|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-555 |
0e+00 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 1205.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 1 MAQFVYTMHRVGKVVPPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQPGIKIGYLPQEPQL 80
Cdd:PRK11819 2 MAQYIYTMNRVSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 81 NPEHTVRESVEEAVSEVVNALKGLDEVYAKYAEPDADFDKLAAQQGKYEEIIQAHDGHNLNVQLERAADALRLPDWDAKI 160
Cdd:PRK11819 82 DPEKTVRENVEEGVAEVKAALDRFNEIYAAYAEPDADFDALAAEQGELQEIIDAADAWDLDSQLEIAMDALRCPPWDAKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 161 ANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRGEGIPW 240
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPW 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 241 EGNYSSWLEQKDQRLAQEASQEAARRKSIEKELEWVRQGAKGRQSKGKARLARFEELNNTEYQKRNETNELFIPPGARLG 320
Cdd:PRK11819 242 EGNYSSWLEQKAKRLAQEEKQEAARQKALKRELEWVRQSPKARQAKSKARLARYEELLSEEYQKRNETNEIFIPPGPRLG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 321 DKVVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETVKLASVDQFRDAMDN 400
Cdd:PRK11819 322 DKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRDALDP 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 401 SKTVWEEVSGGLDIMRIGNTEMPSRAYVGRFNFKGTDQGKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIETL 480
Cdd:PRK11819 402 NKTVWEEISGGLDIIKVGNREIPSRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETL 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489953208 481 RALENALLEFPGCAMVISHDRWFLDRIATHILDYQDEGKVEFFEGNFTEYEEYKKRTLGADALEPKRIKYKRIAK 555
Cdd:PRK11819 482 RALEEALLEFPGCAVVISHDRWFLDRIATHILAFEGDSQVEWFEGNFQEYEEDKKRRLGADAARPHRIKYKKLTR 556
|
|
| 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: 1145.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 2 AQFVYTMHRVGKVVPPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQPGIKIGYLPQEPQLN 81
Cdd:TIGR03719 1 AQYIYTMNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 82 PEHTVRESVEEAVSEVVNALKGLDEVYAKYAEPDADFDKLAAQQGKYEEIIQAHDGHNLNVQLERAADALRLPDWDAKIA 161
Cdd:TIGR03719 81 PTKTVRENVEEGVAEIKDALDRFNEISAKYAEPDADFDKLAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPPWDADVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 162 NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRGEGIPWE 241
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 242 GNYSSWLEQKDQRLAQEASQEAARRKSIEKELEWVRQGAKGRQSKGKARLARFEELNNTEYQKRNETNELFIPPGARLGD 321
Cdd:TIGR03719 241 GNYSSWLEQKQKRLEQEEKEESARQKTLKRELEWVRQSPKGRQAKSKARLARYEELLSQEFQKRNETAEIYIPPGPRLGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 322 KVVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETVKLASVDQFRDAMDNS 401
Cdd:TIGR03719 321 KVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDALDPN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 402 KTVWEEVSGGLDIMRIGNTEMPSRAYVGRFNFKGTDQGKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIETLR 481
Cdd:TIGR03719 401 KTVWEEISGGLDIIKLGKREIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLR 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489953208 482 ALENALLEFPGCAMVISHDRWFLDRIATHILDYQDEGKVEFFEGNFTEYEEYKKRTLGADALEPKRIKYKRI 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: 724.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 8 MHRVGKVVPpKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQPGIKIGYLPQEPQLNPEHTVR 87
Cdd:COG0488 1 LENLSKSFG-GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 88 ESVEEAVSEVVNALKGLDEVYAKYAEPDADFDKLAAQQGKYEEiiqaHDGHNLNVQLERAADALRLP--DWDAKIANLSG 165
Cdd:COG0488 80 DTVLDGDAELRALEAELEELEAKLAEPDEDLERLAELQEEFEA----LGGWEAEARAEEILSGLGFPeeDLDRPVSELSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 166 GERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRGEGIPWEGNYS 245
Cdd:COG0488 156 GWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 246 SWLEQKDQRLAQEASQEAARRKSIEKELEWVRQ-GAKGRQSK-GKARLARFEELNNTEYQKRNETNELFIPPGARLGDKV 323
Cdd:COG0488 236 AYLEQRAERLEQEAAAYAKQQKKIAKEEEFIRRfRAKARKAKqAQSRIKALEKLEREEPPRRDKTVEIRFPPPERLGKKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETVKLASVDQFRDAMDNSKT 403
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELDPDKT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 404 VWEEVSGGLDimriGNTEMPSRAYVGRFNFKGTDQGKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIETLRAL 483
Cdd:COG0488 396 VLDELRDGAP----GGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEAL 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 489953208 484 ENALLEFPGCAMVISHDRWFLDRIATHILDYQDeGKVEFFEGNFTEYEEY 533
Cdd:COG0488 472 EEALDDFPGTVLLVSHDRYFLDRVATRILEFED-GGVREYPGGYDDYLEK 520
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-527 |
7.10e-108 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 336.15 E-value: 7.10e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-IDTDiEGEARPQPGIKIGYLPQEPQLNPEHTVRESVEEAVSEVVN 99
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGeVLLD-DGRIIYEQDLIVARLQQDPPRNVEGTVYDFVAEGIEEQAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 100 ALKGLDEVYAKYA-EPDadfDKLAAQQGKYEEIIQAHDGHNLNVQLERAADALRLpDWDAKIANLSGGERRRVALCRLLL 178
Cdd:PRK11147 97 YLKRYHDISHLVEtDPS---EKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGL-DPDAALSSLSGGWLRKAALGRALV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 179 EKPDMLLLDEPTNHLDAESVAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRGEGIPWEGNYSSWLEQKDQRLAQE 258
Cdd:PRK11147 173 SNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYLLEKEEALRVE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 259 ASQEAARRKSIEKELEWVRQGAKGRQSKGKARLARFEELNNTEYQKRNE--TNELFIPPGARLGDKVVEVTNLRKSYGDR 336
Cdd:PRK11147 253 ELQNAEFDRKLAQEEVWIRQGIKARRTRNEGRVRALKALRRERSERREVmgTAKMQVEEASRSGKIVFEMENVNYQIDGK 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 337 VLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETVKLASVDQFRDAMDNSKTVWEEVSGGLDIMR 416
Cdd:PRK11147 333 QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELDPEKTVMDNLAEGKQEVM 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 417 IGNTEMPSRAYVGRFNFkgtdQGKR----VGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIETLRALENALLEFPG 492
Cdd:PRK11147 413 VNGRPRHVLGYLQDFLF----HPKRamtpVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQG 488
|
490 500 510
....*....|....*....|....*....|....*
gi 489953208 493 CAMVISHDRWFLDRIATHILDYQDEGKVEFFEGNF 527
Cdd:PRK11147 489 TVLLVSHDRQFVDNTVTECWIFEGNGKIGRYVGGY 523
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
24-530 |
1.92e-78 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 256.36 E-value: 1.92e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 24 NISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQPGIKIGYLPQEPQLNPEHTVRESVEEAVSEVVNALKG 103
Cdd:PRK15064 19 NISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFTVLDTVIMGHTELWEVKQE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 104 LDEVYAKYAEPDADFDKLAAQQGKYEEIiqahDGHNLNvqlERAADAL-----RLPDWDAKIANLSGGERRRVALCRLLL 178
Cdd:PRK15064 99 RDRIYALPEMSEEDGMKVADLEVKFAEM----DGYTAE---ARAGELLlgvgiPEEQHYGLMSEVAPGWKLRVLLAQALF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 179 EKPDMLLLDEPTNHLDAESVAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRGEGIPWEGNYSSWLEQKDQRLAQE 258
