqqkfvkdLSGGERGRLHLALTLKQGGNVLLLDEPSNDLDVETLRAL 483
Cdd:cd03221 71 -----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEAL 109
|
170 180 190
....*....|....*....|....*....|....*
gi 15599791 484 EEALLDFPGAAIVISHDRWFLDRIATHILSYEDDG 518
Cdd:cd03221 110 EEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
18-236 |
6.56e-49 |
|
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: 166.08 E-value: 6.56e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARPMPGINVGYLPQepkldpqatvrdiveeavgqi 97
Cdd:cd03221 12 GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ--------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 98 kqaqarldevyaayaepdadfdalaaeqakleailqasdghnlerqlevaadalrlppwdakvehLSGGEKRRVALCRLL 177
Cdd:cd03221 71 -----------------------------------------------------------------LSGGEKMRLALAKLL 85
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15599791 178 LSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPGTVVAITHDRYFLDNVAGWILELDRGH 236
Cdd:cd03221 86 LENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
19-531 |
1.16e-47 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 176.97 E-value: 1.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGvdTEIEGEARpmpGINVGYLPQEPK----------LDPQATVRD 88
Cdd:PLN03073 190 RDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAM--HAIDGIPK---NCQILHVEQEVVgddttalqcvLNTDIERTQ 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 89 IVEEAVgQIKQAQARLDEVYAAYAEPDADFDALAAE--QAKLEAI---LQASDGHNLERQLEVAADALRLPP--WDAKVE 161
Cdd:PLN03073 265 LLEEEA-QLVAQQRELEFETETGKGKGANKDGVDKDavSQRLEEIykrLELIDAYTAEARAASILAGLSFTPemQVKATK 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 162 HLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPGTVVAITHDRYFLDNVAGWILELDRGHGIPFE 241
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVTYK 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 242 GNYSGWLESKAARLAQEAKQEASHAKA---MKAELEWVRQGAKgRQAKSKARLQRFEELQSQEFQKRSETNEIYIPA-GP 317
Cdd:PLN03073 424 GDYDTFERTREEQLKNQQKAFESNERSrshMQAFIDKFRYNAK-RASLVQSRIKALDRLGHVDAVVNDPDYKFEFPTpDD 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 318 RLGDKVIELHNVTKGY-GDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETVQIASVDQSR- 395
Cdd:PLN03073 503 RPGPPIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHv 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 396 DSLEGNKTVWEQVSDGFEqikiGNYEVPSRSYVGRFNFKGADQQKFVKDLSGGERGRLHLALTLKQGGNVLLLDEPSNDL 475
Cdd:PLN03073 583 DGLDLSSNPLLYMMRCFP----GVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHL 658
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599791 476 DVETLRALEEALLDFPGAAIVISHDRwfldriatHILSYE-------DDGKVTFFEGNYTEFE 531
Cdd:PLN03073 659 DLDAVEALIQGLVLFQGGVLMVSHDE--------HLISGSvdelwvvSEGKVTPFHGTFHDYK 713
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
19-512 |
2.08e-36 |
|
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: 141.96 E-value: 2.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV---DTEIEGEAR-----------PMPGINVGYLPQEPK--LDP 82
Cdd:COG1123 19 VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLldgrdllelseALRGRRIGMVFQDPMtqLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 83 qATVRDIVEEAVGQI----KQAQARLDEvyaayaepdadfdalAAEQAKLEAILqasdghnlerqlevaadalrlppwDA 158
Cdd:COG1123 99 -VTVGDQIAEALENLglsrAEARARVLE---------------LLEAVGLERRL------------------------DR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 159 KVEHLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLD----ADSVAWLEHFLHDFPGTVVAITHDRYFLDNVAGWILELDR 234
Cdd:COG1123 139 YPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 235 GhgipfegnysgwleskaarlaqeakqeashakamkaelEWVRQGAKGRQAKSKARLQRFEELQSQEFQKrsetneiyiP 314
Cdd:COG1123 219 G--------------------------------------RIVEDGPPEEILAAPQALAAVPRLGAARGRA---------A 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 315 AGPRLGDKVIELHNVTKGY-----GDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQI 388
Cdd:COG1123 252 PAAAAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFdGKDLTK 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 389 ASVDQSRD--------------SLEGNKTVWEQVSDGFEQIKIGNY-EVPSR--SYVGRFNFKGADQQKFVKDLSGGERG 451
Cdd:COG1123 332 LSRRSLRElrrrvqmvfqdpysSLNPRMTVGDIIAEPLRLHGLLSRaERRERvaELLERVGLPPDLADRYPHELSGGQRQ 411
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599791 452 RLHLALTLKQGGNVLLLDEPSNDLDVET----LRALEEALLDFPGAAIVISHDRWFLDRIATHIL 512
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALDVSVqaqiLNLLRDLQRELGLTYLFISHDLAVVRYIADRVA 476
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
19-236 |
3.42e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 131.09 E-value: 3.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEA----RPMPGIN-------VGYLPQEPKLdPQATVR 87
Cdd:COG4619 13 KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIyldgKPLSAMPppewrrqVAYVPQEPAL-WGGTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 88 DIveeavgqikqaqarLDEVYaayaepdaDFDALAAEQAKLEAILQasdghnlerQLEVAADALrlppwDAKVEHLSGGE 167
Cdd:COG4619 92 DN--------------LPFPF--------QLRERKFDRERALELLE---------RLGLPPDIL-----DKPVERLSGGE 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599791 168 KRRVALCRLLLSAPDMLLLDEPTNHLDADS----VAWLEHFLHDFPGTVVAITHDRYFLDNVAGWILELDRGH 236
Cdd:COG4619 136 RQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
324-513 |
1.05e-33 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 127.87 E-value: 1.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETV---------QIASVDQ 393
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVlGEDVardpaevrrRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 394 SrDSLEGNKTVWEQVS--DGFEQIKIGNYEVPSRSYVGRFNFKGAdQQKFVKDLSGGERGRLHLALTLKQGGNVLLLDEP 471
Cdd:COG1131 81 E-PALYPDLTVRENLRffARLYGLPRKEARERIDELLELFGLTDA-ADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15599791 472 SNDLDVETLRALEEALLDF--PGAAIVIShdrwfldriaTHILS 513
Cdd:COG1131 159 TSGLDPEARRELWELLRELaaEGKTVLLS----------THYLE 192
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
19-225 |
4.31e-33 |
|
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: 125.28 E-value: 4.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGE----------ARPMPGINVGYLPQEPKLDPQATVRD 88
Cdd:COG4133 15 RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEvlwngepirdAREDYRRRLAYLGHADGLKPELTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 89 IVeeavgqikQAQARLDEVYAAYAEPDAdfdalaaeqakleailqasdghnlerqlevAADALRLPP-WDAKVEHLSGGE 167
Cdd:COG4133 95 NL--------RFWAALYGLRADREAIDE------------------------------ALEAVGLAGlADLPVRQLSAGQ 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599791 168 KRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFP---GTVVAITHDRYFLDNV 225
Cdd:COG4133 137 KRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELAAA 197
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-191 |
2.27e-32 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 121.60 E-value: 2.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGE-----------ARPMPGINVGYLPQEPKLDPQATVRDIV 90
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTilldgqdltddERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 91 EEAvgqikqaqarldevyaayaepdadfdalaaeqakleAILQASDGHNLERQLEVAADALRLP-----PWDAKVEHLSG 165
Cdd:pfam00005 81 RLG------------------------------------LLLKGLSKREKDARAEEALEKLGLGdladrPVGERPGTLSG 124
|
170 180
....*....|....*....|....*.
gi 15599791 166 GEKRRVALCRLLLSAPDMLLLDEPTN 191
Cdd:pfam00005 125 GQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
18-236 |
2.59e-32 |
|
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: 123.35 E-value: 2.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpMPGIN------------VGYLPQEPklDPQ-- 83
Cdd:cd03225 13 ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVL-VDGKDltklslkelrrkVGLVFQNP--DDQff 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 84 -ATVRDiveeavgqikqaqarldEVyaayaepdadfdALAAEQAKLeailqasDGHNLERQLEVAADALRLPPW-DAKVE 161
Cdd:cd03225 90 gPTVEE-----------------EV------------AFGLENLGL-------PEEEIEERVEEALELVGLEGLrDRSPF 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599791 162 HLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPG---TVVAITHDRYFLDNVAGWILELDRGH 236
Cdd:cd03225 134 TLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
324-512 |
3.84e-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: 121.74 E-value: 3.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQIASVDQSR------- 395
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlGKDIKKEPEEVKRrigylpe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 396 -DSLEGNKTVWEQVsdgfeqikignyevpsrsyvgrfnfkgadqqkfvkDLSGGERGRLHLALTLKQGGNVLLLDEPSND 474
Cdd:cd03230 81 ePSLYENLTVRENL-----------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSG 125
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15599791 475 LDVETLRALEEALLDFP--GAAIVI-SHDRWFLDRIATHIL 512
Cdd:cd03230 126 LDPESRREFWELLRELKkeGKTILLsSHILEEAERLCDRVA 166
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
323-532 |
1.16e-31 |
|
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: 122.66 E-value: 1.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 323 VIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETV---------QIASVD 392
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIdGEDVrkeprearrQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 393 QSRDSLEGNkTVWEQVSDGFEQIKIGNYEVPSR--SYVGRFNFkGADQQKFVKDLSGGERGRLHLALTLKQGGNVLLLDE 470
Cdd:COG4555 81 DERGLYDRL-TVRENIRYFAELYGLFDEELKKRieELIELLGL-EEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599791 471 PSNDLDVETLRALEEALLDF--PGAAIVIS-HDRWFLDRIATHILsYEDDGKVTfFEGNYTEFEA 532
Cdd:COG4555 159 PTNGLDVMARRLLREILRALkkEGKTVLFSsHIMQEVEALCDRVV-ILHKGKVV-AQGSLDELRE 221
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
17-218 |
1.62e-31 |
|
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: 122.46 E-value: 1.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 17 PKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEA----RPMPGIN-------VGYLPQEPKLDPQAT 85
Cdd:COG1120 12 GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVlldgRDLASLSrrelarrIAYVPQEPPAPFGLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 86 VRDIVeeavgqikqAQARldevYA---AYAEPDADfDALAAEQAkleailqasdghnLERqLEVAADALRLppwdakVEH 162
Cdd:COG1120 92 VRELV---------ALGR----YPhlgLFGRPSAE-DREAVEEA-------------LER-TGLEHLADRP------VDE 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 163 LSGGEKRRVALCRLLLSAPDMLLLDEPTNHLD-ADSVAWLEHF--LHDFPG-TVVAITHD 218
Cdd:COG1120 138 LSGGERQRVLIARALAQEPPLLLLDEPTSHLDlAHQLEVLELLrrLARERGrTVVMVLHD 197
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
18-236 |
1.97e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 122.12 E-value: 1.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV------DTEIEGEARPMPGINVGYLPQEPKLDPQ--ATVRDI 89
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLlpptsgTVRLFGKPPRRARRRIGYVPQRAEVDWDfpITVRDV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 90 VE----EAVGQIKQAQARldevyaayaepdadfDALAAEQAkleailqasdghnLERqleVAADALRlppwDAKVEHLSG 165
Cdd:COG1121 98 VLmgryGRRGLFRRPSRA---------------DREAVDEA-------------LER---VGLEDLA----DRPIGELSG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599791 166 GEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPG---TVVAITHDRYFLDNVAGWILELDRGH 236
Cdd:COG1121 143 GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVREYFDRVLLLNRGL 216
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
323-512 |
9.85e-31 |
|
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: 120.15 E-value: 9.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 323 VIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETV----------QIASV 391
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLdGRDLaslsrrelarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 392 DQSRDSLEGNkTVWEQVSdgfeqikIGNYevPSRSYVGRFNfkGADQQ----------------KFVKDLSGGERGRLHL 455
Cdd:COG1120 81 PQEPPAPFGL-TVRELVA-------LGRY--PHLGLFGRPS--AEDREaveealertglehladRPVDELSGGERQRVLI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599791 456 ALTLKQGGNVLLLDEPSNDLD----VETLRALEEaLLDFPGAAIVIS-HDrwfLD---RIATHIL 512
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDlahqLEVLELLRR-LARERGRTVVMVlHD---LNlaaRYADRLV 209
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
321-512 |
2.62e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 118.65 E-value: 2.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 321 DKVIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETV-----QIASVDQS 394
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfGKPPrrarrRIGYVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 395 RDSlegNK----TVWEQVSDGFeQIKIGNYEVPSRSY----------VGRFNFkgADQQkfVKDLSGGERGRLHLALTLK 460
Cdd:COG1121 84 AEV---DWdfpiTVRDVVLMGR-YGRRGLFRRPSRADreavdealerVGLEDL--ADRP--IGELSGGQQQRVLLARALA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15599791 461 QGGNVLLLDEPSNDLDVETLRALEEALLDFP--GAAI-VISHDRWFLDRIATHIL 512
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAATEEALYELLRELRreGKTIlVVTHDLGAVREYFDRVL 210
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
325-516 |
3.19e-30 |
|
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: 115.80 E-value: 3.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 325 ELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIgetvqiasvdqsrdslegnktv 404
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILI---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 405 weqvsDGFEQIKIGNYEVpsRSYVGrfnfkgadqqkFVKDLSGGERGRLHLALTLKQGGNVLLLDEPSNDLDVETLRALE 484
Cdd:cd00267 59 -----DGKDIAKLPLEEL--RRRIG-----------YVPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLL 120
|
170 180 190
....*....|....*....|....*....|....*
gi 15599791 485 EALLDFPG---AAIVISHDRWFLDRIATHILSYED 516
Cdd:cd00267 121 ELLRELAEegrTVIIVTHDPELAELAADRVIVLKD 155
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
324-512 |
6.12e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 116.84 E-value: 6.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETV-----------QIASVD 392
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPlsampppewrrQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 393 QSRDSLEGnkTVWEQVSDGFEQIKIGNYEVPSRSYVGRFNFKGADQQKFVKDLSGGERGRLHLALTLKQGGNVLLLDEPS 472
Cdd:COG4619 81 QEPALWGG--TVRDNLPFPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15599791 473 NDLDVETLRALEEALLDF---PGAAIV-ISHDRWFLDRIATHIL 512
Cdd:COG4619 159 SALDPENTRRVEELLREYlaeEGRAVLwVSHDPEQIERVADRVL 202
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
18-236 |
7.16e-30 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 117.47 E-value: 7.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpmpgIN--------------VGYLPQEPKLDPQ 83
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVR----VLgedvardpaevrrrIGYVPQEPALYPD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 84 ATVRDIVEeavgqikqAQARLdevyaaYAEPDADFDALAAEqakleailqasdghnlerqlevAADALRLPPW-DAKVEH 162
Cdd:COG1131 88 LTVRENLR--------FFARL------YGLPRKEARERIDE----------------------LLELFGLTDAaDRKVGT 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599791 163 LSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPG---TVVAITHDRYFLDNVAGWILELDRGH 236
Cdd:COG1131 132 LSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAegkTVLLSTHYLEEAERLCDRVAIIDKGR 208
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
16-236 |
2.71e-29 |
|
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: 115.51 E-value: 2.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 16 PPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGE---------ARPMPGI--NVGYLPQEPklDPQa 84
Cdd:COG1122 11 PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEvlvdgkditKKNLRELrrKVGLVFQNP--DDQ- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 85 tvrdIVEEAVgqikqaqarLDEVyaayaepdadfdALAAEQAKLeailqasDGHNLERQLEVAADALRLPPW-DAKVEHL 163
Cdd:COG1122 88 ----LFAPTV---------EEDV------------AFGPENLGL-------PREEIRERVEEALELVGLEHLaDRPPHEL 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599791 164 SGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPG---TVVAITHDRYFLDNVAGWILELDRGH 236
Cdd:COG1122 136 SGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLDDGR 211
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
325-512 |
4.03e-29 |
|
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: 114.49 E-value: 4.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 325 ELHNVTKGYGD--RVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETV-----------QIASV 391
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDltklslkelrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 392 DQSRDSLEGNKTVWEQVSDGFEQIKIGNYEVPSR--SYVGRFNFKGAdQQKFVKDLSGGERGRLHLALTLKQGGNVLLLD 469
Cdd:cd03225 81 FQNPDDQFFGPTVEEEVAFGLENLGLPEEEIEERveEALELVGLEGL-RDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15599791 470 EPSNDLDVETLRALEEALLDFPGA---AIVISHDRWFLDRIATHIL 512
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAEgktIIIVTHDLDLLLELADRVI 205
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
18-249 |
7.68e-29 |
|
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: 114.57 E-value: 7.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpMPGIN-----------VGYLPQEPKLDPQATV 86
Cdd:COG4555 13 KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSIL-IDGEDvrkeprearrqIGVLPDERGLYDRLTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 87 RDIVEeavgqikqaqarldevyaayaepdadfdaLAAEQAKLeailqasDGHNLERQLEVAADALRLPPW-DAKVEHLSG 165
Cdd:COG4555 92 RENIR-----------------------------YFAELYGL-------FDEELKKRIEELIELLGLEEFlDRRVGELST 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 166 GEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDF---PGTVVAITHDRYFLDNVAGWILELDRGHgIPFEG 242
Cdd:COG4555 136 GMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVVILHKGK-VVAQG 214
|
....*..
gi 15599791 243 NYSGWLE 249
Cdd:COG4555 215 SLDELRE 221
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
325-512 |
1.41e-28 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 113.01 E-value: 1.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 325 ELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETV-----QIASVDQSRDSL 398
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfGKPLekerkRIGYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 399 EG-NKTVWEQVSDGFEQiKIGNYEVPSRSY----------VGRFNFkgADQQkfVKDLSGGERGRLHLALTLKQGGNVLL 467
Cdd:cd03235 81 RDfPISVRDVVLMGLYG-HKGLFRRLSKADkakvdealerVGLSEL--ADRQ--IGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15599791 468 LDEPSNDLDVETLRALEEAL--LDFPGAAI-VISHDRWFLDRIATHIL 512
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLreLRREGMTIlVVTHDLGLVLEYFDRVL 203
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
334-538 |
3.20e-28 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 119.12 E-value: 3.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 334 GDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETVQIASVDQSRDSLEgnKTVWEQVSDG-- 411
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALP--QPALEYVIDGdr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 412 -FEQIK------------------------IGNYEVPSR--SYVGRFNFKGADQQKFVKDLSGGERGRLHLALTLKQGGN 464
Cdd:PRK10636 90 eYRQLEaqlhdanerndghaiatihgkldaIDAWTIRSRaaSLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599791 465 VLLLDEPSNDLDVETLRALEEALLDFPGAAIVISHDRWFLDRIATHILSYEDDgkvTFFE--GNYTEFEADRKKRL 538
Cdd:PRK10636 170 LLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQ---SLFEytGNYSSFEVQRATRL 242
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
19-235 |
6.22e-28 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 111.09 E-value: 6.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpMPGIN-------VGYLPQEPKLDPQ--ATVRDI 89
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIR-VFGKPlekerkrIGYVPQRRSIDRDfpISVRDV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 90 VEEAVGQIKQAQARLDevyaayaepdadfdalaaeQAKLEAILQAsdghnLERqleVAADALRlppwDAKVEHLSGGEKR 169
Cdd:cd03235 91 VLMGLYGHKGLFRRLS-------------------KADKAKVDEA-----LER---VGLSELA----DRQIGELSGGQQQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 170 RVALCRLLLSAPDMLLLDEPTNHLDADS----VAWLEHfLHDFPGTVVAITHDRYFLDNVAGWILELDRG 235
Cdd:cd03235 140 RVLLARALVQDPDLLLLDEPFAGVDPKTqediYELLRE-LRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
18-236 |
9.52e-28 |
|
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: 109.41 E-value: 9.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpMPGIN-----------VGYLPQEPKLDPQATV 86
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIK-VLGKDikkepeevkrrIGYLPEEPSLYENLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 87 RDiveeavgqikqaqarldevyaayaepdadfdalaaeqakleailqasdghNLErqlevaadalrlppwdakvehLSGG 166
Cdd:cd03230 91 RE--------------------------------------------------NLK---------------------LSGG 99
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599791 167 EKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDF---PGTVVAITHDRYFLDNVAGWILELDRGH 236
Cdd:cd03230 100 MKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELkkeGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
324-499 |
1.43e-27 |
|
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: 108.62 E-value: 1.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDR--VLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGEtVQIASVDQsrdslegn 401
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDG-VDLRDLDL-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 402 KTVWEQVSdgfeqikignyEVPSRSYVgrfnFKGAdqqkfVKD--LSGGERGRLHLALTLKQGGNVLLLDEPSNDLDVET 479
Cdd:cd03228 72 ESLRKNIA-----------YVPQDPFL----FSGT-----IREniLSGGQRQRIAIARALLRDPPILILDEATSALDPET 131
|
170 180
....*....|....*....|..
gi 15599791 480 LRALEEALLDFPG--AAIVISH 499
Cdd:cd03228 132 EALILEALRALAKgkTVIVIAH 153
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
325-512 |
1.46e-27 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 109.06 E-value: 1.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 325 ELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETvqiaSVDQ-SRDSLEGNKT 403
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGK----DLASlSPKELARKIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 404 VWEQVSDgfeqikignyevpsrsYVGRFNFKgadqQKFVKDLSGGERGRLHLALTLKQGGNVLLLDEPSNDLD----VET 479
Cdd:cd03214 77 YVPQALE----------------LLGLAHLA----DRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDiahqIEL 136
|
170 180 190
....*....|....*....|....*....|...
gi 15599791 480 LRALEEALLDFPGAAIVISHDRWFLDRIATHIL 512
Cdd:cd03214 137 LELLRRLARERGKTVVMVLHDLNLAARYADRVI 169
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
339-473 |
2.02e-27 |
|
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: 107.73 E-value: 2.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 339 IDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGET-----------VQIASVDQSrDSLEGNKTVWEQ 407
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQdltdderkslrKEIGYVFQD-PQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599791 408 VSDGFEQIKIGNYEVPSRSYVGRFNFKGADQQK-----FVKDLSGGERGRLHLALTLKQGGNVLLLDEPSN 473
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
16-236 |
2.04e-27 |
|
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: 116.40 E-value: 2.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 16 PPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEAR----PMPGI-------NVGYLPQEPKLdPQA 84
Cdd:COG4988 347 PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILingvDLSDLdpaswrrQIAWVPQNPYL-FAG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 85 TVRDIVeeavgqikqaqaRLdevyaayAEPDADFDAL--AAEQAKLEAILQAsdghnLERQLE--VAADALRLppwdakv 160
Cdd:COG4988 426 TIRENL------------RL-------GRPDASDEELeaALEAAGLDEFVAA-----LPDGLDtpLGEGGRGL------- 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599791 161 ehlSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPG--TVVAITHDRYFLDNvAGWILELDRGH 236
Cdd:COG4988 475 ---SGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKgrTVILITHRLALLAQ-ADRILVLDDGR 548
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
324-522 |
2.48e-27 |
|
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: 110.11 E-value: 2.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGY-GDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQIASVDQSRDSLeG- 400
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVdGKDITKKNLRELRRKV-Gl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 401 ----------NKTVWEQVSDGFEQIKIGNYEVPSR-----SYVGRFNFKgadqQKFVKDLSGGERGRLHLALTLKQGGNV 465
Cdd:COG1122 80 vfqnpddqlfAPTVEEDVAFGPENLGLPREEIRERveealELVGLEHLA----DRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 466 LLLDEPSNDLDVETLRALEEALLDFPGAA---IVISHDRWFLDRIATHILsYEDDGKVTF 522
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNKEGktvIIVTHDLDLVAELADRVI-VLDDGRIVA 214
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-237 |
4.66e-27 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 115.29 E-value: 4.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 16 PPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGE-ARPmPGINVGYLPQEPKLdPQATVRDIVeeav 94
Cdd:COG4178 373 PDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRiARP-AGARVLFLPQRPYL-PLGTLREAL---- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 95 gqikqaqarldevyaAYAEPDADFDalaaeQAKLEAILQASDGHNLERQLEVAADalrlppWDAKvehLSGGEKRRVALC 174
Cdd:COG4178 447 ---------------LYPATAEAFS-----DAELREALEAVGLGHLAERLDEEAD------WDQV---LSLGEQQRLAFA 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599791 175 RLLLSAPDMLLLDEPTNHLDADSVAWL-EHFLHDFPG-TVVAITHdRYFLDNVAGWILELDRGHG 237
Cdd:COG4178 498 RLLLHKPDWLFLDEATSALDEENEAALyQLLREELPGtTVISVGH-RSTLAAFHDRVLELTGDGS 561
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
324-520 |
7.52e-27 |
|
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: 108.36 E-value: 7.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGD--RVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETVQIASVDQSR------ 395
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARqslgyc 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 396 ---DSLEGNKTVWEQV-----------SDGFEQIKIGNYEVPSRSYvgrfnfkgadQQKFVKDLSGGERGRLHLALTLKQ 461
Cdd:cd03263 81 pqfDALFDELTVREHLrfyarlkglpkSEIKEEVELLLRVLGLTDK----------ANKRARTLSGGMKRKLSLAIALIG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599791 462 GGNVLLLDEPSNDLDVETLRALEEALLDF-PGAAIVI-SHDRWFLDRIATH--ILSyedDGKV 520
Cdd:cd03263 151 GPSVLLLDEPTSGLDPASRRAIWDLILEVrKGRSIILtTHSMDEAEALCDRiaIMS---DGKL 210
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
324-500 |
1.05e-26 |
|
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: 107.94 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDR----VLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQIASVDQS---- 394
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdGEPVTGPGPDRGyvfq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 395 RDSLEGNKTVWEQVSDGFEQIKIGNYEVPSR--SYVGRFNFKGAdQQKFVKDLSGGERGRLHLALTLKQGGNVLLLDEPS 472
Cdd:cd03293 81 QDALLPWLTVLDNVALGLELQGVPKAEARERaeELLELVGLSGF-ENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPF 159
|
170 180 190
....*....|....*....|....*....|..
gi 15599791 473 NDLDVETLRALEEALLDF---PGAAIV-ISHD 500
Cdd:cd03293 160 SALDALTREQLQEELLDIwreTGKTVLlVTHD 191
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-508 |
1.83e-26 |
|
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: 112.97 E-value: 1.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDteiegEARPMPG---INVGYLPQEPKLDPQATVRDIVEEAVGQ 96
Cdd:TIGR03269 14 EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMD-----QYEPTSGriiYHVALCEKCGYVERPSKVGEPCPVCGGT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 97 IKQAQARL----DEVYAAYAEPDA-----DFdALAAEQAKLEAILQASD--GHNLERQLEVAADALRLPPWDAKVEH--- 162
Cdd:TIGR03269 89 LEPEEVDFwnlsDKLRRRIRKRIAimlqrTF-ALYGDDTVLDNVLEALEeiGYEGKEAVGRAVDLIEMVQLSHRITHiar 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 163 -LSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDadsvawlehflhdfPGTVvAITHDRyfldnvagwILELDRGHGIPFE 241
Cdd:TIGR03269 168 dLSGGEKQRVVLARQLAKEPFLFLADEPTGTLD--------------PQTA-KLVHNA---------LEEAVKASGISMV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 242 GNySGWLESkAARLAQEAKqeashakamkaeleWVRQGAKGRQAKSKARLQRFEELQSqEFQKRSETneiyipagpRLGD 321
Cdd:TIGR03269 224 LT-SHWPEV-IEDLSDKAI--------------WLENGEIKEEGTPDEVVAVFMEGVS-EVEKECEV---------EVGE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 322 KVIELHNVTKGYG--DRVLI---DNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-------------- 382
Cdd:TIGR03269 278 PIIKVRNVSKRYIsvDRGVVkavDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkpgp 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 383 ---GETVQIASVDQSRDSLEGNKTVWEQVSD--GFEQIKignyEVPSRSYVGRFNFKGADQQ-------KFVKDLSGGER 450
Cdd:TIGR03269 358 dgrGRAKRYIGILHQEYDLYPHRTVLDNLTEaiGLELPD----ELARMKAVITLKMVGFDEEkaeeildKYPDELSEGER 433
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599791 451 GRLHLALTLKQGGNVLLLDEPSNDLDVETLRALEEALL----DFPGAAIVISHDRWFL----DRIA 508
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILkareEMEQTFIIVSHDMDFVldvcDRAA 499
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
324-527 |
2.46e-26 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 113.51 E-value: 2.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETVQIASVDQS--RDsLEGn 401
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDppRN-VEG- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 402 kTVWEQVSDGFEQI--KIGNYEVPSR---------------------SYVGRFNFK----------GADQQKFVKDLSGG 448
Cdd:PRK11147 82 -TVYDFVAEGIEEQaeYLKRYHDISHlvetdpseknlnelaklqeqlDHHNLWQLEnrinevlaqlGLDPDAALSSLSGG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599791 449 ERGRLHLALTLKQGGNVLLLDEPSNDLDVETLRALEEALLDFPGAAIVISHDRWFLDRIATHILSYeDDGKVTFFEGNY 527
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDL-DRGKLVSYPGNY 238
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
18-253 |
6.14e-26 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 111.52 E-value: 6.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARPMPGINVGYLPQEPKLDPQATVrdIVEEAVGQI 97
Cdd:PRK15064 331 NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYDFENDL--TLFDWMSQW 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 98 KQaqarldevyaayaEPDADfdalaaeqakleailQASDGhNLERQLEVAADALRlppwdaKVEHLSGGEKRRVALCRLL 177
Cdd:PRK15064 409 RQ-------------EGDDE---------------QAVRG-TLGRLLFSQDDIKK------SVKVLSGGEKGRMLFGKLM 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599791 178 LSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPGTVVAITHDRYFLDNVAGWILELDRGHGIPFEGNYSGWLESKAA 253
Cdd:PRK15064 454 MQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLRSQGI 529
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-515 |
8.15e-26 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 111.44 E-value: 8.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 31 PGAKIGVLGLNGAGKSTLLRIMAGvdteiegEARPmpgiNVGYLPQEPKLDpqatvrDIVEEAVGqiKQAQARLDEVYAA 110
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSG-------ELIP----NLGDYEEEPSWD------EVLKRFRG--TELQNYFKKLYNG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 111 ---------YAEpdadfdaLAAEQAK--LEAILQASDGHNLERQLevaADALRLPP-WDAKVEHLSGGEKRRVALCRLLL 178
Cdd:PRK13409 159 eikvvhkpqYVD-------LIPKVFKgkVRELLKKVDERGKLDEV---VERLGLENiLDRDISELSGGELQRVAIAAALL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 179 SAPDMLLLDEPTNHLD-------ADSVAWLEhflhdfPG-TVVAITHDRYFLDNVAGWIleldrgH---GIPfeGNYSgw 247
Cdd:PRK13409 229 RDADFYFFDEPTSYLDirqrlnvARLIRELA------EGkYVLVVEHDLAVLDYLADNV------HiayGEP--GAYG-- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 248 leskaarlaqeakqEASHAKAmkaelewVRQGA----KGRQAKSKARLqRFEELqsqEFQKRSETNEIyipagprLGDKV 323
Cdd:PRK13409 293 --------------VVSKPKG-------VRVGIneylKGYLPEENMRI-RPEPI---EFEERPPRDES-------ERETL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLIDNlSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETV----QIASVDQS---RD 396
Cdd:PRK13409 341 VEYPDLTKKLGDFSLEVE-GGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKIsykpQYIKPDYDgtvED 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 397 SLEGNKT------VWEQVSDGFEQIKIgnYEvpsrsyvgrfnfkgadqqKFVKDLSGGERGRLHLALTLKQGGNVLLLDE 470
Cdd:PRK13409 420 LLRSITDdlgssyYKSEIIKPLQLERL--LD------------------KNVKDLSGGELQRVAIAACLSRDADLYLLDE 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 15599791 471 PSNDLDVE----TLRALEEALLDFPGAAIVISHDRWFLDRIATHILSYE 515
Cdd:PRK13409 480 PSAHLDVEqrlaVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFE 528
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
320-532 |
9.83e-26 |
|
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: 105.83 E-value: 9.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 320 GDKVIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQIASVDQSR--- 395
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVdGQDITGLSEKELYelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 396 -------------DSLegnkTVWEQVsdGF---EQIKIGNYEVPSR--SYVGRFNFKGAdQQKFVKDLSGGERGRLHLA- 456
Cdd:COG1127 82 rrigmlfqggalfDSL----TVFENV--AFplrEHTDLSEAEIRELvlEKLELVGLPGA-ADKMPSELSGGMRKRVALAr 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 457 -LTLKQggNVLLLDEPSNDLDVETLRALEEALLD----FPGAAIVISHDRWFLDRIATHILsYEDDGKVTfFEGNYTEFE 531
Cdd:COG1127 155 aLALDP--EILLYDEPTAGLDPITSAVIDELIRElrdeLGLTSVVVTHDLDSAFAIADRVA-VLADGKII-AEGTPEELL 230
|
.
gi 15599791 532 A 532
Cdd:COG1127 231 A 231
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
324-508 |
1.04e-25 |
|
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: 104.91 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQ--------IASVDQS 394
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIdGRDVTgvpperrnIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 395 rDSLEGNKTVWEQVSDGFEQIKIGNYEVPSRSY-----VGRFNFkgadQQKFVKDLSGGERGRLHLALTLKQGGNVLLLD 469
Cdd:cd03259 81 -YALFPHLTVAENIAFGLKLRGVPKAEIRARVRellelVGLEGL----LNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15599791 470 EPSNDLDVET---LRALEEALLDFPGA-AIVISHDR----WFLDRIA 508
Cdd:cd03259 156 EPLSALDAKLreeLREELKELQRELGItTIYVTHDQeealALADRIA 202
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
17-236 |
1.63e-25 |
|
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: 102.71 E-value: 1.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 17 PKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpmpginvgYLPQEPKLDPQATVRDIVeeavGQ 96
Cdd:cd00267 10 GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL--------IDGKDIAKLPLEELRRRI----GY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 97 IKQaqarldevyaayaepdadfdalaaeqakleailqasdghnlerqlevaadalrlppwdakvehLSGGEKRRVALCRL 176
Cdd:cd00267 78 VPQ---------------------------------------------------------------LSGGQRQRVALARA 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599791 177 LLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPG---TVVAITHDRYFLDNVAGWILELDRGH 236
Cdd:cd00267 95 LLLNPDLLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
324-513 |
1.69e-25 |
|
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: 104.22 E-value: 1.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQIASVDQSR------- 395
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFdGKSYQKNIEALRRigaliea 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 396 DSLEGNKTVWEQVSDGFEQIKIGNYEVpsRSYVGRFNFKGADQQKfVKDLSGGERGRLHLALTLKQGGNVLLLDEPSNDL 475
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRKKRI--DEVLDVVGLKDSAKKK-VKGFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15599791 476 DVETLRALEEALLDFP--GAAIVIShdrwfldriaTHILS 513
Cdd:cd03268 158 DPDGIKELRELILSLRdqGITVLIS----------SHLLS 187
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
16-236 |
2.29e-25 |
|
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: 110.69 E-value: 2.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 16 PPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEAR----PMPGIN-------VGYLPQEPKLDpQA 84
Cdd:COG2274 485 GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILidgiDLRQIDpaslrrqIGVVLQDVFLF-SG 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 85 TVRD-IveeavgqikqaqarldevyaAYAEPDADFDAL--AAEQAKL-EAILQASDGhnLERQLEvaadalrlppwdakv 160
Cdd:COG2274 564 TIREnI--------------------TLGDPDATDEEIieAARLAGLhDFIEALPMG--YDTVVG--------------- 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 161 EH---LSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPG--TVVAITHDRYFLDNvAGWILELDRG 235
Cdd:COG2274 607 EGgsnLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTIRL-ADRIIVLDKG 685
|
.
gi 15599791 236 H 236
Cdd:COG2274 686 R 686
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
324-512 |
2.48e-25 |
|
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: 102.65 E-value: 2.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQ---IASVDQSRDS-- 397
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIdGEDLTdleDELPPLRRRIgm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 398 ------LEGNKTVWEQVSDGfeqikignyevpsrsyvgrfnfkgadqqkfvkdLSGGERGRLHLALTLKQGGNVLLLDEP 471
Cdd:cd03229 81 vfqdfaLFPHLTVLENIALG---------------------------------LSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15599791 472 SNDLDVET---LRALEEALLDFPG-AAIVISHDRWFLDRIATHIL 512
Cdd:cd03229 128 TSALDPITrreVRALLKSLQAQLGiTVVLVTHDLDEAARLADRVV 172
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
325-521 |
2.74e-25 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 103.49 E-value: 2.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 325 ELHNVTKGYGDRVLI-DNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETV--------QIASVDQSR 395
Cdd:cd03226 1 RIENISFSYKKGTEIlDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPikakerrkSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 396 DSLEGNKTVWEQVSDGFEQIKIGNYEVpsRSYVGRFN-FKGADQQKFvkDLSGGERGRLHLALTLKQGGNVLLLDEPSND 474
Cdd:cd03226 81 DYQLFTDSVREELLLGLKELDAGNEQA--ETVLKDLDlYALKERHPL--SLSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15599791 475 LDVETLRALEEALLDFPG---AAIVISHDRWFLDRIATHILsYEDDGKVT 521
Cdd:cd03226 157 LDYKNMERVGELIRELAAqgkAVIVITHDYEFLAKVCDRVL-LLANGAIV 205
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
323-500 |
3.44e-25 |
|
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: 103.33 E-value: 3.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 323 VIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQIASVDQSR------ 395
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWnGEPIRDAREDYRRrlaylg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 396 --DSLEGNKTVWEQVSdgFEQiKIGNYEVPSRSY---VGRFNFKGAdQQKFVKDLSGGERGRLHLALTLKQGGNVLLLDE 470
Cdd:COG4133 82 haDGLKPELTVRENLR--FWA-ALYGLRADREAIdeaLEAVGLAGL-ADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190
....*....|....*....|....*....|...
gi 15599791 471 PSNDLDVETLRALEEALLDFP---GAAIVISHD 500
Cdd:COG4133 158 PFTALDAAGVALLAELIAAHLargGAVLLTTHQ 190
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
324-523 |
3.64e-25 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 104.39 E-value: 3.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGET--VQIASVDQSR------ 395
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLdvATTPSRELAKrlailr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 396 --DSLEGNKTVWEQVsdGFeqikignyevpsrsyvGRFNF-KG----ADQQK----------------FVKDLSGGERGR 452
Cdd:COG4604 82 qeNHINSRLTVRELV--AF----------------GRFPYsKGrltaEDREIideaiayldledladrYLDELSGGQRQR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599791 453 LHLALTLKQGGNVLLLDEPSNDLD----VETLRALEEALLDFpGAAIVIS-HDRWFLDRIATHILSYEdDGKVTFF 523
Cdd:COG4604 144 AFIAMVLAQDTDYVLLDEPLNNLDmkhsVQMMKLLRRLADEL-GKTVVIVlHDINFASCYADHIVAMK-DGRVVAQ 217
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
19-253 |
4.36e-25 |
|
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: 109.09 E-value: 4.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEAR----PMPGIN-------VGYLPQEPKL-DpqATV 86
Cdd:COG4987 348 RPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITlggvDLRDLDeddlrrrIAVVPQRPHLfD--TTL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 87 RDIVeeavgqikqaqaRLdevyaayAEPDADFDAL--AAEQAKLEAILQAS-DGhnlerqlevaadalrlppWDAKV--- 160
Cdd:COG4987 426 RENL------------RL-------ARPDATDEELwaALERVGLGDWLAALpDG------------------LDTWLgeg 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 161 -EHLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSV-AWLEHFLHDFPG-TVVAITHDRYFLDNVAGwILELDRGHg 237
Cdd:COG4987 469 gRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEqALLADLLEALAGrTVLLITHRLAGLERMDR-ILVLEDGR- 546
|
250
....*....|....*.
gi 15599791 238 IPFEGNYSGWLESKAA 253
Cdd:COG4987 547 IVEQGTHEELLAQNGR 562
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
324-499 |
1.84e-24 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 99.81 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQIASVDQSRDSlegnk 402
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVdGKEVSFASPRDARRA----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 403 tvweqvsdgfeqiKIGnyevpsrsyvgrfnfkgadqqkFVKDLSGGERGRLHLALTLKQGGNVLLLDEPSNDLDV----- 477
Cdd:cd03216 76 -------------GIA----------------------MVYQLSVGERQMVEIARALARNARLLILDEPTAALTPaever 120
|
170 180
....*....|....*....|....*
gi 15599791 478 --ETLRALEEAlldfpGAAIV-ISH 499
Cdd:cd03216 121 lfKVIRRLRAQ-----GVAVIfISH 140
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
17-218 |
4.48e-24 |
|
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: 99.05 E-value: 4.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 17 PKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpMPGINVGYLPqepkldpqatvrdiveeavgq 96
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIL-LDGKDLASLS--------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 97 ikqaqarldevyaayaepdadfdalAAEQAKLEAIL-QAsdghnLERqLEVAADALRLppwdakVEHLSGGEKRRVALCR 175
Cdd:cd03214 68 -------------------------PKELARKIAYVpQA-----LEL-LGLAHLADRP------FNELSGGERQRVLLAR 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15599791 176 LLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPG----TVVAITHD 218
Cdd:cd03214 111 ALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARergkTVVMVLHD 157
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-512 |
5.10e-24 |
|
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: 106.02 E-value: 5.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 31 PGAKIGVLGLNGAGKSTLLRIMAGvdteiegEARPmpgiNVGYLPQEPKLDpqatvrDIVEEAVGqiKQAQARLDEVYAA 110
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSG-------ELKP----NLGDYDEEPSWD------EVLKRFRG--TELQDYFKKLANG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 111 ---------YAEpdadfdaLAAEQAKLEA--ILQASDghnlER-QLEVAADALRLPP-WDAKVEHLSGGEKRRVALCRLL 177
Cdd:COG1245 159 eikvahkpqYVD-------LIPKVFKGTVreLLEKVD----ERgKLDELAEKLGLENiLDRDISELSGGELQRVAIAAAL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 178 LSAPDMLLLDEPTNHLDAD---SVAWLEHFLHDFPGTVVAITHDRYFLDNVAGWILELdrgHGIP-----FEGNYS---- 245
Cdd:COG1245 228 LRDADFYFFDEPSSYLDIYqrlNVARLIRELAEEGKYVLVVEHDLAILDYLADYVHIL---YGEPgvygvVSKPKSvrvg 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 246 ------GWLESKAARLAQEAKqeashakamkaelewvrqgakgrqakskarlqRFEELQSQEFQKRSEtneiyipagprl 319
Cdd:COG1245 305 inqyldGYLPEENVRIRDEPI--------------------------------EFEVHAPRREKEEET------------ 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 320 gdkVIELHNVTKGYGDrvlidnLSLSIPKGAI-----VGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETV----QIAS 390
Cdd:COG1245 341 ---LVEYPDLTKSYGG------FSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKIsykpQYIS 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 391 VDQS---RDSLEgnKTVWEQVSDGFEQIKIGNyevpsrsyvgRFNFKGADQQKfVKDLSGGERGRLHLALTLKQGGNVLL 467
Cdd:COG1245 412 PDYDgtvEEFLR--SANTDDFGSSYYKTEIIK----------PLGLEKLLDKN-VKDLSGGELQRVAIAACLSRDADLYL 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 15599791 468 LDEPSNDLDVE----TLRALEEALLDFPGAAIVISHDRWFLDRIATHIL 512
Cdd:COG1245 479 LDEPSAHLDVEqrlaVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
18-236 |
5.24e-24 |
|
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: 100.26 E-value: 5.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEAR----PMPGI-----------NVGYLPQEPKLDP 82
Cdd:cd03255 16 KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRvdgtDISKLsekelaafrrrHIGFVFQSFNLLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 83 QATVRDIVEEAVgQIKQAQARLDEVYAAYAepdadfdalaAEQAKLEAILqasdghnlerqlevaadalrlppwDAKVEH 162
Cdd:cd03255 96 DLTALENVELPL-LLAGVPKKERRERAEEL----------LERVGLGDRL------------------------NHYPSE 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599791 163 LSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADS----VAWLEHFLHDFPGTVVAITHDRyFLDNVAGWILELDRGH 236
Cdd:cd03255 141 LSGGQQQRVAIARALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGK 217
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
10-300 |
5.34e-24 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 106.19 E-value: 5.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 10 RVGKIV---------PPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARPMPGINVGYLPQ-EPK 79
Cdd:PRK11147 314 RSGKIVfemenvnyqIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQhRAE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 80 LDPQATVRDIVEEAvgqiKQaqarldevyaayaepdadfdalaaeqaklEAILQASDGHnlerQLEVAADALrLPPWDAK 159
Cdd:PRK11147 394 LDPEKTVMDNLAEG----KQ-----------------------------EVMVNGRPRH----VLGYLQDFL-FHPKRAM 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 160 --VEHLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPGTVVAITHDRYFLDNVA--GWILELDrG 235
Cdd:PRK11147 436 tpVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVteCWIFEGN-G 514
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599791 236 HGIPFEGNYsgwleskaarlaQEAKQEASHAKAMKAELEWVRQGAKGRQAKSKAR--------LQR-FEELQSQ 300
Cdd:PRK11147 515 KIGRYVGGY------------HDARQQQAQYLALKQPAVKKKEEAAAPKAETVKRsskklsykLQReLEQLPQL 576
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
19-218 |
5.41e-24 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 101.32 E-value: 5.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDT------EIEGEARPMPGINVGYLPQEPKLDPQATVRDIVE- 91
Cdd:COG1116 24 VTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKptsgevLVDGKPVTGPGPDRGVVFQEPALLPWLTVLDNVAl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 92 --EAVGQIK-QAQARLDEVyaayaepdadfdalaaeqakleailqasdghnLER-QLEVAADALrlpPWDakvehLSGGE 167
Cdd:COG1116 104 glELRGVPKaERRERAREL--------------------------------LELvGLAGFEDAY---PHQ-----LSGGM 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15599791 168 KRRVALCRLLLSAPDMLLLDEPTNHLDA-------DsvaWLEHFLHDFPGTVVAITHD 218
Cdd:COG1116 144 RQRVAIARALANDPEVLLMDEPFGALDAltrerlqD---ELLRLWQETGKTVLFVTHD 198
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-235 |
1.35e-23 |
|
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: 99.20 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpMPGI------------NVGYLPQEPKLdPQAT 85
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVL-LDGTdirqldpadlrrNIGYVPQDVTL-FYGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 86 VRDIVeeavgqikqaqarldevyaAYAEPDADfDALAAEQAKLEAILQASDGHNLERQLEVAadalrlppwdakvEH--- 162
Cdd:cd03245 94 LRDNI-------------------TLGAPLAD-DERILRAAELAGVTDFVNKHPNGLDLQIG-------------ERgrg 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599791 163 LSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPG--TVVAITHdRYFLDNVAGWILELDRG 235
Cdd:cd03245 141 LSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITH-RPSLLDLVDRIIVMDSG 214
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
324-532 |
4.85e-23 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 97.96 E-value: 4.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQIASVDQSR------- 395
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIdGEDISGLSEAELYrlrrrmg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 396 ---------DSLegnkTVWEQVSDGFEQikigNYEVPSRSYVGRFNFK------GADQQKFVKDLSGGERGRLHLALTLK 460
Cdd:cd03261 81 mlfqsgalfDSL----TVFENVAFPLRE----HTRLSEEEIREIVLEKleavglRGAEDLYPAELSGGMKKRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599791 461 QGGNVLLLDEPSNDLDVETLRALEEALLD----FPGAAIVISHDRWFLDRIATHILsYEDDGKVTfFEGNYTEFEA 532
Cdd:cd03261 153 LDPELLLYDEPTAGLDPIASGVIDDLIRSlkkeLGLTSIMVTHDLDTAFAIADRIA-VLYDGKIV-AEGTPEELRA 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
323-520 |
7.69e-23 |
|
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: 97.27 E-value: 7.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 323 VIELHNVTKGYGDR----VLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQIASVDQSRD- 396
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVdGTDLTLLSGKELRKa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 397 -----------SLEGNKTVWEQVSDGFEQIKIGNYEVPSRSY-----VGRFNFKGAdqqkFVKDLSGGERGRLHLALTLK 460
Cdd:cd03258 81 rrrigmifqhfNLLSSRTVFENVALPLEIAGVPKAEIEERVLellelVGLEDKADA----YPAQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599791 461 QGGNVLLLDEPSNDLDVETLRALEEALLDFP---GAAIV-ISHDRWFLDRIATHILSYEdDGKV 520
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILALLRDINrelGLTIVlITHEMEVVKRICDRVAVME-KGEV 219
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
324-500 |
8.25e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 97.78 E-value: 8.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETV-----------QIASVD 392
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPismlssrqlarRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 393 QSRDSLEGnKTVWEQVSDGfeqikignyEVPSRSYVGRFNfkGADQQ----------------KFVKDLSGGERGRLHLA 456
Cdd:PRK11231 83 QHHLTPEG-ITVRELVAYG---------RSPWLSLWGRLS--AEDNArvnqameqtrinhladRRLTDLSGGQRQRAFLA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15599791 457 LTLKQGGNVLLLDEPSNDLD----VETLRALEEaLLDFPGAAIVISHD 500
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLDinhqVELMRLMRE-LNTQGKTVVTVLHD 197
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
324-538 |
1.03e-22 |
|
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: 97.25 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGD-RVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETvqiasvDQSRDSLEGNK 402
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGT------DINKLKGKALR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 403 TVWEQVSDGFEQikignYEVPSRSYV------GRFN-----------FKGADQQ----------------KFVKDLSGGE 449
Cdd:cd03256 75 QLRRQIGMIFQQ-----FNLIERLSVlenvlsGRLGrrstwrslfglFPKEEKQralaalervglldkayQRADQLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 450 RGRLHLALTLKQGGNVLLLDEPSNDLDVETLRALEEALLDFP---GAAIVIS-HD----RWFLDRIAthILSyedDGKVt 521
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINreeGITVIVSlHQvdlaREYADRIV--GLK---DGRI- 223
|
250
....*....|....*..