Cdd:PRK15064 172 SNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEYMTAATQARERL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 259 ASQEAARRKSIEKELEWVRQ----GAKGRQSKGKARlaRFEELNNTEYQKRNETNElFI--PPGARLGDKVVEVTNLRKS 332
Cdd:PRK15064 252 LADNAKKKAQIAELQSFVSRfsanASKAKQATSRAK--QIDKIKLEEVKPSSRQNP-FIrfEQDKKLHRNALEVENLTKG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 333 YGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETVKLA-----SVDQFrdamDNSKTVWEE 407
Cdd:PRK15064 329 FDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGyyaqdHAYDF----ENDLTLFDW 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 408 VSgglDIMRIGNTEMPSRAYVGRFNFKGTDQGKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIETLRALENAL 487
Cdd:PRK15064 405 MS---QWRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMAL 481
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 489953208 488 LEFPGCAMVISHDRWFLDRIATHILDYQDEGkVEFFEGNFTEY 530
Cdd:PRK15064 482 EKYEGTLIFVSHDREFVSSLATRIIEITPDG-VVDFSGTYEEY 523
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
326-534 |
2.93e-65 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 221.09 E-value: 2.93e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 326 VTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETVKLASVDQFRDAMDNsKTVW 405
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDD-LTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 406 EEVSGGL----------------------DIMRIGNTE----------MPSRA--YVGRFNFKGTDQGKRVGELSGGERG 451
Cdd:COG0488 80 DTVLDGDaelraleaeleeleaklaepdeDLERLAELQeefealggweAEARAeeILSGLGFPEEDLDRPVSELSGGWRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 452 RLHLAKLLQVGGNVLLLDEPTNDLDIETLRALENALLEFPGCAMVISHDRWFLDRIATHILDYqDEGKVEFFEGNFTEYE 531
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILEL-DRGKLTLYPGNYSAYL 238
|
...
gi 489953208 532 EYK 534
Cdd:COG0488 239 EQR 241
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-533 |
1.29e-64 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 222.35 E-value: 1.29e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-IDTDIEGEARPQpGIKIGYLPQE-PQLNpehtvresvEEAVSE 96
Cdd:PRK10636 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNeISADGGSYTFPG-NWQLAWVNQEtPALP---------QPALEY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 97 VVNALKGLDEVYAKYAEPDA--DFDKLAAQQGKYEEI----IQAHDG---HNL---NVQLERAadalrlpdwdakIANLS 164
Cdd:PRK10636 84 VIDGDREYRQLEAQLHDANErnDGHAIATIHGKLDAIdawtIRSRAAsllHGLgfsNEQLERP------------VSDFS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 165 GGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRGEGIPWEGNY 244
Cdd:PRK10636 152 GGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 245 SSWLEQKDQRLAQEASQEAARRKSIEKELEWVRQgAKGRQSKGKARLARFEELNNTEY----QKRNETNELFIPPGArLG 320
Cdd:PRK10636 232 SSFEVQRATRLAQQQAMYESQQERVAHLQSYIDR-FRAKATKAKQAQSRIKMLERMELiapaHVDNPFHFSFRAPES-LP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 321 DKVVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETVKLASVDQ----FRD 396
Cdd:PRK10636 310 NPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQhqleFLR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 397 AmDNSKTvweevsggLDIMRIG--NTEMPSRAYVGRFNFKGTDQGKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTND 474
Cdd:PRK10636 390 A-DESPL--------QHLARLApqELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNH 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 489953208 475 LDIETLRALENALLEFPGCAMVISHDRWFLdRIATHILDYQDEGKVEFFEGNFTEYEEY 533
Cdd:PRK10636 461 LDLDMRQALTEALIDFEGALVVVSHDRHLL-RSTTDDLYLVHDGKVEPFDGDLEDYQQW 518
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
324-518 |
1.41e-54 |
|
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: 181.11 E-value: 1.41e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETVKLASVDQfrdamdnskt 403
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 404 vweevsggldimrigntempsrayvgrfnfkgtdqgkrvgeLSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIETLRAL 483
Cdd:cd03221 71 -----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEAL 109
|
170 180 190
....*....|....*....|....*....|....*
gi 489953208 484 ENALLEFPGCAMVISHDRWFLDRIATHILDYQDEG 518
Cdd:cd03221 110 EEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
25-538 |
1.56e-50 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 185.06 E-value: 1.56e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 25 ISLSFfpGAKIGVLGLNGAGKSTLLRIMA-----GIDTD-----IEGEArpqPGIKIGYLpqEPQLNPEHTVRESVEEAV 94
Cdd:PLN03073 198 VTLAF--GRHYGLVGRNGTGKTTFLRYMAmhaidGIPKNcqilhVEQEV---VGDDTTAL--QCVLNTDIERTQLLEEEA 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 95 SeVVNALKGLDEVYAKY---AEPDADFDKLAAQQgKYEEIIQAHDGHNLNVQLERAADALR----LPDWDAKIAN-LSGG 166
Cdd:PLN03073 271 Q-LVAQQRELEFETETGkgkGANKDGVDKDAVSQ-RLEEIYKRLELIDAYTAEARAASILAglsfTPEMQVKATKtFSGG 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 167 ERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRGEGIPWEGNYSS 246
Cdd:PLN03073 349 WRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVTYKGDYDT 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 247 WLEQKDQRL-----AQEASQEAarRKSIEKELEWVRQGAKGR---QSKGKA--RLARFEE-LNNTEYQKRnetnelFIPP 315
Cdd:PLN03073 429 FERTREEQLknqqkAFESNERS--RSHMQAFIDKFRYNAKRAslvQSRIKAldRLGHVDAvVNDPDYKFE------FPTP 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 316 GARLGDKVVEVTNLRKSY-GDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETVKLASVDQF 394
Cdd:PLN03073 501 DDRPGPPIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQH 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 395 R-DAMDNSKTVWeevsggLDIMRI--GNTEMPSRAYVGRFNFKGTDQGKRVGELSGGERGRLHLAKLLQVGGNVLLLDEP 471
Cdd:PLN03073 581 HvDGLDLSSNPL------LYMMRCfpGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEP 654
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489953208 472 TNDLDIETLRALENALLEFPGCAMVISHDRWFLDRiATHILDYQDEGKVEFFEGNFTEYeeykKRTL 538
Cdd:PLN03073 655 SNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISG-SVDELWVVSEGKVTPFHGTFHDY----KKTL 716
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
18-236 |
2.33e-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: 167.24 E-value: 2.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQPGIKIGYLPQepqlnpehtvresveeavsev 97
Cdd:cd03221 12 GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ--------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 98 vnalkgldevyakyaepdadfdklaaqqgkyeeiiqahdghnlnvqleraadalrlpdwdakianLSGGERRRVALCRLL 177
Cdd:cd03221 71 -----------------------------------------------------------------LSGGEKMRLALAKLL 85
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489953208 178 LEKPDMLLLDEPTNHLDAESVAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:cd03221 86 LENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
19-512 |
1.67e-48 |
|
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: 175.86 E-value: 1.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI--------------DTDIEGEARPQPGIKIGYLPQEP--QLNP 82
Cdd:COG1123 19 VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphggrisgevlldGRDLLELSEALRGRRIGMVFQDPmtQLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 83 eHTVRESVEEAvsevvnalkgldevyakyaepdadfdkLAAQQGKYEEIIQahdghnlnvQLERAADALRLPD-WDAKIA 161