gi 15599791 522 FFEGNYTEFEADRKKRL 538
Cdd:cd03256 224 VFDGPPAELTDEVLDEI 240
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
16-235 |
1.37e-22 |
|
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: 95.79 E-value: 1.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 16 PPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGE--------ARPMPGINVGYLPQEPklDPQatvr 87
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSillngkpiKAKERRKSIGYVMQDV--DYQ---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 88 dIVEEAVGqikqaqarlDEVYAAyaepdadFDALAAEQAKLEAILQasdghnlerqlevaadalRLPPWDAKVEH---LS 164
Cdd:cd03226 84 -LFTDSVR---------EELLLG-------LKELDAGNEQAETVLK------------------DLDLYALKERHplsLS 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599791 165 GGEKRRVALCRLLLSAPDMLLLDEPTNHLDA---DSVAWLEHFLHDFPGTVVAITHDRYFLDNVAGWILELDRG 235
Cdd:cd03226 129 GGQKQRLAIAAALLSGKDLLIFDEPTSGLDYknmERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
18-226 |
1.71e-22 |
|
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: 96.04 E-value: 1.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG----VDTEIEGEARPMPGIN----------VGYLPQEP--KLD 81
Cdd:cd03257 17 SVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGllkpTSGSIIFDGKDLLKLSrrlrkirrkeIQMVFQDPmsSLN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 82 PQATVRDIVEEAVgqikQAQARLDevyaayaepdadfdalaAEQAKLEAILQASDGHNLERQLevaADalRLPpwdakve 161
Cdd:cd03257 97 PRMTIGEQIAEPL----RIHGKLS-----------------KKEARKEAVLLLLVGVGLPEEV---LN--RYP------- 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599791 162 H-LSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHD----FPGTVVAITHD----RYFLDNVA 226
Cdd:cd03257 144 HeLSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKlqeeLGLTLLFITHDlgvvAKIADRVA 217
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
14-235 |
1.82e-22 |
|
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: 100.98 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 14 IVPP--KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEAR-----------PMPGINVGYLPQEPKL 80
Cdd:COG4618 338 VVPPgsKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRldgadlsqwdrEELGRHIGYLPQDVEL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 81 DPqatvrdiveeavGQIKQAQARLdevyaayaePDADFDAL--AAEQAKL-EAILQASDGHNLErqleVAADALRLppwd 157
Cdd:COG4618 418 FD------------GTIAENIARF---------GDADPEKVvaAAKLAGVhEMILRLPDGYDTR----IGEGGARL---- 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 158 akvehlSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDF---PGTVVAITHDRYFLdNVAGWILELDR 234
Cdd:COG4618 469 ------SGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkarGATVVVITHRPSLL-AAVDKLLVLRD 541
|
.
gi 15599791 235 G 235
Cdd:COG4618 542 G 542
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
324-485 |
3.69e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 97.87 E-value: 3.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQIASVdQSRD------ 396
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIdGEDVTHRSI-QQRDicmvfq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 397 --SLEGNKTVWEQVSDGFEQIKIGNYEVPSR-----SYVGRFNFkgadQQKFVKDLSGGERGRLHL--ALTLKQggNVLL 467
Cdd:PRK11432 86 syALFPHMSLGENVGYGLKMLGVPKEERKQRvkealELVDLAGF----EDRYVDQISGGQQQRVALarALILKP--KVLL 159
|
170
....*....|....*...
gi 15599791 468 LDEPSNDLDVETLRALEE 485
Cdd:PRK11432 160 FDEPLSNLDANLRRSMRE 177
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
22-219 |
5.67e-22 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 97.14 E-value: 5.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDT------EIEGE----ARPMPGINVGYLPQEPKLDPQATVRDIVE 91
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETpdsgriVLNGRdlftNLPPRERRVGFVFQHYALFPHMTVAENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 92 EAVGQIKQaqarldevyaayaePDADFDALAAEQakLEAIlqasdghnlerQLEVAADalRLPPwdakveHLSGGEKRRV 171
Cdd:COG1118 98 FGLRVRPP--------------SKAEIRARVEEL--LELV-----------QLEGLAD--RYPS------QLSGGQRQRV 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15599791 172 ALCRLLLSAPDMLLLDEPTNHLDAdSVA-----WLEHFLHDFPGTVVAITHDR 219
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDA-KVRkelrrWLRRLHDELGGTTVFVTHDQ 194
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
324-500 |
6.56e-22 |
|
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: 94.55 E-value: 6.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTG-----KEQPDSGTIEI-GETV----------- 386
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLdGKDIydldvdvlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 387 -QIASVDQSRDSLEGnkTVWEQVSDGFEQIKIGNYEVpsRSYVGRFNFKGADQQKFVKD------LSGGERGRLHLALTL 459
Cdd:cd03260 81 rRVGMVFQKPNPFPG--SIYDNVAYGLRLHGIKLKEE--LDERVEEALRKAALWDEVKDrlhalgLSGGQQQRLCLARAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15599791 460 KQGGNVLLLDEPSNDLDVETLRALEEALLDF--PGAAIVISHD 500
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELkkEYTIVIVTHN 199
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
323-498 |
7.22e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 95.95 E-value: 7.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 323 VIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQIASVDQ------SR 395
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWdGEPLDPEDRRRigylpeER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 396 dSLEGNKTVWEQV-----------SDGFEQIKignyevpsrSYVGRFNFKGADQQKfVKDLSGGERGRLHLALTL----K 460
Cdd:COG4152 81 -GLYPKMKVGEQLvylarlkglskAEAKRRAD---------EWLERLGLGDRANKK-VEELSKGNQQKVQLIAALlhdpE 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15599791 461 qggnVLLLDEPSNDLDVETLRALEEALLDF--PGAAIVIS 498
Cdd:COG4152 150 ----LLILDEPFSGLDPVNVELLKDVIRELaaKGTTVIFS 185
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
7-218 |
7.42e-22 |
|
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: 94.08 E-value: 7.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 7 TMHRVGKIVPPKR---EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDT------EIEGEARPMPGINVGYLPQE 77
Cdd:cd03293 2 EVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERptsgevLVDGEPVTGPGPDRGYVFQQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 78 PKLDPQATVRDIVE---EAVGQIK-QAQARLDEvyaayaepdadfdalAAEQAKLEAilqasdghnlerqlevAADALrl 153
Cdd:cd03293 82 DALLPWLTVLDNVAlglELQGVPKaEARERAEE---------------LLELVGLSG----------------FENAY-- 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599791 154 pPWDakvehLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDA----DSVAWLEHFLHDFPGTVVAITHD 218
Cdd:cd03293 129 -PHQ-----LSGGMRQRVALARALAVDPDVLLLDEPFSALDAltreQLQEELLDIWRETGKTVLLVTHD 191
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
17-218 |
9.32e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 93.07 E-value: 9.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 17 PKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARPMPGINVGYLPQEPKLDPQ--ATVRDIVEEAV 94
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSlpLTVRDLVAMGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 95 GQIKQAQARLDevyaayaepdadfdalAAEQAKLEAILQAsdghnlerqleVAADALRLPPWDAkvehLSGGEKRRVALC 174
Cdd:NF040873 83 WARRGLWRRLT----------------RDDRAAVDDALER-----------VGLADLAGRQLGE----LSGGQRQRALLA 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15599791 175 RLLLSAPDMLLLDEPTNHLDADSVAWLEHFL---HDFPGTVVAITHD 218
Cdd:NF040873 132 QGLAQEADLLLLDEPTTGLDAESRERIIALLaeeHARGATVVVVTHD 178
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
307-500 |
9.74e-22 |
|
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: 99.52 E-value: 9.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 307 ETNEIYIPAGPRLGDkvIELHNVTKGYGDRV--LIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIG- 383
Cdd:COG2274 459 EEGRSKLSLPRLKGD--IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDg 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 384 --------ETV--QIASVDQS----RDSLEGNKTVW-EQVSDgfEQIkignYEVPSRSyvgrfnfkGADQqkFVKD---- 444
Cdd:COG2274 537 idlrqidpASLrrQIGVVLQDvflfSGTIRENITLGdPDATD--EEI----IEAARLA--------GLHD--FIEAlpmg 600
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599791 445 -----------LSGGERGRLHLALTLKQGGNVLLLDEPSNDLDVETLRALEEALLDFPGAA--IVISHD 500
Cdd:COG2274 601 ydtvvgeggsnLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRtvIIIAHR 669
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
8-236 |
1.91e-21 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 92.81 E-value: 1.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 8 MHRVGKIVPPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGE------------ARPMPGI--NVGY 73
Cdd:COG2884 4 FENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQvlvngqdlsrlkRREIPYLrrRIGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 74 LPQEPKLDPQATVRDIVE---EAVGQ-IKQAQARLDEVyaayaepdadfdalaaeqakLEAIlqasdghNLERQLevaad 149
Cdd:COG2884 84 VFQDFRLLPDRTVYENVAlplRVTGKsRKEIRRRVREV--------------------LDLV-------GLSDKA----- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 150 alrlppwDAKVEHLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSvAW--LEHF--LHDFPGTVVAITHDRYFLDNV 225
Cdd:COG2884 132 -------KALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPET-SWeiMELLeeINRRGTTVLIATHDLELVDRM 203
|
250
....*....|.
gi 15599791 226 AGWILELDRGH 236
Cdd:COG2884 204 PKRVLELEDGR 214
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
19-236 |
2.60e-21 |
|
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: 90.91 E-value: 2.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEAR----PMPGI-------NVGYLPQEPKLdPQATVR 87
Cdd:cd03228 15 KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILidgvDLRDLdleslrkNIAYVPQDPFL-FSGTIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 88 DiveeavgqikqaqarldevyaayaepdadfdalaaeqakleailqasdghNLerqlevaadalrlppwdakvehLSGGE 167
Cdd:cd03228 94 E--------------------------------------------------NI----------------------LSGGQ 101
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599791 168 KRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPG--TVVAITHdRYFLDNVAGWILELDRGH 236
Cdd:cd03228 102 RQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKgkTVIVIAH-RLSTIRDADRIIVLDDGR 171
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
324-476 |
3.20e-21 |
|
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: 91.93 E-value: 3.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETV---------QIASVDQS 394
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDvtdlppkdrDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 395 RdSLEGNKTVWEQVSDGFEQIKIGNYEVPSR-SYVGRFNFKGADQQKFVKDLSGGERGRLHLALTLKQGGNVLLLDEPSN 473
Cdd:cd03301 81 Y-ALYPHMTVYDNIAFGLKLRKVPKDEIDERvREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
...
gi 15599791 474 DLD 476
Cdd:cd03301 160 NLD 162
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
16-226 |
3.43e-21 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 96.90 E-value: 3.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 16 PPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDT----EIEGEARPMPGI----------NVGYLPQEPK-- 79
Cdd:COG1123 275 KGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRptsgSILFDGKDLTKLsrrslrelrrRVQMVFQDPYss 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 80 LDPQATVRDIVEEAV---GQIKQAQARldevyaayaepdadfdalaaeqAKLEAILqasdghnleRQLEVAADALRLPPW 156
Cdd:COG1123 355 LNPRMTVGDIIAEPLrlhGLLSRAERR----------------------ERVAELL---------ERVGLPPDLADRYPH 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599791 157 DakvehLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDAdSVAW-----LEHFLHDFPGTVVAITHD----RYFLDNVA 226
Cdd:COG1123 404 E-----LSGGQRQRVAIARALALEPKLLILDEPTSALDV-SVQAqilnlLRDLQRELGLTYLFISHDlavvRYIADRVA 476
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
294-532 |
3.71e-21 |
|
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: 97.14 E-value: 3.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 294 FEELQSQEFQKRSETNEIyipagPRLGDKVIELHNVTKGYGD-RVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGK 372
Cdd:COG4988 312 FALLDAPEPAAPAGTAPL-----PAAGPPSIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGF 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 373 EQPDSGTIEIGEtVQIASVDQSrdslegnkTVWEQVSdgfeqikignYeVPSRSYVgrfnFKG------------ADQQ- 439
Cdd:COG4988 387 LPPYSGSILING-VDLSDLDPA--------SWRRQIA----------W-VPQNPYL----FAGtirenlrlgrpdASDEe 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 440 -----------KFVKD---------------LSGGERGRLHLALTLKQGGNVLLLDEPSNDLDVETLRALEEALLDFPG- 492
Cdd:COG4988 443 leaaleaagldEFVAAlpdgldtplgeggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKg 522
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 15599791 493 -AAIVISHdRWFLDRIATHILSYeDDGKVTfFEGNYTEFEA 532
Cdd:COG4988 523 rTVILITH-RLALLAQADRILVL-DDGRIV-EQGTHEELLA 560
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
18-236 |
4.51e-21 |
|
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: 92.56 E-value: 4.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGE----ARPMPGI-------NVGYLPQEPK--LDPQA 84
Cdd:COG1124 17 RVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEvtfdGRPVTRRrrkafrrRVQMVFQDPYasLHPRH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 85 TVRDIVEEAVgqikqAQARLDEVyaayaepdadfdalaaeQAKLEAILqasdghnleRQLEVAADAL-RLPpwdakveH- 162
Cdd:COG1124 97 TVDRILAEPL-----RIHGLPDR-----------------EERIAELL---------EQVGLPPSFLdRYP-------Hq 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599791 163 LSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDAdSV-----AWLEHFLHDFPGTVVAITHDRYFLDNVAGWILELDRGH 236
Cdd:COG1124 139 LSGGQRQRVAIARALILEPELLLLDEPTSALDV-SVqaeilNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGR 216
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
21-219 |
5.36e-21 |
|
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: 91.43 E-value: 5.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGE----ARPMPGI-----NVGYLPQEPKLDPQATVRDIVe 91
Cdd:cd03259 15 ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEilidGRDVTGVpperrNIGMVFQDYALFPHLTVAENI- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 92 eavgqikqaqarldevyaAYAEPDADFDALAAEQAKLEAILQASDGHNLERqlevaadalrlppwdaKVEHLSGGEKRRV 171
Cdd:cd03259 94 ------------------AFGLKLRGVPKAEIRARVRELLELVGLEGLLNR----------------YPHELSGGQQQRV 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15599791 172 ALCRLLLSAPDMLLLDEPTNHLDADS----VAWLEHFLHDFPGTVVAITHDR 219
Cdd:cd03259 140 ALARALAREPSLLLLDEPLSALDAKLreelREELKELQRELGITTIYVTHDQ 191
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
332-500 |
5.47e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 90.76 E-value: 5.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 332 GYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETVQIASVDQ-SR--DSLEgnKTVWEQV 408
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQrSEvpDSLP--LTVRDLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 409 SDGFEQiKIGNYEVPSRS----------YVGRFNFkgADQQkfVKDLSGGERGRLHLALTLKQGGNVLLLDEPSNDLDVE 478
Cdd:NF040873 79 AMGRWA-RRGLWRRLTRDdraavddaleRVGLADL--AGRQ--LGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAE 153
|
170 180
....*....|....*....|....*
gi 15599791 479 TLRALEEALLDF--PGAAIV-ISHD 500
Cdd:NF040873 154 SRERIIALLAEEhaRGATVVvVTHD 178
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
324-513 |
7.52e-21 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 91.10 E-value: 7.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLIDNLSLSIPKGaIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETVQIASVDQSRDSLeG--- 400
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRI-Gylp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 401 -------NKTVWEQVsDGFEQIK-IGNYEVPSR-----SYVGRFNFKGadqqKFVKDLSGGERGRLHLALTLKQGGNVLL 467
Cdd:cd03264 79 qefgvypNFTVREFL-DYIAWLKgIPSKEVKARvdevlELVNLGDRAK----KKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15599791 468 LDEPSNDLDVETLRALEEALLDFPGAAIVIshdrwfldrIATHILS 513
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSELGEDRIVI---------LSTHIVE 190
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
324-512 |
8.55e-21 |
|
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: 91.34 E-value: 8.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIE------------------IGET 385
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfdgeditglppheiarlgIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 386 VQIASV---------------DQSRDSL------EGNKTVWEQVSDGFEQIKIGNYevpsrsyvgrfnfkgADQQkfVKD 444
Cdd:cd03219 81 FQIPRLfpeltvlenvmvaaqARTGSGLllararREEREARERAEELLERVGLADL---------------ADRP--AGE 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599791 445 LSGGERGRLHLALTLKQGGNVLLLDEPS---NDLDVETLRALEEALLDFpGAAIV-ISHDRWFLDRIATHIL 512
Cdd:cd03219 144 LSYGQQRRLEIARALATDPKLLLLDEPAaglNPEETEELAELIRELRER-GITVLlVEHDMDVVMSLADRVT 214
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
19-218 |
8.94e-21 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 91.80 E-value: 8.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARPmPGINVGYLP------------QEPKLDPQATV 86
Cdd:TIGR03873 14 RLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDL-AGVDLHGLSrrararrvalveQDSDTAVPLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 87 RDIVeeAVGQIKQAQArldevYAAyaEPDADFDALAAEQAKLEAILQAsdghnlerqlevaadalrlppwDAKVEHLSGG 166
Cdd:TIGR03873 93 RDVV--ALGRIPHRSL-----WAG--DSPHDAAVVDRALARTELSHLA----------------------DRDMSTLSGG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15599791 167 EKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPG---TVVAITHD 218
Cdd:TIGR03873 142 ERQRVHVARALAQEPKLLLLDEPTNHLDVRAQLETLALVRELAAtgvTVVAALHD 196
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
324-479 |
1.24e-20 |
|
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: 90.51 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGtieigeTVQIASVDQSRDSLEGNKT 403
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSG------RATVAGHDVVREPREVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 404 ---VWEQVS-----DGFEQIKI--GNYEVPSR----------SYVGRFNFKgadqQKFVKDLSGGERGRLHLALTLKQGG 463
Cdd:cd03265 75 igiVFQDLSvddelTGWENLYIhaRLYGVPGAerreridellDFVGLLEAA----DRLVKTYSGGMRRRLEIARSLVHRP 150
|
170
....*....|....*.
gi 15599791 464 NVLLLDEPSNDLDVET 479
Cdd:cd03265 151 EVLFLDEPTIGLDPQT 166
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
291-483 |
1.38e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 92.97 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 291 LQRFEELQSQEFQKRSETNEIYIPAGpRLGDKVIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLT 370
Cdd:PRK13536 10 APRRLELSPIERKHQGISEAKASIPG-SMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 371 GKEQPDSGTIEI-GETV---------QIASVDQSrDSLEGNKTVWEQ--VSDGFEQIKIGNYE--VPSRSYVGRFNFKgA 436
Cdd:PRK13536 89 GMTSPDAGKITVlGVPVpararlaraRIGVVPQF-DNLDLEFTVRENllVFGRYFGMSTREIEavIPSLLEFARLESK-A 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15599791 437 DQQkfVKDLSGGERGRLHLALTLKQGGNVLLLDEPSNDLDV-------ETLRAL 483
Cdd:PRK13536 167 DAR--VSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPharhliwERLRSL 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
17-242 |
1.67e-20 |
|
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: 89.94 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 17 PKREILKDISLSFFPGAkIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpMPGINV-----------GYLPQEPKLDPQAT 85
Cdd:cd03264 11 GKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIR-IDGQDVlkqpqklrrriGYLPQEFGVYPNFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 86 VRDIVEEAvgqikqaqARLDEVyaayaePDADFDAlAAEQAkLEAIlqasdghNLErqlEVAadalrlppwDAKVEHLSG 165
Cdd:cd03264 89 VREFLDYI--------AWLKGI------PSKEVKA-RVDEV-LELV-------NLG---DRA---------KKKIGSLSG 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599791 166 GEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPGTVVAI--THDRYFLDNVAGWILELDRGHgIPFEG 242
Cdd:cd03264 134 GMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVIlsTHIVEDVESLCNQVAVLNKGK-LVFEG 211
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
323-508 |
2.44e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 90.60 E-value: 2.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 323 VIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGetvQIASVDQSRDSLEGNK 402
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLN---GRPLADWSPAELARRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 403 TVWEQVSD-GF-----EQIKIGnyevpsrSYVGRFNFKGADQ---------------QKFVKDLSGGERGRLHLALTLKQ 461
Cdd:PRK13548 79 AVLPQHSSlSFpftveEVVAMG-------RAPHGLSRAEDDAlvaaalaqvdlahlaGRDYPQLSGGEQQRVQLARVLAQ 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599791 462 ------GGNVLLLDEPSNDLDV----ETLRALEEALLDFPGAAIVISHD-----RWfLDRIA 508
Cdd:PRK13548 152 lwepdgPPRWLLLDEPTSALDLahqhHVLRLARQLAHERGLAVIVVLHDlnlaaRY-ADRIV 212
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
16-234 |
3.02e-20 |
|
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: 93.89 E-value: 3.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 16 PPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGE----ARPMPGIN-------VGYLPQEPKLdPQA 84
Cdd:TIGR02857 332 PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSiavnGVPLADADadswrdqIAWVPQHPFL-FAG 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 85 TVRDIVeeavgqikqaqarldevyaAYAEPDADFDAL--AAEQAKLEAILQAsdghnLERQLEVAADalrlppwdakvEH 162
Cdd:TIGR02857 411 TIAENI-------------------RLARPDASDAEIreALERAGLDEFVAA-----LPQGLDTPIG-----------EG 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599791 163 ---LSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPG--TVVAITHDRyfldnvaGWILELDR 234
Cdd:TIGR02857 456 gagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRL-------ALAALADR 525
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
323-476 |
3.15e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 91.41 E-value: 3.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 323 VIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETV-QIASVDQSR----- 395
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcGEPVpSRARHARQRvgvvp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 396 --DSLEGNKTVWEQVsdgfeqIKIGNY----------EVPSRSYVGRFNFKgADQQkfVKDLSGGERGRLHLALTLKQGG 463
Cdd:PRK13537 87 qfDNLDPDFTVRENL------LVFGRYfglsaaaaraLVPPLLEFAKLENK-ADAK--VGELSGGMKRRLTLARALVNDP 157
|
170
....*....|...
gi 15599791 464 NVLLLDEPSNDLD 476
Cdd:PRK13537 158 DVLVLDEPTTGLD 170
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
320-499 |
5.96e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 93.17 E-value: 5.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 320 GDKVIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQIASvdqSRDSL 398
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIdGKPVRIRS---PRDAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 399 E-------------GNKTVWEQVSDGFEQIKIGNY-------EVpsRSYVGRFNFKgADQQKFVKDLSGGERGRLHLALT 458
Cdd:COG3845 79 AlgigmvhqhfmlvPNLTVAENIVLGLEPTKGGRLdrkaaraRI--RELSERYGLD-VDPDAKVEDLSVGEQQRVEILKA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15599791 459 LKQGGNVLLLDEP--------SNDLdVETLRALEEAlldfpGAAIV-ISH 499
Cdd:COG3845 156 LYRGARILILDEPtavltpqeADEL-FEILRRLAAE-----GKSIIfITH 199
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
323-508 |
6.13e-20 |
|
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: 88.72 E-value: 6.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 323 VIELHNVTKGY----GDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETvQIASVDQSRDSL 398
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGK-DLLKLSRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 399 EGNK----------------TVWEQVSDGFEQIKIGNYEVPSRSYVGRFNFKGADQQKFVK----DLSGGERGRLHLALT 458
Cdd:cd03257 80 RRKEiqmvfqdpmsslnprmTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNryphELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599791 459 LKQGGNVLLLDEPSNDLDV-------ETLRALEEALldfpGAAIV-ISHD----RWFLDRIA 508
Cdd:cd03257 160 LALNPKLLIADEPTSALDVsvqaqilDLLKKLQEEL----GLTLLfITHDlgvvAKIADRVA 217
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
324-520 |
6.38e-20 |
|
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: 88.23 E-value: 6.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVL-IDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETV------QIASVDQS- 394
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVnGQDVsdlrgrAIPYLRRKi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 395 ----RDS-LEGNKTVWEQVSDGFEQIKIGNYEVPSR--SYVGRFNFKGaDQQKFVKDLSGGERGRLHLALTLKQGGNVLL 467
Cdd:cd03292 81 gvvfQDFrLLPDRNVYENVAFALEVTGVPPREIRKRvpAALELVGLSH-KHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15599791 468 LDEPSNDLDVETLRALEEALLDF--PGAAIVIS-HDRWFLDRIATHILSYEdDGKV 520
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKInkAGTTVVVAtHAKELVDTTRHRVIALE-RGKL 214
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
324-500 |
6.56e-20 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 89.40 E-value: 6.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETvQIAsvDQSRDSLEGNKT 403
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGR-PLA--AWSPWELARRRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 404 VWEQVSD-GF-----EQIKIGNYevpsrsyvGRFNFKGADQQ----------------KFVKDLSGGERGRLHLALTLKQ 461
Cdd:COG4559 79 VLPQHSSlAFpftveEVVALGRA--------PHGSSAAQDRQivrealalvglahlagRSYQTLSGGEQQRVQLARVLAQ 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15599791 462 -------GGNVLLLDEPSNDLDV----ETLRALEEaLLDFPGAAIVISHD 500
Cdd:COG4559 151 lwepvdgGPRWLFLDEPTSALDLahqhAVLRLARQ-LARRGGGVVAVLHD 199
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
324-498 |
8.44e-20 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 87.72 E-value: 8.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQIAS------------ 390
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFdGKPLDIAArnrigylpeerg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 391 -------VDQSR--DSLEG--NKTVWEQVSDGFEQIKIGNYEvpsrsyvgrfnfkgadqQKFVKDLSGGERGRLHLALTL 459
Cdd:cd03269 81 lypkmkvIDQLVylAQLKGlkKEEARRRIDEWLERLELSEYA-----------------NKRVEELSKGNQQKVQFIAAV 143
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15599791 460 KQGGNVLLLDEPSNDLDVETLRALEEALLDF--PGAAIVIS 498
Cdd:cd03269 144 IHDPELLILDEPFSGLDPVNVELLKDVIRELarAGKTVILS 184
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
320-512 |
8.78e-20 |
|
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: 88.94 E-value: 8.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 320 GDKVIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIE------------------ 381
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILfdgrditglpphriarlg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 382 IGETVQIAsvdqsrdSLEGNKTVWEQVsdgfeqiKIGNYEVPSRSYVGR-FNFKGADQQ--------------------- 439
Cdd:COG0411 81 IARTFQNP-------RLFPELTVLENV-------LVAAHARLGRGLLAAlLRLPRARREereareraeellervgladra 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599791 440 -KFVKDLSGGERGRLHLALTLKQGGNVLLLDEPS---NDLDVETLRALEEALLDFPGAAIV-ISHDRWFLDRIATHIL 512
Cdd:COG0411 147 dEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAaglNPEETEELAELIRRLRDERGITILlIEHDMDLVMGLADRIV 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
324-500 |
9.14e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 91.44 E-value: 9.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETV----------QIASVD 392
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVaGDDVealsaraasrRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 393 QSRdSLEGNKTVwEQVsdgfeqIKIGnyEVPSRSYVGR------------FNFKGADQ--QKFVKDLSGGERGRLHLALT 458
Cdd:PRK09536 84 QDT-SLSFEFDV-RQV------VEMG--RTPHRSRFDTwtetdraaveraMERTGVAQfaDRPVTSLSGGERQRVLLARA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15599791 459 LKQGGNVLLLDEPSNDLDV-ETLRALEEA--LLDFPGAAIVISHD 500
Cdd:PRK09536 154 LAQATPVLLLDEPTASLDInHQVRTLELVrrLVDDGKTAVAAIHD 198
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
14-235 |
1.37e-19 |
|
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: 92.03 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 14 IVPP--KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEAR-----------PMPGINVGYLPQEPKL 80
Cdd:TIGR01842 324 IVPPggKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRldgadlkqwdrETFGKHIGYLPQDVEL 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 81 DPqatvrdiveeavGQIKQAQARLDEvyaaYAEPDADFDALAAEQAKlEAILQASDGHNlerqLEVAADAlrlppwdakv 160
Cdd:TIGR01842 404 FP------------GTVAENIARFGE----NADPEKIIEAAKLAGVH-ELILRLPDGYD----TVIGPGG---------- 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599791 161 EHLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFP---GTVVAITHdRYFLDNVAGWILELDRG 235
Cdd:TIGR01842 453 ATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKargITVVVITH-RPSLLGCVDKILVLQDG 529
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
14-238 |
2.07e-19 |
|
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: 85.67 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 14 IVPPKREIL-KDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARPMPGINVGYLPQEPKLdPQATVRDIVee 92
Cdd:cd03223 8 LATPDGRVLlKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYL-PLGTLREQL-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 93 avgqikqaqarldevyaAYaepdadfdalaaeqakleailqasdghnlerqlevaadalrlpPWDAKvehLSGGEKRRVA 172
Cdd:cd03223 85 -----------------IY-------------------------------------------PWDDV---LSGGEQQRLA 101
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599791 173 LCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPGTVVAITHdRYFLDNVAGWILELDRGHGI 238
Cdd:cd03223 102 FARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLDGEGGW 166
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
321-477 |
2.07e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 88.31 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 321 DKVIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETV-----------QIA 389
Cdd:PRK10575 9 DTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPleswsskafarKVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 390 SVDQSRDSLEGnKTVWEQVSdgfeqikIGNYevPSRSYVGRFNfkGADQQK----------------FVKDLSGGERGRL 453
Cdd:PRK10575 89 YLPQQLPAAEG-MTVRELVA-------IGRY--PWHGALGRFG--AADREKveeaislvglkplahrLVDSLSGGERQRA 156
|
170 180
....*....|....*....|....
gi 15599791 454 HLALTLKQGGNVLLLDEPSNDLDV 477
Cdd:PRK10575 157 WIAMLVAQDSRCLLLDEPTSALDI 180
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
324-520 |
4.46e-19 |
|
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: 86.00 E-value: 4.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGD----RVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQIASvDQSRDSL 398
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVdGTDISKLS-EKELAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 399 EGNK--------------TVWEQVSDGFEQIKIGNYEVPSR-----SYVG---RFNfkgadqqKFVKDLSGGERGRLHLA 456
Cdd:cd03255 80 RRRHigfvfqsfnllpdlTALENVELPLLLAGVPKKERRERaeellERVGlgdRLN-------HYPSELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599791 457 LTLKQGGNVLLLDEPSNDLDVETLRALEEALLDF---PGAAIVI-SHDRwFLDRIATHILSYEdDGKV 520
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMELLRELnkeAGTTIVVvTHDP-ELAEYADRIIELR-DGKI 218
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
162-371 |
5.03e-19 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 90.07 E-value: 5.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 162 HLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPGTVVAIthdryfldnvagwILELDRGHGIPFE 241
Cdd:PRK10938 135 YLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITL-------------VLVLNRFDEIPDF 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 242 GNYSGWLeskaarlaqeakqeashakamkAELEWVRQGAKgrqaksKARLQrfEELQSQefQKRSETNE-IYIP------ 314
Cdd:PRK10938 202 VQFAGVL----------------------ADCTLAETGER------EEILQ--QALVAQ--LAHSEQLEgVQLPepdeps 249
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15599791 315 AGPRL--GDKVIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTG 371
Cdd:PRK10938 250 ARHALpaNEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG 308
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
324-483 |
7.58e-19 |
|
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: 85.85 E-value: 7.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQIASVdQSRD------ 396
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFgGEDATDVPV-QERNvgfvfq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 397 --SLEGNKTVWEQVSDGFEQIKIGnyEVPSRSYVGR-----FNFKGAD--QQKFVKDLSGGERGRLHLALTLKQGGNVLL 467
Cdd:cd03296 82 hyALFRHMTVFDNVAFGLRVKPRS--ERPPEAEIRAkvhelLKLVQLDwlADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170
....*....|....*.
gi 15599791 468 LDEPSNDLDVETLRAL 483
Cdd:cd03296 160 LDEPFGALDAKVRKEL 175
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
22-471 |
7.96e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 89.31 E-value: 7.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV---DT---EIEGEARPMPGIN------VGYLPQEPKLDPQATVRD- 88
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVyqpDSgeiLLDGEPVRFRSPRdaqaagIAIIHQELNLVPNLSVAEn 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 89 IveeAVGQIKQAQARLDEvyaayaepdadfdalAAEQAKLEAILqasdghnleRQLEvaadaLRLPPwDAKVEHLSGGEK 168
Cdd:COG1129 100 I---FLGREPRRGGLIDW---------------RAMRRRARELL---------ARLG-----LDIDP-DTPVGDLSVAQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 169 RRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPG---TVVAITHdryFLDNvagwILEL-DR------GHGI 238
Cdd:COG1129 147 QLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAqgvAIIYISH---RLDE----VFEIaDRvtvlrdGRLV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 239 pfegnysgwleskaarlAQEAKQEASHA---KAMkaelewVrqgakGRqakskarlqrfeelqsqefqkrsETNEIYIPA 315
Cdd:COG1129 220 -----------------GTGPVAELTEDelvRLM------V-----GR-----------------------ELEDLFPKR 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 316 GPRLGDKVIELHNVTKGYGdrvlIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQIASVDQS 394
Cdd:COG1129 249 AAAPGEVVLEVEGLSVGGV----VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLdGKPVRIRSPRDA 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 395 -------------RDSLEGNKTVWE--------QVSDGF-----EQIKIgnyevpSRSYVGRFNFKGADQQKFVKDLSGG 448
Cdd:COG1129 325 iragiayvpedrkGEGLVLDLSIREnitlasldRLSRGGlldrrRERAL------AEEYIKRLRIKTPSPEQPVGNLSGG 398
|
490 500
....*....|....*....|...
gi 15599791 449 ERGRLHLALTLKQGGNVLLLDEP 471
Cdd:COG1129 399 NQQKVVLAKWLATDPKVLILDEP 421
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
22-236 |
8.42e-19 |
|
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: 85.85 E-value: 8.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTE------IEGE---ARPMPGINVGYLPQEPKLDPQATVRDIVee 92
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPdsgtilFGGEdatDVPVQERNVGFVFQHYALFRHMTVFDNV-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 93 AVG-QIKQAQARLDEvyaayaepdadfdalAAEQAKLEAILQASdghnlerQLEVAADalRLPPwdakveHLSGGEKRRV 171
Cdd:cd03296 96 AFGlRVKPRSERPPE---------------AEIRAKVHELLKLV-------QLDWLAD--RYPA------QLSGGQRQRV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599791 172 ALCRLLLSAPDMLLLDEPTNHLDA----DSVAWLEHFLHDFPGTVVAITHDRYFLDNVAGWILELDRGH 236
Cdd:cd03296 146 ALARALAVEPKVLLLDEPFGALDAkvrkELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGR 214
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
16-218 |
1.03e-18 |
|
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: 89.34 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 16 PPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---------------VDTEIEGEARPMpginVGYLPQEPKL 80
Cdd:TIGR02868 345 PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGlldplqgevtldgvpVSSLDQDEVRRR----VSVCAQDAHL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 81 DpQATVRDIVeeavgqikqaqaRLdevyaayAEPDADFDAL--AAEQAKLEAILQA-SDGHNLErqleVAADALRLppwd 157
Cdd:TIGR02868 421 F-DTTVRENL------------RL-------ARPDATDEELwaALERVGLADWLRAlPDGLDTV----LGEGGARL---- 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599791 158 akvehlSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHD-FPG-TVVAITHD 218
Cdd:TIGR02868 473 ------SGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAaLSGrTVVLITHH 529
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
324-520 |
1.41e-18 |
|
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: 84.50 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETV-------------QIAS 390
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKltddkkninelrqKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 391 VDQSRDsLEGNKTVWEQVSDGfeQIKIGNY---EVPSRSY-----VGRFNFKgadqQKFVKDLSGGERGRLHLALTLKQG 462
Cdd:cd03262 81 VFQQFN-LFPHLTVLENITLA--PIKVKGMskaEAEERALellekVGLADKA----DAYPAQLSGGQQQRVAIARALAMN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599791 463 GNVLLLDEPSNDLDVETLRALEEALLDfpgAA------IVISHDRWFLDRIATHILsYEDDGKV 520
Cdd:cd03262 154 PKVMLFDEPTSALDPELVGEVLDVMKD---LAeegmtmVVVTHEMGFAREVADRVI-FMDDGRI 213
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
285-516 |
1.76e-18 |
|
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: 88.67 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 285 AKSKARLQRFEELQSQEFQKRSETNEIYIPAGPRLgdkviELHNVTKGY--GDRVLIDNLSLSIPKGAIVGVIGGNGAGK 362
Cdd:COG4987 300 GRVRAAARRLNELLDAPPAVTEPAEPAPAPGGPSL-----ELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGK 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 363 STLFRMLTGKEQPDSGTIEIGEtVQIASVDQSrdslegnkTVWEQVSdgfeqikignyEVPSRSYVgrF------NFKGA 436
Cdd:COG4987 375 STLLALLLRFLDPQSGSITLGG-VDLRDLDED--------DLRRRIA-----------VVPQRPHL--FdttlreNLRLA 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 437 DQQ----------------KFVKD---------------LSGGERGRLHLALTLKQGGNVLLLDEPSNDLDVETLRALEE 485
Cdd:COG4987 433 RPDatdeelwaalervglgDWLAAlpdgldtwlgeggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLA 512
|
250 260 270
....*....|....*....|....*....|...
gi 15599791 486 ALLD-FPGAA-IVISHDRWFLDRiATHILSYED 516
Cdd:COG4987 513 DLLEaLAGRTvLLITHRLAGLER-MDRILVLED 544
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
345-515 |
2.58e-18 |
|
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: 84.38 E-value: 2.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 345 SIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETV----QIASVDQS---RDSLE------GNKTVWE-QVS 409
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIeLDTVsykpQYIKADYEgtvRDLLSsitkdfYTHPYFKtEIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 410 DGFEQIKIGNYEVPsrsyvgrfnfkgadqqkfvkDLSGGERGRLHLALTLKQGGNVLLLDEPSNDLDVE----TLRALEE 485
Cdd:cd03237 101 KPLQIEQILDREVP--------------------ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEqrlmASKVIRR 160
|
170 180 190
....*....|....*....|....*....|
gi 15599791 486 ALLDFPGAAIVISHDRWFLDRIATHILSYE 515
Cdd:cd03237 161 FAENNEKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
324-481 |
3.69e-18 |
|
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: 83.83 E-value: 3.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETV--------QIASVDQS 394
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLdGKDItnlpphkrPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 395 RdSLEGNKTVWEQVSDGFEQIKIGNYEVPSR-----SYVGRFNFkgadQQKFVKDLSGGERGRLHLALTLKQGGNVLLLD 469
Cdd:cd03300 81 Y-ALFPHLTVFENIAFGLRLKKLPKAEIKERvaealDLVQLEGY----ANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170
....*....|..
gi 15599791 470 EPSNDLDVEtLR 481
Cdd:cd03300 156 EPLGALDLK-LR 166
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
323-476 |
4.84e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 86.04 E-value: 4.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 323 VIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIeIGETVQIASVD---------- 392
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQI-MLDGVDLSHVPpyqrpinmmf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 393 QSRdSLEGNKTVWEQVSDGFEQIKIGNYEVPSRsyVGRFnFKGADQQKFVK----DLSGGERGRLHLALTLKQGGNVLLL 468
Cdd:PRK11607 98 QSY-ALFPHMTVEQNIAFGLKQDKLPKAEIASR--VNEM-LGLVHMQEFAKrkphQLSGGQRQRVALARSLAKRPKLLLL 173
|
....*...
gi 15599791 469 DEPSNDLD 476
Cdd:PRK11607 174 DEPMGALD 181
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
18-211 |
5.27e-18 |
|
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: 82.65 E-value: 5.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEArpmpginvgylpqepKLDPQATVRDIveEAVGQI 97
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEI---------------TFDGKSYQKNI--EALRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 98 kqaqarldevyAAYAEPDADFDALAA-EQAKLEAILQASDGHNLERQLEV---AADAlrlppwDAKVEHLSGGEKRRVAL 173
Cdd:cd03268 75 -----------GALIEAPGFYPNLTArENLRLLARLLGIRKKRIDEVLDVvglKDSA------KKKVKGFSLGMKQRLGI 137
|
170 180 190
....*....|....*....|....*....|....*...
gi 15599791 174 CRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPGT 211
Cdd:cd03268 138 ALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQ 175
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
20-190 |
5.30e-18 |
|
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: 82.87 E-value: 5.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGE---------ARPMPGIN---VGYLPQEPKLDPQATVR 87
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSirfdgrditGLPPHERAragIGYVPEGRRIFPELTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 88 D--IVEEAVGQIKQAQARLDEVYAAyaepdadFDALAaeqakleailqasdghnlERqlevaadalrlppWDAKVEHLSG 165
Cdd:cd03224 94 EnlLLGAYARRRAKRKARLERVYEL-------FPRLK------------------ER-------------RKQLAGTLSG 135
|
170 180
....*....|....*....|....*
gi 15599791 166 GEKRRVALCRLLLSAPDMLLLDEPT 190
Cdd:cd03224 136 GEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
18-218 |
5.35e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 83.67 E-value: 5.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpMPGINV------------GYLPQEPKLDPQAT 85
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVR-LNGRPLadwspaelarrrAVLPQHSSLSFPFT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 86 VRDIVeeAVGQikqaqarldevyAAYAEPDADFDALAAEQakleaiLQASDghnlerqleVAADALRLPPwdakveHLSG 165
Cdd:PRK13548 93 VEEVV--AMGR------------APHGLSRAEDDALVAAA------LAQVD---------LAHLAGRDYP------QLSG 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599791 166 GEKRRVALCRLL--LSAPDM----LLLDEPTNHLDadsvawLEH----------FLHDFPGTVVAITHD 218
Cdd:PRK13548 138 GEQQRVQLARVLaqLWEPDGpprwLLLDEPTSALD------LAHqhhvlrlarqLAHERGLAVIVVLHD 200
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
18-218 |
6.56e-18 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 82.78 E-value: 6.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEAR----PMPGIN-----------VGYLPQEPKLDP 82
Cdd:COG1136 20 EVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLidgqDISSLSerelarlrrrhIGFVFQFFNLLP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 83 QATVRDIVEEAvgqikqaqARLDEVYAAYAEPDADfDALaaEQAKLEAILqasdghnlerqlevaadalrlppwDAKVEH 162
Cdd:COG1136 100 ELTALENVALP--------LLLAGVSRKERRERAR-ELL--ERVGLGDRL------------------------DHRPSQ 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 163 LSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADS----VAWLEHFLHDFPGTVVAITHD 218
Cdd:COG1136 145 LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHD 204
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
333-500 |
6.73e-18 |
|
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: 83.15 E-value: 6.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 333 YGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETV----------QIASVDQSRDSLegnk 402
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpwkrrkkflrRIGVVFGQKTQL---- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 403 tVWE-QVSDGFEQIK-IgnYEVPSRSY------------VGRFnfkgADQQkfVKDLSGGERGRLHLALTLKQGGNVLLL 468
Cdd:cd03267 107 -WWDlPVIDSFYLLAaI--YDLPPARFkkrldelselldLEEL----LDTP--VRQLSLGQRMRAEIAAALLHEPEILFL 177
|
170 180 190
....*....|....*....|....*....|....*.
gi 15599791 469 DEPSNDLDVETLRALEEALLDF---PGAAIVI-SHD 500
Cdd:cd03267 178 DEPTIGLDVVAQENIRNFLKEYnreRGTTVLLtSHY 213
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
324-531 |
1.04e-17 |
|
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: 80.82 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYG--DRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGEtVQIASVDQSRDSLEGn 401
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDG-VPVSDLEKALSSLIS- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 402 ktvweqvsdgfeqikignyEVPSRSYVgrfnFKGADQQKFVKDLSGGERGRLHLALTLKQGGNVLLLDEPSNDLDVETLR 481
Cdd:cd03247 79 -------------------VLNQRPYL----FDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITER 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15599791 482 ALEEALLDF--PGAAIVISHdrwfldriatHILSYEDDGKVTFFEGNYTEFE 531
Cdd:cd03247 136 QLLSLIFEVlkDKTLIWITH----------HLTGIEHMDKILFLENGKIIMQ 177
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
18-199 |
1.44e-17 |
|
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: 81.06 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG--VDTEIEGE----ARPMPGIN----VGYLPQEPKLDPQATVR 87
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEvlinGRPLDKRSfrkiIGYVPQDDILHPTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 88 diveEAvgqikqaqarldevyaayaepdadfdalaaeqakleailqasdghnlerqLEVAAdALRlppwdakveHLSGGE 167
Cdd:cd03213 101 ----ET--------------------------------------------------LMFAA-KLR---------GLSGGE 116
|
170 180 190
....*....|....*....|....*....|..
gi 15599791 168 KRRVALCRLLLSAPDMLLLDEPTNHLDADSVA 199
Cdd:cd03213 117 RKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
324-499 |
1.45e-17 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 80.34 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGD--RVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQIASVDQSRDsleg 400
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLdGADISQWDPNELGD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 401 nktvweqvsdgfeqiKIGnyevpsrsYVGRfnfkgaDQQKF---VKD--LSGGERGRLHLALTLKQGGNVLLLDEPSNDL 475
Cdd:cd03246 77 ---------------HVG--------YLPQ------DDELFsgsIAEniLSGGQRQRLGLARALYGNPRILVLDEPNSHL 127
|
170 180
....*....|....*....|....*..
gi 15599791 476 DVETLRALEEALLDFPGA---AIVISH 499
Cdd:cd03246 128 DVEGERALNQAIAALKAAgatRIVIAH 154
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
323-530 |
1.61e-17 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 85.71 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 323 VIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETVQIASVDQSRDSLE--- 399
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEeft 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 400 -------GNKTVWEQVS--------------DGfeqIKIGNYEVPSRSYVG-----RFN--FKGAD---QQKF--VKDLS 446
Cdd:PRK15064 81 vldtvimGHTELWEVKQerdriyalpemseeDG---MKVADLEVKFAEMDGytaeaRAGelLLGVGipeEQHYglMSEVA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 447 GGERGRLHLALTLKQGGNVLLLDEPSNDLDVETLRALEEALLDFPGAAIVISHDRWFLDRIATHI--LSYeddGKVTFFE 524
Cdd:PRK15064 158 PGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMadLDY---GELRVYP 234
|
....*.