Cdd:COG1123 99 -VTVGDQIAEA---------------------------LENLGLSRAEARA---------RVLELLEAVGLERrLDRYPH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 162 NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRGEg 237
Cdd:COG1123 142 QLSGGQRQRVAIAMALALDPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGR- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 238 IPWEGNYSSWLEQkDQRLAQEASQEAARRKSiekelewvrqgakgrqskgkarlarfeelnnteyqkrnetnelfiPPGA 317
Cdd:COG1123 221 IVEDGPPEEILAA-PQALAAVPRLGAARGRA---------------------------------------------APAA 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 318 RLGDKVVEVTNLRKSY-----GDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASV 391
Cdd:COG1123 255 AAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFdGKDLTKLSR 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 392 DQFRD--------------AMDNSKTVWEEVSGGLDIMRIGN-TEMPSRAY--VGRFNFKGTDQGKRVGELSGGERGRLH 454
Cdd:COG1123 335 RSLRElrrrvqmvfqdpysSLNPRMTVGDIIAEPLRLHGLLSrAERRERVAelLERVGLPPDLADRYPHELSGGQRQRVA 414
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489953208 455 LAKLLQVGGNVLLLDEPTNDLD-------IETLRALENALlefpGCAMV-ISHDRWFLDRIATHIL 512
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDvsvqaqiLNLLRDLQREL----GLTYLfISHDLAVVRYIADRVA 476
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
19-236 |
2.19e-37 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 137.25 E-value: 2.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEA----RPQPGI-------KIGYLPQEPQLnpehtVR 87
Cdd:COG4619 13 KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIyldgKPLSAMpppewrrQVAYVPQEPAL-----WG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 88 ESVEEAvsevvnalkgLDEVYaKYAEPDADFDKLAAqqgkyeeiiqahdghnLNVQLERAADALrlpdwDAKIANLSGGE 167
Cdd:COG4619 88 GTVRDN----------LPFPF-QLRERKFDRERALE----------------LLERLGLPPDIL-----DKPVERLSGGE 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489953208 168 RRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:COG4619 136 RQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-191 |
5.17e-37 |
|
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: 134.31 E-value: 5.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE-----------ARPQPGIKIGYLPQEPQLNPEHTVRESV 90
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTilldgqdltddERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 91 EEAVsevvnalkgldevyakyaepdadfdklaaqqgkyeeIIQAHDGHNLNVQLERAADALRLPDWDAKIA-----NLSG 165
Cdd:pfam00005 81 RLGL------------------------------------LLKGLSKREKDARAEEALEKLGLGDLADRPVgerpgTLSG 124
|
170 180
....*....|....*....|....*.
gi 489953208 166 GERRRVALCRLLLEKPDMLLLDEPTN 191
Cdd:pfam00005 125 GQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
324-513 |
2.00e-36 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 135.58 E-value: 2.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSIT-LGETV---------KLASVDQ 393
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvLGEDVardpaevrrRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 394 fRDAMDNSKTVWE--EVSGGLdiMRIGNTEMPSRA--YVGRFNFKGtDQGKRVGELSGGERGRLHLAKLLQVGGNVLLLD 469
Cdd:COG1131 81 -EPALYPDLTVREnlRFFARL--YGLPRKEARERIdeLLELFGLTD-AADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489953208 470 EPTNDLDIETLRALENALLEF--PGCAMVIShdrwfldriaTHILD 513
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELaaEGKTVLLS----------THYLE 192
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
19-225 |
8.64e-36 |
|
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: 132.60 E-value: 8.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE----------ARPQPGIKIGYLPQEPQLNPEHTVRE 88
Cdd:COG4133 15 RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEvlwngepirdAREDYRRRLAYLGHADGLKPELTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 89 SVeeavsEVVNALKGLDevyakyaePDADfdklaaqqgkyeeiiqahdghnlnvQLERAADALRLPD-WDAKIANLSGGE 167
Cdd:COG4133 95 NL-----RFWAALYGLR--------ADRE-------------------------AIDEALEAVGLAGlADLPVRQLSAGQ 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489953208 168 RRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF---EGTVVAITHDRYFLDNV 225
Cdd:COG4133 137 KRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHlarGGAVLLTTHQPLELAAA 197
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
339-473 |
3.11e-35 |
|
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: 129.30 E-value: 3.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 339 IDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGET-----------VKLASVDQFrDAMDNSKTVWEE 407
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQdltdderkslrKEIGYVFQD-PQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489953208 408 VSGGLDIMRIGNTEMPSRAY-----VGRFNFKGTDQGKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTN 473
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEealekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
321-512 |
1.04e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 130.98 E-value: 1.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 321 DKVVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLAS-----VDQf 394
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfGKPPRRARrrigyVPQ- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 395 RDAMDNSK--TVWEEVSGGLDImRIGNTEMPSRAY----------VGRFNFKgtdqGKRVGELSGGERGRLHLAKLLQVG 462
Cdd:COG1121 83 RAEVDWDFpiTVRDVVLMGRYG-RRGLFRRPSRADreavdealerVGLEDLA----DRPIGELSGGQQQRVLLARALAQD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489953208 463 GNVLLLDEPTNDLDIETLRALENALLEFP--GCAM-VISHDRWFLDRIATHIL 512
Cdd:COG1121 158 PDLLLLDEPFAGVDAATEEALYELLRELRreGKTIlVVTHDLGAVREYFDRVL 210
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
18-236 |
1.51e-33 |
|
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: 126.81 E-value: 1.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE---------ARPQPGI--KIGYLPQepqlNPEH-T 85
Cdd:cd03225 13 ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEvlvdgkdltKLSLKELrrKVGLVFQ----NPDDqF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 86 VRESVEEavsEVVNALK--GLDEvyakyaepdadfdklaaqqgkyEEIIQAhdghnlnvqLERAADALRLPDW-DAKIAN 162
Cdd:cd03225 89 FGPTVEE---EVAFGLEnlGLPE----------------------EEIEER---------VEEALELVGLEGLrDRSPFT 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489953208 163 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EG-TVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:cd03225 135 LSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLkaEGkTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
325-513 |
2.27e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 126.08 E-value: 2.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 325 EVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQFR-------- 395
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLdGKPLSAMPPPEWRrqvayvpq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 396 --DAMDNskTVWEEVSGGLDIMRIGNTEMPSRAYVGRFNFKGTDQGKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTN 473
Cdd:COG4619 82 epALWGG--TVRDNLPFPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489953208 474 DLDIETLRALENALLEFP----GCAMVISHDRWFLDRIATHILD 513
Cdd:COG4619 160 ALDPENTRRVEELLREYLaeegRAVLWVSHDPEQIERVADRVLT 203
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
323-512 |
6.19e-33 |
|