gi 15599791 525 GNYTEF 530
Cdd:PRK15064 235 GNYDEY 240
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
22-508 |
2.21e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 85.08 E-value: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDT------EIEGEARPMP--------GInvGYLPQEPKLDPQATVR 87
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQpdsgeiLIDGKPVRIRsprdaialGI--GMVHQHFMLVPNLTVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 88 DIVeeAVGQIKQAQARLDevyaayaepdadfdaLAAEQAKLEAIlqaSDGHNLErqlevaadalrLPPwDAKVEHLSGGE 167
Cdd:COG3845 99 ENI--VLGLEPTKGGRLD---------------RKAARARIREL---SERYGLD-----------VDP-DAKVEDLSVGE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 168 KRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPG---TVVAITHDryfLDNVagwiLEL-DR--------- 234
Cdd:COG3845 147 QQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAegkSIIFITHK---LREV----MAIaDRvtvlrrgkv 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 235 -GHGIPfegnysgwleskaarlAQEAKQEAshAKAMkaelewVrqgakGRQAKSKARlqrfeelqsqefqkrsetneiyi 313
Cdd:COG3845 220 vGTVDT----------------AETSEEEL--AELM------V-----GREVLLRVE----------------------- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 314 PAGPRLGDKVIELHNVT-KGYGDRVLIDNLSLSIPKGAIVGVIG--GNgaGKSTLFRMLTGKEQPDSGTIEI-GETVQIA 389
Cdd:COG3845 248 KAPAEPGEVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGvaGN--GQSELAEALAGLRPPASGSIRLdGEDITGL 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 390 SVDQSRDS-------------LEGNKTVWE------QVSDGFEQ---IKIGNYEVPSRSYVGRFNFKGADQQKFVKDLSG 447
Cdd:COG3845 326 SPRERRRLgvayipedrlgrgLVPDMSVAEnlilgrYRRPPFSRggfLDRKAIRAFAEELIEEFDVRTPGPDTPARSLSG 405
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599791 448 GERGRLHLALTLKQGGNVLLLDEPSNDLDV-------ETLRALEEAlldfpGAAI-VISHDrwfL-------DRIA 508
Cdd:COG3845 406 GNQQKVILARELSRDPKLLIAAQPTRGLDVgaiefihQRLLELRDA-----GAAVlLISED---LdeilalsDRIA 473
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
323-511 |
2.41e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 84.68 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 323 VIELHNVTKGYGD-RVLiDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQIASVDQSRD---- 396
Cdd:COG1129 4 LLEMRGISKSFGGvKAL-DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLdGEPVRFRSPRDAQAagia 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 397 ------SLEGNKTVWeqvsdgfEQIKIGNYevPSRSyvGRFNFK-------------GAD---QQKfVKDLSGGERGRLH 454
Cdd:COG1129 83 iihqelNLVPNLSVA-------ENIFLGRE--PRRG--GLIDWRamrrrarellarlGLDidpDTP-VGDLSVAQQQLVE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599791 455 LALTLKQGGNVLLLDEPS---NDLDVETL----RALEEAlldfpGAAIV-ISHdrwFLD---RIATHI 511
Cdd:COG1129 151 IARALSRDARVLILDEPTaslTEREVERLfriiRRLKAQ-----GVAIIyISH---RLDevfEIADRV 210
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
323-521 |
2.42e-17 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 81.25 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 323 VIELHNVTKGY-GDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETV-------------Q 387
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVnGQDLsrlkrreipylrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 388 IASVDQsrD-SLEGNKTVWEQVSDGFEQIKIGNYEVPSR-----SYVGRFNFKgadqQKFVKDLSGGERGRLHLA----- 456
Cdd:COG2884 81 IGVVFQ--DfRLLPDRTVYENVALPLRVTGKSRKEIRRRvrevlDLVGLSDKA----KALPHELSGGEQQRVAIAralvn 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599791 457 ---LtlkqggnvLLLDEPSNDLDVETLRALEEALLDF--PGAAIVI-SHDRWFLDRIATHILSYEdDGKVT 521
Cdd:COG2884 155 rpeL--------LLADEPTGNLDPETSWEIMELLEEInrRGTTVLIaTHDLELVDRMPKRVLELE-DGRLV 216
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
16-236 |
2.69e-17 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 85.22 E-value: 2.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 16 PPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------------GVD-TEIEGEA-RPmpgiNVGYLPQEPKL 80
Cdd:COG1132 350 PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLrfydptsgrilidGVDiRDLTLESlRR----QIGVVPQDTFL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 81 -DpqATVRD-IveeavgqikqaqarldevyaAYAEPDADFDAL--AAEQAkleailQASDghnlerqlevaaDALRLPP- 155
Cdd:COG1132 426 fS--GTIREnI--------------------RYGRPDATDEEVeeAAKAA------QAHE------------FIEALPDg 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 156 WDAKVE----HLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAW----LEHFLHDfpGTVVAITH--------DR 219
Cdd:COG1132 466 YDTVVGergvNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALiqeaLERLMKG--RTTIVIAHrlstirnaDR 543
|
250
....*....|....*..
gi 15599791 220 yfldnvagwILELDRGH 236
Cdd:COG1132 544 ---------ILVLDDGR 551
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
328-520 |
2.94e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.96 E-value: 2.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 328 NVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQ-IASVDQSRD--------S 397
Cdd:PRK10253 12 QLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLdGEHIQhYASKEVARRigllaqnaT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 398 LEGNKTVWEQVSDG-------FEQIKIGNYEVPSRSYVGRFNFKGADQQkfVKDLSGGERGRLHLALTLKQGGNVLLLDE 470
Cdd:PRK10253 92 TPGDITVQELVARGryphqplFTRWRKEDEEAVTKAMQATGITHLADQS--VDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15599791 471 PSNDLDVETLRALEEALLD------FPGAAIVisHDRWFLDRIATHILSYEdDGKV 520
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSElnrekgYTLAAVL--HDLNQACRYASHLIALR-EGKI 222
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-242 |
3.47e-17 |
|
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: 81.30 E-value: 3.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 28 SFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEArPMPGINVGYLPQEPKLDPQATVRDIVEEavgqikqaqaRLDEV 107
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI-EIELDTVSYKPQYIKADYEGTVRDLLSS----------ITKDF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 108 YAayaepDADFDALAAEQAKLEAILqasdghnlerqlevaadalrlppwDAKVEHLSGGEKRRVALCRLLLSAPDMLLLD 187
Cdd:cd03237 90 YT-----HPYFKTEIAKPLQIEQIL------------------------DREVPELSGGELQRVAIAACLSKDADIYLLD 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599791 188 EPTNHLD------ADSVawLEHFLHDFPGTVVAITHDRYFLDNVAgwilelDRghGIPFEG 242
Cdd:cd03237 141 EPSAYLDveqrlmASKV--IRRFAENNEKTAFVVEHDIIMIDYLA------DR--LIVFEG 191
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
20-238 |
3.53e-17 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 81.21 E-value: 3.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGE-----------ARPMPGI------NVGYLPQEPKLDP 82
Cdd:COG4161 16 QALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQlniaghqfdfsQKPSEKAirllrqKVGMVFQQYNLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 83 QATVRDIVEEA----VGQIKQAqarldevyaayaepdadfdalAAEQAKleailqasdghNLERQLEVAADALRLPpwda 158
Cdd:COG4161 96 HLTVMENLIEApckvLGLSKEQ---------------------AREKAM-----------KLLARLRLTDKADRFP---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 159 kvEHLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPG---TVVAITHDRYFLDNVAGWILELDRG 235
Cdd:COG4161 140 --LHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtgiTQVIVTHEVEFARKVASQVVYMEKG 217
|
...
gi 15599791 236 HGI 238
Cdd:COG4161 218 RII 220
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-189 |
3.89e-17 |
|
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: 82.84 E-value: 3.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 24 DISLSFfPGAKIGVL-GLNGAGKSTLLRIMAGVDTEIEG--------------------EARPmpginVGYLPQEPKLDP 82
Cdd:COG4148 17 DVDFTL-PGRGVTALfGPSGSGKTTLLRAIAGLERPDSGrirlggevlqdsargiflppHRRR-----IGYVFQEARLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 83 QATVRDIVEEAVGQIKQAQARldevyaayaepdADFDALAAeqakLEAIlqasdGHNLERqlevaadalrlppwdaKVEH 162
Cdd:COG4148 91 HLSVRGNLLYGRKRAPRAERR------------ISFDEVVE----LLGI-----GHLLDR----------------RPAT 133
|
170 180
....*....|....*....|....*..
gi 15599791 163 LSGGEKRRVALCRLLLSAPDMLLLDEP 189
Cdd:COG4148 134 LSGGERQRVAIGRALLSSPRLLLMDEP 160
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
30-218 |
3.90e-17 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 80.42 E-value: 3.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 30 FPGAKIGVLGLNGAGKSTLLRIMAGVDT----EIEGEARPM----PGIN-------VGYLPQEPKLDPQATVRDIVEEAV 94
Cdd:cd03297 21 LNEEVTGIFGASGAGKSTLLRCIAGLEKpdggTIVLNGTVLfdsrKKINlppqqrkIGLVFQQYALFPHLNVRENLAFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 95 GQIKQAQARLdevyaayaEPDADFDALAAEQAKleailqasdghnlerqlevaadalrlppwDAKVEHLSGGEKRRVALC 174
Cdd:cd03297 101 KRKRNREDRI--------SVDELLDLLGLDHLL-----------------------------NRYPAQLSGGEKQRVALA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15599791 175 RLLLSAPDMLLLDEPTNHLDADSVAWLEHFLH----DFPGTVVAITHD 218
Cdd:cd03297 144 RALAAQPELLLLDEPFSALDRALRLQLLPELKqikkNLNIPVIFVTHD 191
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
324-513 |
4.51e-17 |
|
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: 80.10 E-value: 4.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDR----VLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEigetvqIASVDQSRDSLE 399
Cdd:cd03266 2 ITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFAT------VDGFDVVKEPAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 400 GNK---------------TVWEQVS--DGFEQIKIGNYEVPSRSYVGRFNFKgADQQKFVKDLSGGERGRLHLALTLKQG 462
Cdd:cd03266 76 ARRrlgfvsdstglydrlTARENLEyfAGLYGLKGDELTARLEELADRLGME-ELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15599791 463 GNVLLLDEPSNDLDVETLRALEEAL--LDFPGAAIVIShdrwfldriaTHILS 513
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIrqLRALGKCILFS----------THIMQ 197
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
19-242 |
4.71e-17 |
|
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: 80.62 E-value: 4.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDT------EIEG---------EARPMPgINVGYLPQEPKLDPQ 83
Cdd:cd03261 13 RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRpdsgevLIDGedisglseaELYRLR-RRMGMLFQSGALFDS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 84 ATVRDIVeeavgqikqaQARLDEvyaAYAEPDADFDALAAEqaKLEAIlqasdghNLErqlevaADALRLPpwdakvEHL 163
Cdd:cd03261 92 LTVFENV----------AFPLRE---HTRLSEEEIREIVLE--KLEAV-------GLR------GAEDLYP------AEL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 164 SGGEKRRVALCRLLLSAPDMLLLDEPTNHLD---ADSVAWLEHFLHDFPG-TVVAITHDRYFLDNVAGWILELDRGHgIP 239
Cdd:cd03261 138 SGGMKKRVALARALALDPELLLYDEPTAGLDpiaSGVIDDLIRSLKKELGlTSIMVTHDLDTAFAIADRIAVLYDGK-IV 216
|
...
gi 15599791 240 FEG 242
Cdd:cd03261 217 AEG 219
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
324-539 |
4.85e-17 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 80.28 E-value: 4.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQIASVDQ-SRD----- 396
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLdGQDITKLPMHKrARLgigyl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 397 ----SLEGNKTVWEQVSDGFEQIKIGNYEVPSR--SYVGRFNFKGADQQKFVKdLSGGERGRLHLALTLKQGGNVLLLDE 470
Cdd:cd03218 81 pqeaSIFRKLTVEENILAVLEIRGLSKKEREEKleELLEEFHITHLRKSKASS-LSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 471 PSNDLD---VETLRALEEALLDFpGAAIVIS-HD-RWFL---DRIatHILSyedDGKVtFFEGNYTEFEAD---RKKRLG 539
Cdd:cd03218 160 PFAGVDpiaVQDIQKIIKILKDR-GIGVLITdHNvRETLsitDRA--YIIY---EGKV-LAEGTPEEIAANelvRKVYLG 232
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
277-538 |
6.90e-17 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 84.14 E-value: 6.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 277 RQGAKGRQAKSKARLQRfeELQSQEFQKRSETNEIYIPA----------GPRLGDkvIELHNVTKGYGDRVLIDNLSLSI 346
Cdd:PLN03073 125 RDLAKIERRKRKEERQR--EVQYQAHVAEMEAAKAGMPGvyvnhdgnggGPAIKD--IHMENFSISVGGRDLIVDASVTL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 347 PKGAIVGVIGGNGAGKSTLFRMLTGK--------------EQPDSG----------------TIEIGETVQIasVDQSRD 396
Cdd:PLN03073 201 AFGRHYGLVGRNGTGKTTFLRYMAMHaidgipkncqilhvEQEVVGddttalqcvlntdierTQLLEEEAQL--VAQQRE 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 397 SLEGNKTVWEQ-----------VSDGFEQI-----KIGNYEVPSR--SYVGRFNFKGADQQKFVKDLSGGERGRLHLALT 458
Cdd:PLN03073 279 LEFETETGKGKgankdgvdkdaVSQRLEEIykrleLIDAYTAEARaaSILAGLSFTPEMQVKATKTFSGGWRMRIALARA 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 459 LKQGGNVLLLDEPSNDLDVETLRALEEALLDFPGAAIVISHDRWFLDRIATHILSYEDDgKVTFFEGNYTEFEADRKKRL 538
Cdd:PLN03073 359 LFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQ-KLVTYKGDYDTFERTREEQL 437
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
21-194 |
7.69e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 81.39 E-value: 7.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEAR----PMPG------INVGYLPQEPKLDPQATVRDIV 90
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgePVPSrarharQRVGVVPQFDNLDPDFTVRENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 91 EeavgqikqaqarldeVYAAYaepdadFDALAAEQAKLEAILqasdghnLE-RQLEVAADAlrlppwdaKVEHLSGGEKR 169
Cdd:PRK13537 102 L---------------VFGRY------FGLSAAAARALVPPL-------LEfAKLENKADA--------KVGELSGGMKR 145
|
170 180
....*....|....*....|....*
gi 15599791 170 RVALCRLLLSAPDMLLLDEPTNHLD 194
Cdd:PRK13537 146 RLTLARALVNDPDVLVLDEPTTGLD 170
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
18-218 |
1.23e-16 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 79.77 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGE----ARPMPGIN-------VGYLPQEPKLDPQATV 86
Cdd:COG4559 13 GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEvrlnGRPLAAWSpwelarrRAVLPQHSSLAFPFTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 87 RDIVeeAVGQikqaqarldevyAAYAEPDADFDALAaeqaklEAILQASD-GHNLERQlevaadalrlppwdakVEHLSG 165
Cdd:COG4559 93 EEVV--ALGR------------APHGSSAAQDRQIV------REALALVGlAHLAGRS----------------YQTLSG 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599791 166 GEKRRVALCRLL--LSAPDM-----LLLDEPTNHLDadsvawLEHFLH------DF---PGTVVAITHD 218
Cdd:COG4559 137 GEQQRVQLARVLaqLWEPVDggprwLFLDEPTSALD------LAHQHAvlrlarQLarrGGGVVAVLHD 199
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
18-236 |
1.25e-16 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 78.00 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGE-------------ARPMPGINVGYLPQEPKLDPQA 84
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSilidgedltdledELPPLRRRIGMVFQDFALFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 85 TVRDIVEEAvgqikqaqarldevyaayaepdadfdalaaeqakleailqasdghnlerqlevaadalrlppwdakvehLS 164
Cdd:cd03229 92 TVLENIALG---------------------------------------------------------------------LS 102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599791 165 GGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHF---LHDFPG-TVVAITHDRYFLDNVAGWILELDRGH 236
Cdd:cd03229 103 GGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALlksLQAQLGiTVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
321-499 |
1.32e-16 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 79.74 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 321 DKVIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSG-TIEI------GETVQ------ 387
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLfgerrgGEDVWelrkri 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 388 -IASVDQSRDsLEGNKTVWEQVSDGFEQIkIGNYEVPS-------RSYVGRFNFKGADQQKFvKDLSGGERGRLHLALTL 459
Cdd:COG1119 81 gLVSPALQLR-FPRDETVLDVVLSGFFDS-IGLYREPTdeqreraRELLELLGLAHLADRPF-GTLSQGEQRRVLIARAL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15599791 460 KQGGNVLLLDEPSNDLDV---ETLRALEEALLDFPGAAIV-ISH 499
Cdd:COG1119 158 VKDPELLILDEPTAGLDLgarELLLALLDKLAAEGAPTLVlVTH 201
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
18-218 |
1.54e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 79.39 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARPMPGINVGYLPQEPKLDPqaTVRDIVEEAVgQI 97
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDT--TLPLTVNRFL-RL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 98 KQAQARLDevyaayaepdadfdalaaeqakleaILQAsdghnLERqleVAADALrlppWDAKVEHLSGGEKRRVALCRLL 177
Cdd:PRK09544 93 RPGTKKED-------------------------ILPA-----LKR---VQAGHL----IDAPMQKLSGGETQRVLLARAL 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15599791 178 LSAPDMLLLDEPTNHLDADSVAWL----EHFLHDFPGTVVAITHD 218
Cdd:PRK09544 136 LNRPQLLVLDEPTQGVDVNGQVALydliDQLRRELDCAVLMVSHD 180
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
19-217 |
1.96e-16 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 78.97 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------GVDTEIEGEARPmpGINV-------GYLPQE--PKLDP 82
Cdd:COG1119 16 KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITgdlpptyGNDVRLFGERRG--GEDVwelrkriGLVSPAlqLRFPR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 83 QATVRDIVeeavgqikqaqarldeVYAAYA------EPDAdfdalaAEQAKLEAILqasdghnleRQLEVAADAlrlppw 156
Cdd:COG1119 94 DETVLDVV----------------LSGFFDsiglyrEPTD------EQRERARELL---------ELLGLAHLA------ 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599791 157 DAKVEHLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADS----VAWLEHFLHDFPGTVVAITH 217
Cdd:COG1119 137 DRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGArellLALLDKLAAEGAPTLVLVTH 201
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
8-205 |
2.17e-16 |
|
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: 78.18 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 8 MHRVGKIVPPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdteiegeARPMPGInvgylpqepkldpqATVR 87
Cdd:cd03266 7 LTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGL-------LEPDAGF--------------ATVD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 88 DIveEAVGQIKQAQARLDEVYAAyaepDADFDALAA-EQAKLEAILQASDGHNLERQLEVAADALRLPPW-DAKVEHLSG 165
Cdd:cd03266 66 GF--DVVKEPAEARRRLGFVSDS----TGLYDRLTArENLEYFAGLYGLKGDELTARLEELADRLGMEELlDRRVGGFST 139
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15599791 166 GEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFL 205
Cdd:cd03266 140 GMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFI 179
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
324-499 |
2.25e-16 |
|
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: 78.43 E-value: 2.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGD-RVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIG----ETVQIASVDQS---- 394
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDgqdiREVTLDSLRRAigvv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 395 -RDSLEGNKTVWEQVSDGF-----EQI-----------KIGNYEVPSRSYVGRFNFKgadqqkfvkdLSGGERGRLHLAL 457
Cdd:cd03253 81 pQDTVLFNDTIGYNIRYGRpdatdEEVieaakaaqihdKIMRFPDGYDTIVGERGLK----------LSGGEKQRVAIAR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15599791 458 TLKQGGNVLLLDEPSNDLDVETLRALEEALLDFPG--AAIVISH 499
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRDVSKgrTTIVIAH 194
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
16-194 |
2.27e-16 |
|
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: 78.43 E-value: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 16 PPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM------AGVDTEIEGEarPMPGINVGYLPQEPKLDPQATV--R 87
Cdd:cd03253 11 DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLfrfydvSSGSILIDGQ--DIREVTLDSLRRAIGVVPQDTVlfN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 88 DIVEEAVgqikqaqarldevyaAYAEPDADFDAL--AAEQAKL-EAILQASDGHNL---ERQLEvaadalrlppwdakve 161
Cdd:cd03253 89 DTIGYNI---------------RYGRPDATDEEVieAAKAAQIhDKIMRFPDGYDTivgERGLK---------------- 137
|
170 180 190
....*....|....*....|....*....|...
gi 15599791 162 hLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLD 194
Cdd:cd03253 138 -LSGGEKQRVAIARAILKNPPILLLDEATSALD 169
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
18-236 |
2.59e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 80.51 E-value: 2.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGE------------ARPMpgiNVGYLPQEPKLDPQAT 85
Cdd:PRK10851 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHirfhgtdvsrlhARDR---KVGFVFQHYALFRHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 86 VRDIVeeAVGQikqaqarldEVYAAYAEPDAdfdalAAEQAKLEAILQASdghnlerQLEVAADalRLPpwdakvEHLSG 165
Cdd:PRK10851 91 VFDNI--AFGL---------TVLPRRERPNA-----AAIKAKVTQLLEMV-------QLAHLAD--RYP------AQLSG 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599791 166 GEKRRVALCRLLLSAPDMLLLDEPTNHLDA----DSVAWLEHFLHDFPGTVVAITHDRYFLDNVAGWILELDRGH 236
Cdd:PRK10851 140 GQKQRVALARALAVEPQILLLDEPFGALDAqvrkELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGN 214
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
314-476 |
2.89e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 80.76 E-value: 2.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 314 PAGPRLGDKVIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETV------ 386
Cdd:PRK09452 5 NKQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLdGQDIthvpae 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 387 --QIASVDQSRdSLEGNKTVWEQVSDGFEQIKIGNYEVPSR-----SYVGRFNFkgADQQkfVKDLSGGERGRLHLALTL 459
Cdd:PRK09452 85 nrHVNTVFQSY-ALFPHMTVFENVAFGLRMQKTPAAEITPRvmealRMVQLEEF--AQRK--PHQLSGGQQQRVAIARAV 159
|
170
....*....|....*..
gi 15599791 460 KQGGNVLLLDEPSNDLD 476
Cdd:PRK09452 160 VNKPKVLLLDESLSALD 176
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
324-383 |
3.55e-16 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 79.74 E-value: 3.55e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599791 324 IELHNVTKGY----GDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIG 383
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVD 65
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
291-501 |
3.64e-16 |
|
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: 81.18 E-value: 3.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 291 LQRFEELQSQEFQKRSEtneiyIPAGPrlgDKVIELHNVTKGYGDR-VLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRML 369
Cdd:TIGR02857 297 LFAVLDAAPRPLAGKAP-----VTAAP---ASSLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 370 TGKEQPDSGTIEI-GETVQIASVDQSRDSLegnktVW-EQVSDGF-----EQIKIGNYEVPSRSYVGRFNFKGADQqkFV 442
Cdd:TIGR02857 369 LGFVDPTEGSIAVnGVPLADADADSWRDQI-----AWvPQHPFLFagtiaENIRLARPDASDAEIREALERAGLDE--FV 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599791 443 KD---------------LSGGERGRLHLALTLKQGGNVLLLDEPSNDLDVETLRALEEALLDFPGAA--IVISHDR 501
Cdd:TIGR02857 442 AAlpqgldtpigeggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRtvLLVTHRL 517
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
20-228 |
3.74e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 78.62 E-value: 3.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARPMpGINVGylpqepkldpQATVRDiVEEAVGQIKQ 99
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVM-GREVN----------AENEKW-VRSKVGLVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 100 AQArlDEVYAAYAEPDADFDALAAEQAKLEailqasdghnLERQLEVAADALRLppWDAKVE---HLSGGEKRRVALCRL 176
Cdd:PRK13647 87 DPD--DQVFSSTVWDDVAFGPVNMGLDKDE----------VERRVEEALKAVRM--WDFRDKppyHLSYGQKKRVAIAGV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15599791 177 LLSAPDMLLLDEPTNHLD---ADSVAWLEHFLHDFPGTVVAITHDryfLDNVAGW 228
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDprgQETLMEILDRLHNQGKTVIVATHD---VDLAAEW 204
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
323-520 |
4.04e-16 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 81.10 E-value: 4.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 323 VIELHNVTKGY--GDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPD---SGTIEIGET-----------V 386
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRdllelsealrgR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 387 QIASVDQSRDSLEGNKTVWEQVSDGFEQIKIGNYEVPSR-----SYVGRFNFKGAdqqkFVKDLSGGERGRLHLALTLKQ 461
Cdd:COG1123 84 RIGMVFQDPMTQLNPVTVGDQIAEALENLGLSRAEARARvlellEAVGLERRLDR----YPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599791 462 GGNVLLLDEPSNDLDV----ETLRALEEALLDFPGAAIVISHDRWFLDRIATHILsYEDDGKV 520
Cdd:COG1123 160 DPDLLIADEPTTALDVttqaEILDLLRELQRERGTTVLLITHDLGVVAEIADRVV-VMDDGRI 221
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
18-189 |
4.36e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 77.76 E-value: 4.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---VDT---EIEGE---ARPMP-----GInvGYLPQEP----K 79
Cdd:COG1137 15 KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGlvkPDSgriFLDGEditHLPMHkrarlGI--GYLPQEAsifrK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 80 LdpqaTVRD---IVEEAVGQIKQAQarldevyaayaepdadfdalaaeQAKLEAILQasdghnlERQLEvaadALRlppw 156
Cdd:COG1137 93 L----TVEDnilAVLELRKLSKKER-----------------------EERLEELLE-------EFGIT----HLR---- 130
|
170 180 190
....*....|....*....|....*....|...
gi 15599791 157 DAKVEHLSGGEKRRVALCRLLLSAPDMLLLDEP 189
Cdd:COG1137 131 KSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
285-509 |
5.78e-16 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 80.98 E-value: 5.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 285 AKSKARLQRFEELQSQEFQKRSETNEIyiPAGPRLGDkvIELHNVTKGY-GDRVLIDNLSLSIPKGAIVGVIGGNGAGKS 363
Cdd:COG1132 305 QRALASAERIFELLDEPPEIPDPPGAV--PLPPVRGE--IEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKS 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 364 TLFRMLTGKEQPDSGTIEIGEtVQIASVDQsrDSLegnktvWEQVS----DGF-------EQIKIGNyevpsrsyvgrfn 432
Cdd:COG1132 381 TLVNLLLRFYDPTSGRILIDG-VDIRDLTL--ESL------RRQIGvvpqDTFlfsgtirENIRYGR------------- 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 433 fKGADQQK------------FVKD---------------LSGGERGRLHLALTLKQGGNVLLLDEPSNDLDVETLRALEE 485
Cdd:COG1132 439 -PDATDEEveeaakaaqaheFIEAlpdgydtvvgergvnLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQE 517
|
250 260
....*....|....*....|....*.
gi 15599791 486 ALLDFPG--AAIVISHdrwfldRIAT 509
Cdd:COG1132 518 ALERLMKgrTTIVIAH------RLST 537
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
322-386 |
5.86e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 77.43 E-value: 5.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 322 KVIELHNVTK----------------------GYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGT 379
Cdd:COG1134 3 SMIEVENVSKsyrlyhepsrslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
....*..
gi 15599791 380 IEIGETV 386
Cdd:COG1134 83 VEVNGRV 89
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
19-217 |
5.88e-16 |
|
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: 76.63 E-value: 5.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV----------DTEIEGEARPMPGINVGYLPQEPKLDPQATVRD 88
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLlrpdsgevrwNGTPLAEQRDEPHENILYLGHLPGLKPELSALE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 89 iveeavgqikqaqaRLDeVYAAYaepdadfdaLAAEQAKLEAILQASDGHNLErqlevaadalrlppwDAKVEHLSGGEK 168
Cdd:TIGR01189 93 --------------NLH-FWAAI---------HGGAQRTIEDALAAVGLTGFE---------------DLPAAQLSAGQQ 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15599791 169 RRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDF---PGTVVAITH 217
Cdd:TIGR01189 134 RRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
323-471 |
6.93e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 77.38 E-value: 6.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 323 VIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETV---------------- 386
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDithlpmhkrarlgigy 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 387 --QIASVdqSRDsLegnkTVWEQVSDGFEQIKIGNYEVPSR--SYVGRFNFKG-ADQQKFVkdLSGGERGRLHLALTLKQ 461
Cdd:COG1137 83 lpQEASI--FRK-L----TVEDNILAVLELRKLSKKEREERleELLEEFGITHlRKSKAYS--LSGGERRRVEIARALAT 153
|
170
....*....|
gi 15599791 462 GGNVLLLDEP 471
Cdd:COG1137 154 NPKFILLDEP 163
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
324-522 |
6.99e-16 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 77.10 E-value: 6.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLidNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQIASVDQS-------- 394
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWnGQDLTALPPAERpvsmlfqe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 395 -----------------RDSLEGNKTVWEQVSDGFEQIKIGNYEvpsrsyvgrfnfkgadqQKFVKDLSGGERGRLHLAL 457
Cdd:COG3840 80 nnlfphltvaqniglglRPGLKLTAEQRAQVEQALERVGLAGLL-----------------DRLPGQLSGGQRQRVALAR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599791 458 TLKQGGNVLLLDEPSNDLD----VETLRALEEALLDFPGAAIVISHDrwfLD---RIATHILsYEDDGKVTF 522
Cdd:COG3840 143 CLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRERGLTVLMVTHD---PEdaaRIADRVL-LVADGRIAA 210
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
18-189 |
7.40e-16 |
|
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: 76.81 E-value: 7.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEAR---------PM---PGINVGYLPQEPKLDPQAT 85
Cdd:cd03218 12 KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILldgqditklPMhkrARLGIGYLPQEASIFRKLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 86 VRDIVEeavgqikqaqARLDEVYAAYAEpdadfdalaaEQAKLEAILQasdghnlERQLEvaadALRlppwDAKVEHLSG 165
Cdd:cd03218 92 VEENIL----------AVLEIRGLSKKE----------REEKLEELLE-------EFHIT----HLR----KSKASSLSG 136
|
170 180
....*....|....*....|....
gi 15599791 166 GEKRRVALCRLLLSAPDMLLLDEP 189
Cdd:cd03218 137 GERRRVEIARALATNPKFLLLDEP 160
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
17-259 |
9.54e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 77.42 E-value: 9.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 17 PKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpMPGINVGYLPQEPKLDPQATVRDIVEEAVGQ 96
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVS-WRGEPLAKLNRAQRKAFRRDIQMVFQDSISA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 97 IKQAQArldeVYAAYAEPDADFDAL--AAEQAKLEAILQASDghnLErqlevAADALRLPPwdakveHLSGGEKRRVALC 174
Cdd:PRK10419 102 VNPRKT----VREIIREPLRHLLSLdkAERLARASEMLRAVD---LD-----DSVLDKRPP------QLSGGQLQRVCLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 175 RLLLSAPDMLLLDEPTNHLD----ADSVAWLEHFLHDFPGTVVAITHD----RYFLDNVA----GWILElDR--GHGIPF 240
Cdd:PRK10419 164 RALAVEPKLLILDEAVSNLDlvlqAGVIRLLKKLQQQFGTACLFITHDlrlvERFCQRVMvmdnGQIVE-TQpvGDKLTF 242
|
250
....*....|....*....
gi 15599791 241 egnysgwlESKAARLAQEA 259
Cdd:PRK10419 243 --------SSPAGRVLQNA 253
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
324-499 |
1.20e-15 |
|
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: 79.85 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQ--PDSGTI--------------------- 380
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 381 ---EIGETVQIASVD--------------------QSRDSLEGNKTVWEQVSDGFEQIkignyEVPSRSYVGRfnfkGAD 437
Cdd:TIGR03269 81 pcpVCGGTLEPEEVDfwnlsdklrrrirkriaimlQRTFALYGDDTVLDNVLEALEEI-----GYEGKEAVGR----AVD 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599791 438 QQKFVK----------DLSGGERGRLHLALTLKQGGNVLLLDEPSNDLDVETLR----ALEEALLDFPGAAIVISH 499
Cdd:TIGR03269 152 LIEMVQlshrithiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKlvhnALEEAVKASGISMVLTSH 227
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
8-235 |
1.36e-15 |
|
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: 75.91 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 8 MHRVGKIVPPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpMPGINVGYLP------------ 75
Cdd:cd03292 3 FINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIR-VNGQDVSDLRgraipylrrkig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 76 ---QEPKLDPQATVRDIVEEAVgQIKQAQARLdevyaayaepdadfdalaaEQAKLEAILqasdghnleRQLEVAADALR 152
Cdd:cd03292 82 vvfQDFRLLPDRNVYENVAFAL-EVTGVPPRE-------------------IRKRVPAAL---------ELVGLSHKHRA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 153 LPpwdakvEHLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADS---VAWLEHFLHDFPGTVVAITHDRYFLDNVAGWI 229
Cdd:cd03292 133 LP------AELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTtweIMNLLKKINKAGTTVVVATHAKELVDTTRHRV 206
|
....*.
gi 15599791 230 LELDRG 235
Cdd:cd03292 207 IALERG 212
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
21-218 |
1.42e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 78.73 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpMPGINVGYL------------PQEPKLDPQATVRD 88
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVL-VAGDDVEALsaraasrrvasvPQDTSLSFEFDVRQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 89 IVEeaVGQIKQaQARLDevyaayaePDADFDALAAEQAkleailqasdghnLERqLEVAADAlrlppwDAKVEHLSGGEK 168
Cdd:PRK09536 97 VVE--MGRTPH-RSRFD--------TWTETDRAAVERA-------------MER-TGVAQFA------DRPVTSLSGGER 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15599791 169 RRVALCRLLLSAPDMLLLDEPTNHLDAD-SVAWLE--HFLHDFPGTVVAITHD 218
Cdd:PRK09536 146 QRVLLARALAQATPVLLLDEPTASLDINhQVRTLElvRRLVDDGKTAVAAIHD 198
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
323-500 |
1.44e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 76.69 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 323 VIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETVQIASVDQsrdSLEGNK 402
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQ---KLYLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 403 TVWEQVSDgFEQIKIGNYE---VPSRSYVGRFNFKGADQQKfvkdLSGGERGRLHLALTLKQGGNVLLLDEPSNDLDVET 479
Cdd:PRK09544 81 TLPLTVNR-FLRLRPGTKKediLPALKRVQAGHLIDAPMQK----LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
170 180
....*....|....*....|....*.
gi 15599791 480 LRALEEaLLD-----FPGAAIVISHD 500
Cdd:PRK09544 156 QVALYD-LIDqlrreLDCAVLMVSHD 180
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
18-113 |
2.26e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 75.89 E-value: 2.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDT------EIEGEARPMPGINVGylpqepkLDPQATVRDIVe 91
Cdd:COG1134 38 EFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEptsgrvEVNGRVSALLELGAG-------FHPELTGRENI- 109
|
90 100
....*....|....*....|....*..
gi 15599791 92 EAVGQI-----KQAQARLDEVyAAYAE 113
Cdd:COG1134 110 YLNGRLlglsrKEIDEKFDEI-VEFAE 135
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
25-218 |
2.68e-15 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 75.18 E-value: 2.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 25 ISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpMPGINVGYLP----------QEPKLDPQATVRDIVeeAV 94
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRIL-WNGQDLTALPpaerpvsmlfQENNLFPHLTVAQNI--GL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 95 GqikqaqarLDevyaayaePDADFDAlaAEQAKLEAILQasdghnlerQLEVAADALRLPpwdakvEHLSGGEKRRVALC 174
Cdd:COG3840 95 G--------LR--------PGLKLTA--EQRAQVEQALE---------RVGLAGLLDRLP------GQLSGGQRQRVALA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15599791 175 RLLLSAPDMLLLDEPTNHLD----ADSVAWLEHFLHDFPGTVVAITHD 218
Cdd:COG3840 142 RCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRERGLTVLMVTHD 189
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
19-218 |
2.99e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 75.87 E-value: 2.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGE----ARPMPGI--NVGYLPQEPKLDPQATVRDIVEE 92
Cdd:PRK11247 25 RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEllagTAPLAEAreDTRLMFQDARLLPWKKVIDNVGL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 93 AV-GQIKQAqarldevyaayaepdadfdalaAEQAkLEAILQASdghnlerqlevaadalRLPPWDAKvehLSGGEKRRV 171
Cdd:PRK11247 105 GLkGQWRDA----------------------ALQA-LAAVGLAD----------------RANEWPAA---LSGGQKQRV 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15599791 172 ALCRLLLSAPDMLLLDEPTNHLDA----------DSVaWLEHFLhdfpgTVVAITHD 218
Cdd:PRK11247 143 ALARALIHRPGLLLLDEPLGALDAltriemqdliESL-WQQHGF-----TVLLVTHD 193
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
22-218 |
3.26e-15 |
|
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: 75.06 E-value: 3.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEAR-------PMPGI--NVGYLPQEPKLDPQATVRDIVee 92
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILlngkditNLPPEkrDISYVPQNYALFPHMTVYKNI-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 93 AVGQIKQAqarldevyaayaEPDADFDALAAEQAKLEAIlqasdGHNLERqlevaadalrlppwdaKVEHLSGGEKRRVA 172
Cdd:cd03299 93 AYGLKKRK------------VDKKEIERKVLEIAEMLGI-----DHLLNR----------------KPETLSGGEQQRVA 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15599791 173 LCRLLLSAPDMLLLDEPTNHLDA---DSVAWLEHFLHD-FPGTVVAITHD 218
Cdd:cd03299 140 IARALVVNPKILLLDEPFSALDVrtkEKLREELKKIRKeFGVTVLHVTHD 189
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
20-236 |
3.37e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 75.44 E-value: 3.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGE-----------ARPMPGI------NVGYLPQEPKLDP 82
Cdd:PRK11124 16 QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTlniagnhfdfsKTPSDKAirelrrNVGMVFQQYNLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 83 QATVRDIVEEAVGQIKqaqarldevyaayaepdadfdALAAEQAKLEAIlqasdgHNLER-QLEVAADalRLPPwdakve 161
Cdd:PRK11124 96 HLTVQQNLIEAPCRVL---------------------GLSKDQALARAE------KLLERlRLKPYAD--RFPL------ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599791 162 HLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPG---TVVAITHDRYFLDNVAGWILELDRGH 236
Cdd:PRK11124 141 HLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtgiTQVIVTHEVEVARKTASRVVYMENGH 218
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
279-500 |
3.41e-15 |
|
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: 78.17 E-value: 3.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 279 GAKGRQAKSKARLQRFEELQSQEFQ---KRSETNEIYIPAGPRLgdkviELHNVTKGY-GDRVLIDNLSLSIPKGAIVGV 354
Cdd:TIGR02868 292 AAAQQLTRVRAAAERIVEVLDAAGPvaeGSAPAAGAVGLGKPTL-----ELRDLSAGYpGAPPVLDGVSLDLPPGERVAI 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 355 IGGNGAGKSTLFRMLTGKEQPDSGTIEIGEtVQIASVDQS--------------------RDSLE-GNKTVW-EQVSDGF 412
Cdd:TIGR02868 367 LGPSGSGKSTLLATLAGLLDPLQGEVTLDG-VPVSSLDQDevrrrvsvcaqdahlfdttvRENLRlARPDATdEELWAAL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 413 EQIKIGNY--EVPSrsyvGRFNFKGADQQKfvkdLSGGERGRLHLALTLKQGGNVLLLDEPSNDLDVETLRALEEALLD- 489
Cdd:TIGR02868 446 ERVGLADWlrALPD----GLDTVLGEGGAR----LSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAa 517
|
250
....*....|..
gi 15599791 490 FPG-AAIVISHD 500
Cdd:TIGR02868 518 LSGrTVVLITHH 529
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
18-217 |
3.89e-15 |
|
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: 73.40 E-value: 3.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEAR----------PMP-GINVGYLPQEPKLDPqATV 86
Cdd:cd03246 14 EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRldgadisqwdPNElGDHVGYLPQDDELFS-GSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 87 RDIVeeavgqikqaqarldevyaayaepdadfdalaaeqakleailqasdghnlerqlevaadalrlppwdakvehLSGG 166
Cdd:cd03246 93 AENI------------------------------------------------------------------------LSGG 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15599791 167 EKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFP---GTVVAITH 217
Cdd:cd03246 101 QRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKaagATRIVIAH 154
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
324-383 |
3.93e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 75.51 E-value: 3.93e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599791 324 IELHNVTK----GYGD-RVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIG 383
Cdd:COG1101 2 LELKNLSKtfnpGTVNeKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILID 66
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
19-217 |
4.16e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 74.14 E-value: 4.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG--------VDTEIEGEARPMPGINVGYLPQEPKLDPQATVRDIV 90
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGllppaagtIKLDGGDIDDPDVAEACHYLGHRNAMKPALTVAENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 91 EeavgqikqaqarldevyaayaepdadFDAlaaeqakleAILQASDGHnlerqLEVAADALRLPPwdakVEH-----LSG 165
Cdd:PRK13539 95 E--------------------------FWA---------AFLGGEELD-----IAAALEAVGLAP----LAHlpfgyLSA 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15599791 166 GEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWL-----EHFLHDfpGTVVAITH 217
Cdd:PRK13539 131 GQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFaelirAHLAQG--GIVIAATH 185
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
24-217 |
4.44e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 74.07 E-value: 4.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 24 DISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGE----------ARPMPGINVGYLPQEPKLDPQATvrdiveea 93
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEvlwqgepirrQRDEYHQDLLYLGHQPGIKTELT-------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 94 vgqikqaqarldevyaayAEPDADFDALAAEQAKLEAILQASDGHNLERQLEVAAdalrlppwdakvEHLSGGEKRRVAL 173
Cdd:PRK13538 91 ------------------ALENLRFYQRLHGPGDDEALWEALAQVGLAGFEDVPV------------RQLSAGQQRRVAL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15599791 174 CRLLLSAPDMLLLDEPTNHLDADSVAWLE-HFLH--DFPGTVVAITH 217
Cdd:PRK13538 141 ARLWLTRAPLWILDEPFTAIDKQGVARLEaLLAQhaEQGGMVILTTH 187
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
319-500 |
4.52e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 75.82 E-value: 4.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 319 LGDKVIELHNVTKGYGD--RVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIG------ETV---- 386
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGgmvlseETVwdvr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 387 -QIASVDQSRDSLEGNKTVWEQVSDGFEqikigNYEVPSRSYVGRFN--FKGADQQKFVKD----LSGGERGRLHLALTL 459
Cdd:PRK13635 81 rQVGMVFQNPDNQFVGATVQDDVAFGLE-----NIGVPREEMVERVDqaLRQVGMEDFLNRephrLSGGQKQRVAIAGVL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15599791 460 KQGGNVLLLDEPSNDLD-------VETLRALEEAlldfpGAAIVIS--HD 500
Cdd:PRK13635 156 ALQPDIIILDEATSMLDprgrrevLETVRQLKEQ-----KGITVLSitHD 200
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
324-386 |
4.59e-15 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 74.49 E-value: 4.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGY----------------------GDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIE 381
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
....*
gi 15599791 382 IGETV 386
Cdd:cd03220 81 VRGRV 85
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
9-194 |
5.23e-15 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 74.53 E-value: 5.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 9 HRVGKIVPPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpmpgINVGYLPQEPKLDPQATVRD 88
Cdd:cd03256 4 ENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVL----IDGTDINKLKGKALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 89 IveeavGQIKQaqarldevyaayaepdaDFdALAAEQAKLEAILQASDG-HNL---------ERQLEVAADALR----LP 154
Cdd:cd03256 80 I-----GMIFQ-----------------QF-NLIERLSVLENVLSGRLGrRSTwrslfglfpKEEKQRALAALErvglLD 136
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15599791 155 PWDAKVEHLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLD 194
Cdd:cd03256 137 KAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLD 176
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
9-379 |
5.49e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 78.24 E-value: 5.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 9 HRVGKIVPpkreiLKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEAR----PM----------PGInvGYL 74
Cdd:NF033858 9 HRYGKTVA-----LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvlggDMadarhrravcPRI--AYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 75 PQ------EPKLDpqatvrdiVEEAVgqikQAQARLdevyaayaepdadFDALAAE-QAKLEAILQASDghnLERQLEVA 147
Cdd:NF033858 82 PQglgknlYPTLS--------VFENL----DFFGRL-------------FGQDAAErRRRIDELLRATG---LAPFADRP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 148 AdalrlppwdAKvehLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVA--W--LEHFLHDFPG-TVVAITHdryFL 222
Cdd:NF033858 134 A---------GK---LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRqfWelIDRIRAERPGmSVLVATA---YM 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 223 DNVAG--WILELDRGHGIpfegnysgwleskAARLAQEAKqeashAKAMKAELEwvrqgakgrQAkskarlqrFEELQSQ 300
Cdd:NF033858 199 EEAERfdWLVAMDAGRVL-------------ATGTPAELL-----ARTGADTLE---------AA--------FIALLPE 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 301 EfqKRSETNEIYIPagPRLGDK----VIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPD 376
Cdd:NF033858 244 E--KRRGHQPVVIP--PRPADDddepAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPAS 319
|
...
gi 15599791 377 SGT 379
Cdd:NF033858 320 EGE 322
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
7-235 |
5.74e-15 |
|
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: 74.39 E-value: 5.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 7 TMHRVGKIVPPkreILKDISLSFFPGAKIGVLGLNGAGKSTLLRImagvdteIEGEARPMPGiNVGYLPQEPKLD-PQAT 85
Cdd:COG4778 15 TLHLQGGKRLP---VLDGVSFSVAAGECVALTGPSGAGKSTLLKC-------IYGNYLPDSG-SILVRHDGGWVDlAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 86 VRDIVE---EAVGQIKQ------AQARLDEVyaayAEPdadfdALAAEQAKLEAILQAsdGHNLERqlevaadaLRLPP- 155
Cdd:COG4778 84 PREILAlrrRTIGYVSQflrvipRVSALDVV----AEP-----LLERGVDREEARARA--RELLAR--------LNLPEr 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 156 -WDAKVEHLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADS----VAWLEHFLHDfpGT-VVAITHDRYFLDNVAGWI 229
Cdd:COG4778 145 lWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANravvVELIEEAKAR--GTaIIGIFHDEEVREAVADRV 222
|
....*.
gi 15599791 230 LELDRG 235
Cdd:COG4778 223 VDVTPF 228
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
18-189 |
5.84e-15 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 74.62 E-value: 5.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKST-------LLRIMAGvDTEIEGE---ARPMPG---INVGYLPQEPKLDPQA 84
Cdd:TIGR04406 13 KRKVVNDVSLSVKSGEIVGLLGPNGAGKTTsfymivgLVRPDAG-KILIDGQditHLPMHErarLGIGYLPQEASIFRKL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 85 TVRDIVeEAVGQIkqaQARLDEvyaayaepdadfdalAAEQAKLEAILQasdghnlerqlEVAADALRlppwDAKVEHLS 164
Cdd:TIGR04406 92 TVEENI-MAVLEI---RKDLDR---------------AEREERLEALLE-----------EFQISHLR----DNKAMSLS 137
|
170 180
....*....|....*....|....*
gi 15599791 165 GGEKRRVALCRLLLSAPDMLLLDEP 189
Cdd:TIGR04406 138 GGERRRVEIARALATNPKFILLDEP 162
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
324-511 |
8.00e-15 |
|
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: 74.26 E-value: 8.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGD-RVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETV----------QIASV 391
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIdGEDIreqdpvelrrKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 392 DQSRdSLEGNKTVWEQVSD-------GFEQIKIGNYE------VPSRSYVGRFNfkgadqqkfvKDLSGGERGRLHLALT 458
Cdd:cd03295 81 IQQI-GLFPHMTVEENIALvpkllkwPKEKIRERADEllalvgLDPAEFADRYP----------HELSGGQQQRVGVARA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15599791 459 LKQGGNVLLLDEPSNDLDVETLRALEEALLDFP---GAAIV-ISHDRWFLDRIATHI 511
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQqelGKTIVfVTHDIDEAFRLADRI 206
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
323-512 |
8.21e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 74.62 E-value: 8.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 323 VIELHnvtKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGE-----------TVQIASV 391
Cdd:PRK10619 8 VIDLH---KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgQLKVADK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 392 DQSRD------------SLEGNKTVWEQVSDGFEQI-KIGNYEVPSRS--YVGRFNFKGADQQKFVKDLSGGERGRLHLA 456
Cdd:PRK10619 85 NQLRLlrtrltmvfqhfNLWSHMTVLENVMEAPIQVlGLSKQEARERAvkYLAKVGIDERAQGKYPVHLSGGQQQRVSIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 457 LTLKQGGNVLLLDEPSNDLDV----ETLRALEEaLLDFPGAAIVISHDRWFLDRIATHIL 512
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPelvgEVLRIMQQ-LAEEGKTMVVVTHEMGFARHVSSHVI 223
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
339-500 |
8.96e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 75.51 E-value: 8.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 339 IDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETV----------QIASVdqsrdslEGNKTvweQ- 407
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVpfkrrkefarRIGVV-------FGQRS---Ql 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 408 -----VSDGFEQIK-IgnYEVPSRSY-------VGRFNFKG-ADQQkfVKDLSGGERGRLHLALTLKQGGNVLLLDEPSN 473
Cdd:COG4586 108 wwdlpAIDSFRLLKaI--YRIPDAEYkkrldelVELLDLGElLDTP--VRQLSLGQRMRCELAAALLHRPKILFLDEPTI 183
|
170 180 190
....*....|....*....|....*....|.
gi 15599791 474 DLDVETLRALEEALLDF---PGAAIVI-SHD 500
Cdd:COG4586 184 GLDVVSKEAIREFLKEYnreRGTTILLtSHD 214
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
19-217 |
9.09e-15 |
|
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: 73.30 E-value: 9.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARPMPGinvgylpqepkldPQATVRDIVEEAVgqik 98
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG-------------PLDFQRDSIARGL---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 99 qaqarldeVYAAYAepdadfDALAAEQAKLEAILQASDGHNLErQLEVAADALRLPPW-DAKVEHLSGGEKRRVALCRLL 177
Cdd:cd03231 76 --------LYLGHA------PGIKTTLSVLENLRFWHADHSDE-QVEEALARVGLNGFeDRPVAQLSAGQQRRVALARLL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15599791 178 LSAPDMLLLDEPTNHLDADSVAWLEHFLHDFP---GTVVAITH 217
Cdd:cd03231 141 LSGRPLWILDEPTTALDKAGVARFAEAMAGHCargGMVVLTTH 183
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
20-236 |
1.02e-14 |
|
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: 73.91 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARPMpginvGYLP--QEPKLDPQATVrdiveeAVGQI 97
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVA-----GLVPwkRRKKFLRRIGV------VFGQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 98 KQAQARLdevyaayaePDADFDALaaeqakLEAILQASDGHNLERqLEVAADALRLPP-WDAKVEHLSGGEKRRVALCRL 176
Cdd:cd03267 104 TQLWWDL---------PVIDSFYL------LAAIYDLPPARFKKR-LDELSELLDLEElLDTPVRQLSLGQRMRAEIAAA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599791 177 LLSAPDMLLLDEPTNHLDADSVAWLEHFLHDF----PGTVVAITHDRYFLDNVAGWILELDRGH 236
Cdd:cd03267 168 LLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnrerGTTVLLTSHYMKDIEALARRVLVIDKGR 231
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
21-194 |
1.07e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 73.08 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV---DT-EIEGEARPM---PGINVGYLPQEPKLDPQATVRDIVeea 93
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIilpDSgEVLFDGKPLdiaARNRIGYLPEERGLYPKMKVIDQL--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 94 vgqikqaqarldeVYAayaepdADFDALAAEQAKleailqasdgHNLERQLEvaadalRL---PPWDAKVEHLSGGEKRR 170
Cdd:cd03269 92 -------------VYL------AQLKGLKKEEAR----------RRIDEWLE------RLelsEYANKRVEELSKGNQQK 136
|
170 180
....*....|....*....|....
gi 15599791 171 VALCRLLLSAPDMLLLDEPTNHLD 194
Cdd:cd03269 137 VQFIAAVIHDPELLILDEPFSGLD 160
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
21-194 |
1.13e-14 |
|
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: 73.31 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---------------VDTEIEgEARPmpgiNVGYLPQEPKLDPQAT 85
Cdd:cd03263 17 AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGelrptsgtayingysIRTDRK-AARQ----SLGYCPQFDALFDELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 86 VRDIVEeavgqikqaqarldevyaayaepdadfdalaaeqakLEAILQASDGHNLERQLEVAADALRLPP-WDAKVEHLS 164
Cdd:cd03263 92 VREHLR------------------------------------FYARLKGLPKSEIKEEVELLLRVLGLTDkANKRARTLS 135
|
170 180 190
....*....|....*....|....*....|
gi 15599791 165 GGEKRRVALCRLLLSAPDMLLLDEPTNHLD 194
Cdd:cd03263 136 GGMKRKLSLAIALIGGPSVLLLDEPTSGLD 165
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
324-386 |
1.20e-14 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 75.49 E-value: 1.20e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599791 324 IELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETV 386
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRD 66
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
324-519 |
1.26e-14 |
|
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: 71.80 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGD-RVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGEtvqiasvdqSRDSLegnk 402
Cdd:cd03223 1 IELENLSLATPDgRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE---------GEDLL---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 403 tvweqvsdgFeqikignyeVPSRSYVGRFNFKGA-----DQQkfvkdLSGGERGRLHLALTLKQGGNVLLLDEPSNDLDV 477
Cdd:cd03223 68 ---------F---------LPQRPYLPLGTLREQliypwDDV-----LSGGEQQRLAFARLLLHKPKFVFLDEATSALDE 124
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15599791 478 ETLRALEEALLDFpGAAIV-ISHdRWFLDRIATHILSYEDDGK 519
Cdd:cd03223 125 ESEDRLYQLLKEL-GITVIsVGH-RPSLWKFHDRVLDLDGEGG 165
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
326-476 |
1.42e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 75.45 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 326 LHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETVQ---------IASVDQSRd 396
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMndvppaergVGMVFQSY- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 397 SLEGNKTVWEQVSDGFEQIKIGNYEVPSR-SYVGRFNFKGADQQKFVKDLSGGERGRLHLALTLKQGGNVLLLDEPSNDL 475
Cdd:PRK11000 85 ALYPHLSVAENMSFGLKLAGAKKEEINQRvNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
|
.
gi 15599791 476 D 476
Cdd:PRK11000 165 D 165
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
324-507 |
1.59e-14 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 73.01 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGD--RVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGET--VQIASVDQSRD--- 396
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTdiRQLDPADLRRNigy 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 397 ----------SLEGNktvweqvsdgfeqIKIGNYEVPSRSYVGRFNFKGADQqkFVKD---------------LSGGERG 451
Cdd:cd03245 83 vpqdvtlfygTLRDN-------------ITLGAPLADDERILRAAELAGVTD--FVNKhpngldlqigergrgLSGGQRQ 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599791 452 RLHLALTLKQGGNVLLLDEPSNDLDVETLRALEEALLDFPG--AAIVISHDRWFL---DRI 507
Cdd:cd03245 148 AVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLLdlvDRI 208
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
22-217 |
1.60e-14 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 71.31 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdteiegearpmpginvgYLPQEpkldpqatvrdiveeavGQIkqaq 101
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGL-----------------YKPDS-----------------GEI---- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 102 aRLDEVYAAYAEPDadfdalAAEQAKLEAILQasdghnlerqlevaadalrlppwdakvehLSGGEKRRVALCRLLLSAP 181
Cdd:cd03216 58 -LVDGKEVSFASPR------DARRAGIAMVYQ-----------------------------LSVGERQMVEIARALARNA 101
|
170 180 190
....*....|....*....|....*....|....*....
gi 15599791 182 DMLLLDEPTNHLDADSVAWLEHFLHDFPG---TVVAITH 217
Cdd:cd03216 102 RLLILDEPTAALTPAEVERLFKVIRRLRAqgvAVIFISH 140
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
35-242 |
1.60e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 76.39 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 35 IGVLGLNGAGKSTLLRIMAGVDTEIEGEarPMPGINVGYLPQEPKLDPQATVRDIveeavgqIKQAQARLDEVYaayaep 114
Cdd:PRK13409 368 IGIVGPNGIGKTTFAKLLAGVLKPDEGE--VDPELKISYKPQYIKPDYDGTVEDL-------LRSITDDLGSSY------ 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 115 dadFDALAAEQAKLEAILqasdghnlerqlevaadalrlppwDAKVEHLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLD 194
Cdd:PRK13409 433 ---YKSEIIKPLQLERLL------------------------DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15599791 195 AD---SVA-WLEHFLHDFPGTVVAITHDRYFLDNVAgwilelDRghGIPFEG 242
Cdd:PRK13409 486 VEqrlAVAkAIRRIAEEREATALVVDHDIYMIDYIS------DR--LMVFEG 529
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
20-195 |
1.84e-14 |
|
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: 72.85 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpMPGINVGYLPQepklDPQATVRdivEEAVGQIKQ 99
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVR-LAGQDLFALDE----DARARLR---ARHVGFVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 100 A-------QArLDEVyaayaepdadfdALAAEQAkleailqasdGHNLERQLevAADAL-------RLppwDAKVEHLSG 165
Cdd:COG4181 98 SfqllptlTA-LENV------------MLPLELA----------GRRDARAR--ARALLervglghRL---DHYPAQLSG 149
|
170 180 190
....*....|....*....|....*....|
gi 15599791 166 GEKRRVALCRLLLSAPDMLLLDEPTNHLDA 195
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDA 179
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
324-499 |
1.94e-14 |
|
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: 73.03 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGD--RVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETV----------QIAS 390
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIdGHDVrdytlaslrrQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 391 VDQsrDSLEGNKTVweqvsdgFEQIKIGNYEVpSRSYVgRFNFKGADQQKFVKD---------------LSGGERGRLHL 455
Cdd:cd03251 81 VSQ--DVFLFNDTV-------AENIAYGRPGA-TREEV-EEAARAANAHEFIMElpegydtvigergvkLSGGQRQRIAI 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15599791 456 ALTLKQGGNVLLLDEPSNDLDVETLRALEEAL--LDFPGAAIVISH 499
Cdd:cd03251 150 ARALLKDPPILILDEATSALDTESERLVQAALerLMKNRTTFVIAH 195
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
18-218 |
2.24e-14 |
|
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: 72.60 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---------VDTEI--EGEARPMPGIN-------VGYLPQEPK 79
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndlipgapDEGEVllDGKDIYDLDVDvlelrrrVGMVFQKPN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 80 LDPqATVRDIVeeAVGQikqaqaRLDEVyaayaEPDADFDALAAEQAKLEAilqasdghnLERQLEVAADALrlppwdak 159
Cdd:cd03260 92 PFP-GSIYDNV--AYGL------RLHGI-----KLKEELDERVEEALRKAA---------LWDEVKDRLHAL-------- 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599791 160 veHLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDF--PGTVVAITHD 218
Cdd:cd03260 141 --GLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELkkEYTIVIVTHN 199
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-242 |
2.32e-14 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 75.98 E-value: 2.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 32 GAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpmPGINVGYLPQEPKLDPQATVRDIVEEAVGQikqaqaRLDEVYaay 111
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD--EDLKISYKPQYISPDYDGTVEEFLRSANTD------DFGSSY--- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 112 aepdadFDALAAEQAKLEAILqasdghnlerqlevaadalrlppwDAKVEHLSGGEKRRVALCRLLLSAPDMLLLDEPTN 191
Cdd:COG1245 435 ------YKTEIIKPLGLEKLL------------------------DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSA 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15599791 192 HLDAD---SVA-WLEHFLHDFPGTVVAITHDRYFLDNVAgwilelDRghGIPFEG 242
Cdd:COG1245 485 HLDVEqrlAVAkAIRRFAENRGKTAMVVDHDIYLIDYIS------DR--LMVFEG 531
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
326-479 |
2.45e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 73.17 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 326 LHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETVQIASVDQSR----DS-LEG 400
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRlmfqDArLLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 401 NKTVWEQVSDGFEqikiGNYEVPSR---SYVGRfnfkgADQ-QKFVKDLSGGERGRLHLALTLKQGGNVLLLDEPSNDLD 476
Cdd:PRK11247 95 WKKVIDNVGLGLK----GQWRDAALqalAAVGL-----ADRaNEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
...
gi 15599791 477 VET 479
Cdd:PRK11247 166 ALT 168
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
21-194 |
2.46e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 74.48 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGE----ARPMPG------INVGYLPQEPKLDPQATVRdiv 90
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKitvlGVPVPArarlarARIGVVPQFDNLDLEFTVR--- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 91 EEAVgqikqaqarldeVYAAYaepdadfdaLAAEQAKLEAILQASdghnLE-RQLEVAADAlrlppwdaKVEHLSGGEKR 169
Cdd:PRK13536 133 ENLL------------VFGRY---------FGMSTREIEAVIPSL----LEfARLESKADA--------RVSDLSGGMKR 179
|
170 180
....*....|....*....|....*
gi 15599791 170 RVALCRLLLSAPDMLLLDEPTNHLD 194
Cdd:PRK13536 180 RLTLARALINDPQLLILDEPTTGLD 204
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
20-235 |
2.84e-14 |
|
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: 72.02 E-value: 2.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpMPGINV-----------GYLPQEPKLDPQATVRD 88
Cdd:cd03265 14 EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRAT-VAGHDVvreprevrrriGIVFQDLSVDDELTGWE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 89 IVEeavgqikqAQARLdevyaaYAEPDADFDALAAEQAKLEAILQASDghnlerqlevaadalRLppwdakVEHLSGGEK 168
Cdd:cd03265 93 NLY--------IHARL------YGVPGAERRERIDELLDFVGLLEAAD---------------RL------VKTYSGGMR 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599791 169 RRVALCRLLLSAPDMLLLDEPTNHLDADSVA--W--LEHFLHDFPGTVVAITHDRYFLDNVAGWILELDRG 235
Cdd:cd03265 138 RRLEIARSLVHRPEVLFLDEPTIGLDPQTRAhvWeyIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHG 208
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
21-219 |
3.02e-14 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 74.36 E-value: 3.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDT------EIEGeaRPMPGI-----NVGYLPQEPKLDPQATVRDI 89
Cdd:COG3842 20 ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETpdsgriLLDG--RDVTGLppekrNVGMVFQDYALFPHLTVAEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 90 VeeAVG-QIK-----QAQARLDEVyaayaepdadfdalaaeqakleailqasdghnLER-QLEVAADalRLPpwdakvEH 162
Cdd:COG3842 98 V--AFGlRMRgvpkaEIRARVAEL--------------------------------LELvGLEGLAD--RYP------HQ 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599791 163 LSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDA---DSV-AWLEHFLHDFPGTVVAITHDR 219
Cdd:COG3842 136 LSGGQQQRVALARALAPEPRVLLLDEPLSALDAklrEEMrEELRRLQRELGITFIYVTHDQ 196
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
19-257 |
3.81e-14 |
|
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: 72.32 E-value: 3.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---------------VDTEIEGEARPMP---GI----------- 69
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGllrpdsgeilvdgqdITGLSEKELYELRrriGMlfqggalfdsl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 70 ----NVGY-LPQEPKLdPQATVRDIVEEavgqikqaqarldevyaayaepdadfdalaaeqaKLEAIlqasdghNLErql 144
Cdd:COG1127 98 tvfeNVAFpLREHTDL-SEAEIRELVLE----------------------------------KLELV-------GLP--- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 145 evaaDALRLPPWDakvehLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHD----FPGTVVAITHDRY 220
Cdd:COG1127 133 ----GAADKMPSE-----LSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRElrdeLGLTSVVVTHDLD 203
|
250 260 270
....*....|....*....|....*....|....*..
gi 15599791 221 FLDNVAGWILELDRGHgIPFEGNYSGWLESKAARLAQ 257
Cdd:COG1127 204 SAFAIADRVAVLADGK-IIAEGTPEELLASDDPWVRQ 239
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
20-190 |
3.92e-14 |
|
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: 71.94 E-value: 3.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-----------DTEIEG---EARPMPGInvGYLPQEPKLDPQAT 85
Cdd:COG0410 17 HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLlpprsgsirfdGEDITGlppHRIARLGI--GYVPEGRRIFPSLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 86 VRD---IVEEAVGQIKQAQARLDEVYAAyaepdadFDALAaeqakleailqasdghnlERqlevaadalrlppWDAKVEH 162
Cdd:COG0410 95 VEEnllLGAYARRDRAEVRADLERVYEL-------FPRLK------------------ER-------------RRQRAGT 136
|
170 180
....*....|....*....|....*...
gi 15599791 163 LSGGEKRRVALCRLLLSAPDMLLLDEPT 190
Cdd:COG0410 137 LSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
17-235 |
3.98e-14 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 71.73 E-value: 3.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 17 PKREILKDISLSFFPGAKIGVLGLNGAGKST----LLRIMAGVDTEIEGEARPMPGINVGYLPQepkldpqatvrdiVEE 92
Cdd:cd03248 25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTvvalLENFYQPQGGQVLLDGKPISQYEHKYLHS-------------KVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 93 AVGQIKQAQARLDEVYAAYAEPDADFDALAAEQAKLEAilqasDGHNLERQLEVAADAlrlppwDAKVEHLSGGEKRRVA 172
Cdd:cd03248 92 LVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHA-----HSFISELASGYDTEV------GEKGSQLSGGQKQRVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599791 173 LCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPG--TVVAITHdRYFLDNVAGWILELDRG 235
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALYDWPErrTVLVIAH-RLSTVERADQILVLDGG 224
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
323-483 |
4.35e-14 |
|
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: 71.04 E-value: 4.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 323 VIELHNVTK------GYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGK--EQPDSGTIEIGET--------V 386
Cdd:cd03213 3 TLSFRNLTVtvksspSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRpldkrsfrK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 387 QIASVDQSrDSLEGNKTVWEQVsdgfeqikignyevpsrsyvgRFNFKgadqqkfVKDLSGGERGRLHLALTLKQGGNVL 466
Cdd:cd03213 83 IIGYVPQD-DILHPTLTVRETL---------------------MFAAK-------LRGLSGGERKRVSIALELVSNPSLL 133
|
170 180
....*....|....*....|....
gi 15599791 467 LLDEPSNDLD-------VETLRAL 483
Cdd:cd03213 134 FLDEPTSGLDsssalqvMSLLRRL 157
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
21-235 |
4.91e-14 |
|
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: 70.96 E-value: 4.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpMPGiNVGYLPQEPKLdPQATVRD-IV------EEa 93
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVS-VPG-SIAYVSQEPWI-QNGTIREnILfgkpfdEE- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 94 vgqikqaqaRLDEVYAAYA-EPDADfdalaaeqakleaILQASDghnlerQLEVAADALrlppwdakveHLSGGEKRRVA 172
Cdd:cd03250 96 ---------RYEKVIKACAlEPDLE-------------ILPDGD------LTEIGEKGI----------NLSGGQKQRIS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599791 173 LCRLLLSAPDMLLLDEPTNHLDADSVAWL-EH----FLHDfPGTVVAITHDRYFLDNVAgWILELDRG 235
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHVGRHIfENcilgLLLN-NKTRILVTHQLQLLPHAD-QIVVLDNG 203
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
324-472 |
5.37e-14 |
|
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: 71.31 E-value: 5.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQ-----------IASV 391
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFdGRDITglppheraragIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 392 DQSRDsLEGNKTVWEqvsdgfeqikigNYEvpsrsyVGRFNFKGADQQK--------F----------VKDLSGGERGRL 453
Cdd:cd03224 81 PEGRR-IFPELTVEE------------NLL------LGAYARRRAKRKArlervyelFprlkerrkqlAGTLSGGEQQML 141
|
170
....*....|....*....
gi 15599791 454 HLALTLKQGGNVLLLDEPS 472
Cdd:cd03224 142 AIARALMSRPKLLLLDEPS 160
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
341-516 |
5.78e-14 |
|
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: 71.17 E-value: 5.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 341 NLSLSIPkGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETV---------------QIASVDQSRdSLEGNKTVW 405
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinlppqqrKIGLVFQQY-ALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 406 EQVSDGFEQIKIGNYEVPSRSYVGRFNFKGAdQQKFVKDLSGGERGRLHLALTLKQGGNVLLLDEPSNDLDVET----LR 481
Cdd:cd03297 94 ENLAFGLKRKRNREDRISVDELLDLLGLDHL-LNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALrlqlLP 172
|
170 180 190
....*....|....*....|....*....|....*
gi 15599791 482 ALEEALLDFPGAAIVISHDRWFLDRIATHILSYED 516
Cdd:cd03297 173 ELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMED 207
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
18-195 |
5.81e-14 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 73.18 E-value: 5.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDT------EIEGE--------ARpmpgiNVGYLPQEPKLDPQ 83
Cdd:COG3839 15 GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDptsgeiLIGGRdvtdlppkDR-----NIAMVFQSYALYPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 84 ATVRD-IveeavgqikqaqarldevyaayaepdadfdALAAEQAKL--EAIlqasdghnlERQLEVAADALRLPPW-DAK 159
Cdd:COG3839 90 MTVYEnI------------------------------AFPLKLRKVpkAEI---------DRRVREAAELLGLEDLlDRK 130
|
170 180 190
....*....|....*....|....*....|....*.
gi 15599791 160 VEHLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDA 195
Cdd:COG3839 131 PKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDA 166
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
19-235 |
6.38e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 72.14 E-value: 6.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEArpmpginvgYLPQEPKldPQATVRDiVEEAVGQIK 98
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSV---------LIRGEPI--TKENIRE-VRKFVGLVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 99 QAQArlDEVYAAYAEPDADFDAlaaeqakleaILQASDGHNLERQLEVAADALRLPPWDAKV-EHLSGGEKRRVALCRLL 177
Cdd:PRK13652 85 QNPD--DQIFSPTVEQDIAFGP----------INLGLDEETVAHRVSSALHMLGLEELRDRVpHHLSGGEKKRVAIAGVI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599791 178 LSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPG----TVVAITHDRYFLDNVAGWILELDRG 235
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtygmTVIFSTHQLDLVPEMADYIYVMDKG 214
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
308-521 |
7.27e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 71.14 E-value: 7.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 308 TNEIYIPAGPRLGDkVIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTG--KEQPDSGTIEIGEt 385
Cdd:COG2401 16 VYSSVLDLSERVAI-VLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPD- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 386 vqiasvdqsrDSLEGNKTVWEQVS------DGFEQIKI-GNYEVPsrSYVGRFnfkgadqqkfvKDLSGGERGRLHLALT 458
Cdd:COG2401 94 ----------NQFGREASLIDAIGrkgdfkDAVELLNAvGLSDAV--LWLRRF-----------KELSTGQKFRFRLALL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599791 459 LKQGGNVLLLDEPSNDLDVETLRALEEALLDF----PGAAIVISHDRWFLDRIATHILSYEDDGKVT 521
Cdd:COG2401 151 LAERPKLLVIDEFCSHLDRQTAKRVARNLQKLarraGITLVVATHHYDVIDDLQPDLLIFVGYGGVP 217
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-218 |
7.47e-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: 70.96 E-value: 7.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEG----EARPM--PGINVGYLPQEPKLDPQATVRDIVEEAVg 95
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGgvilEGKQItePGPDRMVVFQNYSLLPWLTVRENIALAV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 96 qikqaqarlDEVYAAYAEPdadfdalaaEQaklEAILQasdgHNLER-QLEVAADAlrlppwdaKVEHLSGGEKRRVALC 174
Cdd:TIGR01184 80 ---------DRVLPDLSKS---------ER---RAIVE----EHIALvGLTEAADK--------RPGQLSGGMKQRVAIA 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15599791 175 RLLLSAPDMLLLDEPTNHLDADSVAWLEHFL----HDFPGTVVAITHD 218
Cdd:TIGR01184 127 RALSIRPKVLLLDEPFGALDALTRGNLQEELmqiwEEHRVTVLMVTHD 174
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-202 |
7.93e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 72.06 E-value: 7.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEA----RPMPGI---NVGYLPQEPKLDPQATVRDIVeEAV 94
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVlwdgEPLDPEdrrRIGYLPEERGLYPKMKVGEQL-VYL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 95 GQIK-----QAQARLDEVyaayaepdadfdalaaeqakleailqasdghnLERqlevaadaLRLPPW-DAKVEHLSGGEK 168
Cdd:COG4152 96 ARLKglskaEAKRRADEW--------------------------------LER--------LGLGDRaNKKVEELSKGNQ 135
|
170 180 190
....*....|....*....|....*....|....
gi 15599791 169 RRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLE 202
Cdd:COG4152 136 QKVQLIAALLHDPELLILDEPFSGLDPVNVELLK 169
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
323-507 |
8.06e-14 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 70.84 E-value: 8.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 323 VIELHNVTKGYGD-----RVLiDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQIASvdQSRD 396
Cdd:TIGR02211 1 LLKCENLGKRYQEgkldtRVL-KGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFnGQSLSKLS--SNER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 397 SLEGNK---------------TVWEQVSdgfEQIKIGNY---EVPSRSY-----VG---RFNFKGADqqkfvkdLSGGER 450
Cdd:TIGR02211 78 AKLRNKklgfiyqfhhllpdfTALENVA---MPLLIGKKsvkEAKERAYemlekVGlehRINHRPSE-------LSGGER 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599791 451 GRLHLALTLKQGGNVLLLDEPSNDLDVETLRALEEALL----DFPGAAIVISHDRWFLDRI 507
Cdd:TIGR02211 148 QRVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLelnrELNTSFLVVTHDLELAKKL 208
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
324-485 |
8.24e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 71.32 E-value: 8.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETV---------QIASVDQS 394
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITidtarslsqQKGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 395 RD---------SLEGNKTVWEQVSDGFEQIK---IGNYEVPSRSYVGRFNFKGaDQQKFVKDLSGGERGRLHLALTLKQG 462
Cdd:PRK11264 84 RQhvgfvfqnfNLFPHRTVLENIIEGPVIVKgepKEEATARARELLAKVGLAG-KETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190
....*....|....*....|....*....|
gi 15599791 463 GNVLLLDEPSNDLDVE-------TLRALEE 485
Cdd:PRK11264 163 PEVILFDEPTSALDPElvgevlnTIRQLAQ 192
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
22-235 |
8.78e-14 |
|
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: 71.22 E-value: 8.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpMPGINVGYLP-------------QEPKLDPQATVRD 88
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRIL-FDGRDITGLPphriarlgiartfQNPRLFPELTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 89 IVeeAVGqikqAQARLDE-VYAAYAEPDADFDALAAEQAKLEAILqasdghnleRQLEVAADAlrlppwDAKVEHLSGGE 167
Cdd:COG0411 99 NV--LVA----AHARLGRgLLAALLRLPRARREEREARERAEELL---------ERVGLADRA------DEPAGNLSYGQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599791 168 KRRVALCRLLLSAPDMLLLDEPT---NHLDADSVAWLEHFLHDFPG-TVVAITHDRYFLDNVAGWILELDRG 235
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLVMGLADRIVVLDFG 229
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
16-119 |
8.82e-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: 70.64 E-value: 8.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 16 PPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDT------EIEGEARPMPGINVGylpqepkLDPQATVRDI 89
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPpdsgtvTVRGRVSSLLGLGGG-------FNPELTGREN 104
|
90 100 110
....*....|....*....|....*....|....*
gi 15599791 90 VeEAVGQI-----KQAQARLDEVYaAYAEPDADFD 119
Cdd:cd03220 105 I-YLNGRLlglsrKEIDEKIDEII-EFSELGDFID 137
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
22-235 |
1.27e-13 |
|
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: 70.54 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpMPGINVGYLP-------------QEPKLDPQATVRD 88
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVL-FDGEDITGLPpheiarlgigrtfQIPRLFPELTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 89 IVEEAvgqikqAQARLDEVYAAyaepDADFDALAAEQAKLEAILqasdghnlerqlevaaDALRLPP-WDAKVEHLSGGE 167
Cdd:cd03219 95 NVMVA------AQARTGSGLLL----ARARREEREARERAEELL----------------ERVGLADlADRPAGELSYGQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599791 168 KRRVALCRLLLSAPDMLLLDEPT---NHLDADSVAWLEHFLHDFPGTVVAITHDRYFLDNVAGWILELDRG 235
Cdd:cd03219 149 QRRLEIARALATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQG 219
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-218 |
1.31e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 70.64 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdTEIEGEA----RPMPGINV-------GYLPQEpkldpQATVRDIv 90
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEIllngRPLSDWSAaelarhrAYLSQQ-----QSPPFAM- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 91 eeAVGQikqaqarldevYAAYAEPdadfdALAAEQAKLEAILQasdghnLERQLEVaADALRLPpwdakVEHLSGGEKRR 170
Cdd:COG4138 85 --PVFQ-----------YLALHQP-----AGASSEAVEQLLAQ------LAEALGL-EDKLSRP-----LTQLSGGEWQR 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15599791 171 VALCRLLL-------SAPDMLLLDEPTNHLD-ADSVA---WLEHFlHDFPGTVVAITHD 218
Cdd:COG4138 135 VRLAAVLLqvwptinPEGQLLLLDEPMNSLDvAQQAAldrLLREL-CQQGITVVMSSHD 192
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
323-482 |
1.77e-13 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 71.76 E-value: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 323 VIELHNVTKGY----GDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQIASVDQSRD- 396
Cdd:PRK11153 1 MIELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVdGQDLTALSEKELRKa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 397 -----------SLEGNKTVWEQVSDGFEQIKIGNYEVPSR-----SYVGRfnfkgADQ-QKFVKDLSGGERGRLHLALTL 459
Cdd:PRK11153 81 rrqigmifqhfNLLSSRTVFDNVALPLELAGTPKAEIKARvtellELVGL-----SDKaDRYPAQLSGGQKQRVAIARAL 155
|
170 180
....*....|....*....|...
gi 15599791 460 KQGGNVLLLDEPSNDLDVETLRA 482
Cdd:PRK11153 156 ASNPKVLLCDEATSALDPATTRS 178
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
19-218 |
1.89e-13 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 69.43 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV---DTEIEGE---------ARPMPGINVGYLPQEPKLDPQATV 86
Cdd:COG4136 14 RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTlspAFSASGEvllngrrltALPAEQRRIGILFQDDLLFPHLSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 87 RDIVeeavgqikqaqarldevyaAYAEPDAdfdalAAEQAKLEAILQAsdghnLErQLEVAADALRLPpwdakvEHLSGG 166
Cdd:COG4136 94 GENL-------------------AFALPPT-----IGRAQRRARVEQA-----LE-EAGLAGFADRDP------ATLSGG 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15599791 167 EKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHF----LHDFPGTVVAITHD 218
Cdd:COG4136 138 QRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFvfeqIRQRGIPALLVTHD 193
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
3-195 |
2.06e-13 |
|
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: 69.61 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 3 QYVYTMHRVGKIVP---PKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTE---------IEGEARPmPGI- 69
Cdd:cd03234 1 QRVLPWWDVGLKAKnwnKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggttsgqilFNGQPRK-PDQf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 70 --NVGYLPQEPKLDPQATVRDIVeeavgqikqaqarldeVYAAyaepdadfdALAAEQAKLEAILQASDGHNLERQLeva 147
Cdd:cd03234 80 qkCVAYVRQDDILLPGLTVRETL----------------TYTA---------ILRLPRKSSDAIRKKRVEDVLLRDL--- 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15599791 148 ADA-LRlppwDAKVEHLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDA 195
Cdd:cd03234 132 ALTrIG----GNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
321-500 |
2.13e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 70.40 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 321 DKVIELHNVTKGYGD--RVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQIASVDQSRDS 397
Cdd:PRK13632 5 SVMIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIdGITISKENLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 398 L------EGNK----TVWEQVSDGFEQIKIGNYEVPSRSY-----VGRFNFKGADQQKfvkdLSGGERGRLHLALTLKQG 462
Cdd:PRK13632 85 IgiifqnPDNQfigaTVEDDIAFGLENKKVPPKKMKDIIDdlakkVGMEDYLDKEPQN----LSGGQKQRVAIASVLALN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15599791 463 GNVLLLDEPSNDLDVETLRALEEALLDFPGAA----IVISHD 500
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkktlISITHD 202
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
20-243 |
2.47e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 69.74 E-value: 2.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDtEIEGEARPMPGINVgylpqepkLDPQATVRDIVEEAvGQIKQ 99
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLE-EITSGDLIVDGLKV--------NDPKVDERLIRQEA-GMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 100 aQARLdevyaayaepdadFDALAA------------EQAKLEAILQASDghnLERQLEVAADALRLPpwdakvEHLSGGE 167
Cdd:PRK09493 85 -QFYL-------------FPHLTAlenvmfgplrvrGASKEEAEKQARE---LLAKVGLAERAHHYP------SELSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 168 KRRVALCRLLLSAPDMLLLDEPTNHLDADsvawLEH-------FLHDFPGTVVAITHDRYFLDNVAGWILELDRGHgIPF 240
Cdd:PRK09493 142 QQRVAIARALAVKPKLMLFDEPTSALDPE----LRHevlkvmqDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGR-IAE 216
|
...
gi 15599791 241 EGN 243
Cdd:PRK09493 217 DGD 219
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-218 |
2.50e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 69.42 E-value: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 2 AQYVYTMHRVGKIV---PPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpMPGINVGYLPQEP 78
Cdd:PRK10584 3 AENIVEVHHLKKSVgqgEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVS-LVGQPLHQMDEEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 79 KLDPQAtvrdiveEAVGQIKQAQARLDEVYAAyaepdadfdalaaEQAKLEAILQ-ASDGHNLERqlevAADALRLPPWD 157
Cdd:PRK10584 82 RAKLRA-------KHVGFVFQSFMLIPTLNAL-------------ENVELPALLRgESSRQSRNG----AKALLEQLGLG 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599791 158 AKVEH----LSGGEKRRVALCRLLLSAPDMLLLDEPTNHLD---ADSVAWLEHFL-HDFPGTVVAITHD 218
Cdd:PRK10584 138 KRLDHlpaqLSGGEQQRVALARAFNGRPDVLFADEPTGNLDrqtGDKIADLLFSLnREHGTTLILVTHD 206
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
321-535 |
2.71e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 70.26 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 321 DKVIELHNVTKGYGDRV-LIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTI---------------EIGE 384
Cdd:PRK13636 3 DYILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdgkpidysrkglmKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 385 TVQIasVDQSRDSLEGNKTVWEQVSDGFEQIKIGNYEVPSR-----SYVGRFNFKgadqQKFVKDLSGGERGRLHLALTL 459
Cdd:PRK13636 83 SVGM--VFQDPDNQLFSASVYQDVSFGAVNLKLPEDEVRKRvdnalKRTGIEHLK----DKPTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 460 KQGGNVLLLDEPSNDLD----VETLRALEEALLDFPGAAIVISHDrwfLDRIATHI--LSYEDDGKVtFFEGNYTEFEAD 533
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHD---IDIVPLYCdnVFVMKEGRV-ILQGNPKEVFAE 232
|
..
gi 15599791 534 RK 535
Cdd:PRK13636 233 KE 234
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
7-217 |
3.05e-13 |
|
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: 69.53 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 7 TMHRVGKIVPPKR---EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARPMpGINVGYLpQEPKLDPQ 83
Cdd:cd03258 3 ELKNVSKVFGDTGgkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVD-GTDLTLL-SGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 84 AtvRDIveeavGQIKQAQARLDE--VYaayaepdaDFDALAAEQAKLEAILQASDGHNLERQLEVAADAlrlppwDAKVE 161
Cdd:cd03258 81 R--RRI-----GMIFQHFNLLSSrtVF--------ENVALPLEIAGVPKAEIEERVLELLELVGLEDKA------DAYPA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 162 HLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDA---DSVAWLEHFLHDFPG-TVVAITH 217
Cdd:cd03258 140 QLSGGQKQRVGIARALANNPKVLLCDEATSALDPettQSILALLRDINRELGlTIVLITH 199
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
17-218 |
3.35e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 69.82 E-value: 3.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 17 PKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEA----RPMPGIN-------VGYLPQEPkldPQA- 84
Cdd:PRK10575 22 PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIlldaQPLESWSskafarkVAYLPQQL---PAAe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 85 --TVRDIVeeAVGQI--KQAQARLdevyaayaepdadfdalaaeqakleailqasdGHNLERQLEVAADALRLPPWDAK- 159
Cdd:PRK10575 99 gmTVRELV--AIGRYpwHGALGRF--------------------------------GAADREKVEEAISLVGLKPLAHRl 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599791 160 VEHLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLD----ADSVAWLEHFLHDFPGTVVAITHD 218
Cdd:PRK10575 145 VDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDiahqVDVLALVHRLSQERGLTVIAVLHD 207
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
323-512 |
3.44e-13 |
|
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: 69.00 E-value: 3.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 323 VIELHNVTKGY-----GDRVL--IDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI---GETVQIASVD 392
Cdd:COG4778 4 LLEVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdGGWVDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 393 QsRDSLEGNKTVweqvsdgfeqikIGnyevpsrsYVGRF--------------------NFKGADQQKFVKDL------- 445
Cdd:COG4778 84 P-REILALRRRT------------IG--------YVSQFlrviprvsaldvvaepllerGVDREEARARARELlarlnlp 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 446 -----------SGGERGRLHLALTLKQGGNVLLLDEPSNDLDVETLRA----LEEALLDfpGAAIV-ISHDRWFLDRIAT 509
Cdd:COG4778 143 erlwdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVvvelIEEAKAR--GTAIIgIFHDEEVREAVAD 220
|
...
gi 15599791 510 HIL 512
Cdd:COG4778 221 RVV 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
18-236 |
3.68e-13 |
|
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: 68.71 E-value: 3.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDT------EIEGEARPMPGIN-------VGYLPQEPKLDPQA 84
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEpdsgtiIIDGLKLTDDKKNinelrqkVGMVFQQFNLFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 85 TVRDIVEEAVGQIKQaqarldevyaayaEPDADFDALAAEQakleailqasdghnLER-QLEVAADALrlpPwdakvEHL 163
Cdd:cd03262 92 TVLENITLAPIKVKG-------------MSKAEAEERALEL--------------LEKvGLADKADAY---P-----AQL 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599791 164 SGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPG---TVVAITHDRYFLDNVAGWILELDRGH 236
Cdd:cd03262 137 SGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEegmTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
20-218 |
4.84e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 68.69 E-value: 4.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEarpmpginVGYLPQEPKLDPQATVRDIVEEAVGQIKQ 99
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGD--------VIFNGQPMSKLSSAAKAELRNQKLGFIYQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 100 AQARLdevyaayaepdADFDALAAEQAKLeAILQASDGHNLERQLEVAAdALRLppwDAKVEH----LSGGEKRRVALCR 175
Cdd:PRK11629 95 FHHLL-----------PDFTALENVAMPL-LIGKKKPAEINSRALEMLA-AVGL---EHRANHrpseLSGGERQRVAIAR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15599791 176 LLLSAPDMLLLDEPTNHLD---ADSVAWLEHFLHDFPGTV-VAITHD 218
Cdd:PRK11629 159 ALVNNPRLVLADEPTGNLDarnADSIFQLLGELNRLQGTAfLVVTHD 205
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
22-228 |
5.15e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 69.73 E-value: 5.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEarpmpgINVGYLPQEPKLDPQATVRDIVEEAVG------ 95
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGT------IEWIFKDEKNKKKTKEKEKVLEKLVIQktrfkk 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 96 --QIKQAQARLDEVY--AAYA------EPDADFDALAAEQAKLEAILQASDGHNLerqLEVAADALRLPPWDakvehLSG 165
Cdd:PRK13651 97 ikKIKEIRRRVGVVFqfAEYQlfeqtiEKDIIFGPVSMGVSKEEAKKRAAKYIEL---VGLDESYLQRSPFE-----LSG 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599791 166 GEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVA-WLEHF--LHDFPGTVVAITHDryfLDNVAGW 228
Cdd:PRK13651 169 GQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKeILEIFdnLNKQGKTIILVTHD---LDNVLEW 231
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
230-306 |
5.81e-13 |
|
ABC transporter; This domain is an extension of some members of pfam00005 and other ABC-transporter families.
Pssm-ID: 463731 [Multi-domain] Cd Length: 85 Bit Score: 64.52 E-value: 5.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 230 LELDRGHGIPFEGNYSGWLESKAARLAQEAKQEASHAKAMKAELEWVRQ----GAKGRQAKSKA-RLQRFEELQSQEFQK 304
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRfrakASKAKQAQSRIkALEKMERIEKPERDK 80
|
..
gi 15599791 305 RS 306
Cdd:pfam12848 81 PK 82
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
17-194 |
6.75e-13 |
|
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: 71.39 E-value: 6.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 17 PKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---VDteiEGEARpMPGINVGYLPQepkldpqATVRdiveEA 93
Cdd:COG5265 369 PERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRfydVT---SGRIL-IDGQDIRDVTQ-------ASLR----AA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 94 VGQIKQaqarlDEV-------Y-AAYAEPDADFDAL--AAEQAKLEA-ILQASDGHNL---ERQLEvaadalrlppwdak 159
Cdd:COG5265 434 IGIVPQ-----DTVlfndtiaYnIAYGRPDASEEEVeaAARAAQIHDfIESLPDGYDTrvgERGLK-------------- 494
|
170 180 190
....*....|....*....|....*....|....*
gi 15599791 160 vehLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLD 194
Cdd:COG5265 495 ---LSGGEKQRVAIARTLLKNPPILIFDEATSALD 526
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
24-235 |
1.02e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 69.86 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 24 DISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpMPGINVGYLP----------QEPKLDPQATVRDIVEEA 93
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIM-LDGVDLSHVPpyqrpinmmfQSYALFPHMTVEQNIAFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 94 VGQIKQAQARLdevyaayaepdadfdalaaeQAKLEAILqasdghNLERQLEVAAdalRLPpwdakvEHLSGGEKRRVAL 173
Cdd:PRK11607 116 LKQDKLPKAEI--------------------ASRVNEML------GLVHMQEFAK---RKP------HQLSGGQRQRVAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599791 174 CRLLLSAPDMLLLDEPTNHLDADSVAWLEH----FLHDFPGTVVAITHDRYFLDNVAGWILELDRG 235
Cdd:PRK11607 161 ARSLAKRPKLLLLDEPMGALDKKLRDRMQLevvdILERVGVTCVMVTHDQEEAMTMAGRIAIMNRG 226
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
17-218 |
1.04e-12 |
|
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: 67.28 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 17 PKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpMPGINVGYLP----------QEPKLDPQATV 86
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIY-IGGRDVTDLPpkdrdiamvfQNYALYPHMTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 87 RDIVEEAvgqIKQAQARLDEVyaayaepdadfDALAAEQAKLEAIlqasdGHNLERqlevaadalrlppwdaKVEHLSGG 166
Cdd:cd03301 90 YDNIAFG---LKLRKVPKDEI-----------DERVREVAELLQI-----EHLLDR----------------KPKQLSGG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15599791 167 EKRRVALCRLLLSAPDMLLLDEPTNHLDA----DSVAWLEHFLHDFPGTVVAITHD 218
Cdd:cd03301 135 QRQRVALGRAIVREPKVFLMDEPLSNLDAklrvQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
18-198 |
1.06e-12 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 68.06 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVD----------------TEIEGEARPMPGINVGYlpQEPKLD 81
Cdd:TIGR01978 12 DKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPsyevtsgtilfkgqdlLELEPDERARAGLFLAF--QYPEEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 82 PQATVRDIVEEAVGQIKQAQArldevyaayaEPDADFDALAAEQAKLEAILQAsDGHNLERQLEVAadalrlppwdakve 161
Cdd:TIGR01978 90 PGVSNLEFLRSALNARRSARG----------EEPLDLLDFEKLLKEKLALLDM-DEEFLNRSVNEG-------------- 144
|
170 180 190
....*....|....*....|....*....|....*..
gi 15599791 162 hLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSV 198
Cdd:TIGR01978 145 -FSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDAL 180
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-194 |
1.07e-12 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 67.13 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 24 DISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpMPGINVGYLP----------QEPKLDPQATVrdivEEA 93
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVL-INGVDVTAAPpadrpvsmlfQENNLFAHLTV----EQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 94 VGQIKQAQARLDEVyaayaepdadfdalaaEQAKLEAILqasdghnleRQLEVAADALRLPpwdakvEHLSGGEKRRVAL 173
Cdd:cd03298 91 VGLGLSPGLKLTAE----------------DRQAIEVAL---------ARVGLAGLEKRLP------GELSGGERQRVAL 139
|
170 180
....*....|....*....|.
gi 15599791 174 CRLLLSAPDMLLLDEPTNHLD 194
Cdd:cd03298 140 ARVLVRDKPVLLLDEPFAALD 160
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
21-231 |
1.09e-12 |
|
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: 68.29 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpMPGINVGYLPQEPKLDPQATVRDIVEEAVGQIKQA 100
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVS-FRGQDLYQLDRKQRRAFRRDVQLVFQDSPSAVNPR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 101 QArldeVYAAYAEPDADFDAL--AAEQAKLEAILQASDGHnlerqlevAADALRLPPwdakveHLSGGEKRRVALCRLLL 178
Cdd:TIGR02769 105 MT----VRQIIGEPLRHLTSLdeSEQKARIAELLDMVGLR--------SEDADKLPR------QLSGGQLQRINIARALA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599791 179 SAPDMLLLDEPTNHLD----ADSVAWLEHFLHDFPGTVVAITHD----RYFLDNVA----GWILE 231
Cdd:TIGR02769 167 VKPKLIVLDEAVSNLDmvlqAVILELLRKLQQAFGTAYLFITHDlrlvQSFCQRVAvmdkGQIVE 231
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
323-521 |
1.15e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 67.81 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 323 VIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQIASVDQSRDSLEGN 401
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVdGLKVNDPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 402 kTVWEQVS-----DGFEQIKIGNYEVPSRSyvgrfnfkGADQQKFVKD-----------------LSGGERGRLHLALTL 459
Cdd:PRK09493 81 -MVFQQFYlfphlTALENVMFGPLRVRGAS--------KEEAEKQAREllakvglaerahhypseLSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 460 KQGGNVLLLDEPSNDLDVE-------TLRAL-EEALldfpgAAIVISHDRWFLDRIATHILsYEDDGKVT 521
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDPElrhevlkVMQDLaEEGM-----TMVIVTHEIGFAEKVASRLI-FIDKGRIA 215
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
324-476 |
1.38e-12 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 67.13 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLidNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGEtVQIASVDQSR-------- 395
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING-VDVTAAPPADrpvsmlfq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 396 -DSLEGNKTVWEQVSDGF---------EQIKIgnyevpsRSYVGRFNFKGADQQKfVKDLSGGERGRLHLALTLKQGGNV 465
Cdd:cd03298 78 eNNLFAHLTVEQNVGLGLspglkltaeDRQAI-------EVALARVGLAGLEKRL-PGELSGGERQRVALARVLVRDKPV 149
|
170
....*....|.