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: 126.31 E-value: 6.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 323 VVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETV----------KLASV 391
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLdGRDLaslsrrelarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 392 DQFRDAMDNSkTVWEEVSGGLdimrigntempsRAYVGRF-NFKGTDQ----------------GKRVGELSGGERGRLH 454
Cdd:COG1120 81 PQEPPAPFGL-TVRELVALGR------------YPHLGLFgRPSAEDReaveealertglehlaDRPVDELSGGERQRVL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489953208 455 LAKLLQVGGNVLLLDEPTNDLDI----ETLRALEnALLEFPGCAMVIS-HDrwfLD---RIATHIL 512
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLahqlEVLELLR-RLARERGRTVVMVlHD---LNlaaRYADRLV 209
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
16-236 |
7.08e-33 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 125.52 E-value: 7.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEGEARPQPGIKIGYLPQepqlNPEH 84
Cdd:COG1122 11 PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLlkptsgevlvdGKDITKKNLRELRRKVGLVFQ----NPDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 85 T-VRESVEEavsEVVNALK--GLDEvyakyaepdadfdklaaqqgkyEEIIQahdghnlnvQLERAADALRLPDW-DAKI 160
Cdd:COG1122 87 QlFAPTVEE---DVAFGPEnlGLPR----------------------EEIRE---------RVEEALELVGLEHLaDRPP 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489953208 161 ANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EG-TVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:COG1122 133 HELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnkEGkTVIIVTHDLDLVAELADRVIVLDDGR 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
325-516 |
8.96e-33 |
|
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: 122.74 E-value: 8.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 325 EVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLgetvklasvdqfrdamdnsktv 404
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILI---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 405 weevsGGLDIMRIGNTEMpsRAYVGrfnfkgtdqgkRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIETLRALE 484
Cdd:cd00267 59 -----DGKDIAKLPLEEL--RRRIG-----------YVPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLL 120
|
170 180 190
....*....|....*....|....*....|....*
gi 489953208 485 NALLEF--PGCAMV-ISHDRWFLDRIATHILDYQD 516
Cdd:cd00267 121 ELLRELaeEGRTVIiVTHDPELAELAADRVIVLKD 155
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
324-512 |
9.90e-33 |
|
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: 123.28 E-value: 9.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSIT-LGETVKLASVDQFRdamdnsk 402
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKvLGKDIKKEPEEVKR------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 403 tvweevsggldimRIGntempsraYV-GRFNFKGTDQGKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIETLR 481
Cdd:cd03230 74 -------------RIG--------YLpEEPSLYENLTVRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRR 132
|
170 180 190
....*....|....*....|....*....|....
gi 489953208 482 ALENALLEFP--GCAMVI-SHDRWFLDRIATHIL 512
Cdd:cd03230 133 EFWELLRELKkeGKTILLsSHILEEAERLCDRVA 166
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
18-235 |
2.41e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 124.43 E-value: 2.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEAR------PQPGIKIGYLPQEPQLNPEHTVreSVE 91
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRlfgkppRRARRRIGYVPQRAEVDWDFPI--TVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 92 EAVSEVVNALKGLdevyakyaepdadFDKLAAQQgkYEEIIQAhdghnlnvqLERA-ADALRlpdwDAKIANLSGGERRR 170
Cdd:COG1121 96 DVVLMGRYGRRGL-------------FRRPSRAD--REAVDEA---------LERVgLEDLA----DRPIGELSGGQQQR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489953208 171 VALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EG-TVVAITHDRYFLDNVAGWILELDRG 235
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrrEGkTILVVTHDLGAVREYFDRVLLLNRG 215
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
325-520 |
3.23e-32 |
|
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: 124.20 E-value: 3.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 325 EVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETVKLASVDQFRDAM------ 398
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIgvlpde 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 399 ---DNSKTVWEEVSGGLDIMRIGNTEMPSRA--YVGRFNFkGTDQGKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTN 473
Cdd:COG4555 83 rglYDRLTVRENIRYFAELYGLFDEELKKRIeeLIELLGL-EEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489953208 474 DLDIETLRALENALLEF---PGCAMVISHDRWFLDRIATHILdYQDEGKV 520
Cdd:COG4555 162 GLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVV-ILHKGKV 210
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
325-512 |
3.72e-32 |
|
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: 121.77 E-value: 3.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 325 EVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLgetvklasvdqfrdamdnsktv 404
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILL---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 405 weevsGGLDIMRIGNTEM-PSRAYV-------GRFNFKgtdqGKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLD 476
Cdd:cd03214 59 -----DGKDLASLSPKELaRKIAYVpqalellGLAHLA----DRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLD 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489953208 477 I-------ETLRALENALlefpGCAMVIS-HDRWFLDRIATHIL 512
Cdd:cd03214 130 IahqiellELLRRLARER----GKTVVMVlHDLNLAARYADRVI 169
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
325-512 |
6.15e-32 |
|
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: 122.26 E-value: 6.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 325 EVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETV-----KLASVDQFRDAM 398
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfGKPLekerkRIGYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 399 DNSK-TVWEEVSGGLDImRIGNTEMPSRAY----------VGRFNFKgtdqGKRVGELSGGERGRLHLAKLLQVGGNVLL 467
Cdd:cd03235 81 RDFPiSVRDVVLMGLYG-HKGLFRRLSKADkakvdealerVGLSELA----DRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489953208 468 LDEPTNDLDIETLRALENALLEF--PGCAM-VISHDRWFLDRIATHIL 512
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELrrEGMTIlVVTHDLGLVLEYFDRVL 203
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
324-532 |
1.12e-31 |
|
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: 122.06 E-value: 1.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSY-GDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQFRDAM--- 398
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVdGKDITKKNLRELRRKVglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 399 ----DN---SKTVWEEVSGGLDIMRIGNTEMPSR-----AYVGRFNFKgtdqGKRVGELSGGERGRLHLAKLLQVGGNVL 466
Cdd:COG1122 81 fqnpDDqlfAPTVEEDVAFGPENLGLPREEIRERveealELVGLEHLA----DRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489953208 467 LLDEPTNDLDIETLRALENALLEFP--GCAMV-ISHDRWFLDRIATHILdYQDEGKVeFFEGN----FTEYEE 532
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNkeGKTVIiVTHDLDLVAELADRVI-VLDDGRI-VADGTprevFSDYEL 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
325-512 |
2.08e-31 |
|