gi 15599791 466 LLLDEPSNDLD 476
Cdd:cd03298 150 LLLDEPFAALD 160
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
325-499 |
1.65e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.94 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 325 ELHNVTKGY-GDRVLiDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQIASVdqsRDSLEG-- 400
Cdd:PRK11288 6 SFDGIGKTFpGVKAL-DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIdGQEMRFAST---TAALAAgv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 401 -----------NKTVWEQV-------SDGFEQIKIGNYEVpsRSYVGRFNFKgADQQKFVKDLSGGERGRLHLALTLKQG 462
Cdd:PRK11288 82 aiiyqelhlvpEMTVAENLylgqlphKGGIVNRRLLNYEA--REQLEHLGVD-IDPDTPLKYLSIGQRQMVEIAKALARN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15599791 463 GNVLLLDEPSNDL---DVETLRALEEALLDFPGAAIVISH 499
Cdd:PRK11288 159 ARVIAFDEPTSSLsarEIEQLFRVIRELRAEGRVILYVSH 198
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
21-224 |
1.87e-12 |
|
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: 65.80 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRImagvdteIEGEARPMPGinvgylpqEPKLD--PQATVRDIVEEAVGQIK 98
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQL-------LTGDLKPQQG--------EITLDgvPVSDLEKALSSLISVLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 99 QaqarldEVYAayaepdadFDAlaaeqakleailqaSDGHNLERQLevaadalrlppwdakvehlSGGEKRRVALCRLLL 178
Cdd:cd03247 82 Q------RPYL--------FDT--------------TLRNNLGRRF-------------------SGGERQRLALARILL 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15599791 179 SAPDMLLLDEPTNHLDADS-VAWLEHFLHDFPG-TVVAITH--------DR-YFLDN 224
Cdd:cd03247 115 QDAPIVLLDEPTVGLDPITeRQLLSLIFEVLKDkTLIWITHhltgiehmDKiLFLEN 171
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
324-499 |
1.88e-12 |
|
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: 66.87 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGY-GDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI----GETVQIASVDQS---- 394
Cdd:cd03254 3 IEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIdgidIRDISRKSLRSMigvv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 395 -RDSLEGNKTVweqvsdgFEQIKIGNYEVPSRSYVGRFNFKGADQqkFV---------------KDLSGGERGRLHLALT 458
Cdd:cd03254 83 lQDTFLFSGTI-------MENIRLGRPNATDEEVIEAAKEAGAHD--FImklpngydtvlgengGNLSQGERQLLAIARA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15599791 459 LKQGGNVLLLDEPSNDLDVETLRALEEALLD-FPG-AAIVISH 499
Cdd:cd03254 154 MLRDPKILILDEATSNIDTETEKLIQEALEKlMKGrTSIIIAH 196
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
324-501 |
2.06e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 68.57 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVqiaSVDQSRD------ 396
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFhGTDV---SRLHARDrkvgfv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 397 ----SLEGNKTVWEQVSDGFEQIKigNYEVPSRSYVGRFNFKGADQ-------QKFVKDLSGGERGRLHLALTLKQGGNV 465
Cdd:PRK10851 80 fqhyALFRHMTVFDNIAFGLTVLP--RRERPNAAAIKAKVTQLLEMvqlahlaDRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15599791 466 LLLDEPSNDLDVET-------LRALEEAlLDFpgAAIVISHDR 501
Cdd:PRK10851 158 LLLDEPFGALDAQVrkelrrwLRQLHEE-LKF--TSVFVTHDQ 197
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
328-529 |
2.25e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 67.43 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 328 NVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETVQIA-SVDQSRDSLEGNKTVWE 406
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGrSIFNYRDVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 407 --QVSDGFEQIKIGNYEVPSRSY--VGRFNFKGADQQKF--------VKD--------LSGGERGRLHLALTLKQGGNVL 466
Cdd:PRK14271 106 lfQRPNPFPMSIMDNVLAGVRAHklVPRKEFRGVAQARLtevglwdaVKDrlsdspfrLSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599791 467 LLDEPSNDLDVETLRALEEALLDFPG--AAIVISHDRWFLDRIAthilsyedDGKVTFFEGNYTE 529
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHNLAQAARIS--------DRAALFFDGRLVE 242
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
321-508 |
2.68e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 67.45 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 321 DKVIELHNVTKGYG---DRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIG------ETV----- 386
Cdd:PRK13650 2 SNIIEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDgdllteENVwdirh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 387 QIASVDQSRDSLEGNKTVWEQVSDGFEQIKIGNYEVPSR-----SYVGRFNFKGADQQKfvkdLSGGERGRLHLALTLKQ 461
Cdd:PRK13650 82 KIGMVFQNPDNQFVGATVEDDVAFGLENKGIPHEEMKERvnealELVGMQDFKEREPAR----LSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15599791 462 GGNVLLLDEPSNDLD----VETLRALEEALLDFPGAAIVISHDrwfLDRIA 508
Cdd:PRK13650 158 RPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHD---LDEVA 205
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
31-194 |
3.10e-12 |
|
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: 68.21 E-value: 3.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 31 PGAKI-GVLGLNGAGKSTLLRIMAGVDTEIEGE--------ARPMPGI-------NVGYLPQEPKLDPQATVRDIVEeav 94
Cdd:TIGR02142 21 PGQGVtAIFGRSGSGKTTLIRLIAGLTRPDEGEivlngrtlFDSRKGIflppekrRIGYVFQEARLFPHLSVRGNLR--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 95 gqikqaqarldevyaaYAEPDADFDALAAEQAKLEAILQAsdGHNLERqlevaadalrlPPWDakvehLSGGEKRRVALC 174
Cdd:TIGR02142 98 ----------------YGMKRARPSERRISFERVIELLGI--GHLLGR-----------LPGR-----LSGGEKQRVAIG 143
|
170 180
....*....|....*....|
gi 15599791 175 RLLLSAPDMLLLDEPTNHLD 194
Cdd:TIGR02142 144 RALLSSPRLLLMDEPLAALD 163
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-195 |
3.12e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 69.31 E-value: 3.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 17 PKREILKDISLSFFPGAKIGVLGLNGAGKSTLL-----RIMAGV----DTEIEGEARPMPGINV--GYLPQEPKLDPQAT 85
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMnalafRSPKGVkgsgSVLLNGMPIDAKEMRAisAYVQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 86 VRDIVeeavgqIKQAQARLDEVYAAyaepdadfdalAAEQAKLEAILQASDghnlerqLEVAADALRLPPWDAKVehLSG 165
Cdd:TIGR00955 116 VREHL------MFQAHLRMPRRVTK-----------KEKRERVDEVLQALG-------LRKCANTRIGVPGRVKG--LSG 169
|
170 180 190
....*....|....*....|....*....|
gi 15599791 166 GEKRRVALCRLLLSAPDMLLLDEPTNHLDA 195
Cdd:TIGR00955 170 GERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
324-499 |
3.19e-12 |
|
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: 68.97 E-value: 3.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYG--DRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTI-----EIGETV------QIAS 390
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQIlldghDLADYTlaslrrQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 391 VDQsrDSLEGNKTVWEQVSDGfEQIKIGNYEVPS-------RSYVGRFNfKGADQQKFVK--DLSGGERGRLHLALTLKQ 461
Cdd:TIGR02203 411 VSQ--DVVLFNDTIANNIAYG-RTEQADRAEIERalaaayaQDFVDKLP-LGLDTPIGENgvLLSGGQRQRLAIARALLK 486
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15599791 462 GGNVLLLDEPSNDLDVETLRALEEAL--LDFPGAAIVISH 499
Cdd:TIGR02203 487 DAPILILDEATSALDNESERLVQAALerLMQGRTTLVIAH 526
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
324-508 |
3.20e-12 |
|
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: 66.59 E-value: 3.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLiDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETV--------QIASVDQS 394
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLnGKDItnlppekrDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 395 RdSLEGNKTVWEQVSDGFEQIKIGNYEVPSRsyVGRF-NFKGADQ--QKFVKDLSGGERGRLHLALTLKQGGNVLLLDEP 471
Cdd:cd03299 80 Y-ALFPHMTVYKNIAYGLKKRKVDKKEIERK--VLEIaEMLGIDHllNRKPETLSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15599791 472 SNDLDVET----LRALEEALLDFPGAAIVISHD----RWFLDRIA 508
Cdd:cd03299 157 FSALDVRTkeklREELKKIRKEFGVTVLHVTHDfeeaWALADKVA 201
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
324-520 |
3.80e-12 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 66.19 E-value: 3.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGEtvqiASVDQSRDSLEGNKT 403
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAG----HQFDFSQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 404 VWEQ-VSDGFEQIKIGNY--------EVPSRsyVGRFNFKGADQQ---------------KFVKDLSGGERGRLHLALTL 459
Cdd:COG4161 79 LLRQkVGMVFQQYNLWPHltvmenliEAPCK--VLGLSKEQAREKamkllarlrltdkadRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599791 460 KQGGNVLLLDEPSNDLDVETLRALEEALLDFPGAAI---VISHDRWFLDRIATHILsYEDDGKV 520
Cdd:COG4161 157 MMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGItqvIVTHEVEFARKVASQVV-YMEKGRI 219
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
323-534 |
4.14e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 66.57 E-value: 4.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 323 VIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFR----MLTGKEQPDSGTIEIGETVQIA-----SVDQ 393
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGSHIELLGRTVQREgrlarDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 394 SRD---------SLEGNKTVWEQVSDG--------------FEQI-KIGNYEVPSRsyVGRFNFkgADQQkfVKDLSGGE 449
Cdd:PRK09984 84 SRAntgyifqqfNLVNRLSVLENVLIGalgstpfwrtcfswFTREqKQRALQALTR--VGMVHF--AHQR--VSTLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 450 RGRLHLALTLKQGGNVLLLDEPSNDLDVETLRALEEALLDF---PGAAIVIS-HDRWFLDRIATHILSYEdDGKVtFFEG 525
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInqnDGITVVVTlHQVDYALRYCERIVALR-QGHV-FYDG 235
|
....*....
gi 15599791 526 NYTEFEADR 534
Cdd:PRK09984 236 SSQQFDNER 244
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
21-218 |
4.22e-12 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 66.11 E-value: 4.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDT----EIEGEARPMPGI-----NVGYLPQEPKLDPQATVRDIVe 91
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETptsgEILLDGKDITNLpphkrPVNTVFQNYALFPHLTVFENI- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 92 eAVGqIKQAQARLDEVYAAYAEpdadfdalAAEQAKLEailqasdghNLERQlevaadalrlppwdaKVEHLSGGEKRRV 171
Cdd:cd03300 94 -AFG-LRLKKLPKAEIKERVAE--------ALDLVQLE---------GYANR---------------KPSQLSGGQQQRV 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15599791 172 ALCRLLLSAPDMLLLDEPTNHLDADSVAWLE---HFLHDFPG-TVVAITHD 218
Cdd:cd03300 140 AIARALVNEPKVLLLDEPLGALDLKLRKDMQlelKRLQKELGiTFVFVTHD 190
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
20-194 |
4.81e-12 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 65.79 E-value: 4.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDT------EIEGEARPMPGIN-------VGYLPQEPKLDPQATV 86
Cdd:COG1126 15 EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEpdsgtiTVDGEDLTDSKKDinklrrkVGMVFQQFNLFPHLTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 87 RDIVEEA---VGQIKQAQARldevyaayaepdadfdALAAEQakleailqasdghnLERqLEVAADAlrlppwDAKVEHL 163
Cdd:COG1126 95 LENVTLApikVKKMSKAEAE----------------ERAMEL--------------LER-VGLADKA------DAYPAQL 137
|
170 180 190
....*....|....*....|....*....|.
gi 15599791 164 SGGEKRRVALCRLLLSAPDMLLLDEPTNHLD 194
Cdd:COG1126 138 SGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
324-520 |
5.98e-12 |
|
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: 64.86 E-value: 5.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKE--QPDSGTIEigetvqiasvdqsrdslegn 401
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEIL-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 402 ktvweqvsdgFEQIKIGNYEVPSRSYVGRF-------NFKGADQQKFVKDL----SGGERGRLHLALTLKQGGNVLLLDE 470
Cdd:cd03217 61 ----------FKGEDITDLPPEERARLGIFlafqyppEIPGVKNADFLRYVnegfSGGEKKRNEILQLLLLEPDLAILDE 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15599791 471 PSNDLDVETLRALEEA---LLDFPGAAIVISHDRWFLDRIAT---HILsyeDDGKV 520
Cdd:cd03217 131 PDSGLDIDALRLVAEVinkLREEGKSVLIITHYQRLLDYIKPdrvHVL---YDGRI 183
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-217 |
7.21e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 67.93 E-value: 7.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------GvdtEIEGEARPMPGINVGYLPQEPKLDPQ------ATVR 87
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTrawdpqqG---EILLNGQPIADYSEAALRQAISVVSQrvhlfsATLR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 88 DIVeeavgqikqaqarldevyaAYAEPDADFDALAA--EQAKLEAILQASDGHNL-----ERQLevaadalrlppwdakv 160
Cdd:PRK11160 432 DNL-------------------LLAAPNASDEALIEvlQQVGLEKLLEDDKGLNAwlgegGRQL---------------- 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599791 161 ehlSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADS-----VAWLEHFLHDfpgTVVAITH 217
Cdd:PRK11160 477 ---SGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETerqilELLAEHAQNK---TVLMITH 532
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
324-520 |
7.40e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 67.93 E-value: 7.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDR--VLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGET-----------VQIAS 390
Cdd:PRK11160 339 LTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQpiadyseaalrQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 391 VDQS--------RDSL---------EGNKTVWEQVsdGFEqiKIGNYEVPSRSYVGrfnfKGADQqkfvkdLSGGERGRL 453
Cdd:PRK11160 419 VSQRvhlfsatlRDNLllaapnasdEALIEVLQQV--GLE--KLLEDDKGLNAWLG----EGGRQ------LSGGEQRRL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599791 454 HLALTLKQGGNVLLLDEPSNDLDVETLRALEEALLDFpgAA----IVISHDRWFL---DRIatHILsyeDDGKV 520
Cdd:PRK11160 485 GIARALLHDAPLLLLDEPTEGLDAETERQILELLAEH--AQnktvLMITHRLTGLeqfDRI--CVM---DNGQI 551
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
323-472 |
8.94e-12 |
|
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: 65.00 E-value: 8.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 323 VIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQ-----------IAS 390
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFdGEDITglpphriarlgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 391 VDQSRD---SLegnkTVWeqvsdgfEQIKIGNYEVPSRSYVG---------------RFNFKGAdqqkfvkDLSGGER-- 450
Cdd:COG0410 83 VPEGRRifpSL----TVE-------ENLLLGAYARRDRAEVRadlervyelfprlkeRRRQRAG-------TLSGGEQqm 144
|
170 180
....*....|....*....|....*..
gi 15599791 451 ---GRlhlALTlkqgGN--VLLLDEPS 472
Cdd:COG0410 145 laiGR---ALM----SRpkLLLLDEPS 164
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-229 |
1.17e-11 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 65.08 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 31 PGAKIGVLGLNGAGKSTLLRIMAGvdteiegEARPmpgiNVGYLPQEPKLDpqatvrDIVEEAVG---QIKQAQARLDEV 107
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAG-------KLKP----NLGKFDDPPDWD------EILDEFRGselQNYFTKLLEGDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 108 YAAYAEPDADFDALAAeQAKLEAILQASDghnlER-QLEVAADALRLPP-WDAKVEHLSGGEKRRVALCRLLLSAPDMLL 185
Cdd:cd03236 88 KVIVKPQYVDLIPKAV-KGKVGELLKKKD----ERgKLDELVDQLELRHvLDRNIDQLSGGELQRVAIAAALARDADFYF 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15599791 186 LDEPTNHLDAD---SVAWLEHFLHDFPGTVVAITHDRYFLDNVAGWI 229
Cdd:cd03236 163 FDEPSSYLDIKqrlNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
19-195 |
1.19e-11 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 65.27 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV------DTEIEGEARPMPGINVGYLPQEPKLDPQATVRDIVee 92
Cdd:COG4525 20 QPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFlapssgEITLDGVPVTGPGADRGVVFQKDALLPWLNVLDNV-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 93 AVGqikqaqARLDEVyaayaepdadfdALAAEQAKLEAILQASDghnlerqLEVAADAlrlPPWdakveHLSGGEKRRVA 172
Cdd:COG4525 98 AFG------LRLRGV------------PKAERRARAEELLALVG-------LADFARR---RIW-----QLSGGMRQRVG 144
|
170 180
....*....|....*....|...
gi 15599791 173 LCRLLLSAPDMLLLDEPTNHLDA 195
Cdd:COG4525 145 IARALAADPRFLLMDEPFGALDA 167
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
19-218 |
1.31e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 65.23 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGvdtEIEGEARPMpginvgylpqepkldpQATVRDIVE---EAVG 95
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG---DLTGGGAPR----------------GARVTGDVTlngEPLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 96 QIKQAQ-ARLDEVYAAYAEPDADFDALAA------EQAKLEAILQASDGHNLERQLEVA-ADALrlppwDAK-VEHLSGG 166
Cdd:PRK13547 75 AIDAPRlARLRAVLPQAAQPAFAFSAREIvllgryPHARRAGALTHRDGEIAWQALALAgATAL-----VGRdVTTLSGG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599791 167 EKRRVALCRLL---------LSAPDMLLLDEPTNHLDadsvawLEHfLHDFPGTVVAITHD 218
Cdd:PRK13547 150 ELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALD------LAH-QHRLLDTVRRLARD 203
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
16-238 |
1.57e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 65.14 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 16 PPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpMPGINVGYLPQEPKLDPqatVRDIVEeAVG 95
Cdd:PRK13643 16 PFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVT-VGDIVVSSTSKQKEIKP---VRKKVG-VVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 96 QIKQAQARLDEVYAAYAEPDADFDALAAEQAKLEAilqasdghnleRQLEVAAdaLRLPPWDAKVEHLSGGEKRRVALCR 175
Cdd:PRK13643 91 QFPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAA-----------EKLEMVG--LADEFWEKSPFELSGGQMRRVAIAG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599791 176 LLLSAPDMLLLDEPTNHLDADS-VAWLEHF--LHDFPGTVVAITHDRYFLDNVAGWILELDRGHGI 238
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKArIEMMQLFesIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHII 223
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
18-257 |
1.73e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 64.61 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpmpgINVGYLPQEPKLDPQATVRDiveeaVGQI 97
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIV----VNGQTINLVRDKDGQLKVAD-----KNQL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 98 KQAQARLDEVYAAYAepdadfdaLAAEQAKLEAILQA-------SDGHNLERQL----EVAADALRLPPWDAkveHLSGG 166
Cdd:PRK10619 88 RLLRTRLTMVFQHFN--------LWSHMTVLENVMEApiqvlglSKQEARERAVkylaKVGIDERAQGKYPV---HLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 167 EKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFP---GTVVAITHDRYFLDNVAGWILELDRGHgIPFEGN 243
Cdd:PRK10619 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeegKTMVVVTHEMGFARHVSSHVIFLHQGK-IEEEGA 235
|
250
....*....|....*
gi 15599791 244 YSGWLES-KAARLAQ 257
Cdd:PRK10619 236 PEQLFGNpQSPRLQQ 250
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
324-499 |
2.05e-11 |
|
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: 64.04 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYG--DRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIgETVQIASVDQS------- 394
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLV-DGHDLALADPAwlrrqvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 395 ---RDSLEGNKTVweqvsdgFEQIKIGNYEVPSRSYVGRFNFKGAdqQKFVKD---------------LSGGERGRLHLA 456
Cdd:cd03252 80 vvlQENVLFNRSI-------RDNIALADPGMSMERVIEAAKLAGA--HDFISElpegydtivgeqgagLSGGQRQRIAIA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15599791 457 LTLKQGGNVLLLDEPSNDLDVETLRALEEALLDFPG--AAIVISH 499
Cdd:cd03252 151 RALIHNPRILIFDEATSALDYESEHAIMRNMHDICAgrTVIIIAH 195
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
297-499 |
2.16e-11 |
|
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: 66.69 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 297 LQSQEFQKRSETNEIYIPagprLGDKVIELHNVTKGYGDRVLiDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPD 376
Cdd:TIGR01193 453 LVDSEFINKKKRTELNNL----NGDIVINDVSYSYGYGSNIL-SDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQAR 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 377 SGTIEIGETvQIASVDqsRDSLEGNKTVWEQ---VSDG--FEQIKIGNYEVPSRSYVGRF-----------NFKGADQQK 440
Cdd:TIGR01193 528 SGEILLNGF-SLKDID--RHTLRQFINYLPQepyIFSGsiLENLLLGAKENVSQDEIWAAceiaeikddieNMPLGYQTE 604
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599791 441 FVKD---LSGGERGRLHLALTLKQGGNVLLLDEPSNDLDVETLRALEEALLDFPGAAIV-ISH 499
Cdd:TIGR01193 605 LSEEgssISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDKTIIfVAH 667
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
18-218 |
2.20e-11 |
|
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: 64.37 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARPMpGIN-------------VGYLPQEPklDPQ- 83
Cdd:TIGR04520 14 EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVD-GLDtldeenlweirkkVGMVFQNP--DNQf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 84 --ATVRDIVeeAVG----QIKQAQ--ARLDEvyaayaepdadfdalAAEQAKLEAILQAsdghnlerqlevaadalrlPP 155
Cdd:TIGR04520 91 vgATVEDDV--AFGlenlGVPREEmrKRVDE---------------ALKLVGMEDFRDR-------------------EP 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599791 156 wdakvEHLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADS---VAWLEHFLHDFPG-TVVAITHD 218
Cdd:TIGR04520 135 -----HLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGrkeVLETIRKLNKEEGiTVISITHD 196
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
16-218 |
2.27e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 64.71 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 16 PPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEArpmpginvgYLPQEP-KLDPQATVRdiVEEAV 94
Cdd:PRK13639 12 PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEV---------LIKGEPiKYDKKSLLE--VRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 95 GQIKQAQArlDEVYAAYAEPDADFDALAAEQAKLEailqasdghnLERQLEVAADALRLPPWDAKV-EHLSGGEKRRVAL 173
Cdd:PRK13639 81 GIVFQNPD--DQLFAPTVEEDVAFGPLNLGLSKEE----------VEKRVKEALKAVGMEGFENKPpHHLSGGQKKRVAI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15599791 174 CRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPG---TVVAITHD 218
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKegiTIIISTHD 196
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
20-218 |
2.61e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 66.29 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpMPGINVGYLPQepklDPQATVRdivEEAVGQIKQ 99
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYR-VAGQDVATLDA----DALAQLR---REHFGFIFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 100 AQARLDEVYAAY-AEPDADFDALAAEQAKLEAIlqasdghNLERQLEVAaDALRLPPwdakvEHLSGGEKRRVALCRLLL 178
Cdd:PRK10535 94 RYHLLSHLTAAQnVEVPAVYAGLERKQRLLRAQ-------ELLQRLGLE-DRVEYQP-----SQLSGGQQQRVSIARALM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15599791 179 SAPDMLLLDEPTNHLDADS---VAWLEHFLHDFPGTVVAITHD 218
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSgeeVMAILHQLRDRGHTVIIVTHD 203
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
334-499 |
2.67e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 62.90 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 334 GDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQiasvdQSRDSLEGN----------K 402
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWqGEPIR-----RQRDEYHQDllylghqpgiK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 403 ---TVWE---------------QVSDGFEQIKIGNYE-VPSRSyvgrfnfkgadqqkfvkdLSGGERGRLHLALTLKQGG 463
Cdd:PRK13538 87 telTALEnlrfyqrlhgpgddeALWEALAQVGLAGFEdVPVRQ------------------LSAGQQRRVALARLWLTRA 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 15599791 464 NVLLLDEPSNDLD---VETLRALEEALLDFPGAAIVISH 499
Cdd:PRK13538 149 PLWILDEPFTAIDkqgVARLEALLAQHAEQGGMVILTTH 187
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
339-500 |
3.06e-11 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 63.25 E-value: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 339 IDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQIASVDQ----SRDSLEGNKTVWEQ----VS 409
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILeGKQITEPGPDRmvvfQNYSLLPWLTVRENialaVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 410 DGFEQIKIGNYEVPSRSYVGRFNFKGAdQQKFVKDLSGGERGRLHLALTLKQGGNVLLLDEPSNDLDVETLRALEEALL- 488
Cdd:TIGR01184 81 RVLPDLSKSERRAIVEEHIALVGLTEA-ADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMq 159
|
170
....*....|....*
gi 15599791 489 ---DFPGAAIVISHD 500
Cdd:TIGR01184 160 iweEHRVTVLMVTHD 174
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
335-483 |
3.06e-11 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 63.44 E-value: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 335 DRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPD---SGTIEIG------ETVQ--IASVDQSrDSLEGNKT 403
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNgqprkpDQFQkcVAYVRQD-DILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 404 VWEQVSdgFEQIKIGNYEVPSRSYVGRFNFKG----ADQQ---KFVKDLSGGERGRLHLALTLKQGGNVLLLDEPSNDLD 476
Cdd:cd03234 98 VRETLT--YTAILRLPRKSSDAIRKKRVEDVLlrdlALTRiggNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170
....*....|....
gi 15599791 477 -------VETLRAL 483
Cdd:cd03234 176 sftalnlVSTLSQL 189
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
14-217 |
3.68e-11 |
|
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: 65.93 E-value: 3.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 14 IVPPKREIL-KDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGE-ARPMPGiNVGYLPQEPKLDpQATVRDive 91
Cdd:TIGR00954 459 LVTPNGDVLiESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRlTKPAKG-KLFYVPQRPYMT-LGTLRD--- 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 92 eavgQIkqaqarldeVYaayaePDA--DFDALAAEQAKLEAILQASD-GHNLERqlEVAADALRlpPWdakVEHLSGGEK 168
Cdd:TIGR00954 534 ----QI---------IY-----PDSseDMKRRGLSDKDLEQILDNVQlTHILER--EGGWSAVQ--DW---MDVLSGGEK 588
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15599791 169 RRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPGTVVAITH 217
Cdd:TIGR00954 589 QRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
287-487 |
4.25e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 65.37 E-value: 4.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 287 SKARLQRFEELQSQEFQKRSETNEIyiPAGPRLGDkvIELHNVTKGY-GDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTL 365
Cdd:PRK13657 302 AAPKLEEFFEVEDAVPDVRDPPGAI--DLGRVKGA--VEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 366 FRMLTGKEQPDSGTIEIgETVQIASVdqSRDSLEGNKTVWEQVSDGF-----EQIKIGN--------YEVPSRSYVGRFN 432
Cdd:PRK13657 378 INLLQRVFDPQSGRILI-DGTDIRTV--TRASLRRNIAVVFQDAGLFnrsieDNIRVGRpdatdeemRAAAERAQAHDFI 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 433 FKGADQQKFV-----KDLSGGERGRLHLALTLKQGGNVLLLDEPSNDLDVETLRALEEAL 487
Cdd:PRK13657 455 ERKPDGYDTVvgergRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAAL 514
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-244 |
4.38e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 62.67 E-value: 4.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRimagvdtEIEGEARPMPGINVGYLPQEPkLDPQATVRDIVeeavgqi 97
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLR-------LLAGALKGTPVAGCVDVPDNQ-FGREASLIDAI------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 98 kqaqARLDEVYAAyaepdadFDALAAeqAKLeailqasdghnlerqlevaADAlrlPPWDAKVEHLSGGEKRRVALCRLL 177
Cdd:COG2401 107 ----GRKGDFKDA-------VELLNA--VGL-------------------SDA---VLWLRRFKELSTGQKFRFRLALLL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599791 178 LSAPDMLLLDEPTNHLDADSVAWLEHFLHDF----PGTVVAITHDryflDNVAGWiLELDR----GHGIPFEGNY 244
Cdd:COG2401 152 AERPKLLVIDEFCSHLDRQTAKRVARNLQKLarraGITLVVATHH----YDVIDD-LQPDLlifvGYGGVPEEKR 221
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
37-194 |
4.38e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 64.51 E-value: 4.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 37 VLGLNGAGKSTLLRIMAG----------------VDTEiEGEARPMPGINVGYLPQEPKLDPQATVRdiveeavGQIKQA 100
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGltrpqkgrivlngrvlFDAE-KGICLPPEKRRIGYVFQDARLFPHYKVR-------GNLRYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 101 QARLDevyaayaepDADFDALAaeqaKLEAIlqasdGHNLERQlevaadalrlpPWDakvehLSGGEKRRVALCRLLLSA 180
Cdd:PRK11144 101 MAKSM---------VAQFDKIV----ALLGI-----EPLLDRY-----------PGS-----LSGGEKQRVAIGRALLTA 146
|
170
....*....|....
gi 15599791 181 PDMLLLDEPTNHLD 194
Cdd:PRK11144 147 PELLLMDEPLASLD 160
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-477 |
5.07e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.19 E-value: 5.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 1 MAQYVYTMHRVGKIVPPKREiLKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEarpmpgINVGYLpQEPKL 80
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVHA-LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGT------ITINNI-NYNKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 81 DPqatvRDIVEEAVGQIKQAQARLDE-------------VYAAYAEPDADFDALAAEQAKLEAILqasdghNLERQLeva 147
Cdd:PRK09700 73 DH----KLAAQLGIGIIYQELSVIDEltvlenlyigrhlTKKVCGVNIIDWREMRVRAAMMLLRV------GLKVDL--- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 148 adalrlppwDAKVEHLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPGTVVAITHDRYFLDNvag 227
Cdd:PRK09700 140 ---------DEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAE--- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 228 wILELDRGHGIPFEGNYSGwleskaARLAQEAKQEashakamkaelEWVRQGAkGRQAKSKarlqrfeelqsqeFQKRSE 307
Cdd:PRK09700 208 -IRRICDRYTVMKDGSSVC------SGMVSDVSND-----------DIVRLMV-GRELQNR-------------FNAMKE 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 308 TneiyipAGPRLGDKVIELHNVTKgyGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETV 386
Cdd:PRK09700 256 N------VSNLAHETVFEVRNVTS--RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLnGKDI 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 387 QIAS-----------VDQSR--DSLEGNKTVWEQVSDGfEQIKIGNYevpsRSYVGRFN----FKGADQQK--------- 440
Cdd:PRK09700 328 SPRSpldavkkgmayITESRrdNGFFPNFSIAQNMAIS-RSLKDGGY----KGAMGLFHevdeQRTAENQRellalkchs 402
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15599791 441 ---FVKDLSGGERGRLHLALTLKQGGNVLLLDEPSNDLDV 477
Cdd:PRK09700 403 vnqNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDV 442
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
19-198 |
5.15e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 62.99 E-value: 5.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEG--------------EARPMPGInvGYLPQEPKLDPQA 84
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGniiiddedisllplHARARRGI--GYLPQEASIFRRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 85 TVRDIVeEAVGQIKqaqarldevyaayaepdadfDALAAEQAKLEAIlqasdghnlERQLEVAADALRlppwDAKVEHLS 164
Cdd:PRK10895 94 SVYDNL-MAVLQIR--------------------DDLSAEQREDRAN---------ELMEEFHIEHLR----DSMGQSLS 139
|
170 180 190
....*....|....*....|....*....|....
gi 15599791 165 GGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSV 198
Cdd:PRK10895 140 GGERRRVEIARALAANPKFILLDEPFAGVDPISV 173
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
18-201 |
5.24e-11 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 61.88 E-value: 5.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTE--IEGE----ARPMPG---INVGYLPQEPKLDPQATVRd 88
Cdd:cd03232 19 KRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEilinGRPLDKnfqRSTGYVEQQDVHSPNLTVR- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 89 iveeavgqikqaqarldevyaayaepdadfdalaaeqaklEAILqasdghnlerqlevaadalrlppWDAKVEHLSGGEK 168
Cdd:cd03232 98 ----------------------------------------EALR-----------------------FSALLRGLSVEQR 114
|
170 180 190
....*....|....*....|....*....|...
gi 15599791 169 RRVALCRLLLSAPDMLLLDEPTNHLDADSvAWL 201
Cdd:cd03232 115 KRLTIGVELAAKPSILFLDEPTSGLDSQA-AYN 146
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-477 |
5.36e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.07 E-value: 5.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDT------EIEGEAR----PMPGINVG-YL-PQEPKLDPQATVR 87
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPpdsgtlEIGGNPCarltPAKAHQLGiYLvPQEPLLFPNLSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 88 DIVeeAVGQIKQAQArldevyaayaepdadfdalaaeQAKLEAILQASDGH-NLERQ---LEVAadalrlppwdakvehl 163
Cdd:PRK15439 105 ENI--LFGLPKRQAS----------------------MQKMKQLLAALGCQlDLDSSagsLEVA---------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 164 sggEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLehF-----LHDFPGTVVAITHDRYFLDNVAGWILELDRGHgI 238
Cdd:PRK15439 145 ---DRQIVEILRGLMRDSRILILDEPTASLTPAETERL--FsrireLLAQGVGIVFISHKLPEIRQLADRISVMRDGT-I 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 239 PFEGnysgwleskaarlaqeAKQEASHAKAMKAelewVRQGAKGRQAKSKARLqrFEELQSQEFQKRSetneiyipagpr 318
Cdd:PRK15439 219 ALSG----------------KTADLSTDDIIQA----ITPAAREKSLSASQKL--WLELPGNRRQQAA------------ 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 319 lGDKVIELHNVTkGYGDRvlidNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTI-----EIGETVQIASVDQ 393
Cdd:PRK15439 265 -GAPVLTVEDLT-GEGFR----NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRImlngkEINALSTAQRLAR 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 394 SRDSLEGNKTV----------WEQVSDGFEQIKIGNYEVPSRSYVGRF----NFKGADQQKFVKDLSGGERGRLHLALTL 459
Cdd:PRK15439 339 GLVYLPEDRQSsglyldaplaWNVCALTHNRRGFWIKPARENAVLERYrralNIKFNHAEQAARTLSGGNQQKVLIAKCL 418
|
490
....*....|....*...
gi 15599791 460 KQGGNVLLLDEPSNDLDV 477
Cdd:PRK15439 419 EASPQLLIVDEPTRGVDV 436
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
334-508 |
5.37e-11 |
|
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: 63.43 E-value: 5.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 334 GDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIgETVQIASVDQS------RDS---------L 398
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLI-DGQDIAAMSRKelrelrRKKismvfqsfaL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 399 EGNKTVWEQVSDGFEQIKIGNYEVPSRS-----YVGRfnfkGADQQKFVKDLSGGERGRLHLALTLKQGGNVLLLDEPSN 473
Cdd:cd03294 114 LPHRTVLENVAFGLEVQGVPRAEREERAaealeLVGL----EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15599791 474 DLDVETLRALEEALLDFP---GAAIV-ISHDrwfL-------DRIA 508
Cdd:cd03294 190 ALDPLIRREMQDELLRLQaelQKTIVfITHD---LdealrlgDRIA 232
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
323-500 |
5.92e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 63.17 E-value: 5.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 323 VIELHNVTKGYGD-RVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQ------------I 388
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIkGEPIKydkksllevrktV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 389 ASVDQSRDSLEGNKTVWEQVSDGFEQIKIGNYEVPSRSY-----VGRFNFkgadQQKFVKDLSGGERGRLHLALTLKQGG 463
Cdd:PRK13639 81 GIVFQNPDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKealkaVGMEGF----ENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15599791 464 NVLLLDEPSNDLD----VETLRALEEalLDFPGAAIVIS-HD 500
Cdd:PRK13639 157 EIIVLDEPTSGLDpmgaSQIMKLLYD--LNKEGITIIIStHD 196
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
323-511 |
6.14e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.20 E-value: 6.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 323 VIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQIASVDQS------R 395
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLdGGDIDDPDVAEAchylghR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 396 DSLEGNKTVWEQVSdgFEQIKIGNYEVPSRSYVGRFNFKGADQQKFvKDLSGGERGRLHLALTLKQGGNVLLLDEPSNDL 475
Cdd:PRK13539 82 NAMKPALTVAENLE--FWAAFLGGEELDIAAALEAVGLAPLAHLPF-GYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 15599791 476 DVETLRALEEALLD-FPGAAIVIshdrwfldrIATHI 511
Cdd:PRK13539 159 DAAAVALFAELIRAhLAQGGIVI---------AATHI 186
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
21-241 |
6.35e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 63.72 E-value: 6.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLrimagvdTEIEGEARPMPG-INVGYLPQEPKLDPQATVRDIVEEAVGQIKQ 99
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLV-------THFNGLIKSKYGtIQVGDIYIGDKKNNHELITNPYSKKIKNFKE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 100 AQARLDEVYA--AYA------EPDADFDALAAEQAKLEAILQASdgHNLERqLEVAADALRLPPWDakvehLSGGEKRRV 171
Cdd:PRK13631 114 LRRRVSMVFQfpEYQlfkdtiEKDIMFGPVALGVKKSEAKKLAK--FYLNK-MGLDDSYLERSPFG-----LSGGQKRRV 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599791 172 ALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPG---TVVAITHDRYFLDNVAGWILELDRG----HGIPFE 241
Cdd:PRK13631 186 AIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAnnkTVFVITHTMEHVLEVADEVIVMDKGkilkTGTPYE 262
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
18-220 |
6.44e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 62.72 E-value: 6.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLL----RIMAGVDTEIEGEARPMPGIN-------VGYLPQEPkLDPQA-T 85
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLkcfaRLLTPQSGTVFLGDKPISMLSsrqlarrLALLPQHH-LTPEGiT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 86 VRDIVEEAVGQIKQAQARLDEvyaayaepdadfdalaAEQAKLEAILQasdghnlerQLEVAADAlrlppwDAKVEHLSG 165
Cdd:PRK11231 93 VRELVAYGRSPWLSLWGRLSA----------------EDNARVNQAME---------QTRINHLA------DRRLTDLSG 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599791 166 GEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHF---LHDFPGTVVAITHD-----RY 220
Cdd:PRK11231 142 GQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLmreLNTQGKTVVTVLHDlnqasRY 204
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-226 |
7.27e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 63.11 E-value: 7.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdteiegeARPMPG-INVGYLPqepkLDPQaTVRDIvEEAVGQ 96
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGL-------LLPEAGtITVGGMV----LSEE-TVWDV-RRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 97 IKQaqarldevyaayaEPDADF-------D-ALAAEQAKLEAILQASDGHNLERQLEVAADALRLPpwdakvEHLSGGEK 168
Cdd:PRK13635 86 VFQ-------------NPDNQFvgatvqdDvAFGLENIGVPREEMVERVDQALRQVGMEDFLNREP------HRLSGGQK 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599791 169 RRVALCRLLLSAPDMLLLDEPTNHLD----ADSVAWLEHFLHDFPGTVVAITHDryfLDNVA 226
Cdd:PRK13635 147 QRVAIAGVLALQPDIIILDEATSMLDprgrREVLETVRQLKEQKGITVLSITHD---LDEAA 205
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-477 |
7.28e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.55 E-value: 7.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGE----ARPM----------PGINVGYlpQEPKLDPQATVR 87
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSilidGQEMrfasttaalaAGVAIIY--QELHLVPEMTVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 88 DIVeeAVGQIKQAQARLDEvyaayaepdadfdalaaEQAKLEAILQasdghnLERQlevaadALRLPPwDAKVEHLSGGE 167
Cdd:PRK11288 98 ENL--YLGQLPHKGGIVNR-----------------RLLNYEAREQ------LEHL------GVDIDP-DTPLKYLSIGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 168 KRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDF--PGTVVA-ITHDryfLDNvagwILELdrghgipfegny 244
Cdd:PRK11288 146 RQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELraEGRVILyVSHR---MEE----IFAL------------ 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 245 sgwleSKAARLAQEAKQEASHAKAMKAELEWVRQGAKGRqakskarlqrfeelqsqefqkrsETNEIYipaG--PR-LGD 321
Cdd:PRK11288 207 -----CDAITVFKDGRYVATFDDMAQVDRDQLVQAMVGR-----------------------EIGDIY---GyrPRpLGE 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 322 KVIELHNVtKGYGDRVLIdnlSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQIASV--------- 391
Cdd:PRK11288 256 VRLRLDGL-KGPGLREPI---SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLdGKPIDIRSPrdairagim 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 392 ----DQSRDSLEGNKTVWEQV--------SDGFEQIKIGNYEVPSRSYVGRFNFKGADQQKFVKDLSGGERGRLHLALTL 459
Cdd:PRK11288 332 lcpeDRKAEGIIPVHSVADNInisarrhhLRAGCLINNRWEAENADRFIRSLNIKTPSREQLIMNLSGGNQQKAILGRWL 411
|
490
....*....|....*...
gi 15599791 460 KQGGNVLLLDEPSNDLDV 477
Cdd:PRK11288 412 SEDMKVILLDEPTRGIDV 429
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
26-194 |
7.47e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 62.29 E-value: 7.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 26 SLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpMPGIN----------VGYLPQEPKLDPQATVrdivEEAVG 95
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLT-LNGQDhtttppsrrpVSMLFQENNLFSHLTV----AQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 96 QIKQAQARLDevyaayaepdadfdalAAEQAKLEAILQASdghNLERQLEvaadalRLPpwdakvEHLSGGEKRRVALCR 175
Cdd:PRK10771 94 LGLNPGLKLN----------------AAQREKLHAIARQM---GIEDLLA------RLP------GQLSGGQRQRVALAR 142
|
170
....*....|....*....
gi 15599791 176 LLLSAPDMLLLDEPTNHLD 194
Cdd:PRK10771 143 CLVREQPILLLDEPFSALD 161
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
322-499 |
8.05e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.42 E-value: 8.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 322 KVIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIeigeTVQIASVDQ--SRDSLE 399
Cdd:PRK09700 4 PYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTI----TINNINYNKldHKLAAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 400 -GNKTVWEQVS-----DGFEQIKIGnyEVPSRSYVG------------------RFNFKgADQQKFVKDLSGGERGRLHL 455
Cdd:PRK09700 80 lGIGIIYQELSvidelTVLENLYIG--RHLTKKVCGvniidwremrvraammllRVGLK-VDLDEKVANLSISHKQMLEI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15599791 456 ALTLKQGGNVLLLDEPSNDL---DVETLRALEEALLDfPGAAIV-ISH 499
Cdd:PRK09700 157 AKTLMLDAKVIIMDEPTSSLtnkEVDYLFLIMNQLRK-EGTAIVyISH 203
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
22-236 |
8.74e-11 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 62.71 E-value: 8.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 22 LKDISLSFFPGAKIGVL-GLNGAGKSTLLRIMA----GVDTEIEGEARPMPGINVGylpqepKLDPQATV-------RDI 89
Cdd:COG3950 14 FEDLEIDFDNPPRLTVLvGENGSGKTTLLEAIAlalsGLLSRLDDVKFRKLLIRNG------EFGDSAKLilyygtsRLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 90 VEEAVGQIKQAQARLDEVYAAYAE---PDADFDALAAEQAKLEAILQASDGHNLERQLEVAADALR--LPPWDA------ 158
Cdd:COG3950 88 LDGPLKKLERLKEEYFSRLDGYDSlldEDSNLREFLEWLREYLEDLENKLSDELDEKLEAVREALNklLPDFKDiridrd 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 159 --------------KVEHLSGGEKRRVALC-----RLLLSAPDM---------LLLDEPTNHLdadSVAWLEHFLHD--- 207
Cdd:COG3950 168 pgrlvildkngeelPLNQLSDGERSLLALVgdlarRLAELNPALenplegegiVLIDEIDLHL---HPKWQRRILPDlrk 244
|
250 260 270
....*....|....*....|....*....|..
gi 15599791 208 -FPGT-VVAITHDRYFLDNV-AGWILELDRGH 236
Cdd:COG3950 245 iFPNIqFIVTTHSPLILSSLeDEEVIVLERDE 276
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
321-500 |
8.85e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 62.83 E-value: 8.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 321 DKVIELHNVTKGY--GDRVLiDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETV----------Q 387
Cdd:PRK13647 2 DNIIEVEDLHFRYkdGTKAL-KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVmGREVnaenekwvrsK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 388 IASVDQSRDSLEGNKTVWEQVSDGFEQIKIGNYEVPSR-----SYVGRFNFKgadqQKFVKDLSGGERGRLHLALTLKQG 462
Cdd:PRK13647 81 VGLVFQDPDDQVFSSTVWDDVAFGPVNMGLDKDEVERRveealKAVRMWDFR----DKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15599791 463 GNVLLLDEPSNDLDVETLRALEEAL--LDFPGAAIVIS-HD 500
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILdrLHNQGKTVIVAtHD 197
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
285-396 |
9.91e-11 |
|
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: 64.05 E-value: 9.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 285 AKSKARLQRFEELQSQEFQKRSETNEIYIPAGPRLGDKvIELHNVTKGY----GDRVL-IDNLSLSIPKGAIVGVIGGNG 359
Cdd:COG4615 290 SRANVALRKIEELELALAAAEPAAADAAAPPAPADFQT-LELRGVTYRYpgedGDEGFtLGPIDLTIRRGELVFIVGGNG 368
|
90 100 110
....*....|....*....|....*....|....*...
gi 15599791 360 AGKSTLFRMLTGKEQPDSGTIEI-GETVQIASVDQSRD 396
Cdd:COG4615 369 SGKSTLAKLLTGLYRPESGEILLdGQPVTADNREAYRQ 406
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
346-515 |
1.25e-10 |
|
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: 60.66 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 346 IPKGAIVGVIGGNGAGKSTLFRMLTGKEQPdsgtieigetvqiasvdqsrdslEGNKTVWEQVSDGFEQIKIgnyevpsr 425
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIP-----------------------NGDNDEWDGITPVYKPQYI-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 426 syvgrfnfkgadqqkfvkDLSGGERGRLHLALTLKQGGNVLLLDEPSNDLDVE----TLRALEEALLDFPGAAIVISHDR 501
Cdd:cd03222 71 ------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnAARAIRRLSEEGKKTALVVEHDL 132
|
170
....*....|....
gi 15599791 502 WFLDRIATHILSYE 515
Cdd:cd03222 133 AVLDYLSDRIHVFE 146
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
321-476 |
1.61e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 62.08 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 321 DKVIELHNVTKGY-GDRVL-IDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTI-------------EIGET 385
Cdd:PRK13648 5 NSIIVFKNVSFQYqSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitddnfeKLRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 386 VQIasVDQSRDSLEGNKTVWEQVSDGFEqikigNYEVP----------SRSYVGRFNFKGADQQKfvkdLSGGERGRLHL 455
Cdd:PRK13648 85 IGI--VFQNPDNQFVGSIVKYDVAFGLE-----NHAVPydemhrrvseALKQVDMLERADYEPNA----LSGGQKQRVAI 153
|
170 180
....*....|....*....|.
gi 15599791 456 ALTLKQGGNVLLLDEPSNDLD 476
Cdd:PRK13648 154 AGVLALNPSVIILDEATSMLD 174
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
20-194 |
1.62e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 63.04 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpMPGINVGYLPQEPK----------LDPQATVRDI 89
Cdd:PRK09452 28 EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIM-LDGQDITHVPAENRhvntvfqsyaLFPHMTVFEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 90 VeeAVGqikqaqARLDEVYAAYAEPDAdFDALAAEQakleailqasdghnlerqLEVAADAlrlppwdaKVEHLSGGEKR 169
Cdd:PRK09452 107 V--AFG------LRMQKTPAAEITPRV-MEALRMVQ------------------LEEFAQR--------KPHQLSGGQQQ 151
|
170 180
....*....|....*....|....*
gi 15599791 170 RVALCRLLLSAPDMLLLDEPTNHLD 194
Cdd:PRK09452 152 RVAIARAVVNKPKVLLLDESLSALD 176
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
18-235 |
1.72e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 62.12 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-------DTEIEgearpMPGINVGylpqepkldpQATVRDIv 90
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpddnpNSKIT-----VDGITLT----------AKTVWDI- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 91 EEAVGQIKQAQArlDEVYAAYAEPDADF--DALAAEQAKLEAILQasdghnlerqlEVAADALRLPPWDAKVEHLSGGEK 168
Cdd:PRK13640 83 REKVGIVFQNPD--NQFVGATVGDDVAFglENRAVPRPEMIKIVR-----------DVLADVGMLDYIDSEPANLSGGQK 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599791 169 RRVALCRLLLSAPDMLLLDEPTNHLDADS----VAWLEHFLHDFPGTVVAITHDryfLD--NVAGWILELDRG 235
Cdd:PRK13640 150 QRVAIAGILAVEPKIIILDESTSMLDPAGkeqiLKLIRKLKKKNNLTVISITHD---IDeaNMADQVLVLDDG 219
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
341-523 |
1.83e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 61.82 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 341 NLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQ-------IASVDQSRDSLEGNKTVWEQVsdgf 412
Cdd:PRK15056 25 DASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISIlGQPTRqalqknlVAYVPQSEEVDWSFPVLVEDV---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 413 eqIKIGNYevpsrSYVGRFNFKGADQQKFVKD-----------------LSGGERGRLHLALTLKQGGNVLLLDEPSNDL 475
Cdd:PRK15056 101 --VMMGRY-----GHMGWLRRAKKRDRQIVTAalarvdmvefrhrqigeLSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15599791 476 DVETlraleealldfpgAAIVISHDRWFLDRIATHILSYEDDGKVTFF 523
Cdd:PRK15056 174 DVKT-------------EARIISLLRELRDEGKTMLVSTHNLGSVTEF 208
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
324-500 |
1.94e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 61.64 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQIASVDQ----SRDSL 398
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdGKPVEGPGAERgvvfQNEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 399 EGNKTVWEQVSDGFEQIKIGNYE--VPSRSYVGRFNFKGADQqKFVKDLSGGERGRLHLALTLKQGGNVLLLDEPSNDLD 476
Cdd:PRK11248 82 LPWRNVQDNVAFGLQLAGVEKMQrlEIAHQMLKKVGLEGAEK-RYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180
....*....|....*....|....*...
gi 15599791 477 VETLRALEEALL----DFPGAAIVISHD 500
Cdd:PRK11248 161 AFTREQMQTLLLklwqETGKQVLLITHD 188
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
328-500 |
1.95e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 61.06 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 328 NVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIE------------------IGETVQIA 389
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIiddedisllplhararrgIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 390 SVDQsRDSLEGNKTVWEQVSDGF--EQIKIGNYEVPSRSYVGRFnfkgadQQKFVKDLSGGERGRLHLALTLKQGGNVLL 467
Cdd:PRK10895 88 SIFR-RLSVYDNLMAVLQIRDDLsaEQREDRANELMEEFHIEHL------RDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 15599791 468 LDEPSNDLD---VETLRALEEALLDFPGAAIVISHD 500
Cdd:PRK10895 161 LDEPFAGVDpisVIDIKRIIEHLRDSGLGVLITDHN 196
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
21-195 |
2.02e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 62.74 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDtEIE------GEAR----PMPGINVGYLPQEPKLDPQATVRDiv 90
Cdd:PRK11000 18 ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLE-DITsgdlfiGEKRmndvPPAERGVGMVFQSYALYPHLSVAE-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 91 EEAVGqIKQAQARLDEVYAAYAEpdadfdalAAEqakleaILQAsdGHNLERQlevaadalrlpPWDakvehLSGGEKRR 170
Cdd:PRK11000 95 NMSFG-LKLAGAKKEEINQRVNQ--------VAE------VLQL--AHLLDRK-----------PKA-----LSGGQRQR 141
|
170 180
....*....|....*....|....*
gi 15599791 171 VALCRLLLSAPDMLLLDEPTNHLDA 195
Cdd:PRK11000 142 VAIGRTLVAEPSVFLLDEPLSNLDA 166
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
321-476 |
2.72e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 61.35 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 321 DKVIELHNVTKGYGD--RVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDS---------GTIEIGETV--- 386
Cdd:PRK13640 3 DNIVEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnskitvdGITLTAKTVwdi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 387 --QIASVDQSRDSLEGNKTVWEQVSDGFEqikigNYEVPSR----------SYVGRFNFKGADQQkfvkDLSGGERGRLH 454
Cdd:PRK13640 83 reKVGIVFQNPDNQFVGATVGDDVAFGLE-----NRAVPRPemikivrdvlADVGMLDYIDSEPA----NLSGGQKQRVA 153
|
170 180
....*....|....*....|..
gi 15599791 455 LALTLKQGGNVLLLDEPSNDLD 476
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLD 175
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
323-498 |
2.73e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 61.36 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 323 VIELHNVTKGY-GDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQIASVDQSR----- 395
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrGEPITKENIREVRkfvgl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 396 -----DSLEGNKTVWEQVSDGFEQIKIGNYEVPSR-SYVGRFNFKGADQQKFVKDLSGGERGRLHLALTLKQGGNVLLLD 469
Cdd:PRK13652 83 vfqnpDDQIFSPTVEQDIAFGPINLGLDEETVAHRvSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190
....*....|....*....|....*....|..
gi 15599791 470 EPSNDLDVETLRALEEALLDFP---GAAIVIS 498
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLNDLPetyGMTVIFS 194
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
18-236 |
2.83e-10 |
|
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: 59.85 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-DTEI-EGEARpMPGINVGYLPqepkldpqatvrdiVEEavg 95
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpKYEVtEGEIL-FKGEDITDLP--------------PEE--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 96 qikqaQARLDeVYAAYAEPdadfdalaaeqaklEAIlqasDGHNLerqlevaADALRlppwdaKV-EHLSGGEKRRVALC 174
Cdd:cd03217 74 -----RARLG-IFLAFQYP--------------PEI----PGVKN-------ADFLR------YVnEGFSGGEKKRNEIL 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599791 175 RLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDF--PGT-VVAITHDRYFLDNVAGwilelDRGH 236
Cdd:cd03217 117 QLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLreEGKsVLIITHYQRLLDYIKP-----DRVH 176
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
321-484 |
2.97e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 61.29 E-value: 2.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 321 DKVIELHNVTKGYGDRVLIDnLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETV-------------- 386
Cdd:PRK13643 5 EKVNYTYQPNSPFASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVvsstskqkeikpvr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 387 -QIASVDQSRDSLEGNKTVWEQVSDGFEQIKIGNYEVpSRSYVGRFNFKGADQQKFVK---DLSGGERGRLHLALTLKQG 462
Cdd:PRK13643 84 kKVGVVFQFPESQLFEETVLKDVAFGPQNFGIPKEKA-EKIAAEKLEMVGLADEFWEKspfELSGGQMRRVAIAGILAME 162
|
170 180
....*....|....*....|....*.
gi 15599791 463 GNVLLLDEPSNDLD----VETLRALE 484
Cdd:PRK13643 163 PEVLVLDEPTAGLDpkarIEMMQLFE 188
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
314-507 |
3.06e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 62.68 E-value: 3.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 314 PAGPRLGD-KVIELHNVTKGYGDRVL-IDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQIAS 390
Cdd:PRK10522 312 PRPQAFPDwQTLELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLdGKPVTAEQ 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 391 VDQSR-------------DSL---EGNKTVWEQVSDGFEQIKIGNyevpsrsyvgRFNFKgaDQQKFVKDLSGGERGRLH 454
Cdd:PRK10522 392 PEDYRklfsavftdfhlfDQLlgpEGKPANPALVEKWLERLKMAH----------KLELE--DGRISNLKLSKGQKKRLA 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599791 455 LALTLKQGGNVLLLDEPSNDLDVETLRALEEALLdfP-----GAAIV-ISH-DRWFL--DRI 507
Cdd:PRK10522 460 LLLALAEERDILLLDEWAADQDPHFRREFYQVLL--PllqemGKTIFaISHdDHYFIhaDRL 519
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
320-500 |
3.11e-10 |
|
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: 59.37 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 320 GDKVIELHNVTKGygDRVliDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQIASV------- 391
Cdd:cd03215 1 GEPVLEVRGLSVK--GAV--RDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLdGKPVTRRSPrdairag 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 392 ------DQSRDSLEGNKTVWEQVSdgfeqikIGNYevpsrsyvgrfnFKGADQQKFVkdlsggergrlhLALTLKQGGNV 465
Cdd:cd03215 77 iayvpeDRKREGLVLDLSVAENIA-------LSSL------------LSGGNQQKVV------------LARWLARDPRV 125
|
170 180 190
....*....|....*....|....*....|....*...
gi 15599791 466 LLLDEPSNDLDVETLRALEEALLDF--PGAAI-VISHD 500
Cdd:cd03215 126 LILDEPTRGVDVGAKAEIYRLIRELadAGKAVlLISSE 163
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
323-381 |
3.69e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 62.83 E-value: 3.69e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 15599791 323 VIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIE 381
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVE 59
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-217 |
3.75e-10 |
|
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: 60.25 E-value: 3.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 17 PKREILKDISLSFFPGAKIGVLGLNGAGKST----LLRIMAGVDTEIEGEARPMPGINV-------GYLPQEPKLDPqAT 85
Cdd:cd03249 14 PDVPILKGLSLTIPPGKTVALVGSSGCGKSTvvslLERFYDPTSGEILLDGVDIRDLNLrwlrsqiGLVSQEPVLFD-GT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 86 VRDIVeeavgqikqaqarldevyaAYAEPDADfDALAAEQAKLEAIlqasdgHNLERQL------EVAADALRLppwdak 159
Cdd:cd03249 93 IAENI-------------------RYGKPDAT-DEEVEEAAKKANI------HDFIMSLpdgydtLVGERGSQL------ 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 160 vehlSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPG--TVVAITH 217
Cdd:cd03249 141 ----SGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKgrTTIVIAH 196
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
324-499 |
3.91e-10 |
|
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: 59.43 E-value: 3.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETvqiaSVDQSRDSL----- 398
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG----PLDFQRDSIargll 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 399 --------------EGNKTVW------EQVSDGFEQIKIGNYE-VPsrsyvgrfnfkgadqqkfVKDLSGGERGRLHLAL 457
Cdd:cd03231 77 ylghapgikttlsvLENLRFWhadhsdEQVEEALARVGLNGFEdRP------------------VAQLSAGQQRRVALAR 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15599791 458 TLKQGGNVLLLDEPSNDLDVETLRALEEAL---LDFPGAAIVISH 499
Cdd:cd03231 139 LLLSGRPLWILDEPTTALDKAGVARFAEAMaghCARGGMVVLTTH 183
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
323-504 |
4.02e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 60.31 E-value: 4.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 323 VIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFR------------------MLTGKEQPDSGTIEIGE 384
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRvfnrlielypearvsgevYLDGQDIFKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 385 TVQIasVDQSRDSLEgNKTVWEQVSDGFEQIKIGNYEVPSRSYVgRFNFKGADQQKFVKD--------LSGGERGRLHLA 456
Cdd:PRK14247 83 RVQM--VFQIPNPIP-NLSIFENVALGLKLNRLVKSKKELQERV-RWALEKAQLWDEVKDrldapagkLSGGQQQRLCIA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 457 LTLKQGGNVLLLDEPSNDLDVETLRALEEALLD------------FPGAAIVISHDRWFL 504
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFLElkkdmtivlvthFPQQAARISDYVAFL 218
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
19-194 |
4.37e-10 |
|
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: 62.45 E-value: 4.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGE----ARPMPGINVG-------YLPQEPKLDPQATVR 87
Cdd:TIGR01193 487 SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEillnGFSLKDIDRHtlrqfinYLPQEPYIFSGSILE 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 88 DIVEEAVGQIKQaqarlDEVYAA--YAEPDADfdalaaeqakleaILQASDGHnlerQLEVAADAlrlppwdakvEHLSG 165
Cdd:TIGR01193 567 NLLLGAKENVSQ-----DEIWAAceIAEIKDD-------------IENMPLGY----QTELSEEG----------SSISG 614
|
170 180
....*....|....*....|....*....
gi 15599791 166 GEKRRVALCRLLLSAPDMLLLDEPTNHLD 194
Cdd:TIGR01193 615 GQKQRIALARALLTDSKVLILDESTSNLD 643
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
21-217 |
4.63e-10 |
|
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: 59.81 E-value: 4.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 21 ILKDISLSFFPGAKIGVLGLNGAGKST----LLRIMAGVDTEIEGEARPMPGI-------NVGYLPQEPKLDpQATVR-- 87
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLVELSSGSILIDGVDISKIglhdlrsRISIIPQDPVLF-SGTIRsn 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 88 -DIVEEAvgqikqaqarldevyaayaePDAD-FDALaaEQAKLEAILQASDGHNlerqlevaadalrlppwDAKVE---- 161
Cdd:cd03244 98 lDPFGEY--------------------SDEElWQAL--ERVGLKEFVESLPGGL-----------------DTVVEegge 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15599791 162 HLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHD-FPG-TVVAITH 217
Cdd:cd03244 139 NLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREaFKDcTVLTIAH 196
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
320-380 |
6.08e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 60.16 E-value: 6.08e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599791 320 GDKVIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTI 380
Cdd:PRK11831 4 VANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI 64
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-274 |
6.16e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 62.49 E-value: 6.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 17 PKrEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGvDTEIEgEARPMPGINVGYLPQEPKLdPQATVRDIV----EE 92
Cdd:PTZ00243 672 PK-VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLS-QFEIS-EGRVWAERSIAYVPQQAWI-MNATVRGNIlffdEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 93 AvgqikqaQARLDevyaayaepdadfDALAAEQakLEAILqASDGHNLERQLevaadalrlppwDAKVEHLSGGEKRRVA 172
Cdd:PTZ00243 748 D-------AARLA-------------DAVRVSQ--LEADL-AQLGGGLETEI------------GEKGVNLSGGQKARVS 792
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 173 LCRLLLSAPDMLLLDEPTNHLDAdSVAwlEHFLHD-FPG-----TVVAITHDRYFLDNvAGWILELDRGHgIPFEGNYSG 246
Cdd:PTZ00243 793 LARAVYANRDVYLLDDPLSALDA-HVG--ERVVEEcFLGalagkTRVLATHQVHVVPR-ADYVVALGDGR-VEFSGSSAD 867
|
250 260 270
....*....|....*....|....*....|....*
gi 15599791 247 WLESK-----AARLA--QEAKQEASHAKAMKAELE 274
Cdd:PTZ00243 868 FMRTSlyatlAAELKenKDSKEGDADAEVAEVDAA 902
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
324-520 |
6.68e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 59.64 E-value: 6.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-------GETVQIASVDQSRd 396
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfdfSKTPSDKAIRELR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 397 slegnktvwEQVSDGFEQIK-------IGNY-EVPSRsyVGRFNFKGADQQ---------------KFVKDLSGGERGRL 453
Cdd:PRK11124 82 ---------RNVGMVFQQYNlwphltvQQNLiEAPCR--VLGLSKDQALARaekllerlrlkpyadRFPLHLSGGQQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 454 HLALTLKQGGNVLLLDEPSNDLDVETLRALEEALLDFPGAAI---VISHDRWFLDRIATHILsYEDDGKV 520
Cdd:PRK11124 151 AIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGItqvIVTHEVEVARKTASRVV-YMENGHI 219
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
339-506 |
9.61e-10 |
|
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: 57.72 E-value: 9.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 339 IDNLSLSIPKGAIVGVIGGNGAGKSTLfrmltgkeqpdsgTIEIGETVQIASVDQSRDSLEGNKTVW-EQVSDgfeQIKI 417
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL-------------VNEGLYASGKARLISFLPKFSRNKLIFiDQLQF---LIDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 418 G-NYEVPSRSyvgrfnfkgadqqkfVKDLSGGERGRLHLA--LTLKQGGNVLLLDEPSNDLDVETLRALEEA---LLDFP 491
Cdd:cd03238 75 GlGYLTLGQK---------------LSTLSGGELQRVKLAseLFSEPPGTLFILDEPSTGLHQQDINQLLEVikgLIDLG 139
|
170
....*....|....*
gi 15599791 492 GAAIVISHDRWFLDR 506
Cdd:cd03238 140 NTVILIEHNLDVLSS 154
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
336-498 |
9.66e-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: 61.57 E-value: 9.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 336 RVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETVQIASVDQSRDSLE---------GNKTVWE 406
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGmcpqhnilfHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 407 QVSdGFEQIKIGNYEVPSRSYVGRFNFKGADQQKF--VKDLSGGERGRLHLALTLKQGGNVLLLDEPSNDLDVETLRALE 484
Cdd:TIGR01257 1023 HIL-FYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNeeAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101
|
170
....*....|....*
gi 15599791 485 EALLDF-PGAAIVIS 498
Cdd:TIGR01257 1102 DLLLKYrSGRTIIMS 1116
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
323-499 |
1.14e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.79 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 323 VIELHNVTKGY-GDRVLiDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIE-IGETVQIASvdqSRDSLEG 400
Cdd:PRK10762 4 LLQLKGIDKAFpGVKAL-SGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILyLGKEVTFNG---PKSSQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 401 NKTVWEQVSDGFEQIKIGNYEVPSRSYVGRFN-------FKGADQ-----------QKFVKDLSGGERGRLHLALTLKQG 462
Cdd:PRK10762 80 GIGIIHQELNLIPQLTIAENIFLGREFVNRFGridwkkmYAEADKllarlnlrfssDKLVGELSIGEQQMVEIAKVLSFE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15599791 463 GNVLLLDEPSNDL-DVETlraleEAL------LDFPGAAIV-ISH 499
Cdd:PRK10762 160 SKVIIMDEPTDALtDTET-----ESLfrvireLKSQGRGIVyISH 199
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-217 |
1.28e-09 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 58.65 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 16 PPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpMPGINVGYLpqepklDPQATVRDiveeaVG 95
Cdd:cd03252 12 PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVL-VDGHDLALA------DPAWLRRQ-----VG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 96 QIKQAQARLDEVYAayaepdaDFDALAAEQAKLEAILQAS---DGHNLERQLEVAADALRlppwDAKVEHLSGGEKRRVA 172
Cdd:cd03252 80 VVLQENVLFNRSIR-------DNIALADPGMSMERVIEAAklaGAHDFISELPEGYDTIV----GEQGAGLSGGQRQRIA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15599791 173 LCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPG--TVVAITH 217
Cdd:cd03252 149 IARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAgrTVIIIAH 195
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
22-242 |
1.74e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 58.85 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLrimagvdTEIEGEARPMPGinvgylpqepkldpQATVRDIveeAVGQIKQAQ 101
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLA-------LHLNGLLRPQKG--------------KVLVSGI---DTGDFSKLQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 102 ARLDEVYAAYAEPDADFDalaaeqakleailqasdGHNLERQLEVAADALRLPPWD--------------AKVEH----- 162
Cdd:PRK13644 74 GIRKLVGIVFQNPETQFV-----------------GRTVEEDLAFGPENLCLPPIEirkrvdralaeiglEKYRHrspkt 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 163 LSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADS-VAWLEHF--LHDFPGTVVAITHDRYFLdNVAGWILELDRGHgIP 239
Cdd:PRK13644 137 LSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSgIAVLERIkkLHEKGKTIVYITHNLEEL-HDADRIIVMDRGK-IV 214
|
...
gi 15599791 240 FEG 242
Cdd:PRK13644 215 LEG 217
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
339-517 |
1.82e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 59.07 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 339 IDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQIASVDQSRDSLEGNKTVWEQVSDG--FEQI 415
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIaGYHITPETGNKNLKKLRKKVSLVFQFPEAqlFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 416 KIGNYEvpsrsyVGRFNFKGADQQ------KFVK--------------DLSGGERGRLHLALTLKQGGNVLLLDEPSNDL 475
Cdd:PRK13641 103 VLKDVE------FGPKNFGFSEDEakekalKWLKkvglsedliskspfELSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15599791 476 DVETLRALEEALLDFPGAA---IVISHDrwfLDRIAthilSYEDD 517
Cdd:PRK13641 177 DPEGRKEMMQLFKDYQKAGhtvILVTHN---MDDVA----EYADD 214
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
331-489 |
1.95e-09 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 58.72 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 331 KGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQIASVDQS----RDSLEGNKTVW 405
Cdd:COG4525 15 GGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLdGVPVTGPGADRGvvfqKDALLPWLNVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 406 EQVSDGFEQIKIGNYEVPSRS--YVGRFNFKGAdQQKFVKDLSGGERGRLHLALTLKQGGNVLLLDEPSNDLDVETLRAL 483
Cdd:COG4525 95 DNVAFGLRLRGVPKAERRARAeeLLALVGLADF-ARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQM 173
|
....*.
gi 15599791 484 EEALLD 489
Cdd:COG4525 174 QELLLD 179
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
324-544 |
2.09e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 58.91 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYG-----DRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGEtVQIAS-------- 390
Cdd:PRK13637 3 IKIENLTHIYMegtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDG-VDITDkkvklsdi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 391 ------VDQSRDSLEGNKTVWEQVSDGFEQIKIGNYEVPSRSY-----VGRFNFKGADQQKFvkDLSGGERGRLHLALTL 459
Cdd:PRK13637 82 rkkvglVFQYPEYQLFEETIEKDIAFGPINLGLSEEEIENRVKramniVGLDYEDYKDKSPF--ELSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 460 KQGGNVLLLDEPSNDLD-------VETLRALEEallDFPGAAIVISHDRWFLDRIATHILSYeDDGKVTfFEGNYTEF-- 530
Cdd:PRK13637 160 AMEPKILILDEPTAGLDpkgrdeiLNKIKELHK---EYNMTIILVSHSMEDVAKLADRIIVM-NKGKCE-LQGTPREVfk 234
|
250
....*....|....
gi 15599791 531 EADRKKRLGDAASQ 544
Cdd:PRK13637 235 EVETLESIGLAVPQ 248
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-218 |
2.13e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 58.95 E-value: 2.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 16 PPKREI--LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpmpgINvGYLPQEpklDPQATVRDIveeA 93
Cdd:COG4586 30 REYREVeaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR----VL-GYVPFK---RRKEFARRI---G 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 94 V--GQiKQaQARLD-------EVYAA-YAEPDADFDALAAEqakLEAILqasdghNLERQLEVAadalrlppwdakVEHL 163
Cdd:COG4586 99 VvfGQ-RS-QLWWDlpaidsfRLLKAiYRIPDAEYKKRLDE---LVELL------DLGELLDTP------------VRQL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15599791 164 SGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHD----FPGTVVAITHD 218
Cdd:COG4586 156 SLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEynreRGTTILLTSHD 214
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
324-520 |
2.17e-09 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 57.89 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGY---GDRVLiDNLSLSIPKGAIVGVIGGNGAGKST----LFRMLtgkeQPDSGTIEIGEtVQIASVD--QS 394
Cdd:cd03244 3 IEFKNVSLRYrpnLPPVL-KNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILIDG-VDISKIGlhDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 395 RDSL----------EGnkTV------WEQVSDgfEQIKIGNYEVPSRSYVGRFNFKGADQQKFVKD-LSGGERGRLHLAL 457
Cdd:cd03244 77 RSRIsiipqdpvlfSG--TIrsnldpFGEYSD--EELWQALERVGLKEFVESLPGGLDTVVEEGGEnLSVGQRQLLCLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 458 TLKQGGNVLLLDEPSNDLDVETLRALEEALLD-FPGAA-IVISHdrwfldRIAThILSYE-----DDGKV 520
Cdd:cd03244 153 ALLRKSKILVLDEATASVDPETDALIQKTIREaFKDCTvLTIAH------RLDT-IIDSDrilvlDKGRV 215
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
327-500 |
2.30e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 58.40 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 327 HNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI----GETVQIASVDQSRDSLEGnK 402
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrdGQLRDLYALSEAERRRLL-R 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 403 TVW------------EQVSDGfeqikiGN-----YEVPSRSYvGRFNFKGAD-------QQKFVKDL----SGGERGRLH 454
Cdd:PRK11701 89 TEWgfvhqhprdglrMQVSAG------GNigerlMAVGARHY-GDIRATAGDwlerveiDAARIDDLpttfSGGMQQRLQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15599791 455 LALTLKQGGNVLLLDEPSNDLDV-------ETLRALeeaLLDFPGAAIVISHD 500
Cdd:PRK11701 162 IARNLVTHPRLVFMDEPTGGLDVsvqarllDLLRGL---VRELGLAVVIVTHD 211
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
323-383 |
2.46e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.68 E-value: 2.46e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599791 323 VIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIG 383
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIG 71
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
344-511 |
2.47e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 58.15 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 344 LSIPK-GAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIE------------------------IGETVQIASVDQSRDSL 398
Cdd:cd03236 20 LPVPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdwdeildefrgselqnyftklLEGDVKVIVKPQYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 399 EgnKTVWEQVSDGFEQI-KIGNYEvpsrSYVGRFNFKGADQQKfVKDLSGGERGRLHLALTLKQGGNVLLLDEPSNDLDV 477
Cdd:cd03236 100 P--KAVKGKVGELLKKKdERGKLD----ELVDQLELRHVLDRN-IDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 15599791 478 E---TLRALEEALLDFPGAAIVISHDRWFLDRIATHI 511
Cdd:cd03236 173 KqrlNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
22-261 |
2.76e-09 |
|
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: 58.23 E-value: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEarpmpgINVG--YLPQEPKLDpqatVRDIVEEaVG---Q 96
Cdd:TIGR04521 21 LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGT------VTIDgrDITAKKKKK----LKDLRKK-VGlvfQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 97 IKQAQARLDEVYA--AYA-----EPDADFDALAAEQAKL----EAILQASdghnlerqlevaadalrlpPWDakvehLSG 165
Cdd:TIGR04521 90 FPEHQLFEETVYKdiAFGpknlgLSEEEAEERVKEALELvgldEEYLERS-------------------PFE-----LSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 166 GEKRRVALCRLLLSAPDMLLLDEPTNHLDADS-VAWLEHF--LHDFPG-TVVAITHDryfLDNVAGW---ILELDRG--- 235
Cdd:TIGR04521 146 GQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGrKEILDLFkrLHKEKGlTVILVTHS---MEDVAEYadrVIVMHKGkiv 222
|
250 260 270
....*....|....*....|....*....|....
gi 15599791 236 -HGIPFE-GNYSGWLES------KAARLAQEAKQ 261
Cdd:TIGR04521 223 lDGTPREvFSDVDELEKigldvpEITELARKLKE 256
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
321-487 |
3.19e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 57.87 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 321 DKVIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFR------------------MLTGKEQPDSGTIEI 382
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndlipgfrvegkvTFHGKNLYAPDVDPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 383 GETVQIASVDQSRDSLEgnKTVWEQVSDGfeqIKIGNYEVPSRSYVGRfNFKGADQQKFVKD--------LSGGERGRLH 454
Cdd:PRK14243 88 EVRRRIGMVFQKPNPFP--KSIYDNIAYG---ARINGYKGDMDELVER-SLRQAALWDEVKDklkqsglsLSGGQQQRLC 161
|
170 180 190
....*....|....*....|....*....|....
gi 15599791 455 LALTLKQGGNVLLLDEPSNDLD-VETLRaLEEAL 487
Cdd:PRK14243 162 IARAIAVQPEVILMDEPCSALDpISTLR-IEELM 194
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
339-470 |
3.21e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 59.52 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 339 IDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETVQIASVDQsrdSLEGNKTVWEQVS-DGF----- 412
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISS---GLNGQLTGIENIElKGLmmglt 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 15599791 413 -EQIKIGNYEVPSRSYVGRFNFKGadqqkfVKDLSGGERGRLHLALTLKQGGNVLLLDE 470
Cdd:PRK13545 117 kEKIKEIIPEIIEFADIGKFIYQP------VKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
321-499 |
3.38e-09 |
|
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: 57.48 E-value: 3.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 321 DKVIELHNVTKGY---GDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETV----------- 386
Cdd:cd03248 9 KGIVKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPisqyehkylhs 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 387 QIASVDQSRDSLEGnkTVWEQVSDG-----FEQIKIGNYEVPSRSYVGRFNfKGADQQKFVK--DLSGGERGRLHLALTL 459
Cdd:cd03248 89 KVSLVGQEPVLFAR--SLQDNIAYGlqscsFECVKEAAQKAHAHSFISELA-SGYDTEVGEKgsQLSGGQKQRVAIARAL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15599791 460 KQGGNVLLLDEPSNDLDVETLRALEEALLDFPG--AAIVISH 499
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPErrTVLVIAH 207
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
288-522 |
3.77e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 59.44 E-value: 3.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 288 KARLQRFEELQS--QEFQKRSETNE-IYIPAGPRLgdkviELHNVT-KGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKS 363
Cdd:COG4178 329 RATVDRLAGFEEalEAADALPEAASrIETSEDGAL-----ALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKS 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 364 TLFRMLTGKEQPDSGTIEIGETVQIASVDQS--------RDSLEGNKTVwEQVSDgfEQIKignyEVPSR----SYVGRF 431
Cdd:COG4178 404 TLLRAIAGLWPYGSGRIARPAGARVLFLPQRpylplgtlREALLYPATA-EAFSD--AELR----EALEAvglgHLAERL 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 432 NfkgaDQQKFVKDLSGGERGRLHLALTLKQGGNVLLLDEPSNDLDVETLRALEEALLD-FPGAAIV-ISHdRWFLDRIAT 509
Cdd:COG4178 477 D----EEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREeLPGTTVIsVGH-RSTLAAFHD 551
|
250
....*....|...
gi 15599791 510 HILSYEDDGKVTF 522
Cdd:COG4178 552 RVLELTGDGSWQL 564
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
17-217 |
3.85e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 59.35 E-value: 3.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 17 PKREILKDISLSFFPGAKIGVLGLNGAGKST----LLRIMAGVDTEIEGEARPMPGINVGYLPQEpkldpqatVRdivee 92
Cdd:TIGR00958 492 PDVPVLKGLTFTLHPGEVVALVGPSGSGKSTvaalLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQ--------VA----- 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 93 AVGQIKQAQARLDEVYAAYAEPDAdfdalaaEQAKLEAILQASDGHNLERQLEVAADAlrlpPWDAKVEHLSGGEKRRVA 172
Cdd:TIGR00958 559 LVGQEPVLFSGSVRENIAYGLTDT-------PDEEIMAAAKAANAHDFIMEFPNGYDT----EVGEKGSQLSGGQKQRIA 627
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15599791 173 LCRLLLSAPDMLLLDEPTNHLDADSvawlEHFLHDFPG----TVVAITH 217
Cdd:TIGR00958 628 IARALVRKPRVLILDEATSALDAEC----EQLLQESRSrasrTVLLIAH 672
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
328-521 |
4.25e-09 |
|
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: 58.58 E-value: 4.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 328 NVTKGYGDRVLidNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQiasvdqsrDSLEGNKTVWE 406
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLnGRTLF--------DSRKGIFLPPE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 407 QVSDG--FEQIKI-GNYEVPSRSYVGRFNFKGADQQ-----------------KFVKDLSGGERGRLHLALTLKQGGNVL 466
Cdd:TIGR02142 74 KRRIGyvFQEARLfPHLSVRGNLRYGMKRARPSERRisferviellgighllgRLPGRLSGGEKQRVAIGRALLSSPRLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15599791 467 LLDEPSNDLDV----ETLRALEEALLDFPGAAIVISHDRWFLDRIATHILSYEdDGKVT 521
Cdd:TIGR02142 154 LMDEPLAALDDprkyEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLE-DGRVA 211
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-235 |
4.42e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 59.09 E-value: 4.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdteiegearpMP--------GI------------NVGYLPQEPKL 80
Cdd:PRK11174 365 LAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF----------LPyqgslkinGIelreldpeswrkHLSWVGQNPQL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 81 dPQATVRDIVeeavgqikqaqarldevyaAYAEPDADFDAL--AAEQAKL-EAILQASDGHNLErqleVAADALRLppwd 157
Cdd:PRK11174 435 -PHGTLRDNV-------------------LLGNPDASDEQLqqALENAWVsEFLPLLPQGLDTP----IGDQAAGL---- 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 158 akvehlSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADS---------VAWLEHflhdfpgTVVAITHDryfLDNVAGW 228
Cdd:PRK11174 487 ------SVGQAQRLALARALLQPCQLLLLDEPTASLDAHSeqlvmqalnAASRRQ-------TTLMVTHQ---LEDLAQW 550
|
....*....
gi 15599791 229 --ILELDRG 235
Cdd:PRK11174 551 dqIWVMQDG 559
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-229 |
4.49e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 57.54 E-value: 4.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLR-----IMAGVDTEIEGEARpMPGINVgylpQEPKLDPQAtvrdiVEEAV 94
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrlLELNEEARVEGEVR-LFGRNI----YSPDVDPIE-----VRREV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 95 GQIKQaqarldevyaaYAEPdadFDALA-----AEQAKLEAILQASDghNLERQLEVAADALRLppWDA-------KVEH 162
Cdd:PRK14267 88 GMVFQ-----------YPNP---FPHLTiydnvAIGVKLNGLVKSKK--ELDERVEWALKKAAL--WDEvkdrlndYPSN 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599791 163 LSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPG--TVVAITHDRYFLDNVAGWI 229
Cdd:PRK14267 150 LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKeyTIVLVTHSPAQAARVSDYV 218
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
25-218 |
4.50e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 57.25 E-value: 4.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 25 ISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdTEIEGEArpmpginvgYLPQEPKLDPQATvrdiveeavgqiKQAQARl 104
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSI---------QFAGQPLEAWSAA------------ELARHR- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 105 devyaAYaepdadfdaLAAEQAKLEAI-------LQASDGHNL---ERQLEVAADALRLppwDAK----VEHLSGGEKRR 170
Cdd:PRK03695 72 -----AY---------LSQQQTPPFAMpvfqyltLHQPDKTRTeavASALNEVAEALGL---DDKlgrsVNQLSGGEWQR 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15599791 171 VALCRLLLS-APD------MLLLDEPTNHLDADSVAWLEHFLHDFP---GTVVAITHD 218
Cdd:PRK03695 135 VRLAAVVLQvWPDinpagqLLLLDEPMNSLDVAQQAALDRLLSELCqqgIAVVMSSHD 192
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
17-218 |
4.71e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 57.40 E-value: 4.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 17 PKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDT------EIEGEARPMPGINVGYLPQEPKLDPQATVRDIV 90
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPyqhgsiTLDGKPVEGPGAERGVVFQNEGLLPWRNVQDNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 91 eeavgqikqaqarldevyaayaepdadfdALAAEQAkleailqasdGHNLERQLEVAADALRL---------PPWdakve 161
Cdd:PRK11248 92 -----------------------------AFGLQLA----------GVEKMQRLEIAHQMLKKvglegaekrYIW----- 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599791 162 HLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFL----HDFPGTVVAITHD 218
Cdd:PRK11248 128 QLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLlklwQETGKQVLLITHD 188
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
323-472 |
4.83e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 57.20 E-value: 4.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 323 VIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIG-------ETVQI-----AS 390
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDgkditdwQTAKImreavAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 391 VDQSRDSLeGNKTVWEQVSDG--------FEQIKIGNYEVPSRSYVGRFNFKGAdqqkfvkdLSGGERGRLHLALTLKQG 462
Cdd:PRK11614 85 VPEGRRVF-SRMTVEENLAMGgffaerdqFQERIKWVYELFPRLHERRIQRAGT--------MSGGEQQMLAIGRALMSQ 155
|
170
....*....|
gi 15599791 463 GNVLLLDEPS 472
Cdd:PRK11614 156 PRLLLLDEPS 165
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
324-499 |
5.37e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 58.88 E-value: 5.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGY--GDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETV----------QIAS 390
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLdGHDLrdytlaslrnQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 391 VDQ---------------------SRDSLEGNKTVW------EQVSDGFEQIkIGNyevpsrsyvgrfnfKGADqqkfvk 443
Cdd:PRK11176 422 VSQnvhlfndtianniayarteqySREQIEEAARMAyamdfiNKMDNGLDTV-IGE--------------NGVL------ 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15599791 444 dLSGGERGRLHLALTLKQGGNVLLLDEPSNDLDVETLRALEEAL--LDFPGAAIVISH 499
Cdd:PRK11176 481 -LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALdeLQKNRTSLVIAH 537
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
19-219 |
5.67e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 56.65 E-value: 5.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEG----EARPMPGIN-------VGYLPQEPKLDPQaTVR 87
Cdd:PRK10247 20 AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGtllfEGEDISTLKpeiyrqqVSYCAQTPTLFGD-TVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 88 DIVeeavgqIKQAQARLDEVyaayaEPDADFDALAaeQAKL-EAILQASdghnlerqlevaadalrlppwdakVEHLSGG 166
Cdd:PRK10247 99 DNL------IFPWQIRNQQP-----DPAIFLDDLE--RFALpDTILTKN------------------------IAELSGG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15599791 167 EKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPG----TVVAITHDR 219
Cdd:PRK10247 142 EKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVReqniAVLWVTHDK 198
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
287-530 |
5.99e-09 |
|
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: 59.19 E-value: 5.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 287 SKARLQRF---EELQSQEFQKRSetneiyIPAGprlGDKVIELHNVTKGY--GDRVLIDNLSLSIPKGAIVGVIGGNGAG 361
Cdd:TIGR00957 606 SLKRLRIFlshEELEPDSIERRT------IKPG---EGNSITVHNATFTWarDLPPTLNGITFSIPEGALVAVVGQVGCG 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 362 KSTLFRMLTGKEQPDSGTIEIGETVqiASVDQ----SRDSLEGNKTVWEQVSDGFEQIKI------GNYEV-PS--RSYV 428
Cdd:TIGR00957 677 KSSLLSALLAEMDKVEGHVHMKGSV--AYVPQqawiQNDSLRENILFGKALNEKYYQQVLeacallPDLEIlPSgdRTEI 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 429 GRfnfKGAdqqkfvkDLSGGERGRLHLALTLKQGGNVLLLDEPSNDLDVETLRALEEALLDFPG-----AAIVISHDRWF 503
Cdd:TIGR00957 755 GE---KGV-------NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGvlknkTRILVTHGISY 824
|
250 260
....*....|....*....|....*..
gi 15599791 504 LDRIATHILSyeDDGKVTFFeGNYTEF 530
Cdd:TIGR00957 825 LPQVDVIIVM--SGGKISEM-GSYQEL 848
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
321-509 |
6.15e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 57.41 E-value: 6.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 321 DKVIELHNVTKGY---GDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETV---------- 386
Cdd:PRK13642 2 NKILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIdGELLtaenvwnlrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 387 QIASVDQSRDSLEGNKTVWEQVSDGFEQIKIGNYEVPSRS-----YVGRFNFKGADQQKfvkdLSGGERGRLHLALTLKQ 461
Cdd:PRK13642 82 KIGMVFQNPDNQFVGATVEDDVAFGMENQGIPREEMIKRVdeallAVNMLDFKTREPAR----LSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15599791 462 GGNVLLLDEPSNDLD----VETLRALEEALLDFPGAAIVISHDrwfLDRIAT 509
Cdd:PRK13642 158 RPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHD---LDEAAS 206
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
2-218 |
6.38e-09 |
|
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: 57.27 E-value: 6.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 2 AQYVYTMHRVGKivpPKREILK---------DISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV------DTEIEGEarPM 66
Cdd:cd03294 14 PQKAFKLLAKGK---SKEEILKktgqtvgvnDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLieptsgKVLIDGQ--DI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 67 PGINVGYLP-----------QEPKLDPQATVRDIVeeavgqikqaqarldevyaAYAepdadfdalaaeqakLEaiLQas 135
Cdd:cd03294 89 AAMSRKELRelrrkkismvfQSFALLPHRTVLENV-------------------AFG---------------LE--VQ-- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 136 dGHNLERQLEVAADALR---LPPW-DAKVEHLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDAdsvawL------EHFL 205
Cdd:cd03294 131 -GVPRAEREERAAEALElvgLEGWeHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDP-----LirremqDELL 204
|
250
....*....|....*.
gi 15599791 206 H---DFPGTVVAITHD 218
Cdd:cd03294 205 RlqaELQKTIVFITHD 220
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
20-236 |
6.48e-09 |
|
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: 56.27 E-value: 6.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 20 EILKDISLSFFPGAKIGVLGLNGAGKSTL----LRIMAGVDTEIEGEARPMPGINVGYL-------PQEPKLdPQATVRd 88
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLilalFRFLEAEEGKIEIDGIDISTIPLEDLrssltiiPQDPTL-FSGTIR- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 89 iveeavgqikqaqARLDeVYAAYAEpdadfdalaaeqAKLEAILQASDGHNlerqlevaadalrlppwdakveHLSGGEK 168
Cdd:cd03369 100 -------------SNLD-PFDEYSD------------EEIYGALRVSEGGL----------------------NLSQGQR 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599791 169 RRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHD-FPG-TVVAITHDryfLDNVAGW--ILELDRGH 236
Cdd:cd03369 132 QLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREeFTNsTILTIAHR---LRTIIDYdkILVMDAGE 200
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
343-511 |
6.72e-09 |
|
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: 58.64 E-value: 6.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 343 SLSIPK-GAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEigetvqiasvdqsrdslegNKTVWEQVSDGFEQIKIGNY- 420
Cdd:COG1245 92 GLPVPKkGKVTGILGPNGIGKSTALKILSGELKPNLGDYD-------------------EEPSWDEVLKRFRGTELQDYf 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 421 ------------------EVP-------------------SRSYVGRFNFKGADQQKfVKDLSGGERGRLHLALTLKQGG 463
Cdd:COG1245 153 kklangeikvahkpqyvdLIPkvfkgtvrellekvdergkLDELAEKLGLENILDRD-ISELSGGELQRVAIAAALLRDA 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15599791 464 NVLLLDEPSNDLDV----ETLRALEEaLLDFPGAAIVISHDRWFLDRIATHI 511
Cdd:COG1245 232 DFYFFDEPSSYLDIyqrlNVARLIRE-LAEEGKYVLVVEHDLAILDYLADYV 282
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
17-194 |
7.23e-09 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 56.46 E-value: 7.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 17 PKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGE----ARPMPGIN-------VGYLPQEPKLDPqAT 85
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQilidGIDIRDISrkslrsmIGVVLQDTFLFS-GT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 86 VRDiveeavgQIKqaqarldevyaaYAEPDADfdalaaeQAKLEAILQASDGHNLERQLEVAadalrlppWDAKVEH--- 162
Cdd:cd03254 93 IME-------NIR------------LGRPNAT-------DEEVIEAAKEAGAHDFIMKLPNG--------YDTVLGEngg 138
|
170 180 190
....*....|....*....|....*....|...
gi 15599791 163 -LSGGEKRRVALCRLLLSAPDMLLLDEPTNHLD 194
Cdd:cd03254 139 nLSQGERQLLAIARAMLRDPKILILDEATSNID 171
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
19-223 |
7.64e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 56.61 E-value: 7.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVD----------------TEIEGEARPMPGINVGYlpQEPKLDP 82
Cdd:COG0396 13 KEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyevtsgsilldgediLELSPDERARAGIFLAF--QYPVEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 83 QATVRDIVEEAVGQIkqaqaRLDEVYAAyaepdaDFDALAAEQAKLeailqasdghnlerqLEVAADALRLPpwdakV-E 161
Cdd:COG0396 91 GVSVSNFLRTALNAR-----RGEELSAR------EFLKLLKEKMKE---------------LGLDEDFLDRY-----VnE 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599791 162 HLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWL-EHF--LHDFPGTVVAITHDRYFLD 223
Cdd:COG0396 140 GFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVaEGVnkLRSPDRGILIITHYQRILD 204
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
336-476 |
7.83e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 56.95 E-value: 7.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 336 RVLIDnLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETVQIASVDQSRdslegNKTVWEQV------- 408
Cdd:PRK13634 21 RALYD-VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKK-----LKPLRKKVgivfqfp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 409 -SDGFEQ-----IKIG--NYEVPSR----------SYVGrFNFKGADQQKFvkDLSGGERGRLHLALTLKQGGNVLLLDE 470
Cdd:PRK13634 95 eHQLFEEtvekdICFGpmNFGVSEEdakqkaremiELVG-LPEELLARSPF--ELSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
....*.
gi 15599791 471 PSNDLD 476
Cdd:PRK13634 172 PTAGLD 177
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
19-235 |
8.46e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 56.30 E-value: 8.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLR------------IMAGvDTEIEGeARPMPGI---------NVGYLPQE 77
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRcinlleqpeagtIRVG-DITIDT-ARSLSQQkglirqlrqHVGFVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 78 PKLDPQATVRDIVEEAVGQIKQaqarldevyaayaEPDADFDALAAEqakleaiLQASDGHNLERqlevaadalrlppwD 157
Cdd:PRK11264 94 FNLFPHRTVLENIIEGPVIVKG-------------EPKEEATARARE-------LLAKVGLAGKE--------------T 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 158 AKVEHLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHF---LHDFPGTVVAITHDRYFLDNVAGWILELDR 234
Cdd:PRK11264 140 SYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTirqLAQEKRTMVIVTHEMSFARDVADRAIFMDQ 219
|
.
gi 15599791 235 G 235
Cdd:PRK11264 220 G 220
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-194 |
8.79e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 58.18 E-value: 8.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 21 ILKDISLSFFPGAKIGVLGLNGAGKST----LLRIMAGvDTEIEGEARPMPGINV-GYLP---------QEP--KLDPQA 84
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-QGEIWFDGQPLHNLNRrQLLPvrhriqvvfQDPnsSLNPRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 85 TVRDIVEEAVgQIKQAQarldevyaayaepdadfdaLAAEQAKLEAIlqasdghnlERQLEVAADAL---RLPpwdakvE 161
Cdd:PRK15134 380 NVLQIIEEGL-RVHQPT-------------------LSAAQREQQVI---------AVMEEVGLDPEtrhRYP------A 424
|
170 180 190
....*....|....*....|....*....|...
gi 15599791 162 HLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLD 194
Cdd:PRK15134 425 EFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
20-243 |
8.95e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 56.78 E-value: 8.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEarpmpgINVGYLPqepkLDPQATVRDIVEEAVGQIKQ 99
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGR------ILFDGKP----IDYSRKGLMKLRESVGMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 100 AQArlDEVYAAYAEPDADFDALAAEQAKLEailqasdghnLERQLEVAADALRLPPWDAKVEH-LSGGEKRRVALCRLLL 178
Cdd:PRK13636 90 DPD--NQLFSASVYQDVSFGAVNLKLPEDE----------VRKRVDNALKRTGIEHLKDKPTHcLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599791 179 SAPDMLLLDEPTNHLDADSVA----WLEHFLHDFPGTVVAITHDryfLDNVAGW---ILELDRGHGIpFEGN 243
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSeimkLLVEMQKELGLTIIIATHD---IDIVPLYcdnVFVMKEGRVI-LQGN 225
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
323-500 |
9.12e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 56.53 E-value: 9.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 323 VIELHNVTKGYGDRV-LIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTI--------------EIGETVQ 387
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsgidtgdfsklqGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 388 IasVDQSRDSLEGNKTVWEQVSDGFEQIKIGNYEVPSRSYVGRFNFK-GADQQKFVKDLSGGERGRLHLALTLKQGGNVL 466
Cdd:PRK13644 81 I--VFQNPETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGlEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 15599791 467 LLDEPSNDLDVETLRALEEAL--LDFPGAAIV-ISHD 500
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIkkLHEKGKTIVyITHN 195
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
317-520 |
9.89e-09 |
|
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: 55.50 E-value: 9.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 317 PRLGDkvIELHNVTKGYGDRV--LIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIgETVQIASVDQS 394
Cdd:cd03369 2 PEHGE--IEVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEI-DGIDISTIPLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 395 RdsLEGNKTVWEQVSDGFEqikiGNYevpsRSYVGRFNfKGADQQKF----VK----DLSGGERGRLHLALTLKQGGNVL 466
Cdd:cd03369 79 D--LRSSLTIIPQDPTLFS----GTI----RSNLDPFD-EYSDEEIYgalrVSegglNLSQGQRQLLCLARALLKRPRVL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599791 467 LLDEPSNDLDVETLRALEEALLD-FPGAAIV-ISHdrwfldRIAThILSYE-----DDGKV 520
Cdd:cd03369 148 VLDEATASIDYATDALIQKTIREeFTNSTILtIAH------RLRT-IIDYDkilvmDAGEV 201
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
327-520 |
1.05e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 56.62 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 327 HNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGtieigeTVQIASVDQSRDSLEGNKTVWE 406
Cdd:PRK10419 16 GGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQG------NVSWRGEPLAKLNRAQRKAFRR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 407 QVSDGFeQIKIGnyEVPSRSYVGRF---------NFKGADQQ------------------KFVKDLSGGERGRLHLALTL 459
Cdd:PRK10419 90 DIQMVF-QDSIS--AVNPRKTVREIireplrhllSLDKAERLarasemlravdlddsvldKRPPQLSGGQLQRVCLARAL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599791 460 KQGGNVLLLDEPSNDLDV----ETLRALEEALLDFPGAAIVISHDRWFLDRIATHILSYeDDGKV 520
Cdd:PRK10419 167 AVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVM-DNGQI 230
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
323-512 |
1.10e-08 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 57.81 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 323 VIELHNVTKGY---GDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETV----------QI 388
Cdd:TIGR00958 478 LIEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLdGVPLvqydhhylhrQV 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 389 ASVDQsrDSLEGNKTVWEQVSDGF-----EQIKIGNYEVPSRSYVGRFNfKGADQQKFVKD--LSGGERGRLHLALTLKQ 461
Cdd:TIGR00958 558 ALVGQ--EPVLFSGSVRENIAYGLtdtpdEEIMAAAKAANAHDFIMEFP-NGYDTEVGEKGsqLSGGQKQRIAIARALVR 634
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15599791 462 GGNVLLLDEPSNDLDVETLRALEEALLDFPGAAIVISHdRWFLDRIATHIL 512
Cdd:TIGR00958 635 KPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH-RLSTVERADQIL 684
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
18-217 |
1.22e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 55.94 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRI---MAGVDTE--IEGEARpMPGINVgylpQEPKLDpqaTVrDIVEE 92
Cdd:PRK14239 17 KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSinrMNDLNPEvtITGSIV-YNGHNI----YSPRTD---TV-DLRKE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 93 aVGQIKQAQARL------DEVYAayaepdadfdaLAAEQAKLEAILQASdghnLERQLEVAAdalrlpPWDAKVEHL--- 163
Cdd:PRK14239 88 -IGMVFQQPNPFpmsiyeNVVYG-----------LRLKGIKDKQVLDEA----VEKSLKGAS------IWDEVKDRLhds 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 164 ----SGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPG--TVVAITH 217
Cdd:PRK14239 146 alglSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDdyTMLLVTR 205
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
324-516 |
1.23e-08 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 55.17 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRV-----LIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETvqIASVDQS---- 394
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--IAYVSQEpwiq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 395 RDSLEGN------------KTV---------WEQVSDGfEQIKIGNyevpsrsyvgrfnfKGAdqqkfvkDLSGGERGRL 453
Cdd:cd03250 79 NGTIRENilfgkpfdeeryEKVikacalepdLEILPDG-DLTEIGE--------------KGI-------NLSGGQKQRI 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599791 454 HLALTLKQGGNVLLLDEPSNDLDVETLRAL-EEALLDF---PGAAIVISHDRWFLDRiATHILSYED 516
Cdd:cd03250 137 SLARAVYSDADIYLLDDPLSAVDAHVGRHIfENCILGLllnNKTRILVTHQLQLLPH-ADQIVVLDN 202
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
317-477 |
1.33e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.32 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 317 PRL----GDKVIELHNVTkGYGdrvlIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQIA-- 389
Cdd:PRK10762 247 PRLdkapGEVRLKVDNLS-GPG----VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLdGHEVVTRsp 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 390 -----------SVDQSRDSLEGNKTVWE--------QVSDGFEQIKIGNYEVPSRSYVGRFNFKGADQQKFVKDLSGGER 450
Cdd:PRK10762 322 qdglangivyiSEDRKRDGLVLGMSVKEnmsltalrYFSRAGGSLKHADEQQAVSDFIRLFNIKTPSMEQAIGLLSGGNQ 401
|
170 180
....*....|....*....|....*..
gi 15599791 451 GRLHLALTLKQGGNVLLLDEPSNDLDV 477
Cdd:PRK10762 402 QKVAIARGLMTRPKVLILDEPTRGVDV 428
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-477 |
1.46e-08 |
|
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: 57.14 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV------DTEIEGEARPMPGINvgylpqepkldpqatVRDIVEEAVG 95
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVyphgtwDGEIYWSGSPLKASN---------------IRDTERAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 96 QIKQAQARLDEVyaAYAEPDADFDALAAEQAKLEAILQASDGHNLERQLEVAADALRLPpwdakVEHLSGGEKRRVALCR 175
Cdd:TIGR02633 82 IIHQELTLVPEL--SVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRP-----VGDYGGGQQQLVEIAK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 176 LLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPGTVVAITHDRYFLDNVagwileldrghgipfegnysgwleskaarl 255
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEV------------------------------ 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 256 aqeakqeashaKAMKAELEWVRQGAkgRQAKSKARLQRFEELQSQEFQKrsETNEIYiPAGPR-LGDKVIELHNVTKGYG 334
Cdd:TIGR02633 205 -----------KAVCDTICVIRDGQ--HVATKDMSTMSEDDIITMMVGR--EITSLY-PHEPHeIGDVILEARNLTCWDV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 335 D---RVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGK-EQPDSGTIEI-GETVQIASV-------------DQSRD 396
Cdd:TIGR02633 269 InphRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFInGKPVDIRNPaqairagiamvpeDRKRH 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 397 SLEGNKTVWEQVS-------DGFEQIKIGNYEVPSRSYVGRFNFKGADQQKFVKDLSGGERGRLHLALTLKQGGNVLLLD 469
Cdd:TIGR02633 349 GIVPILGVGKNITlsvlksfCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILD 428
|
....*...