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: 120.65 E-value: 2.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 325 EVTNLRKSYGD--RVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQFR------ 395
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVdGKDLTKLSLKELRrkvglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 396 ----DAMDNSKTVWEEVSGGLDIMRIGNTEMPSRA--YVGRFNFKGTdQGKRVGELSGGERGRLHLAKLLQVGGNVLLLD 469
Cdd:cd03225 81 fqnpDDQFFGPTVEEEVAFGLENLGLPEEEIEERVeeALELVGLEGL-RDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489953208 470 EPTNDLDIETLRALENALLEFPGCAM---VISHDRWFLDRIATHIL 512
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAEGKtiiIVTHDLDLLLELADRVI 205
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
18-236 |
2.11e-31 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 121.71 E-value: 2.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEAR----------PQPGIKIGYLPQEPQLNPEHTVR 87
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgedvardpAEVRRRIGYVPQEPALYPDLTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 88 ESVeeavsEVVNALKGLDEvyakyAEPDADFDKLAAQqgkyeeiiqahdghnlnVQLERAAdalrlpdwDAKIANLSGGE 167
Cdd:COG1131 92 ENL-----RFFARLYGLPR-----KEARERIDELLEL-----------------FGLTDAA--------DRKVGTLSGGM 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489953208 168 RRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EG-TVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:COG1131 137 KQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELaaEGkTVLLSTHYLEEAERLCDRVAIIDKGR 208
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
17-218 |
2.66e-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: 121.69 E-value: 2.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE----------------ARpqpgiKIGYLPQEPQL 80
Cdd:COG1120 12 GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEvlldgrdlaslsrrelAR-----RIAYVPQEPPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 81 NPEHTVRESVEeavsevvnalkgldevYAKYAEPDAdFDKLAAQQgkyEEIIqahdghnlnvqlERAADALRLPDW-DAK 159
Cdd:COG1120 87 PFGLTVRELVA----------------LGRYPHLGL-FGRPSAED---REAV------------EEALERTGLEHLaDRP 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489953208 160 IANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD-AESVAWLE--RFLHDFEG-TVVAITHD 218
Cdd:COG1120 135 VDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDlAHQLEVLEllRRLARERGrTVVMVLHD 197
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
323-513 |
3.13e-31 |
|
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: 120.28 E-value: 3.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 323 VVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETVKLASVDQFR------- 395
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRrrlaylg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 396 --DAMDNSKTVWEEVS-----GGLDIMRIGNTEMPSRAYVGRFnfkgtdQGKRVGELSGGERGRLHLAKLLQVGGNVLLL 468
Cdd:COG4133 82 haDGLKPELTVRENLRfwaalYGLRADREAIDEALEAVGLAGL------ADLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489953208 469 DEPTNDLDIETLRALENALLEFP---GCAMVISHDRwfLDRIATHILD 513
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHLargGAVLLTTHQP--LELAAARVLD 201
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
324-508 |
1.03e-30 |
|
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: 119.16 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQFRDAM---D 399
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIdGRDVTGVPPERRNIGMvfqD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 400 NS----KTVWEEVSGGLDIMRIGNTEMPSRAYVGRFNFKGTDQGKR-VGELSGGERGRLHLAKLLQVGGNVLLLDEPTND 474
Cdd:cd03259 81 YAlfphLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRyPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489953208 475 LDIET---LRALENALLEFPGCAMV-ISHDR----WFLDRIA 508
Cdd:cd03259 161 LDAKLreeLREELKELQRELGITTIyVTHDQeealALADRIA 202
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
19-235 |
1.99e-30 |
|
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: 118.02 E-value: 1.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEAR--PQPGIK----IGYLPQEPQLNPEHTVreSVEE 92
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfGKPLEKerkrIGYVPQRRSIDRDFPI--SVRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 93 AVSEVVNALKGLdevyakyaepdadFDKLAAQQgkYEEIIQAHDghnlNVQLEraadALRlpdwDAKIANLSGGERRRVA 172
Cdd:cd03235 90 VVLMGLYGHKGL-------------FRRLSKAD--KAKVDEALE----RVGLS----ELA----DRQIGELSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489953208 173 LCRLLLEKPDMLLLDEPTNHLDAESVAWLERF---LHDFEGTVVAITHDRYFLDNVAGWILELDRG 235
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELlreLRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
16-258 |
2.20e-29 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 123.02 E-value: 2.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEarpqpgIK-----------------IGYLPQEP 78
Cdd:COG2274 485 GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGR------ILidgidlrqidpaslrrqIGVVLQDV 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 79 QLNPEhTVRESVeeavsevvnalkgldevyaKYAEPDADFDKL--AAQqgkyeeIIQAHDghnlnvqleraaDALRLPD- 155
Cdd:COG2274 559 FLFSG-TIRENI-------------------TLGDPDATDEEIieAAR------LAGLHD------------FIEALPMg 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 156 WDAKI----ANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEG--TVVAITHDRYFLDNvAGWI 229
Cdd:COG2274 601 YDTVVgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTIRL-ADRI 679
|
250 260 270
....*....|....*....|....*....|.
gi 489953208 230 LELDRGEgIPWEGNYSSWLEQKD--QRLAQE 258
Cdd:COG2274 680 IVLDKGR-IVEDGTHEELLARKGlyAELVQQ 709
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
18-236 |
5.54e-29 |
|
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: 112.88 E-value: 5.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEA--------RPQPGIK--IGYLPQEPQLNPEHTVR 87
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIkvlgkdikKEPEEVKrrIGYLPEEPSLYENLTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 88 EsveeavsevvnalkgldevyakyaepdadfdklaaqqgkyeeiiqahdghNLnvqleraadalrlpdwdakiaNLSGGE 167
Cdd:cd03230 92 E--------------------------------------------------NL---------------------KLSGGM 100
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489953208 168 RRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF---EGTVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:cd03230 101 KQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELkkeGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
16-251 |
6.48e-29 |
|
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: 120.63 E-value: 6.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE-----------ARPQPGIKIGYLPQEPQLnPEH 84
Cdd:COG4988 347 PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSilingvdlsdlDPASWRRQIAWVPQNPYL-FAG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 85 TVRESVeeavsevvnALkgldevyakyAEPDADfDklaaqqgkyEEIIQAhdghnlnvqLERA-ADAL--RLPD-WDAKI 160
Cdd:COG4988 426 TIRENL---------RL----------GRPDAS-D---------EELEAA---------LEAAgLDEFvaALPDgLDTPL 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 161 ----ANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD-FEG-TVVAITHDRYFLDNvAGWILELDR 234
Cdd:COG4988 468 geggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRlAKGrTVILITHRLALLAQ-ADRILVLDD 546
|
250
....*....|....*..