gi 15599791 470 EPSNDLDV 477
Cdd:TIGR02633 429 EPTRGVDV 436
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
324-490 |
1.48e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 55.62 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRM------------------LTGKE--QPDSGTIEIG 383
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrllelneearvegevrLFGRNiySPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 384 EtvQIASVDQSRDSLEgNKTVWEQVSDGFEQIKI--GNYEVPSRSyvgRFNFKGADQQKFVKD--------LSGGERGRL 453
Cdd:PRK14267 85 R--EVGMVFQYPNPFP-HLTIYDNVAIGVKLNGLvkSKKELDERV---EWALKKAALWDEVKDrlndypsnLSGGQRQRL 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 15599791 454 HLALTLKQGGNVLLLDEPSNDLDVETLRALEEALLDF 490
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTAKIEELLFEL 195
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
19-223 |
1.55e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 55.80 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVD----------------TEIEGEARPMPGINVGYlpQEPKLDP 82
Cdd:CHL00131 20 NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPaykilegdilfkgesiLDLEPEERAHLGIFLAF--QYPIEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 83 QATVRDIVEEAVGQiKQAQARLDEVyaayaEPDADFDALaaeQAKLEaiLQASDGHNLERQLEvaadalrlppwdakvEH 162
Cdd:CHL00131 98 GVSNADFLRLAYNS-KRKFQGLPEL-----DPLEFLEII---NEKLK--LVGMDPSFLSRNVN---------------EG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599791 163 LSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPGT---VVAITHDRYFLD 223
Cdd:CHL00131 152 FSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSensIILITHYQRLLD 215
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
4-226 |
1.88e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 55.94 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 4 YVYTmhrvgKIVPPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRimagvdtEIEGEARPMPG-INVGYLPQEPKLDP 82
Cdd:PRK13646 10 YTYQ-----KGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQ-------NINALLKPTTGtVTVDDITITHKTKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 83 QaTVRDIVEEA--VGQIKQAQARLDEVYAAYAEPDADFDaLAAEQAKleailqaSDGHNLERQLEVAADALRLPPWdakv 160
Cdd:PRK13646 78 K-YIRPVRKRIgmVFQFPESQLFEDTVEREIIFGPKNFK-MNLDEVK-------NYAHRLLMDLGFSRDVMSQSPF---- 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 161 eHLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADS----VAWLEHFLHDFPGTVVAITHDryfLDNVA 226
Cdd:PRK13646 145 -QMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSkrqvMRLLKSLQTDENKTIILVSHD---MNEVA 210
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-508 |
1.90e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.17 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 22 LKDISLSFFPGAKIGVLGLNGAGKS----TLLRIMAGVDTEIEGEarpmpginvgylpqepkldpQATVRDIVEEAVGQI 97
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAGGLVQCD--------------------KMLLRRRSRQVIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 98 KQAQARLDEVYAA-----YAEPDADFDALAAEQAKLEAILQASDGHNLERQLEVAA---DALRLPPWDAKV----EHLSG 165
Cdd:PRK10261 92 EQSAAQMRHVRGAdmamiFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKrmlDQVRIPEAQTILsrypHQLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 166 GEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFL----HDFPGTVVAITHDRYFLDNVAGWILELDRGHGIpfe 241
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIkvlqKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV--- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 242 gnysgwlESKAARLAQEAKQEaSHAKAMKAELEwvRQGA-KGRQAKSKARLQRFEELQSQEFQKRSETneiYIPagprlG 320
Cdd:PRK10261 249 -------ETGSVEQIFHAPQH-PYTRALLAAVP--QLGAmKGLDYPRRFPLISLEHPAKQEPPIEQDT---VVD-----G 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 321 DKVIELHN-VTK-----GYGDRV-----LIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQI 388
Cdd:PRK10261 311 EPILQVRNlVTRfplrsGLLNRVtrevhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFnGQRIDT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 389 ASVDQ----SRD----------SLEGNKTVWEQVSDGFEQIKIGNYEVPSRS---YVGRFNFKGADQQKFVKDLSGGERG 451
Cdd:PRK10261 391 LSPGKlqalRRDiqfifqdpyaSLDPRQTVGDSIMEPLRVHGLLPGKAAAARvawLLERVGLLPEHAWRYPHEFSGGQRQ 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599791 452 RLHLALTLKQGGNVLLLDEPSNDLDVETLRALEEALLD----FPGAAIVISHDRWFLDRIA 508
Cdd:PRK10261 471 RICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDlqrdFGIAYLFISHDMAVVERIS 531
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
320-511 |
1.91e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 55.44 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 320 GDKVIELHNVTKGY---GDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETVQIASVDQSR- 395
Cdd:PRK14246 4 GKSAEDVFNISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 396 DSLEGNKTVWE--QVSDGFEQIKI-GNYEVPSRSY----------VGRFNFKGADQQKFVKD--------LSGGERGRLH 454
Cdd:PRK14246 84 DAIKLRKEVGMvfQQPNPFPHLSIyDNIAYPLKSHgikekreikkIVEECLRKVGLWKEVYDrlnspasqLSGGQQQRLT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15599791 455 LALTLKQGGNVLLLDEPSNDLDVETLRALEEALLDFPG--AAIVISHDRWFLDRIATHI 511
Cdd:PRK14246 164 IARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYV 222
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-235 |
1.97e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 55.30 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdTEIEGEARpmpginvgyLPQEPKLDPQATVR-DIVE-----EA 93
Cdd:PRK14247 17 EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRL-IELYPEAR---------VSGEVYLDGQDIFKmDVIElrrrvQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 94 VGQIKQAQARLdEVYAAYAEpDADFDALAAEQAKLEAILQASdghnLER-QL-EVAADALrlppwDAKVEHLSGGEKRRV 171
Cdd:PRK14247 87 VFQIPNPIPNL-SIFENVAL-GLKLNRLVKSKKELQERVRWA----LEKaQLwDEVKDRL-----DAPAGKLSGGQQQRL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599791 172 ALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPG--TVVAITHDRYFLDNVAGWILELDRG 235
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTHFPQQAARISDYVAFLYKG 221
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
31-205 |
2.03e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.85 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 31 PGAKIGVLGLNGAGKSTLLRIMAGVdteiegearpmpginvgylpqepkLDPQATVRDIVEEAVGQIKQAQarldevYAA 110
Cdd:PRK13543 36 AGEALLVQGDNGAGKTTLLRVLAGL------------------------LHVESGQIQIDGKTATRGDRSR------FMA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 111 YAepdADFDALAAEQAKLEAI--LQASDGHNLERQLEVAADALRLPPW-DAKVEHLSGGEKRRVALCRLLLSAPDMLLLD 187
Cdd:PRK13543 86 YL---GHLPGLKADLSTLENLhfLCGLHGRRAKQMPGSALAIVGLAGYeDTLVRQLSAGQKKRLALARLWLSPAPLWLLD 162
|
170
....*....|....*...
gi 15599791 188 EPTNHLDADSVAWLEHFL 205
Cdd:PRK13543 163 EPYANLDLEGITLVNRMI 180
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
324-487 |
2.16e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 57.04 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGY-GDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQ----------IASV 391
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLdGRPLSslshsvlrqgVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 392 DQS----RDSLEGNKTVW-----EQVSDGFEQIKIGNYevpSRSYVGRFNFKGADQQkfvKDLSGGERGRLHLALTLKQG 462
Cdd:PRK10790 421 QQDpvvlADTFLANVTLGrdiseEQVWQALETVQLAEL---ARSLPDGLYTPLGEQG---NNLSVGQKQLLALARVLVQT 494
|
170 180
....*....|....*....|....*
gi 15599791 463 GNVLLLDEPSNDLDVETLRALEEAL 487
Cdd:PRK10790 495 PQILILDEATANIDSGTEQAIQQAL 519
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
20-241 |
2.37e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 55.40 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdteiegearpmpginvgYLPQEPKLDPQATVRDIVEEAVGQIKQ 99
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGL-----------------LRPQKGAVLWQGKPLDYSKRGLLALRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 100 aqarldEVYAAYAEPD-----ADFDALAAEQAKLEAILQASDGHNLERQLE-VAADALRLPPwdakVEHLSGGEKRRVAL 173
Cdd:PRK13638 78 ------QVATVFQDPEqqifyTDIDSDIAFSLRNLGVPEAEITRRVDEALTlVDAQHFRHQP----IQCLSHGQKKRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599791 174 CRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPGT---VVAITHDRYFLDNVAGWILELDRG----HGIPFE 241
Cdd:PRK13638 148 AGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQgnhVIISSHDIDLIYEISDAVYVLRQGqiltHGAPGE 222
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
16-218 |
2.54e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 55.38 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 16 PPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdteiegearpmpginvgYLPQ--EPKLDPQATVRDIVEEA 93
Cdd:PRK13632 19 NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGL-----------------LKPQsgEIKIDGITISKENLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 94 ---VGQIKQaqarldevyaayaEPDADFDALAAE-------------QAKLEA-ILQASDGHNLERQLEvaadalRLPpw 156
Cdd:PRK13632 82 rkkIGIIFQ-------------NPDNQFIGATVEddiafglenkkvpPKKMKDiIDDLAKKVGMEDYLD------KEP-- 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599791 157 dakvEHLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDF----PGTVVAITHD 218
Cdd:PRK13632 141 ----QNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLrktrKKTLISITHD 202
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
24-226 |
2.73e-08 |
|
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: 55.44 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 24 DISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-------VDTEI-----------EGEARPMPGINVGYLPQEPK--LDPQ 83
Cdd:COG0444 23 GVSFDVRRGETLGLVGESGSGKSTLARAILGllpppgiTSGEIlfdgedllklsEKELRKIRGREIQMIFQDPMtsLNPV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 84 ATVRDIVEEAV---GQIKQAQARldevyaayaepdadfdALAAEQakleailqasdghnLER-QLEVAADALRLPPwdak 159
Cdd:COG0444 103 MTVGDQIAEPLrihGGLSKAEAR----------------ERAIEL--------------LERvGLPDPERRLDRYP---- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599791 160 veH-LSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDAdSVAW--LEHFL---HDFPGTVVAITHD----RYFLDNVA 226
Cdd:COG0444 149 --HeLSGGMRQRVMIARALALEPKLLIADEPTTALDV-TIQAqiLNLLKdlqRELGLAILFITHDlgvvAEIADRVA 222
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-194 |
2.81e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 55.09 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpMPGINVGYLP------------QEPKLD--PQA 84
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIL-IDGKDVTKLPeykrakyigrvfQDPMMGtaPSM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 85 TvrdiVEE--AVGQIKQAQARLdevyaAYAEPDADFDALAAEQAKLeailqasdGHNLERQLevaadalrlppwDAKVEH 162
Cdd:COG1101 98 T----IEEnlALAYRRGKRRGL-----RRGLTKKRRELFRELLATL--------GLGLENRL------------DTKVGL 148
|
170 180 190
....*....|....*....|....*....|....*
gi 15599791 163 LSGGEkrRVALCrLL---LSAPDMLLLDEPTNHLD 194
Cdd:COG1101 149 LSGGQ--RQALS-LLmatLTKPKLLLLDEHTAALD 180
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
324-500 |
2.93e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 56.66 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGY----GDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETvQIASVDqsRDSLE 399
Cdd:PRK10535 5 LELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQ-DVATLD--ADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 400 GNKTvwEQVSDGFEQIKI-------GNYEVPSrSYVGRfnFKGADQQKFVK----------------DLSGGERGRLHLA 456
Cdd:PRK10535 82 QLRR--EHFGFIFQRYHLlshltaaQNVEVPA-VYAGL--ERKQRLLRAQEllqrlgledrveyqpsQLSGGQQQRVSIA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15599791 457 LTLKQGGNVLLLDEPSNDLDV---ETLRALEEALLDFPGAAIVISHD 500
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDShsgEEVMAILHQLRDRGHTVIIVTHD 203
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
19-236 |
3.10e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 54.50 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpMPGINVGYLPQE--PKLDPQatvrdiveeaVGQ 96
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIW-FSGHDITRLKNRevPFLRRQ----------IGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 97 IKQAQARLdevyaayaepdadFDALAAEQAKLEAILQASDGHNLERQLEVAADALRLPPWDAKVE-HLSGGEKRRVALCR 175
Cdd:PRK10908 84 IFQDHHLL-------------MDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPiQLSGGEQQRVGIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599791 176 LLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPG---TVVAITHDRYFLDNVAGWILELDRGH 236
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
22-218 |
3.19e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 55.14 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEArpmpginvgyLPQEPKLDPQaTVRDIvEEAVGQIKQaq 101
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI----------FYNNQAITDD-NFEKL-RKHIGIVFQ-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 102 arldevyaayaEPDADFdalaaeqakLEAILQASDGHNLERQL-----------EVAADALRLPPWDAKVEHLSGGEKRR 170
Cdd:PRK13648 91 -----------NPDNQF---------VGSIVKYDVAFGLENHAvpydemhrrvsEALKQVDMLERADYEPNALSGGQKQR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15599791 171 VALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPG----TVVAITHD 218
Cdd:PRK13648 151 VAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSehniTIISITHD 202
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-194 |
3.25e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 56.84 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRI---MAGVDTEIEgearpMPGI--NVGYLPQEPKldpqatvrdiveeA 93
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSAllrLLSTEGEIQ-----IDGVswNSVTLQTWRK-------------A 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 94 VGQIKQAQARLDEVYAAYAEPdadfdalaAEQAKLEAILQASDGHNLERQLEVAADALRLPPWDAKVEhLSGGEKRRVAL 173
Cdd:TIGR01271 1294 FGVIPQKVFIFSGTFRKNLDP--------YEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYV-LSNGHKQLMCL 1364
|
170 180
....*....|....*....|.
gi 15599791 174 CRLLLSAPDMLLLDEPTNHLD 194
Cdd:TIGR01271 1365 ARSILSKAKILLLDEPSAHLD 1385
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
333-476 |
3.30e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 55.01 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 333 YGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIeigeTVQIASVDQSRDSLEGNKtvwEQVSDGF 412
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAV----LWQGKPLDYSKRGLLALR---QQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 413 ----EQI-----------KIGNYEVPSRSYVGRFN--FKGADQQKF----VKDLSGGERGRLHLALTLKQGGNVLLLDEP 471
Cdd:PRK13638 84 qdpeQQIfytdidsdiafSLRNLGVPEAEITRRVDeaLTLVDAQHFrhqpIQCLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
....*
gi 15599791 472 SNDLD 476
Cdd:PRK13638 164 TAGLD 168
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
343-512 |
3.67e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.97 E-value: 3.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 343 SLSIPK-GAIVGVIGGNGAGKSTLFRMLTG---------KEQPD--------SGTI-----------EIGETVQIASVDQ 393
Cdd:PRK13409 92 GLPIPKeGKVTGILGPNGIGKTTAVKILSGelipnlgdyEEEPSwdevlkrfRGTElqnyfkklyngEIKVVHKPQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 394 SRDSLEGNktvweqVSDGFEQI-KIGNYevpsRSYVGRFNFKGADQQKfVKDLSGGERGRLHLALTLKQGGNVLLLDEPS 472
Cdd:PRK13409 172 IPKVFKGK------VRELLKKVdERGKL----DEVVERLGLENILDRD-ISELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15599791 473 NDLDV-ETL---RALEEALLDfpGAAIVISHDRWFLDRIA--THIL 512
Cdd:PRK13409 241 SYLDIrQRLnvaRLIRELAEG--KYVLVVEHDLAVLDYLAdnVHIA 284
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
15-199 |
4.03e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 56.39 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 15 VPPKR-EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDT--EIEGEARpMPGIN---------VGYLPQEPKLDP 82
Cdd:PLN03140 888 VTEDRlQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIR-ISGFPkkqetfariSGYCEQNDIHSP 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 83 QATVRDIVeeavgqikqaqarldeVYAAyaepdadFDALAAEQAKLEAILQASDGHNLErQLEVAADAL-RLPpwdaKVE 161
Cdd:PLN03140 967 QVTVRESL----------------IYSA-------FLRLPKEVSKEEKMMFVDEVMELV-ELDNLKDAIvGLP----GVT 1018
|
170 180 190
....*....|....*....|....*....|....*...
gi 15599791 162 HLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVA 199
Cdd:PLN03140 1019 GLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAA 1056
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
10-218 |
4.56e-08 |
|
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: 54.23 E-value: 4.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 10 RVGKIVPPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpMPGINV------------GYLPQE 77
Cdd:cd03295 5 NVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIF-IDGEDIreqdpvelrrkiGYVIQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 78 PKLDPQATVRDIVEeAVGQI-----KQAQARLDEVYAAYAEPDADFdalaaeqakleailqasdghnlerqlevaadALR 152
Cdd:cd03295 84 IGLFPHMTVEENIA-LVPKLlkwpkEKIRERADELLALVGLDPAEF-------------------------------ADR 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 153 LPpwdakvEHLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWL-EHFLH---DFPGTVVAITHD 218
Cdd:cd03295 132 YP------HELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLqEEFKRlqqELGKTIVFVTHD 195
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
323-499 |
5.04e-08 |
|
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: 55.60 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 323 VIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI---GETVQIASVDQSRD--- 396
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIywsGSPLKASNIRDTERagi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 397 -------SLEGNKTVWEQVSDGFEQIKIG---NYEVPSR---SYVGRFNFKGADQQKFVKDLSGGERGRLHLALTLKQGG 463
Cdd:TIGR02633 81 viihqelTLVPELSVAENIFLGNEITLPGgrmAYNAMYLrakNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 15599791 464 NVLLLDEPSNDLDVETLRALEEALLDFPG---AAIVISH 499
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAhgvACVYISH 199
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
9-194 |
5.12e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 54.64 E-value: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 9 HRVGKIVPPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-----------DTEIEGEARPMP--------GI 69
Cdd:PRK13634 10 HRYQYKTPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLlqptsgtvtigERVITAGKKNKKlkplrkkvGI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 70 nVGYLPqEPKLDPQATVRDIveeAVGQIKqaqarldevyaaYAEPDADFDALAAEQAKL----EAILQASdghnlerqle 145
Cdd:PRK13634 90 -VFQFP-EHQLFEETVEKDI---CFGPMN------------FGVSEEDAKQKAREMIELvglpEELLARS---------- 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15599791 146 vaadalrlpPWDakvehLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLD 194
Cdd:PRK13634 143 ---------PFE-----LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
18-217 |
5.28e-08 |
|
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: 53.77 E-value: 5.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLR-IMAGVDTEiEGEARpMPGINV------------GYLPQEPKLdpqa 84
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNlIPRFYDVD-SGRIL-IDGHDVrdytlaslrrqiGLVSQDVFL---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 85 tVRDIVEEAVgqikqaqarldevyaAYAEPDADFDAL--AAEQAKL-EAILQASDGhnlerqlevaadalrlppWDAKVE 161
Cdd:cd03251 88 -FNDTVAENI---------------AYGRPGATREEVeeAARAANAhEFIMELPEG------------------YDTVIG 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599791 162 H----LSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADS----VAWLEHFLHDfpGTVVAITH 217
Cdd:cd03251 134 ErgvkLSGGQRQRIAIARALLKDPPILILDEATSALDTESerlvQAALERLMKN--RTTFVIAH 195
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
323-499 |
6.80e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.32 E-value: 6.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 323 VIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI---GETVQIASVdqsRDSLE 399
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEIifeGEELQASNI---RDTER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 400 G-------NKTVWEQVSDGfEQIKIGNYEVPSrsyvGRFNFKG--ADQQKF-------------VKDLSGGERGRLHLAL 457
Cdd:PRK13549 82 AgiaiihqELALVKELSVL-ENIFLGNEITPG----GIMDYDAmyLRAQKLlaqlkldinpatpVGNLGLGQQQLVEIAK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15599791 458 TLKQGGNVLLLDEPSNDL---DVETLRALEEALLDFPGAAIVISH 499
Cdd:PRK13549 157 ALNKQARLLILDEPTASLtesETAVLLDIIRDLKAHGIACIYISH 201
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
311-470 |
7.36e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 53.67 E-value: 7.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 311 IYIPAGPRLGDKVIELHNVTKGYGdrvlIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETVQIAS 390
Cdd:PRK13546 16 IYRTNKERMKDALIPKHKNKTFFA----LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 391 VDQsrdSLEGNKTVWEQVS-----DGF--EQIKIGNYEVPSRSYVGRFNFKGadqqkfVKDLSGGERGRLHLALTLKQGG 463
Cdd:PRK13546 92 ISA---GLSGQLTGIENIEfkmlcMGFkrKEIKAMTPKIIEFSELGEFIYQP------VKKYSSGMRAKLGFSINITVNP 162
|
....*..
gi 15599791 464 NVLLLDE 470
Cdd:PRK13546 163 DILVIDE 169
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
318-487 |
7.99e-08 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 55.21 E-value: 7.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 318 RLGDKVIELHNVTKGY-GDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETvQIASVDQsrD 396
Cdd:COG5265 352 VVGGGEVRFENVSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQ-DIRDVTQ--A 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 397 SLEG------------NKT----------------VWE-----QVSDGFEQIKIGnYEVPsrsyVGRFNFKgadqqkfvk 443
Cdd:COG5265 429 SLRAaigivpqdtvlfNDTiayniaygrpdaseeeVEAaaraaQIHDFIESLPDG-YDTR----VGERGLK--------- 494
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15599791 444 dLSGGERGRLHLALTLKQGGNVLLLDEPSNDLDVETLRALEEAL 487
Cdd:COG5265 495 -LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAAL 537
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
21-218 |
9.03e-08 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 53.55 E-value: 9.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpMPGINVG------------YLPQEPKLDPQATVRD 88
Cdd:COG4604 16 VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVL-VDGLDVAttpsrelakrlaILRQENHINSRLTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 89 IVeeAVGQIKQAQARLDEvyaayaepdADfdalaaeqakLEAILQASDGHNLErqlevaadALRlppwDAKVEHLSGGEK 168
Cdd:COG4604 95 LV--AFGRFPYSKGRLTA---------ED----------REIIDEAIAYLDLE--------DLA----DRYLDELSGGQR 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15599791 169 RRVALCRLLLSAPDMLLLDEPTNHLD-ADSVAW---LEHFLHDFPGTVVAITHD 218
Cdd:COG4604 142 QRAFIAMVLAQDTDYVLLDEPLNNLDmKHSVQMmklLRRLADELGKTVVIVLHD 195
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
323-476 |
1.05e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 52.79 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 323 VIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQIASVDQSRD----- 396
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFeGEDISTLKPEIYRQqvsyc 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 397 ----SLEGNkTVWEQVSDGFEQIKIGNYEVPSRSYVGRFNFKGADQQKFVKDLSGGERGRLHLALTLKQGGNVLLLDEPS 472
Cdd:PRK10247 87 aqtpTLFGD-TVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEIT 165
|
....
gi 15599791 473 NDLD 476
Cdd:PRK10247 166 SALD 169
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
310-499 |
1.13e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 53.70 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 310 EIYIPaGPRLGDKVIELHNVTKGYGDR-----VLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGE 384
Cdd:PRK13631 9 KLKVP-NPLSDDIILRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 385 TVQIASVDQSRDSLEGNK---------------------------TVWEQVSDGFEQIKIGNYEVPSRS--YVGRFNFKG 435
Cdd:PRK13631 88 IYIGDKKNNHELITNPYSkkiknfkelrrrvsmvfqfpeyqlfkdTIEKDIMFGPVALGVKKSEAKKLAkfYLNKMGLDD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599791 436 A--DQQKFvkDLSGGERGRLHLALTLKQGGNVLLLDEPSNDLDVETLRALEEALLDFPG---AAIVISH 499
Cdd:PRK13631 168 SylERSPF--GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAnnkTVFVITH 234
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
20-216 |
1.28e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.65 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGE-----ARPMPGIN-------VGYLPQEPKLDPQaTVR 87
Cdd:PTZ00265 399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDiiindSHNLKDINlkwwrskIGVVSQDPLLFSN-SIK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 88 DIVEEAVGQIKQAQARLDEV----YAAYAEPDADFDALAAEQAKLEAILQASDGHNL---ERQLEVAADA---------- 150
Cdd:PTZ00265 478 NNIKYSLYSLKDLEALSNYYnedgNDSQENKNKRNSCRAKCAGDLNDMSNTTDSNELiemRKNYQTIKDSevvdvskkvl 557
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599791 151 -----LRLP-PWDAKV----EHLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPGTVVAIT 216
Cdd:PTZ00265 558 ihdfvSALPdKYETLVgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRIT 633
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
18-197 |
1.90e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 54.12 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-------VDTEIEGEARPMPGI--NVGYLPQEPKLDPQATVRD 88
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGriqgnnfTGTILANNRKPTKQIlkRTGFVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 89 -IVEEAVGQIKQAQARLDEVYAAyaepdadfDALAAEQ--AKLEAILQAsdghnlerqlevaadalrlppwDAKVEHLSG 165
Cdd:PLN03211 160 tLVFCSLLRLPKSLTKQEKILVA--------ESVISELglTKCENTIIG----------------------NSFIRGISG 209
|
170 180 190
....*....|....*....|....*....|..
gi 15599791 166 GEKRRVALCRLLLSAPDMLLLDEPTNHLDADS 197
Cdd:PLN03211 210 GERKRVSIAHEMLINPSLLILDEPTSGLDATA 241
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
333-506 |
1.91e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 51.87 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 333 YGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQ--IASVDQS------RDSLEGNKT 403
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFeRQSIKkdLCTYQKQlcfvghRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 404 VWEQVSDGFeQIKIGNYEVPSRSYVgrfnFKGADQQKF-VKDLSGGERGRLHLALTLKQGGNVLLLDEPSNDLD---VET 479
Cdd:PRK13540 91 LRENCLYDI-HFSPGAVGITELCRL----FSLEHLIDYpCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDelsLLT 165
|
170 180
....*....|....*....|....*..
gi 15599791 480 LRALEEALLDFPGAAIVISHDRWFLDR 506
Cdd:PRK13540 166 IITKIQEHRAKGGAVLLTSHQDLPLNK 192
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
342-500 |
1.92e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 52.24 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 342 LSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKeQPDSGTIEIGETV--QIASVDQSR--------DSLEGNKTVWeQVSDG 411
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPleAWSAAELARhraylsqqQTPPFAMPVF-QYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 412 FEQIKIGNYEVPSR-SYVGRFnFKGADQ-QKFVKDLSGGERGRLHLALTLKQ-------GGNVLLLDEPSNDLDVETLRA 482
Cdd:PRK03695 93 HQPDKTRTEAVASAlNEVAEA-LGLDDKlGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVAQQAA 171
|
170 180
....*....|....*....|.
gi 15599791 483 LEEALLDFPGAAIVI---SHD 500
Cdd:PRK03695 172 LDRLLSELCQQGIAVvmsSHD 192
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
336-500 |
1.96e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 52.52 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 336 RVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRM----LTGKEQPDSGTIEIGETVQ---IASVDQSRdsLEGNKTVWEQV 408
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKAlagdLTGGGAPRGARVTGDVTLNgepLAAIDAPR--LARLRAVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 409 SD-GF-----EQIKIGNYEVPSRSYVGR----------FNFKGADQ--QKFVKDLSGGERGRLHLALTLKQ--------- 461
Cdd:PRK13547 92 AQpAFafsarEIVLLGRYPHARRAGALThrdgeiawqaLALAGATAlvGRDVTTLSGGELARVQFARVLAQlwpphdaaq 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15599791 462 GGNVLLLDEPSNDLD-------VETLRALEEallDFPGAAIVISHD 500
Cdd:PRK13547 172 PPRYLLLDEPTAALDlahqhrlLDTVRRLAR---DWNLGVLAIVHD 214
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
327-499 |
2.04e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.77 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 327 HNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIgETVQIASVDQSRD-SLEGNKTVW 405
Cdd:PRK13543 15 HALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI-DGKTATRGDRSRFmAYLGHLPGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 406 EQVSDGFEQIKIGN-------YEVPSRSY--VGRFNFkgadQQKFVKDLSGGERGRLHLALTLKQGGNVLLLDEPSNDLD 476
Cdd:PRK13543 94 KADLSTLENLHFLCglhgrraKQMPGSALaiVGLAGY----EDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
170 180
....*....|....*....|....*.
gi 15599791 477 VETLRALEEAL---LDFPGAAIVISH 499
Cdd:PRK13543 170 LEGITLVNRMIsahLRGGGAALVTTH 195
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
323-498 |
2.52e-07 |
|
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: 53.86 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 323 VIELHNVTKGYG--DRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETVQIASVDQSRDSLeG 400
Cdd:TIGR01257 1937 ILRLNELTKVYSgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNM-G 2015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 401 NKTVWEQVSD---GFEQIKIgnYE----VPSRSY--VGRFNFKGADQQKFVKDL----SGGERGRLHLALTLKQGGNVLL 467
Cdd:TIGR01257 2016 YCPQFDAIDDlltGREHLYL--YArlrgVPAEEIekVANWSIQSLGLSLYADRLagtySGGNKRKLSTAIALIGCPPLVL 2093
|
170 180 190
....*....|....*....|....*....|...
gi 15599791 468 LDEPSNDLDVETLRALEEALLDF--PGAAIVIS 498
Cdd:TIGR01257 2094 LDEPTTGMDPQARRMLWNTIVSIirEGRAVVLT 2126
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
324-501 |
2.93e-07 |
|
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: 52.16 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGY--GDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLF----RMLTGKeqpdsGTIEI-GETVQIASVDQSRD 396
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLsaflRLLNTE-----GDIQIdGVSWNSVPLQKWRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 397 --------------SLEGNKTVWEQVSDgfEQIKIGNYEVPSRSYVGRFnfkgADQQKFVKD-----LSGGERGRLHLAL 457
Cdd:cd03289 78 afgvipqkvfifsgTFRKNLDPYGKWSD--EEIWKVAEEVGLKSVIEQF----PGQLDFVLVdggcvLSHGHKQLMCLAR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15599791 458 TLKQGGNVLLLDEPSNDLDVETLRALEEALLD-FPGAAIVISHDR 501
Cdd:cd03289 152 SVLSKAKILLLDEPSAHLDPITYQVIRKTLKQaFADCTVILSEHR 196
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-286 |
2.95e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 53.80 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 16 PPKreiLKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpMPGiNVGYLPQepkldpQATVR-DIVEEAV 94
Cdd:TIGR00957 651 PPT---LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVH-MKG-SVAYVPQ------QAWIQnDSLRENI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 95 GQIKQAQarlDEVYAAYAEPdadfdalAAEQAKLEaILQASDghnlerQLEVAADALrlppwdakveHLSGGEKRRVALC 174
Cdd:TIGR00957 720 LFGKALN---EKYYQQVLEA-------CALLPDLE-ILPSGD------RTEIGEKGV----------NLSGGQKQRVSLA 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 175 RLLLSAPDMLLLDEPTNHLDAdSVAwlEHFLHDFPG--------TVVAITHDRYFLDNVaGWILELDRGHgIPFEGNYSG 246
Cdd:TIGR00957 773 RAVYSNADIYLFDDPLSAVDA-HVG--KHIFEHVIGpegvlknkTRILVTHGISYLPQV-DVIIVMSGGK-ISEMGSYQE 847
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 15599791 247 WLESKAArLAQEAKQEASHAKAMKAELEWVR-QGAKGRQAK 286
Cdd:TIGR00957 848 LLQRDGA-FAEFLRTYAPDEQQGHLEDSWTAlVSGEGKEAK 887
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-218 |
3.55e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 52.02 E-value: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEG---------------------EARPmpgiNVGYLPQE 77
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgdvllggrsifnyrdvlEFRR----RVGMLFQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 78 PKLDPQATVRDIveeavgqikqaqarLDEVYAAYAEPDADFDALAaeQAKLEAIlqasdghnleRQLEVAADALRLPPWd 157
Cdd:PRK14271 110 PNPFPMSIMDNV--------------LAGVRAHKLVPRKEFRGVA--QARLTEV----------GLWDAVKDRLSDSPF- 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599791 158 akveHLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPG--TVVAITHD 218
Cdd:PRK14271 163 ----RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHN 221
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
324-476 |
3.59e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 52.05 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGD------RVLIDnLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETV----------- 386
Cdd:PRK13649 3 INLQNVSYTYQAgtpfegRALFD-VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitstsknkdik 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 387 ----QIASVDQSRDSLEGNKTVWEQVSDGFEQIKIGNYEVPSRSYvGRFNFKGADQQKFVK---DLSGGERGRLHLALTL 459
Cdd:PRK13649 82 qirkKVGLVFQFPESQLFEETVLKDVAFGPQNFGVSQEEAEALAR-EKLALVGISESLFEKnpfELSGGQMRRVAIAGIL 160
|
170
....*....|....*..
gi 15599791 460 KQGGNVLLLDEPSNDLD 476
Cdd:PRK13649 161 AMEPKILVLDEPTAGLD 177
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-500 |
3.72e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.79 E-value: 3.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 19 REILKDISLSFFPGAKIGVLGLNGAGKS-TLLRIM----------AGVDTEIEGEA---------RPMPGINVGYLPQEP 78
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvTALSILrllpsppvvyPSGDIRFHGESllhaseqtlRGVRGNKIAMIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 79 --KLDPQATVRdiveeavgqiKQaqarLDEVYAAYAepdadfdALAAEQAKLEaILQAsdghnLER-QLEVAADALRLPP 155
Cdd:PRK15134 102 mvSLNPLHTLE----------KQ----LYEVLSLHR-------GMRREAARGE-ILNC-----LDRvGIRQAAKRLTDYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 156 wdakvEHLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPG----TVVAITHD----RYFLDNVAg 227
Cdd:PRK15134 155 -----HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelnmGLLFITHNlsivRKLADRVA- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 228 wILEldrgHGIPFEGNYSGWLESkaarlaqeAKQEASHAKAMKAELEwvrqGAKGRQAKSKARLQRFEELQsqefqkrse 307
Cdd:PRK15134 229 -VMQ----NGRCVEQNRAATLFS--------APTHPYTQKLLNSEPS----GDPVPLPEPASPLLDVEQLQ--------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 308 tneIYIPAGPRLGDKVIELHNVTKgygdrvlidNLSLSIPKGAIVGVIGGNGAGKST----LFRMLtgkeqPDSGTIEI- 382
Cdd:PRK15134 283 ---VAFPIRKGILKRTVDHNVVVK---------NISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFd 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 383 GETV-------------QIASVDQSRDS-LEGNKTVWEQVSDGFE----QIKIGNYEVPSRSYVGRFNFKGADQQKFVKD 444
Cdd:PRK15134 346 GQPLhnlnrrqllpvrhRIQVVFQDPNSsLNPRLNVLQIIEEGLRvhqpTLSAAQREQQVIAVMEEVGLDPETRHRYPAE 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599791 445 LSGGERGRLHLALTLKQGGNVLLLDEPSNDLDvETLRALEEALL-----DFPGAAIVISHD 500
Cdd:PRK15134 426 FSGGQRQRIAIARALILKPSLIILDEPTSSLD-KTVQAQILALLkslqqKHQLAYLFISHD 485
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
16-195 |
4.14e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 52.66 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 16 PPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpMPGINVGYLPQEPKLDPQATV--------R 87
Cdd:PRK13657 345 DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRIL-IDGTDIRTVTRASLRRNIAVVfqdaglfnR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 88 DIVEEAvgQIKQAQARLDEVYaayaepdadfDALAAEQAkLEAILQASDGHNL---ERQLEvaadalrlppwdakvehLS 164
Cdd:PRK13657 424 SIEDNI--RVGRPDATDEEMR----------AAAERAQA-HDFIERKPDGYDTvvgERGRQ-----------------LS 473
|
170 180 190
....*....|....*....|....*....|.
gi 15599791 165 GGEKRRVALCRLLLSAPDMLLLDEPTNHLDA 195
Cdd:PRK13657 474 GGERQRLAIARALLKDPPILILDEATSALDV 504
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
13-241 |
4.51e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 51.55 E-value: 4.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 13 KIVPPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpmpginVGYLPQEPKLDPQATVRDIVEE 92
Cdd:PRK13645 18 KKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTI------VGDYAIPANLKKIKEVKRLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 93 A--VGQIKQAQARLDEVyaayaEPDADFDALAAEQAKLEAILQASDghnLERQLEVAADALRLPPWDakvehLSGGEKRR 170
Cdd:PRK13645 92 IglVFQFPEYQLFQETI-----EKDIAFGPVNLGENKQEAYKKVPE---LLKLVQLPEDYVKRSPFE-----LSGGQKRR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599791 171 VALCRLLLSAPDMLLLDEPTNHLDA----DSVAWLEHFLHDFPGTVVAITHDRYFLDNVAGWILELDRGH----GIPFE 241
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPkgeeDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKvisiGSPFE 237
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
324-386 |
4.83e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 52.15 E-value: 4.83e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599791 324 IELHNVTKGY-GDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETV 386
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRV 67
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
324-501 |
4.91e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.99 E-value: 4.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGY--GDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDsGTIEI-GETVQIASVDQSRD---- 396
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIdGVSWNSVTLQTWRKafgv 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 397 ----------SLEGNKTVWEQVSDgfEQIKIGNYEVPSRSYVGRFnfkgADQQKFVKD-----LSGGERGRLHLALTLKQ 461
Cdd:TIGR01271 1297 ipqkvfifsgTFRKNLDPYEQWSD--EEIWKVAEEVGLKSVIEQF----PDKLDFVLVdggyvLSNGHKQLMCLARSILS 1370
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15599791 462 GGNVLLLDEPSNDLDVETLRALEEALLD-FPGAAIVISHDR 501
Cdd:TIGR01271 1371 KAKILLLDEPSAHLDPVTLQIIRKTLKQsFSNCTVILSEHR 1411
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
320-539 |
5.65e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 51.24 E-value: 5.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 320 GDKVIELHNVTKGYGD------RVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTI--------EIGET 385
Cdd:PRK13633 1 MNEMIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVyvdgldtsDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 386 VQIAS----VDQSRDSLEGNKTVWEQVSDGFEQIKIGNYEVPSR-----SYVGRFNFKgadqqKFVKD-LSGGERGRLHL 455
Cdd:PRK13633 81 WDIRNkagmVFQNPDNQIVATIVEEDVAFGPENLGIPPEEIRERvdeslKKVGMYEYR-----RHAPHlLSGGQKQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 456 ALTLKQGGNVLLLDEPSNDLD----VETLRALEEALLDFPGAAIVISHdrwFL------DRIATHilsyeDDGKVTfFEG 525
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDpsgrREVVNTIKELNKKYGITIILITH---YMeeaveaDRIIVM-----DSGKVV-MEG 226
|
250
....*....|....*.
gi 15599791 526 NYTEF--EADRKKRLG 539
Cdd:PRK13633 227 TPKEIfkEVEMMKKIG 242
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
22-218 |
6.58e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 51.25 E-value: 6.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEArpmpginvgylpqepKLDPQAtvrdIVEEAVGQIKQaq 101
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKV---------------KIDGEL----LTAENVWNLRR-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 102 arldEVYAAYAEPDADF-DALAAEQAKLEAILQASDGHNLERQLEVAADALRLPPWDAK-VEHLSGGEKRRVALCRLLLS 179
Cdd:PRK13642 82 ----KIGMVFQNPDNQFvGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTRePARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15599791 180 APDMLLLDEPTNHLDADSVAWLEHFLHDFPG----TVVAITHD 218
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIHEIKEkyqlTVLSITHD 200
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
331-484 |
6.65e-07 |
|
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: 49.95 E-value: 6.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 331 KGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKeqpdsgtieIGETVQIasvdqsrdslEGNKTVweqvsD 410
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR---------TEGNVSV----------EGDIHY-----N 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 411 GFEQIKIGNYEVPSRSYVG---------------RF--NFKGADqqkFVKDLSGGERGRLHLALTLKQGGNVLLLDEPSN 473
Cdd:cd03233 71 GIPYKEFAEKYPGEIIYVSeedvhfptltvretlDFalRCKGNE---FVRGISGGERKRVSIAEALVSRASVLCWDNSTR 147
|
170
....*....|.
gi 15599791 474 DLDVETlrALE 484
Cdd:cd03233 148 GLDSST--ALE 156
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
334-498 |
7.73e-07 |
|
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: 49.55 E-value: 7.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 334 GDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEqpDSGTIE---------IGETVQ--IASVDQSrDSLEGNK 402
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRK--TAGVITgeilingrpLDKNFQrsTGYVEQQ-DVHSPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 403 TVWEQVsdgfeqikignyevpsrsyvgRFNFKgadqqkfVKDLSGGERGRLHLALTLKQGGNVLLLDEPSNDLD------ 476
Cdd:cd03232 95 TVREAL---------------------RFSAL-------LRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDsqaayn 146
|
170 180
....*....|....*....|...
gi 15599791 477 -VETLRALEEAlldfpGAAIVIS 498
Cdd:cd03232 147 iVRFLKKLADS-----GQAILCT 164
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
16-236 |
8.86e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 50.51 E-value: 8.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 16 PPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpmpginVGylpqEPKLDPQATVRDI--VEEA 93
Cdd:PRK13649 17 PFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVR------VD----DTLITSTSKNKDIkqIRKK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 94 VG---QIKQAQARLDEVYAAYAEPDADF-------DALAAEQAKLEAILQASDGHNlerqlevaadalrlpPWDakvehL 163
Cdd:PRK13649 87 VGlvfQFPESQLFEETVLKDVAFGPQNFgvsqeeaEALAREKLALVGISESLFEKN---------------PFE-----L 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599791 164 SGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHF---LHDFPGTVVAITHDRYFLDNVAGWILELDRGH 236
Cdd:PRK13649 147 SGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLfkkLHQSGMTIVLVTHLMDDVANYADFVYVLEKGK 222
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
163-217 |
1.07e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.95 E-value: 1.07e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 15599791 163 LSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPG----TVVAITH 217
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkadkTIITIAH 1417
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
324-500 |
1.15e-06 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 49.84 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVtkGYGDRVLidNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGkEQPDSGTIEIGETvQIASVDQS--------- 394
Cdd:COG4138 1 LQLNDV--AVAGRLG--PISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGR-PLSDWSAAelarhrayl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 395 --RDSLEGNKTVW-------------EQVSDGFEQIkignyevpsrsyVGRFNFkgADQ-QKFVKDLSGGERGRLHLALT 458
Cdd:COG4138 75 sqQQSPPFAMPVFqylalhqpagassEAVEQLLAQL------------AEALGL--EDKlSRPLTQLSGGEWQRVRLAAV 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15599791 459 LKQ-------GGNVLLLDEPSNDLDVETLRALEEALLDF--PGAAIVIS-HD 500
Cdd:COG4138 141 LLQvwptinpEGQLLLLDEPMNSLDVAQQAALDRLLRELcqQGITVVMSsHD 192
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-190 |
1.27e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 51.17 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEAR----------PMPGIN--VGYLPQEPKLD---PQ 83
Cdd:COG1129 265 GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRldgkpvrirsPRDAIRagIAYVPEDRKGEglvLD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 84 ATVRDIVeeavgqikqAQARLDEVYAAYAEPDADFDALAAEQAKleailqasdghnlerQLEVaadalRLPPWDAKVEHL 163
Cdd:COG1129 345 LSIRENI---------TLASLDRLSRGGLLDRRRERALAEEYIK---------------RLRI-----KTPSPEQPVGNL 395
|
170 180
....*....|....*....|....*..
gi 15599791 164 SGGEKRRVALCRLLLSAPDMLLLDEPT 190
Cdd:COG1129 396 SGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
322-380 |
1.43e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 49.99 E-value: 1.43e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 15599791 322 KVIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTI 380
Cdd:PRK11300 4 PLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTI 62
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
324-499 |
1.47e-06 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 49.46 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYGDR--VLI-DNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETV----------QIA 389
Cdd:cd03249 1 IEFKNVSFRYPSRpdVPIlKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLdGVDIrdlnlrwlrsQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 390 SVDQSRDSLEGnkTVweqvsdgFEQIKIGNY-----EVPSRSyvgrfnfKGADQQKFVKD---------------LSGGE 449
Cdd:cd03249 81 LVSQEPVLFDG--TI-------AENIRYGKPdatdeEVEEAA-------KKANIHDFIMSlpdgydtlvgergsqLSGGQ 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15599791 450 RGRLHLALTLKQGGNVLLLDEPSNDLDVETLRALEEALLDFPGA--AIVISH 499
Cdd:cd03249 145 KQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGrtTIVIAH 196
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
18-196 |
1.47e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 50.49 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEArpmpginvgYLPQEPKLDPQATVRDIVEeavgqi 97
Cdd:PRK11432 18 SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQI---------FIDGEDVTHRSIQQRDICM------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 98 kqaqarldeVYAAYAE-PDADFDALAAEQAKLEAILQAsdghnlERQLEVAaDALRLPPW----DAKVEHLSGGEKRRVA 172
Cdd:PRK11432 83 ---------VFQSYALfPHMSLGENVGYGLKMLGVPKE------ERKQRVK-EALELVDLagfeDRYVDQISGGQQQRVA 146
|
170 180
....*....|....*....|....
gi 15599791 173 LCRLLLSAPDMLLLDEPTNHLDAD 196
Cdd:PRK11432 147 LARALILKPKVLLFDEPLSNLDAN 170
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
17-198 |
1.79e-06 |
|
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: 48.80 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 17 PKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdteIEGEARPMPGINVGYLPqepkldpqatvrdiveeavgq 96
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR---TEGNVSVEGDIHYNGIP--------------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 97 ikqaqarldevyaaYAEpdadfdalAAEQAKLEAIL-QASDGHN----LERQLEVAADALRlppwDAKVEHLSGGEKRRV 171
Cdd:cd03233 74 --------------YKE--------FAEKYPGEIIYvSEEDVHFptltVRETLDFALRCKG----NEFVRGISGGERKRV 127
|
170 180
....*....|....*....|....*..
gi 15599791 172 ALCRLLLSAPDMLLLDEPTNHLDADSV 198
Cdd:cd03233 128 SIAEALVSRASVLCWDNSTRGLDSSTA 154
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
324-476 |
1.86e-06 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 49.20 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVTKGYgdrvliDNL----SLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQIASVDQSRDSL 398
Cdd:PRK10771 2 LKLTDITWLY------HHLpmrfDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLnGQDHTTTPPSRRPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 399 ---EGN----KTVWEQVSDGFEqikignyevPSRsyvgRFNfkgADQQKFVKD-----------------LSGGERGRLH 454
Cdd:PRK10771 76 lfqENNlfshLTVAQNIGLGLN---------PGL----KLN---AAQREKLHAiarqmgiedllarlpgqLSGGQRQRVA 139
|
170 180
....*....|....*....|..
gi 15599791 455 LALTLKQGGNVLLLDEPSNDLD 476
Cdd:PRK10771 140 LARCLVREQPILLLDEPFSALD 161
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-477 |
1.92e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.70 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 1 MAQYVYTMHRVGKIVPPKREiLKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV------DTEI--EGEarpmpginvg 72
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKA-LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVyphgtyEGEIifEGE---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 73 ylPQEPKldpqaTVRDIVEEAVGQIKQAQARLDEVYAAY-----AEPDA----DFDALAAEQAKleailqasdghnLERQ 143
Cdd:PRK13549 70 --ELQAS-----NIRDTERAGIAIIHQELALVKELSVLEniflgNEITPggimDYDAMYLRAQK------------LLAQ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 144 LEVAADAlrlppwDAKVEHLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPGTVVA---ITHDry 220
Cdd:PRK13549 131 LKLDINP------ATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIAciyISHK-- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 221 fLDNV---AGWILELDRGHGIpfegnysgwleskaarlAQEAKQEASHAK--AMKAelewvrqgakGRqakskarlqrfe 295
Cdd:PRK13549 203 -LNEVkaiSDTICVIRDGRHI-----------------GTRPAAGMTEDDiiTMMV----------GR------------ 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 296 elqsqefqkrsETNEIYiPAGPR-LGDKVIELHNVTKGYGD---RVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTG 371
Cdd:PRK13549 243 -----------ELTALY-PREPHtIGEVILEVRNLTAWDPVnphIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 372 KEQPDS-GTIEI-GETVQ-----------IASV--DQSRD------SLEGNKTV--------WEQVSDGFEQIKIgnyev 422
Cdd:PRK13549 311 AYPGRWeGEIFIdGKPVKirnpqqaiaqgIAMVpeDRKRDgivpvmGVGKNITLaaldrftgGSRIDDAAELKTI----- 385
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 15599791 423 psRSYVGRFNFKGADQQKFVKDLSGGERGRLHLALTLKQGGNVLLLDEPSNDLDV 477
Cdd:PRK13549 386 --LESIQRLKVKTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDV 438
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-218 |
2.06e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 49.26 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdTEIEGEARpMPGiNVGYLPQepkldpqatvrDIVEEAVgQIK 98
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVR-VEG-RVEFFNQ-----------NIYERRV-NLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 99 QAQARLDEVYAA-YAEPDADFDALA------AEQAKLEailqasdghnLERQLEVAADALRLppWDaKVEH--------L 163
Cdd:PRK14258 85 RLRRQVSMVHPKpNLFPMSVYDNVAygvkivGWRPKLE----------IDDIVESALKDADL--WD-EIKHkihksaldL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15599791 164 SGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFP----GTVVAITHD 218
Cdd:PRK14258 152 SGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrseLTMVIVSHN 210
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
21-303 |
2.25e-06 |
|
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: 49.47 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRI---MAGVDTEIEgearpMPGINVGYLP-QEPKldpqatvrdiveEAVGQ 96
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAflrLLNTEGDIQ-----IDGVSWNSVPlQKWR------------KAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 97 IKQaqarldEVYAAYAEPDADFDALaaEQAKLEAILQASDGHNLERQLEVAADALRLPPWDAKVEhLSGGEKRRVALCRL 176
Cdd:cd03289 82 IPQ------KVFIFSGTFRKNLDPY--GKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCV-LSHGHKQLMCLARS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 177 LLSAPDMLLLDEPTNHLDADSVAWLEHFL-HDFPGTVVAITHDRyfldnvAGWILELDRGHGIpfEGNYSGWLESKAARL 255
Cdd:cd03289 153 VLSKAKILLLDEPSAHLDPITYQVIRKTLkQAFADCTVILSEHR------IEAMLECQRFLVI--EENKVRQYDSIQKLL 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 15599791 256 AQEA--KQEASHAKAMKAeleWVRQGAKGRQAKSKARLQRFEELQSQEFQ 303
Cdd:cd03289 225 NEKShfKQAISPSDRLKL---FPRRNSSKSKRKPRPQIQALQEETEEEVQ 271
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
321-369 |
2.86e-06 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 48.88 E-value: 2.86e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 15599791 321 DKVIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRML 369
Cdd:COG1117 9 EPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCL 57
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
323-516 |
3.18e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 48.33 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 323 VIELHNVTKGY-GDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGE--------------TVQ 387
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhditrlknrevpflRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 388 IASVDQSRDSLEgNKTVWEQVSDGFEQIKIGNYEVPSRSYVGRFNFKGADQQK-FVKDLSGGERGRLHLALTLKQGGNVL 466
Cdd:PRK10908 81 IGMIFQDHHLLM-DRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKnFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15599791 467 LLDEPSNDLDVE----TLRALEEalLDFPGAAIVI-SHDRWFLDRIATHILSYED 516
Cdd:PRK10908 160 LADEPTGNLDDAlsegILRLFEE--FNRVGVTVLMaTHDIGLISRRSYRMLTLSD 212
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
11-195 |
3.35e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 49.46 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 11 VGKIVPPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpMPGINVGYLpqEPKLdpqatvRDIv 90
Cdd:PRK11650 9 VRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIW-IGGRVVNEL--EPAD------RDI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 91 eeavgqikqaqARLDEVYAAYaePDAD-FDALA-----AEQAKLEailqasdghnLERQLEVAADALRLPPW-DAKVEHL 163
Cdd:PRK11650 79 -----------AMVFQNYALY--PHMSvRENMAyglkiRGMPKAE----------IEERVAEAARILELEPLlDRKPREL 135
|
170 180 190
....*....|....*....|....*....|..