gi 489953208 235 GEGIPwEGNYSSWLEQK 251
Cdd:COG4988 547 GRIVE-QGTHEELLAKN 562
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
18-236 |
1.99e-28 |
|
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: 113.41 E-value: 1.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG--------IDTDIEGEARPQPGIK--IGYLPQEPQLNPEHTVR 87
Cdd:COG4555 13 KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGllkpdsgsILIDGEDVRKEPREARrqIGVLPDERGLYDRLTVR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 88 ESVeeavsEVVNALKGLdevyakyaepdadfdKLAAQQGKYEEIIQAhdghnlnVQLERAAdalrlpdwDAKIANLSGGE 167
Cdd:COG4555 93 ENI-----RYFAELYGL---------------FDEELKKRIEELIEL-------LGLEEFL--------DRRVGELSTGM 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489953208 168 RRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF---EGTVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:COG4555 138 KKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVVILHKGK 209
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-512 |
3.58e-28 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 118.76 E-value: 3.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 31 PGAKIGVLGLNGAGKSTLLRIMAGIDT----DIEGEARP--------------------QPGIKIGYLPQEPQLNPEH-- 84
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIpnlgDYEEEPSWdevlkrfrgtelqnyfkklyNGEIKVVHKPQYVDLIPKVfk 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 85 -TVREsveeavsevvnALKGLDEvyakyaepdadfdklaaqQGKYEEIIQAHDGHNLnvqleraadalrlpdWDAKIANL 163
Cdd:PRK13409 178 gKVRE-----------LLKKVDE------------------RGKLDEVVERLGLENI---------------LDRDISEL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 164 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE---SVAWLERFLHDfEGTVVAITHDRYFLDNVAGWIlELDRGE---- 236
Cdd:PRK13409 214 SGGELQRVAIAAALLRDADFYFFDEPTSYLDIRqrlNVARLIRELAE-GKYVLVVEHDLAVLDYLADNV-HIAYGEpgay 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 237 GIpwegnysswleqkdqrlaqeASQEAARRKSIEKEL------EWVRqgakgrqskgkarlARFEELNNTEYQKRNETNe 310
Cdd:PRK13409 292 GV--------------------VSKPKGVRVGINEYLkgylpeENMR--------------IRPEPIEFEERPPRDESE- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 311 lfippgarlGDKVVEVTNLRKSYGDrvliddltFS-------VPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLg 383
Cdd:PRK13409 337 ---------RETLVEYPDLTKKLGD--------FSleveggeIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 384 eTVKLA------------SVDQF-RDAMD--NSKTVWEEVSGGLDIMRIGNtempsrayvgrfnfkgtdqgKRVGELSGG 448
Cdd:PRK13409 399 -ELKISykpqyikpdydgTVEDLlRSITDdlGSSYYKSEIIKPLQLERLLD--------------------KNVKDLSGG 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489953208 449 ERGRLHLAKLLQVGGNVLLLDEPTNDLDIE----TLRALENALLEFPGCAMVISHDRWFLDRIATHIL 512
Cdd:PRK13409 458 ELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlaVAKAIRRIAEEREATALVVDHDIYMIDYISDRLM 525
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
320-529 |
4.44e-28 |
|
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: 112.38 E-value: 4.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 320 GDKVVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSIT-LGETVKLASVDQFRDAM 398
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILvDGQDITGLSEKELYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 399 DN------------SKTVWEEVSGGLDImrigNTEMPS-------RAYVGRFNFKGTdQGKRVGELSGGERGRLHLAKLL 459
Cdd:COG1127 82 RRigmlfqggalfdSLTVFENVAFPLRE----HTDLSEaeirelvLEKLELVGLPGA-ADKMPSELSGGMRKRVALARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489953208 460 QVGGNVLLLDEPTNDLDIETLRALENALLE----FPGCAMVISHDRWFLDRIATHILdYQDEGKVEfFEGNFTE 529
Cdd:COG1127 157 ALDPEILLYDEPTAGLDPITSAVIDELIRElrdeLGLTSVVVTHDLDSAFAIADRVA-VLADGKII-AEGTPEE 228
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
14-235 |
5.93e-28 |
|
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: 117.93 E-value: 5.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 14 VVPP--KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEGEARPQPGIKIGYLPQEPQL 80
Cdd:COG4618 338 VVPPgsKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVwpptagsvrldGADLSQWDREELGRHIGYLPQDVEL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 81 NPEhTVRESVeeavsevvnalkgldevyAKYAEPDAdfdklaaqqgkyEEIIQAhdghnlnvqlERAADA----LRLPD- 155
Cdd:COG4618 418 FDG-TIAENI------------------ARFGDADP------------EKVVAA----------AKLAGVhemiLRLPDg 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 156 WDAKI----ANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFE---GTVVAITHDRYFLdNVAGW 228
Cdd:COG4618 457 YDTRIgeggARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKargATVVVITHRPSLL-AAVDK 535
|
....*..
gi 489953208 229 ILELDRG 235
Cdd:COG4618 536 LLVLRDG 542
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
19-251 |
2.30e-27 |
|
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: 116.02 E-value: 2.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEGEARPQPGIKIGYLPQEPQL-NpeHTV 86
Cdd:COG4987 348 RPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFldpqsgsitlgGVDLRDLDEDDLRRRIAVVPQRPHLfD--TTL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 87 RESVeeavsevvnalkgldevyaKYAEPDADfDklaaqqgkyEEIIQAhdghnlnvqLERA--ADALR-LPD-WDAKI-- 160
Cdd:COG4987 426 RENL-------------------RLARPDAT-D---------EELWAA---------LERVglGDWLAaLPDgLDTWLge 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 161 --ANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESV-AWLERFLHDFEG-TVVAITHDRYFLDNVAGwILELDRGE 236
Cdd:COG4987 468 ggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEqALLADLLEALAGrTVLLITHRLAGLERMDR-ILVLEDGR 546
|
250
....*....|....*
gi 489953208 237 GIPwEGNYSSWLEQK 251
Cdd:COG4987 547 IVE-QGTHEELLAQN 560
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
7-218 |
3.02e-27 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 110.56 E-value: 3.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 7 TMHRVGKVVPPK---RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTD------IEGEARPQPGIKIGYLPQE 77
Cdd:COG1116 9 ELRGVSKRFPTGgggVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPtsgevlVDGKPVTGPGPDRGVVFQE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 78 PQLNPEHTVRESVEEAVSevvnaLKGLdevyakyaePDADFDKLAaqqgkyEEIIQAhdghnlnVQLERAADALrlPdwd 157
Cdd:COG1116 89 PALLPWLTVLDNVALGLE-----LRGV---------PKAERRERA------RELLEL-------VGLAGFEDAY--P--- 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489953208 158 akiANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVA----WLERFLHDFEGTVVAITHD 218
Cdd:COG1116 137 ---HQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRErlqdELLRLWQETGKTVLFVTHD 198
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
324-511 |
3.32e-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: 109.52 E-value: 3.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGD--RVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETVKLASVDQFR------ 395
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARqslgyc 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 396 ---DAMDNSKTVWE--EVSGGLDimRIGNTEMPSRA--YVGRFNFKGtDQGKRVGELSGGERGRLHLAKLLqVGGN-VLL 467
Cdd:cd03263 81 pqfDALFDELTVREhlRFYARLK--GLPKSEIKEEVelLLRVLGLTD-KANKRARTLSGGMKRKLSLAIAL-IGGPsVLL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489953208 468 LDEPTNDLDIETLRALENALLEF-PGCAMVI-SHDRWFLDRIATHI 511
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVrKGRSIILtTHSMDEAEALCDRI 202
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
323-508 |
3.73e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 110.25 E-value: 3.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 323 VVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLG-------ETVKLAsvdQFR 395
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNgrpladwSPAELA---RRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 396 DAMDNSK------TVWEEVSGGLDIMRIGNTEMPS-----------RAYVGRFnfkgtdqgkrVGELSGGERGRLHLAKL 458
Cdd:PRK13548 79 AVLPQHSslsfpfTVEEVVAMGRAPHGLSRAEDDAlvaaalaqvdlAHLAGRD----------YPQLSGGEQQRVQLARV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489953208 459 L-QV-----GGNVLLLDEPTNDLDI----ETLRALENALLEFPGCAMVISHD-----RWfLDRIA 508
Cdd:PRK13548 149 LaQLwepdgPPRWLLLDEPTSALDLahqhHVLRLARQLAHERGLAVIVVLHDlnlaaRY-ADRIV 212
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
324-520 |
6.53e-27 |
|
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: 108.35 E-value: 6.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGD----RVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASvDQFRDAM 398
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVdGTDISKLS-EKELAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 399 DNSK--------------TVWEEVSGGLDIMRIGNTEMPSRA-----YVG---RFNfkgtdqgKRVGELSGGERGRLHLA 456
Cdd:cd03255 80 RRRHigfvfqsfnllpdlTALENVELPLLLAGVPKKERRERAeelleRVGlgdRLN-------HYPSELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489953208 457 KLLQVGGNVLLLDEPTNDLDIETLRALENALLEF---PGCAMVI-SHDRwFLDRIATHILDYQDeGKV 520
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMELLRELnkeAGTTIVVvTHDP-ELAEYADRIIELRD-GKI 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
17-236 |
7.39e-27 |
|
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: 106.18 E-value: 7.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARpqpgikigYLPQEPQLNPEHTVRESVeeavse 96
Cdd:cd00267 10 GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL--------IDGKDIAKLPLEELRRRI------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 97 vvnalkgldeVYakyaepdadfdklaaqqgkyeeIIQahdghnlnvqleraadalrlpdwdakianLSGGERRRVALCRL 176
Cdd:cd00267 76 ----------GY----------------------VPQ-----------------------------LSGGQRQRVALARA 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489953208 177 LLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EG-TVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:cd00267 95 LLLNPDLLLLDEPTSGLDPASRERLLELLRELaeEGrTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
291-483 |
1.15e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 111.08 E-value: 1.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 291 LARFEELNNTEYQKRNETNELFIPPGArLGDKVVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMS 370
Cdd:PRK13536 10 APRRLELSPIERKHQGISEAKASIPGS-MSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 371 GQEQPDSGSIT-LGETV---------KLASVDQFrDAMDNSKTVWEE--VSGGLDIMRIGNTE--MPSRAYVGRFNFKGT 436
Cdd:PRK13536 89 GMTSPDAGKITvLGVPVpararlaraRIGVVPQF-DNLDLEFTVRENllVFGRYFGMSTREIEavIPSLLEFARLESKAD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489953208 437 dqgKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLD-------IETLRAL 483
Cdd:PRK13536 168 ---ARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDpharhliWERLRSL 218
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-512 |
1.47e-26 |
|
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: 113.73 E-value: 1.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 31 PGAKIGVLGLNGAGKSTLLRIMAGidtdiegEARPQPGIkigylpqepqlnpehtvresVEEAVS--EVVNALKG----- 103
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSG-------ELKPNLGD--------------------YDEEPSwdEVLKRFRGtelqd 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 104 -LDEVYAKyaepdadfDKLAAQQGKY-EEIIQAHDGhnlNVQ--LERA---------ADALRL-PDWDAKIANLSGGERR 169
Cdd:COG1245 151 yFKKLANG--------EIKVAHKPQYvDLIPKVFKG---TVRelLEKVdergkldelAEKLGLeNILDRDISELSGGELQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 170 RVALCRLLLEKPDMLLLDEPTNHLDAE---SVAWLERFLHDFEGTVVAITHDRYFLDNVAGWIlELDRGE---------- 236
Cdd:COG1245 220 RVAIAAALLRDADFYFFDEPSSYLDIYqrlNVARLIRELAEEGKYVLVVEHDLAILDYLADYV-HILYGEpgvygvvskp 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 237 -----GIpweGNY-SSWLEQKDQRLaqeasqeaaRRKSIEkelewvrqgakgrqskgkarlarFEELNNTEYQKRnetne 310
Cdd:COG1245 299 ksvrvGI---NQYlDGYLPEENVRI---------RDEPIE-----------------------FEVHAPRREKEE----- 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 311 lfippgarlgDKVVEVTNLRKSYGDRVLiddltfSVPKGAI-----VGIIGPNGAGKSTLFRMMSGQEQPDSGSITlgET 385
Cdd:COG1245 339 ----------ETLVEYPDLTKSYGGFSL------EVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEVD--ED 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 386 VKLA------------SVDQF-----RDAMDNSKtVWEEVSGGLDIMRIGNtempsrayvgrfnfkgtdqgKRVGELSGG 448
Cdd:COG1245 401 LKISykpqyispdydgTVEEFlrsanTDDFGSSY-YKTEIIKPLGLEKLLD--------------------KNVKDLSGG 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489953208 449 ERGRLHLAKLLQVGGNVLLLDEPTNDLDIE----TLRALENALLEFPGCAMVISHDRWFLDRIATHIL 512
Cdd:COG1245 460 ELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlaVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
18-236 |
1.59e-26 |
|
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: 108.35 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTD------IEGEARPQPGIK-----IGYLPQEPQ--LNPEH 84
Cdd:COG1124 17 RVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPwsgevtFDGRPVTRRRRKafrrrVQMVFQDPYasLHPRH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 85 TVRESVEEAVsevvnALKGLDEVyakyaepDADFDKLAAQQGKYEEIIQahdghnlnvqleraadalRLPdwdakiANLS 164
Cdd:COG1124 97 TVDRILAEPL-----RIHGLPDR-------EERIAELLEQVGLPPSFLD------------------RYP------HQLS 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489953208 165 GGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:COG1124 141 GGQRQRVAIARALILEPELLLLDEPTSALDvsvqAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGR 216
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
324-544 |
2.18e-26 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 113.51 E-value: 2.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETVKLASVDQF--RDAmdnS 401
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDppRNV---E 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 402 KTVWEEVSGGL-----------DIMRIGNTEmPSRAYVGRF---------------------NFK--GTDQGKRVGELSG 447
Cdd:PRK11147 81 GTVYDFVAEGIeeqaeylkryhDISHLVETD-PSEKNLNELaklqeqldhhnlwqlenrineVLAqlGLDPDAALSSLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 448 GERGRLHLAKLLQVGGNVLLLDEPTNDLDIETLRALENALLEFPGCAMVISHDRWFLDRIATHILDYqDEGKVEFFEGNF 527
Cdd:PRK11147 160 GWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDL-DRGKLVSYPGNY 238
|
250
....*....|....*..