gi 15599791 164 SGGEKRRVALCRLLLSAPDMLLLDEPTNHLDA 195
Cdd:PRK11650 136 SGGQRQRVAMGRAIVREPAVFLFDEPLSNLDA 167
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
336-530 |
3.47e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.16 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 336 RVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGtiEIGETVQIASVDQS----RDSLEGNKTVW--EQVS 409
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEG--RVWAERSIAYVPQQawimNATVRGNILFFdeEDAA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 410 DGFEQIKIGNYEVPSRSYVG----RFNFKGAdqqkfvkDLSGGERGRLHLALTLKQGGNVLLLDEPSNDLDVET-LRALE 484
Cdd:PTZ00243 751 RLADAVRVSQLEADLAQLGGgletEIGEKGV-------NLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgERVVE 823
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15599791 485 EALLdfpGA-----AIVISHDRWFLDRiATHILSYEdDGKVTfFEGNYTEF 530
Cdd:PTZ00243 824 ECFL---GAlagktRVLATHQVHVVPR-ADYVVALG-DGRVE-FSGSSADF 868
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
22-194 |
3.80e-06 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 48.92 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDT------EIEG------------EARPmpgiNVGYLPQEPKLDPQ 83
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERptsgsvLVDGvdltalserelrAARR----KIGMIFQHFNLLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 84 ATVRDIVE---EAVGQIK-QAQARLDEVyaayaepdadfdalaaeqakleailqasdghnLER-QLEVAADALrlpPwda 158
Cdd:COG1135 97 RTVAENVAlplEIAGVPKaEIRKRVAEL--------------------------------LELvGLSDKADAY---P--- 138
|
170 180 190
....*....|....*....|....*....|....*.
gi 15599791 159 kvEHLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLD 194
Cdd:COG1135 139 --SQLSGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
19-214 |
4.17e-06 |
|
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: 49.72 E-value: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdTEIEGEARPMPGINVgylpQEPKLDPqatvrdiVEEAVGQIK 98
Cdd:TIGR02203 345 RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRF-YEPDSGQILLDGHDL----ADYTLAS-------LRRQVALVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 99 QAQARLDEVYA---AYAEPDAdfdalaAEQAKLEAILQASDGHNLERQLEVAADAlrlpPWDAKVEHLSGGEKRRVALCR 175
Cdd:TIGR02203 413 QDVVLFNDTIAnniAYGRTEQ------ADRAEIERALAAAYAQDFVDKLPLGLDT----PIGENGVLLSGGQRQRLAIAR 482
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15599791 176 LLLSAPDMLLLDEPTNHLDADS----VAWLEHFLHDFPGTVVA 214
Cdd:TIGR02203 483 ALLKDAPILILDEATSALDNESerlvQAALERLMQGRTTLVIA 525
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
22-234 |
4.38e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 48.55 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------------AGVDTEIEG---EARPmpgiNVGYLPQEPklDPQaT 85
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMnallipsegkvyvDGLDTSDEEnlwDIRN----KAGMVFQNP--DNQ-I 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 86 VRDIVEEAVG--------QIKQAQARLDEVyaayaepdadfdalaaeqakleaiLQASDGHNLERQlevaadalrlPPwd 157
Cdd:PRK13633 99 VATIVEEDVAfgpenlgiPPEEIRERVDES------------------------LKKVGMYEYRRH----------AP-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 158 akveH-LSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDA----DSVAWLEHFLHDFPGTVVAITHdryFLDNVAgwilEL 232
Cdd:PRK13633 143 ----HlLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPsgrrEVVNTIKELNKKYGITIILITH---YMEEAV----EA 211
|
..
gi 15599791 233 DR 234
Cdd:PRK13633 212 DR 213
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
350-518 |
4.80e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 47.60 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 350 AIVGViggNGAGKSTLFR----MLTGKEQPDSgtieigetvqiaSVDQSRDSLEGNKTVWEQVSDGFEQIKIGNYEVpSR 425
Cdd:cd03240 26 LIVGQ---NGAGKTTIIEalkyALTGELPPNS------------KGGAHDPKLIREGEVRAQVKLAFENANGKKYTI-TR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 426 SYVgrfNFKGA------DQQKFVKD----LSGGERG------RLHLALTLKQGGNVLLLDEPSNDLDVETLR-----ALE 484
Cdd:cd03240 90 SLA---ILENVifchqgESNWPLLDmrgrCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEeslaeIIE 166
|
170 180 190
....*....|....*....|....*....|....
gi 15599791 485 EALLDFPGAAIVISHDRWFLDRiATHILSYEDDG 518
Cdd:cd03240 167 ERKSQKNFQLIVITHDEELVDA-ADHIYRVEKDG 199
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
22-194 |
5.06e-06 |
|
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: 49.30 E-value: 5.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLR-IMAGVDTEieGEARpMPGINVGYLP---------------QEP--KLDPQ 83
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLaLLRLIPSE--GEIR-FDGQDLDGLSrralrplrrrmqvvfQDPfgSLSPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 84 ATVRDIVEE--AVGQIKQ-AQARLDEVYAAyaepdadfdalaaeqakleailqasdghnLErqlEV---AADALRLPpwd 157
Cdd:COG4172 379 MTVGQIIAEglRVHGPGLsAAERRARVAEA-----------------------------LE---EVgldPAARHRYP--- 423
|
170 180 190
....*....|....*....|....*....|....*...
gi 15599791 158 akveH-LSGGEKRRVALCRLLLSAPDMLLLDEPTNHLD 194
Cdd:COG4172 424 ----HeFSGGQRQRIAIARALILEPKLLVLDEPTSALD 457
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
9-194 |
6.14e-06 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 48.64 E-value: 6.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 9 HRVGKIVP-PKREI--LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpMPGINVGYLPqEPKLdpQAT 85
Cdd:PRK11153 5 KNISKVFPqGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVL-VDGQDLTALS-EKEL--RKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 86 VRDIveeavGQIKQ----AQARldEVYAAYA-------EPDADFDALAAEqakLEAILQASDGHNlerqlevaadalRLP 154
Cdd:PRK11153 81 RRQI-----GMIFQhfnlLSSR--TVFDNVAlplelagTPKAEIKARVTE---LLELVGLSDKAD------------RYP 138
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15599791 155 pwdakvEHLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLD 194
Cdd:PRK11153 139 ------AQLSGGQKQRVAIARALASNPKVLLCDEATSALD 172
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
22-218 |
6.26e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 48.49 E-value: 6.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpMPGINVGYLPQepkldpqATVRDIVEEAVGQIKQAQ 101
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVL-IDGVDIAKISD-------AELREVRRKKIAMVFQSF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 102 ARLDEVYAAyaepdaDFDALAAEQAKLEAILQASDGHNLERQLEVAADALRLPpwdakvEHLSGGEKRRVALCRLLLSAP 181
Cdd:PRK10070 116 ALMPHMTVL------DNTAFGMELAGINAEERREKALDALRQVGLENYAHSYP------DELSGGMRQRVGLARALAINP 183
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15599791 182 DMLLLDEPTNHLDADSVAWLEHFLHDFPG----TVVAITHD 218
Cdd:PRK10070 184 DILLMDEAFSALDPLIRTEMQDELVKLQAkhqrTIVFISHD 224
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
328-499 |
7.56e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.57 E-value: 7.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 328 NVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQIASvdqSRDSLEGNKTVWE 406
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFqGKEIDFKS---SKEALENGISMVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 407 QvsdgfEQIKIGNYEVPSRSYVGRFNFKG--ADQQKFVKD--------------------LSGGERGRLHLALTLKQGGN 464
Cdd:PRK10982 80 Q-----ELNLVLQRSVMDNMWLGRYPTKGmfVDQDKMYRDtkaifdeldididprakvatLSVSQMQMIEIAKAFSYNAK 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 15599791 465 VLLLDEPSNDL---DVETLRALEEALLDFPGAAIVISH 499
Cdd:PRK10982 155 IVIMDEPTSSLtekEVNHLFTIIRKLKERGCGIVYISH 192
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-194 |
8.94e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.46 E-value: 8.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpmpginvgylpqepkLDPQATVrdiveeavgqIKQAQ 101
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVT---------------LDGHEVV----------TRSPQ 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 102 ARLDEvYAAYAEPDADFDAL-----AAEQAKLEAILQAS-DGHNLERQLEVAA--DALRL-----PPWDAKVEHLSGGEK 168
Cdd:PRK10762 323 DGLAN-GIVYISEDRKRDGLvlgmsVKENMSLTALRYFSrAGGSLKHADEQQAvsDFIRLfniktPSMEQAIGLLSGGNQ 401
|
170 180
....*....|....*....|....*.
gi 15599791 169 RRVALCRLLLSAPDMLLLDEPTNHLD 194
Cdd:PRK10762 402 QKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
337-522 |
8.96e-06 |
|
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: 48.59 E-value: 8.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 337 VLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETVQIASVDQsRDSLeGNKTVWEQV--SDGFEQ 414
Cdd:TIGR00954 466 VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQ-RPYM-TLGTLRDQIiyPDSSED 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 415 IKIGNY---------EVPSRSYVGRFNFKGADQQKFVKDLSGGERGRLHLALTLKQGGNVLLLDEPSNDLDVETLRALEE 485
Cdd:TIGR00954 544 MKRRGLsdkdleqilDNVQLTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYR 623
|
170 180 190
....*....|....*....|....*....|....*..
gi 15599791 486 ALLDFPGAAIVISHdRWFLDRIATHILSYEDDGKVTF 522
Cdd:TIGR00954 624 LCREFGITLFSVSH-RKSLWKYHEYLLYMDGRGGYQF 659
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
22-238 |
1.03e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 47.52 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRimagvdtEIEGEARPMPG-INV-GYlpqepKLDPQATVRDI--VEEAVG-- 95
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQ-------HFNALLKPSSGtITIaGY-----HITPETGNKNLkkLRKKVSlv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 96 -QIKQAQARLDEVYAayaepDADFDAL---AAEQAKLEAILQasdghnLERQLEVAADALRLPPWDakvehLSGGEKRRV 171
Cdd:PRK13641 91 fQFPEAQLFENTVLK-----DVEFGPKnfgFSEDEAKEKALK------WLKKVGLSEDLISKSPFE-----LSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599791 172 ALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPG---TVVAITHDryfLDNVAGW---ILELDRGHGI 238
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaghTVILVTHN---MDDVAEYaddVLVLEHGKLI 224
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
329-490 |
1.06e-05 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 46.94 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 329 VTKGY----GDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTI-----EIGETVQIASVDQSRDSLE 399
Cdd:cd03290 3 VTNGYfswgSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnkNESEPSFEATRSRNRYSVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 400 G--------NKTVWEQVSDGF----EQIKIGNYEVPSRSYVGRFNFkgADQQKFVK---DLSGGERGRLHLALTLKQGGN 464
Cdd:cd03290 83 YaaqkpwllNATVEENITFGSpfnkQRYKAVTDACSLQPDIDLLPF--GDQTEIGErgiNLSGGQRQRICVARALYQNTN 160
|
170 180
....*....|....*....|....*..
gi 15599791 465 VLLLDEPSNDLDVE-TLRALEEALLDF 490
Cdd:cd03290 161 IVFLDDPFSALDIHlSDHLMQEGILKF 187
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
18-217 |
1.09e-05 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 46.95 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AGVdtEIEGEARPM------PGIN-------VGYLPQE 77
Cdd:COG1117 23 DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndliPGA--RVEGEILLDgediydPDVDvvelrrrVGMVFQK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 78 P------------------KLDPQATVRDIVEEAvgqIKQAqARLDEVyaayaepdADfdalaaeqakleaILQASdghn 139
Cdd:COG1117 101 PnpfpksiydnvayglrlhGIKSKSELDEIVEES---LRKA-ALWDEV--------KD-------------RLKKS---- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 140 lerqlevaadALRLppwdakvehlSGGEKRRvaLC--RLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPG--TVVAI 215
Cdd:COG1117 152 ----------ALGL----------SGGQQQR--LCiaRALAVEPEVLLMDEPTSALDPISTAKIEELILELKKdyTIVIV 209
|
..
gi 15599791 216 TH 217
Cdd:COG1117 210 TH 211
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
336-500 |
1.10e-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: 45.81 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 336 RVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRmltgkeqpdsgtiEIGETVQIASVDQSRDSlegnktvweqvsdgfeQI 415
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTILD-------------AIGLALGGAQSATRRRS----------------GV 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 416 KIGnYEVPSRSYvgRFNFkgadqqkFVKDLSGGERGRLHLALTL----KQGGNVLLLDEPSNDLDVETLRALEEALLDF- 490
Cdd:cd03227 59 KAG-CIVAAVSA--ELIF-------TRLQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHl 128
|
170
....*....|..
gi 15599791 491 -PGA-AIVISHD 500
Cdd:cd03227 129 vKGAqVIVITHL 140
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
21-226 |
1.11e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 47.42 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV------DTEIEGEArpmpginvgylpqepkldpqatvrdIVEEAV 94
Cdd:PRK13650 22 TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLleaesgQIIIDGDL-------------------------LTEENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 95 GQIKQaqarldEVYAAYAEPDADFDALAAEQA---KLEailqaSDGHNLERQLEVAADALRLPPW----DAKVEHLSGGE 167
Cdd:PRK13650 77 WDIRH------KIGMVFQNPDNQFVGATVEDDvafGLE-----NKGIPHEEMKERVNEALELVGMqdfkEREPARLSGGQ 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599791 168 KRRVALCRLLLSAPDMLLLDEPTNHLDA----DSVAWLEHFLHDFPGTVVAITHDryfLDNVA 226
Cdd:PRK13650 146 KQRVAIAGAVAMRPKIIILDEATSMLDPegrlELIKTIKGIRDDYQMTVISITHD---LDEVA 205
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
7-236 |
1.26e-05 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 46.93 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 7 TMHRVGKIVPP--KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdteIEGEARPMPGInvgylpqepkldpqa 84
Cdd:PRK09984 3 TIIRVEKLAKTfnQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL---ITGDKSAGSHI--------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 85 tvrdiveEAVGQIKQAQARL-DEVYAAYAEPDADFDA--LAAEQAKLEAILQASDGHN----------LERQLEVAADAL 151
Cdd:PRK09984 65 -------ELLGRTVQREGRLaRDIRKSRANTGYIFQQfnLVNRLSVLENVLIGALGSTpfwrtcfswfTREQKQRALQAL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 152 RLPPW----DAKVEHLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPG----TVVAITHDRYFLD 223
Cdd:PRK09984 138 TRVGMvhfaHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndgiTVVVTLHQVDYAL 217
|
250
....*....|...
gi 15599791 224 NVAGWILELDRGH 236
Cdd:PRK09984 218 RYCERIVALRQGH 230
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
20-194 |
1.27e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 47.09 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV----DTEIEGEARPMPGINVGYLPQEPKL---DPQATVRDivEE 92
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMieptSGELLIDDHPLHFGDYSYRSQRIRMifqDPSTSLNP--RQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 93 AVGQIKQAQARLdevyaayaepDADFDALAAEQAKLEAIlqasdghnleRQLEVAADALRLPPwdakvEHLSGGEKRRVA 172
Cdd:PRK15112 105 RISQILDFPLRL----------NTDLEPEQREKQIIETL----------RQVGLLPDHASYYP-----HMLAPGQKQRLG 159
|
170 180
....*....|....*....|..
gi 15599791 173 LCRLLLSAPDMLLLDEPTNHLD 194
Cdd:PRK15112 160 LARALILRPKVIIADEALASLD 181
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-197 |
1.40e-05 |
|
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: 48.02 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpMPGINVG------------YLPQEPKLDpQATVRd 88
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEII-IDGLNIAkiglhdlrfkitIIPQDPVLF-SGSLR- 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 89 iveeavgqikqaqARLDEvYAAYAEPDAdfdALAAEQAKLEAILQA-SDGHNLErqlevAADAlrlppwdakVEHLSGGE 167
Cdd:TIGR00957 1378 -------------MNLDP-FSQYSDEEV---WWALELAHLKTFVSAlPDKLDHE-----CAEG---------GENLSVGQ 1426
|
170 180 190
....*....|....*....|....*....|
gi 15599791 168 KRRVALCRLLLSAPDMLLLDEPTNHLDADS 197
Cdd:TIGR00957 1427 RQLVCLARALLRKTKILVLDEATAAVDLET 1456
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-235 |
1.77e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 46.58 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV----DTEIEGEARpmpginVGYLPQEpkldpqatvrdiveeaV 94
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiyDSKIKVDGK------VLYFGKD----------------I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 95 GQIKQAQARlDEVYAAYAEPDAdFDALAAeqakLEAILQASDGHNLERQLEV---AADALR-LPPW-------DAKVEHL 163
Cdd:PRK14246 81 FQIDAIKLR-KEVGMVFQQPNP-FPHLSI----YDNIAYPLKSHGIKEKREIkkiVEECLRkVGLWkevydrlNSPASQL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599791 164 SGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPG--TVVAITHDRYFLDNVAGWILELDRG 235
Cdd:PRK14246 155 SGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNG 228
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
14-194 |
1.83e-05 |
|
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: 47.51 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 14 IVPPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-DTEIEGEA----------RPMPGINVG--YLPQEPKL 80
Cdd:TIGR02633 268 VINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVfingkpvdirNPAQAIRAGiaMVPEDRKR 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 81 D---PQATVRDIVEEAVGQIKQAQARLDEvyaayaepdadfdalAAEQAKLEAILQasdghnlerQLEVAADALRLPpwd 157
Cdd:TIGR02633 348 HgivPILGVGKNITLSVLKSFCFKMRIDA---------------AAELQIIGSAIQ---------RLKVKTASPFLP--- 400
|
170 180 190
....*....|....*....|....*....|....*..
gi 15599791 158 akVEHLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLD 194
Cdd:TIGR02633 401 --IGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
22-194 |
1.96e-05 |
|
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: 45.50 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpmpginvgylpqepkLDPQATVRDIVEEAVgqikqaQ 101
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEIT---------------LDGKPVTRRSPRDAI------R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 102 ARLdevyaayaepdadfdALAAEQAKLEAI-LQASDGHNLerqlevaadALRLppwdakveHLSGGEKRRVALCRLLLSA 180
Cdd:cd03215 75 AGI---------------AYVPEDRKREGLvLDLSVAENI---------ALSS--------LLSGGNQQKVVLARWLARD 122
|
170
....*....|....
gi 15599791 181 PDMLLLDEPTNHLD 194
Cdd:cd03215 123 PRVLILDEPTRGVD 136
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
339-500 |
2.66e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 46.31 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 339 IDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGE-TV--------------QIASVDQSRDSLEGNKT 403
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDiTIthktkdkyirpvrkRIGMVFQFPESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 404 VWEQVSDGFEQIKIGNYEVPSRSY--VGRFNFKGADQQKFVKDLSGGERGRLHLALTLKQGGNVLLLDEPSNDLD----V 477
Cdd:PRK13646 103 VEREIIFGPKNFKMNLDEVKNYAHrlLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDpqskR 182
|
170 180
....*....|....*....|...
gi 15599791 478 ETLRALEEALLDFPGAAIVISHD 500
Cdd:PRK13646 183 QVMRLLKSLQTDENKTIILVSHD 205
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
163-223 |
2.81e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 45.29 E-value: 2.81e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599791 163 LSGGEKR------RVALCRLLLSAPDMLLLDEPTNHLDADSVAW-----LEHFLHDFPGTVVAITHDRYFLD 223
Cdd:cd03240 116 CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEEslaeiIEERKSQKNFQLIVITHDEELVD 187
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
285-486 |
2.82e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 46.76 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 285 AKSKA-----RLQRFeeLQSQEFQKRSETNEIyipagprLGDKVIELHN---VTKGYGDRVLIDNLSLSIPKGAIVGVIG 356
Cdd:PRK11174 313 AKAQAvgaaeSLVTF--LETPLAHPQQGEKEL-------ASNDPVTIEAedlEILSPDGKTLAGPLNFTLPAGQRIALVG 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 357 GNGAGKSTLFRMLTGKeQPDSGTIEIGET-----------VQIASVDQS----RDSLEGNKTV-WEQVSDgfEQIkignY 420
Cdd:PRK11174 384 PSGAGKTSLLNALLGF-LPYQGSLKINGIelreldpeswrKHLSWVGQNpqlpHGTLRDNVLLgNPDASD--EQL----Q 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599791 421 EVPSRSYVGRF---NFKGADQQkfVKD----LSGGERGRLHLALTLKQGGNVLLLDEPSNDLDVET----LRALEEA 486
Cdd:PRK11174 457 QALENAWVSEFlplLPQGLDTP--IGDqaagLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSeqlvMQALNAA 531
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
323-380 |
2.99e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 45.25 E-value: 2.99e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 15599791 323 VIELHNVTKGYGDRVLIDnLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTI 380
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLFD-LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNI 57
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
22-235 |
3.06e-05 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 45.40 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEG---------------EARPMPGINVGYLPQEPKLDPQATV 86
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGkvhwsnknesepsfeATRSRNRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 87 RDIVEEAVGQIKQAQARLDevyAAYAEPDADfdalaaeqakleaILQASDghnlerQLEVAADALrlppwdakveHLSGG 166
Cdd:cd03290 97 ENITFGSPFNKQRYKAVTD---ACSLQPDID-------------LLPFGD------QTEIGERGI----------NLSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599791 167 EKRRVALCRLLLSAPDMLLLDEPTNHLD---ADSV--AWLEHFLHDFPGTVVAITHDRYFLDNvAGWILELDRG 235
Cdd:cd03290 145 QRQRICVARALYQNTNIVFLDDPFSALDihlSDHLmqEGILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
324-382 |
3.34e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 45.85 E-value: 3.34e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599791 324 IELHNVTKGYGDRV-----LIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI 382
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEW 66
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
327-507 |
3.95e-05 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 45.19 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 327 HNVTKGYGD-RVLID---NLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTI---------------------E 381
Cdd:PRK11629 9 DNLCKRYQEgSVQTDvlhNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifngqpmsklssaakaelrnqK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 382 IGETVQIASVDQSRDSLE--------GNKTVWEQVSDGFEQIKIGNYEvpSRSyvgrfnfkgadqQKFVKDLSGGERGRL 453
Cdd:PRK11629 89 LGFIYQFHHLLPDFTALEnvamplliGKKKPAEINSRALEMLAAVGLE--HRA------------NHRPSELSGGERQRV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15599791 454 HLALTLKQGGNVLLLDEPSNDLDVETLRALEEALLDF---PGAA-IVISHDRWFLDRI 507
Cdd:PRK11629 155 AIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnrlQGTAfLVVTHDLQLAKRM 212
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
139-223 |
4.21e-05 |
|
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: 43.90 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 139 NLERQLEVAADALRLPPWDAKVEHLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWL---------EHFLHDFP 209
Cdd:smart00382 37 DGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllleelrllLLLKSEKN 116
|
90
....*....|....
gi 15599791 210 GTVVAITHDRYFLD 223
Cdd:smart00382 117 LTVILTTNDEKDLG 130
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
19-225 |
4.34e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 45.17 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVD----------------TEIEGEARPMPGINVGYlpQEPKLDP 82
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyevtggtvefkgkdlLELSPEDRAGEGIFMAF--QYPVEIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 83 QATVRDIVEEAVGQIKQ--AQARLDEVyaayaepdaDFDALAAEQAKLeailqasdghnlerqLEVAADALRlppwDAKV 160
Cdd:PRK09580 92 GVSNQFFLQTALNAVRSyrGQEPLDRF---------DFQDLMEEKIAL---------------LKMPEDLLT----RSVN 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599791 161 EHLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADS---VAWLEHFLHDFPGTVVAITHDRYFLDNV 225
Cdd:PRK09580 144 VGFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDAlkiVADGVNSLRDGKRSFIIVTHYQRILDYI 211
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
348-509 |
4.86e-05 |
|
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: 43.52 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 348 KGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETVQIASVDQSRDSLEGNKTvweqvsdgfeqikignyevpsrsy 427
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGG------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 428 vgrfnfkgadqqkFVKDLSGGERGRLHLALTLKQGGNVLLLDEPSNDLDVET---------LRALEEALLDFPGAAIVIS 498
Cdd:smart00382 57 -------------KKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQeallllleeLRLLLLLKSEKNLTVILTT 123
|
170
....*....|.
gi 15599791 499 HDRWFLDRIAT 509
Cdd:smart00382 124 NDEKDLGPALL 134
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
320-500 |
5.18e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 45.34 E-value: 5.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 320 GDKVIELHNVTKGY--------GDRVL--IDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI-GETVQI 388
Cdd:PRK11308 2 QQPLLQAIDLKKHYpvkrglfkPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYqGQDLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 389 ASVDQSRD--------------SLEGNKTVWEQVSdgfEQIKIgNYEVPS-------RSYVGRFNFKGADQQKFVKDLSG 447
Cdd:PRK11308 82 ADPEAQKLlrqkiqivfqnpygSLNPRKKVGQILE---EPLLI-NTSLSAaerrekaLAMMAKVGLRPEHYDRYPHMFSG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599791 448 GERGRLHLALTLKQGGNVLLLDEPSNDLDVeTLRA--------LEEallDFPGAAIVISHD 500
Cdd:PRK11308 158 GQRQRIAIARALMLDPDVVVADEPVSALDV-SVQAqvlnlmmdLQQ---ELGLSYVFISHD 214
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
332-511 |
6.13e-05 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 44.57 E-value: 6.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 332 GYGDRVLIDNLSLSipKGAIVGVIGGNGAGKSTLFrmltgkeqpDSGTIEI-GETVQIASVDQSRDSLE-GNKTVWeqVS 409
Cdd:cd03279 13 PFREEQVIDFTGLD--NNGLFLICGPTGAGKSTIL---------DAITYALyGKTPRYGRQENLRSVFApGEDTAE--VS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 410 DGFeQIKIGNYEVpSRSYvgrfnfkGADQQKF------------------VKDLSGGERGRLHLALTL------KQGGNV 465
Cdd:cd03279 80 FTF-QLGGKKYRV-ERSR-------GLDYDQFtrivllpqgefdrflarpVSTLSGGETFLASLSLALalsevlQNRGGA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15599791 466 ----LLLDEPSNDLDVETLRALEEAL--LDFPGAAI-VISHDRWFLDRIATHI 511
Cdd:cd03279 151 rleaLFIDEGFGTLDPEALEAVATALelIRTENRMVgVISHVEELKERIPQRL 203
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-198 |
6.41e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 44.17 E-value: 6.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdteiegeARPMPGiNVGYLPQEPKLDPQATVRDI--VEEAVGQIK 98
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGL-------LNPEKG-EILFERQSIKKDLCTYQKQLcfVGHRSGINP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 99 QAQARLDEVYaayaepDADFDALAAEQAKLEAILqaSDGHNLerqlevaadalrlppwDAKVEHLSGGEKRRVALCRLLL 178
Cdd:PRK13540 88 YLTLRENCLY------DIHFSPGAVGITELCRLF--SLEHLI----------------DYPCGLLSSGQKRQVALLRLWM 143
|
170 180
....*....|....*....|
gi 15599791 179 SAPDMLLLDEPTNHLDADSV 198
Cdd:PRK13540 144 SKAKLWLLDEPLVALDELSL 163
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
13-200 |
6.66e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.87 E-value: 6.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 13 KIVPPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTE--IEGEARPMPGI--------NVGYLPQEPKLDP 82
Cdd:TIGR00956 770 KIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgvITGGDRLVNGRpldssfqrSIGYVQQQDLHLP 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 83 QATVRdiveEAVgqikQAQARL---DEVyaayaePDADFDALAAEQAKLeailqasdghnLErqLEVAADALRLPPWdak 159
Cdd:TIGR00956 850 TSTVR----ESL----RFSAYLrqpKSV------SKSEKMEYVEEVIKL-----------LE--MESYADAVVGVPG--- 899
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15599791 160 vEHLSGGEKRRVALCRLLLSAPDMLL-LDEPTNHLDADSvAW 200
Cdd:TIGR00956 900 -EGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQT-AW 939
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
163-194 |
6.77e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 45.04 E-value: 6.77e-05
10 20 30
....*....|....*....|....*....|..
gi 15599791 163 LSGGEKRRVALCRLLLSAPDMLLLDEPTNHLD 194
Cdd:PRK13637 145 LSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
164-227 |
9.01e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 44.72 E-value: 9.01e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599791 164 SGGEKRRVALCRLLLSAPDMLLLDEPTNHLD----ADSVAWLEHFLHDFPGTVVAITHDryfLDNVAG 227
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDvtvqAQIMTLLNELKREFNTAIIMITHD---LGVVAG 227
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
321-382 |
9.02e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 44.40 E-value: 9.02e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599791 321 DKVIELHNVTKGYGDRV---------LIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEI 382
Cdd:PRK15112 2 ETLLEVRNLSKTFRYRTgwfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLI 72
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
22-194 |
9.88e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 44.57 E-value: 9.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEARpMPGINV-GYLPQEPK----------------LDPQA 84
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELY-YQGQDLlKADPEAQKllrqkiqivfqnpygsLNPRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 85 TVRDIVEEAVgQIkqaqarldevyaayaepDADFDAlAAEQAKLEAILqasdghnlerqlevaadalrlppwdAKV---- 160
Cdd:PRK11308 110 KVGQILEEPL-LI-----------------NTSLSA-AERREKALAMM-------------------------AKVglrp 145
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15599791 161 EH-------LSGGEKRRVALCRLLLSAPDMLLLDEPTNHLD 194
Cdd:PRK11308 146 EHydryphmFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
35-218 |
9.99e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 43.46 E-value: 9.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 35 IGVLGLNGAGKSTLLRimaGVDTEIEGEARPMPG-----INVGylPQEPKLD--------------PQATVRDIVEEAVG 95
Cdd:COG0419 26 NLIVGPNGAGKSTILE---AIRYALYGKARSRSKlrsdlINVG--SEEASVElefehggkryrierRQGEFAEFLEAKPS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 96 QIKQAQARL--DEVYAAYAEpdadfdALAAEQAKLEAILQAsdghnLERQLEVAADALRLPPWDAKVEHLSGGEKRRVAL 173
Cdd:COG0419 101 ERKEALKRLlgLEIYEELKE------RLKELEEALESALEE-----LAELQKLKQEILAQLSGLDPIETLSGGERLRLAL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15599791 174 CRLLlsapdMLLLDepTNHLDADSVAWLEHFLHDfpgtVVAITHD 218
Cdd:COG0419 170 ADLL-----SLILD--FGSLDEERLERLLDALEE----LAIITHV 203
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
163-218 |
1.16e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 44.00 E-value: 1.16e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 15599791 163 LSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADSVAWLEHFLHDFPG--TVVAITHD 218
Cdd:PRK14243 152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEqyTIIIVTHN 209
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
324-500 |
1.16e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 43.46 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 324 IELHNVtKGYGDRVLIDnlslsIPKGaIVGVIGGNGAGKSTLFR----MLTGK-------------EQPDSGTIEI---- 382
Cdd:COG0419 5 LRLENF-RSYRDTETID-----FDDG-LNLIVGPNGAGKSTILEairyALYGKarsrsklrsdlinVGSEEASVELefeh 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 383 -----------GETVQIASVDQS--RDSLEG--NKTVWEQVSDGFEQIKignyEVPSRSYVGRFNFKGADQQKF------ 441
Cdd:COG0419 78 ggkryrierrqGEFAEFLEAKPSerKEALKRllGLEIYEELKERLKELE----EALESALEELAELQKLKQEILaqlsgl 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599791 442 --VKDLSGGERGRLHLALTLKqggnvLLLDEPSndLDVETLRALEEALLDfpgaAIVISHD 500
Cdd:COG0419 154 dpIETLSGGERLRLALADLLS-----LILDFGS--LDEERLERLLDALEE----LAIITHV 203
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
22-194 |
1.17e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 43.32 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGvdteiegearpmpginvgylpqepkldpqatvrdIVEEAVGQIKQAQ 101
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAG----------------------------------IMQPSSGNIYYKN 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 102 ARLDEVYAAYAEPDADFDALAAEQAKLEAILQASDGHNLERQLEVAADALRLPPW-DAKVEHLSGGEKRRVALCRLLLSA 180
Cdd:PRK13541 62 CNINNIAKPYCTYIGHNLGLKLEMTVFENLKFWSEIYNSAETLYAAIHYFKLHDLlDEKCYSLSSGMQKIVAIARLIACQ 141
|
170
....*....|....
gi 15599791 181 PDMLLLDEPTNHLD 194
Cdd:PRK13541 142 SDLWLLDEVETNLS 155
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
163-238 |
1.19e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 43.08 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 163 LSGGEKRRVALCRLLLSAPD--MLLLDEPTNHLDADSvawLEHFLHDFPG------TVVAITHDRYFLDNvAGWILELDR 234
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQD---INQLLEVIKGlidlgnTVILIEHNLDVLSS-ADWIIDFGP 163
|
....
gi 15599791 235 GHGI 238
Cdd:cd03238 164 GSGK 167
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
24-218 |
1.33e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 43.76 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 24 DISLSFFPGAKIGVLGLNGAGKSTLLRIMAgvdteieGEARPMPGiNVGYlpqepkldpqaTVRDIVEEAVGQIKQAQAR 103
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALS-------ARLAPDAG-EVHY-----------RMRDGQLRDLYALSEAERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 104 LdevyaaYAEPDADFdalaAEQAKLEAI-LQASDGHNL-ERQLEVA--------ADALRlppWDAKVE-----------H 162
Cdd:PRK11701 85 R------LLRTEWGF----VHQHPRDGLrMQVSAGGNIgERLMAVGarhygdirATAGD---WLERVEidaariddlptT 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599791 163 LSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDAdSVA-----WLEHFLHDFPGTVVAITHD 218
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDV-SVQarlldLLRGLVRELGLAVVIVTHD 211
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
339-500 |
1.42e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 44.25 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 339 IDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIgETVQIASVDQSR---------------DSLEGNKT 403
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLI-DGVDIAKISDAElrevrrkkiamvfqsFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 404 VWEQVSDGFEQIKIGNYEVPSRSY-----VGRFNFKgadqQKFVKDLSGGERGRLHLALTLKQGGNVLLLDEPSNDLDVE 478
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALdalrqVGLENYA----HSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180
....*....|....*....|....*.
gi 15599791 479 TLRALEEALLDFPG----AAIVISHD 500
Cdd:PRK10070 199 IRTEMQDELVKLQAkhqrTIVFISHD 224
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
32-80 |
1.53e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 42.56 E-value: 1.53e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 15599791 32 GAKIGVLGLNGAGKSTLLRIMAGVDtEIEGEARPMPGINVGYLPQEPKL 80
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQL-IPNGDNDEWDGITPVYKPQYIDL 72
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
163-232 |
1.63e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.62 E-value: 1.63e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599791 163 LSGGEKRRVALCRLLL---SAPDMLLLDEPTNHLDADSVAWLEHFLH---DFPGTVVAITHDryfLD--NVAGWILEL 232
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLHFDDIKKLLEVLQrlvDKGNTVVVIEHN---LDviKTADYIIDL 904
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
338-483 |
1.70e-04 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 44.27 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 338 LIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPD---SGTIEI-GETV------QIASVDQSRDSLEGNKTVWEQ 407
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLnGMPIdakemrAISAYVQQDDLFIPTLTVREH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 408 ---------------------VSDGFEQI--------KIGnyeVPSRsyvgrfnfkgadqqkfVKDLSGGERGRLHLALT 458
Cdd:TIGR00955 120 lmfqahlrmprrvtkkekrerVDEVLQALglrkcantRIG---VPGR----------------VKGLSGGERKRLAFASE 180
|
170 180 190
....*....|....*....|....*....|..
gi 15599791 459 LKQGGNVLLLDEPSNDLD-------VETLRAL 483
Cdd:TIGR00955 181 LLTDPPLLFCDEPTSGLDsfmaysvVQVLKGL 212
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
312-477 |
2.08e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.01 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 312 YIPAGPRLGDKVIELHNVT---KGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKE--QPDSGTIEI-GET 385
Cdd:NF040905 246 YPERTPKIGEVVFEVKNWTvyhPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKdGKE 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 386 VQIASVDQS-----------R--------DSLEGNKTV--WEQVS-----DGFEQIKIGNyevpsrSYVGRFNFKGADQQ 439
Cdd:NF040905 326 VDVSTVSDAidaglayvtedRkgyglnliDDIKRNITLanLGKVSrrgviDENEEIKVAE------EYRKKMNIKTPSVF 399
|
170 180 190
....*....|....*....|....*....|....*...
gi 15599791 440 KFVKDLSGGERGRLHLALTLKQGGNVLLLDEPSNDLDV 477
Cdd:NF040905 400 QKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDV 437
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-194 |
2.74e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.56 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEArpmpginvgylpqepKLDPQATVRDIVEEAvgqIKQAQ 101
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTI---------------TLHGKKINNHNANEA---INHGF 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 102 ARLDEVYAA---YAEPDADFDALAAEQAKLEAILQASDGHNLERQLEVAADALRL--PPWDAKVEHLSGGEKRRVALCRL 176
Cdd:PRK10982 326 ALVTEERRStgiYAYLDIGFNSLISNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVktPGHRTQIGSLSGGNQQKVIIGRW 405
|
170
....*....|....*...
gi 15599791 177 LLSAPDMLLLDEPTNHLD 194
Cdd:PRK10982 406 LLTQPEILMLDEPTRGID 423
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
18-190 |
2.89e-04 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 42.56 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGvdteiegearpmpginvgylpqepklDPQATVRDIV--EEAVG 95
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCG--------------------------DPRATSGRIVfdGKDIT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 96 QIKQAQArLDEVYAAYAEPDADFDALAAEQAKLEAILQASDGHNLERQLEVAADALRLppWDAKVEH---LSGGEKRRVA 172
Cdd:PRK11614 71 DWQTAKI-MREAVAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPRL--HERRIQRagtMSGGEQQMLA 147
|
170
....*....|....*...
gi 15599791 173 LCRLLLSAPDMLLLDEPT 190
Cdd:PRK11614 148 IGRALMSQPRLLLLDEPS 165
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-197 |
3.32e-04 |
|
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: 43.85 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 16 PPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGEarpmpgINVGYLPQEPKLdpqatvrDIVEEAVG 95
Cdd:TIGR01257 940 PSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGT------VLVGGKDIETNL-------DAVRQSLG 1006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 96 QIKQAQARLDEVYAA-----YAEpdadFDALAAEQAKL--EAILQASDGHNleRQLEVAADalrlppwdakvehLSGGEK 168
Cdd:TIGR01257 1007 MCPQHNILFHHLTVAehilfYAQ----LKGRSWEEAQLemEAMLEDTGLHH--KRNEEAQD-------------LSGGMQ 1067
|
170 180
....*....|....*....|....*....
gi 15599791 169 RRVALCRLLLSAPDMLLLDEPTNHLDADS 197
Cdd:TIGR01257 1068 RKLSVAIAFVGDAKVVVLDEPTSGVDPYS 1096
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
163-365 |
4.14e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 163 LSGGEKRRVALCRLLLSA---PDMLLLDEPTNHLDADSVAWLEHFLHDFP---GTVVAITHDRYFLdNVAGWILELDrgh 236
Cdd:PRK00635 810 LSGGEIQRLKLAYELLAPskkPTLYVLDEPTTGLHTHDIKALIYVLQSLThqgHTVVIIEHNMHVV-KVADYVLELG--- 885
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 237 giPFEGNYSGWLeskaarLAQEAKQEASH-----AKAMKAELEwvrqgakgrqakskarlqrfeelQSQEFQKRSETNei 311
Cdd:PRK00635 886 --PEGGNLGGYL------LASCSPEELIHlhtptAKALRPYLS-----------------------SPQELPYLPDPS-- 932
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15599791 312 yiPAGPRLGDKVIE--LHNVTKgygdrvlidNLSLSIPKGAIVGVIGGNGAGKSTL 365
Cdd:PRK00635 933 --PKPPVPADITIKnaYQHNLK---------HIDLSLPRNALTAVTGPSASGKHSL 977
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
321-371 |
5.51e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 41.94 E-value: 5.51e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 15599791 321 DKVIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTG 371
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
322-520 |
6.83e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 41.61 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 322 KVIELHNVTKgYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPdsGTIEIGETVQIASVDQSRDSLEGN 401
Cdd:PRK10418 3 QQIELRNIAL-QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA--GVRQTAGRVLLDGKPVAPCALRGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 402 K--TVWEQVSDGFEQIK-IGNYEVPSRSYVGRfnfKGADQ------------------QKFVKDLSGGERGRLHLALTLK 460
Cdd:PRK10418 80 KiaTIMQNPRSAFNPLHtMHTHARETCLALGK---PADDAtltaaleavglenaarvlKLYPFEMSGGMLQRMMIALALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599791 461 QGGNVLLLDEPSNDLD-VETLRALE--EALLDFPGAAIVI-SHDRWFLDRIATHIlSYEDDGKV 520
Cdd:PRK10418 157 CEAPFIIADEPTTDLDvVAQARILDllESIVQKRALGMLLvTHDMGVVARLADDV-AVMSHGRI 219
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
328-523 |
7.25e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 41.78 E-value: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 328 NVTKGYGDRVLidNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKEQPDSGTIEIGETVQiasVDQSrdslegnKTVWEQ 407
Cdd:PRK11144 5 NFKQQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVL---FDAE-------KGICLP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 408 VsdgfEQIKIGnyevpsrsYV-------------G--RFNFKGADQQKFVK----------------DLSGGERGRLHLA 456
Cdd:PRK11144 73 P----EKRRIG--------YVfqdarlfphykvrGnlRYGMAKSMVAQFDKivallgieplldrypgSLSGGEKQRVAIG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599791 457 LTLKQGGNVLLLDEPSNDLDV----ETLRALEEALLDFPGAAIVISHDrwfLD---RIATHILSYeDDGKVTFF 523
Cdd:PRK11144 141 RALLTAPELLLMDEPLASLDLprkrELLPYLERLAREINIPILYVSHS---LDeilRLADRVVVL-EQGKVKAF 210
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
139-194 |
7.48e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.08 E-value: 7.48e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599791 139 NLERQLEVAAD-----ALRLPPWDAKVEHLSGGEKRRVALCRLLLSAPDMLLLDEPTNHLD 194
Cdd:NF040905 376 DENEEIKVAEEyrkkmNIKTPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
163-243 |
8.91e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 41.45 E-value: 8.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 163 LSGGEKRRVALCRLLL---SAPDMLLLDEPTNHLDADSVAWLEHFLH---DFPGTVVAITHDryfLD--NVAGWILEL-- 232
Cdd:cd03271 170 LSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLHFHDVKKLLEVLQrlvDKGNTVVVIEHN---LDviKCADWIIDLgp 246
|
90
....*....|....
gi 15599791 233 ---DRGHGIPFEGN 243
Cdd:cd03271 247 eggDGGGQVVASGT 260
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
323-371 |
1.51e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.31 E-value: 1.51e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 15599791 323 VIELHNVTKGYGDRVLIDNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTG 371
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
6-62 |
1.59e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.57 E-value: 1.59e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599791 6 YTMHRVGK------IVPPKRE----ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEGE 62
Cdd:PRK13546 14 YRIYRTNKermkdaLIPKHKNktffALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK 80
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
163-253 |
2.14e-03 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 40.77 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 163 LSGGEKRRVALCRLLLSAPDMLLLDEPTNHLDADS----VAWLEHFLHDfpGTVVAITHDRYFLDNvAGWILELDRGHgI 238
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESeraiQAALDELQKN--RTSLVIAHRLSTIEK-ADEILVVEDGE-I 556
|
90
....*....|....*
gi 15599791 239 PFEGNYSGWLESKAA 253
Cdd:PRK11176 557 VERGTHAELLAQNGV 571
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
160-237 |
2.18e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 160 VEHLSGGEKR------RVALCRLLLSAPDMLLLDEPTNHLDADSVAWL----EHFLHDFPG--TVVAITHDRYFLdNVAG 227
Cdd:PRK01156 799 IDSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLkdiiEYSLKDSSDipQVIMISHHRELL-SVAD 877
|
90
....*....|
gi 15599791 228 WILELDRGHG 237
Cdd:PRK01156 878 VAYEVKKSSG 887
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
340-500 |
2.22e-03 |
|
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: 40.82 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 340 DNLSLSIPKGAIVGVIGGNGAGKSTLFRMLTGKeQPDSGTIEI-GETVQIASVDQSRD--------------SLEGNKTV 404
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFdGQDLDGLSRRALRPlrrrmqvvfqdpfgSLSPRMTV 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 405 WEQVSDGFEQIKIGNYEVPSRSYVGRF----NFKGADQQKFVKDLSGGERGRLHLA--LTLKQggNVLLLDEPSNDLDV- 477
Cdd:COG4172 382 GQIIAEGLRVHGPGLSAAERRARVAEAleevGLDPAARHRYPHEFSGGQRQRIAIAraLILEP--KLLVLDEPTSALDVs 459
|
170 180 190
....*....|....*....|....*....|
gi 15599791 478 ------ETLRALEEALldfpGAA-IVISHD 500
Cdd:COG4172 460 vqaqilDLLRDLQREH----GLAyLFISHD 485
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
443-509 |
2.73e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.78 E-value: 2.73e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599791 443 KDLSGGERGRLHLALTLKQGGNVLLLDEPSNDLDVETLRALEEALLDFPGAA----IVISHdrwfldRIAT 509
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdktiITIAH------RIAS 1421
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
162-223 |
2.92e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.07 E-value: 2.92e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599791 162 HLSGGEKR---RVALCRLLLSAPDMLLLDEPTNHLDadsVAWLEHFL------HDFPGTVVAITHDRYFLD 223
Cdd:pfam13304 236 ELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLH---PKLLRRLLellkelSRNGAQLILTTHSPLLLD 303
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
21-145 |
3.67e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599791 21 ILKDISLSFFPGAKIgVLGLNGAGKSTLLR-IMAGVDTEIEGEARPM-------PGINVGYLPQ-EPKLDPQATVRDIVE 91
Cdd:COG4717 13 KFRDRTIEFSPGLNV-IYGPNEAGKSTLLAfIRAMLLERLEKEADELfkpqgrkPELNLKELKElEEELKEAEEKEEEYA 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 15599791 92 EAVGQIKQAQARLDEVYAAYAEPDADFDALAAEQAKLEAILQASDghnLERQLE 145
Cdd:COG4717 92 ELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA---LEAELA 142
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
22-61 |
6.02e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 39.49 E-value: 6.02e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 15599791 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDTEIEG 61
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKG 79
|
|
| |