gi 489953208 528 TEYEEYKKRTLGADALE 544
Cdd:PRK11147 239 DQYLLEKEEALRVEELQ 255
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
324-512 |
2.63e-26 |
|
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: 105.35 E-value: 2.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLgetvklasvdqfrdamdnskt 403
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILI--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 404 vweevsGGLDIMRIGNTEMPSRAYVG----RFN-FKGTDQGKRVGE-LSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDI 477
Cdd:cd03229 60 ------DGEDLTDLEDELPPLRRRIGmvfqDFAlFPHLTVLENIALgLSGGQQQRVALARALAMDPDVLLLDEPTSALDP 133
|
170 180 190
....*....|....*....|....*....|....*....
gi 489953208 478 ET---LRALENALLEFPGCAMV-ISHDRWFLDRIATHIL 512
Cdd:cd03229 134 ITrreVRALLKSLQAQLGITVVlVTHDLDEAARLADRVV 172
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
324-489 |
2.96e-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: 106.79 E-value: 2.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDR----VLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQ---F- 394
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdGEPVTGPGPDRgyvFq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 395 RDAMDNSKTVWEEVSGGLDIMRIGNTEMPSRA--YVGRFNFKGTdQGKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPT 472
Cdd:cd03293 81 QDALLPWLTVLDNVALGLELQGVPKAEARERAeeLLELVGLSGF-ENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPF 159
|
170
....*....|....*..
gi 489953208 473 NDLDIETLRALENALLE 489
Cdd:cd03293 160 SALDALTREQLQEELLD 176
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
7-218 |
2.99e-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: 106.79 E-value: 2.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 7 TMHRVGKVVPPKR---HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTD------IEGEARPQPGIKIGYLPQE 77
Cdd:cd03293 2 EVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPtsgevlVDGEPVTGPGPDRGYVFQQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 78 PQLNPEHTVREsveeavsevvNALKGLDEVYAKYAEPDADFDKLAAQqgkyeeiiqahdghnlnVQLERAADalRLPdwd 157
Cdd:cd03293 82 DALLPWLTVLD----------NVALGLELQGVPKAEARERAEELLEL-----------------VGLSGFEN--AYP--- 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489953208 158 akiANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA---ESV-AWLERFLHDFEGTVVAITHD 218
Cdd:cd03293 130 ---HQLSGGMRQRVALARALAVDPDVLLLDEPFSALDAltrEQLqEELLDIWRETGKTVLLVTHD 191
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-237 |
3.41e-26 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 112.59 E-value: 3.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE-ARPqPGIKIGYLPQEPQLnPEHTVREsveeAV 94
Cdd:COG4178 373 PDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRiARP-AGARVLFLPQRPYL-PLGTLRE----AL 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 95 SevvnalkgldevyakYAEPDADFDKlaaqqgkyEEIIQAhdghnLN-VQLERAADALRLP-DWDAKianLSGGERRRVA 172
Cdd:COG4178 447 L---------------YPATAEAFSD--------AELREA-----LEaVGLGHLAERLDEEaDWDQV---LSLGEQQRLA 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489953208 173 LCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD--FEGTVVAITHdRYFLDNVAGWILELDRGEG 237
Cdd:COG4178 496 FARLLLHKPDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGH-RSTLAAFHDRVLELTGDGS 561
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
22-472 |
5.90e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 111.26 E-value: 5.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTD------IEGEARPQPGIK------IGYLPQEPQLNPEHTVRES 89
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPdsgeilLDGEPVRFRSPRdaqaagIAIIHQELNLVPNLSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 90 V---EEAVSevvnalKGLdevyakyaepdADFDKLAAQqgkYEEIIQAhdghnLNVQLeraadalrlpDWDAKIANLSGG 166
Cdd:COG1129 100 IflgREPRR------GGL-----------IDWRAMRRR---ARELLAR-----LGLDI----------DPDTPVGDLSVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 167 ERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EG-TVVAITHdryFLDNvagwILEL-DR------GE 236
Cdd:COG1129 145 QQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLkaQGvAIIYISH---RLDE----VFEIaDRvtvlrdGR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 237 GIpwegnysswleqkDQRLAQEASQEAARRKSIEKELEwvrqgakgrqskgkarlarfeelnnteyqkrnetnELFIPPG 316
Cdd:COG1129 218 LV-------------GTGPVAELTEDELVRLMVGRELE-----------------------------------DLFPKRA 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 317 ARLGDKVVEVTNLRksygDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVdqfR 395
Cdd:COG1129 250 AAPGEVVLEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLdGKPVRIRSP---R 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 396 DAMDN----------------SKTVWEEVS----------GGLDIMRIGNTempSRAYVGRFNFKGTDQGKRVGELSGGE 449
Cdd:COG1129 323 DAIRAgiayvpedrkgeglvlDLSIRENITlasldrlsrgGLLDRRRERAL---AEEYIKRLRIKTPSPEQPVGNLSGGN 399
|
490 500
....*....|....*....|...
gi 489953208 450 RGRLHLAKLLQVGGNVLLLDEPT 472
Cdd:COG1129 400 QQKVVLAKWLATDPKVLILDEPT 422
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
324-511 |
9.92e-26 |
|
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: 104.99 E-value: 9.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL--GETVKLASVDQFRDAMDNS 401
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFdgKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 402 KTVWEEVSGGLDIMRIGNTEMPSRAYV----GRFNFKGTDqGKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLD- 476
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRKKRIdevlDVVGLKDSA-KKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDp 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 489953208 477 --IETLRALENALLEFPGCAMVISHDRWFLDRIATHI 511
Cdd:cd03268 160 dgIKELRELILSLRDQGITVLISSHLLSEIQKVADRI 196
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
17-219 |
1.15e-25 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 108.31 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDT-D-----IEGE---------ARpqpgiKIGYLPQEPQLN 81
Cdd:COG1118 13 GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETpDsgrivLNGRdlftnlpprER-----RVGFVFQHYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 82 PEHTVREsveeavsevvNALKGLdevyaKYAEPDAdfdklAAQQGKYEEIIQAhdghnlnVQLERAADalRLPdwdakiA 161
Cdd:COG1118 88 PHMTVAE----------NIAFGL-----RVRPPSK-----AEIRARVEELLEL-------VQLEGLAD--RYP------S 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489953208 162 NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAeSVA-----WLERFLHDFEGTVVAITHDR 219
Cdd:COG1118 133 QLSGGQRQRVALARALAVEPEVLLLDEPFGALDA-KVRkelrrWLRRLHDELGGTTVFVTHDQ 194
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
324-499 |
1.43e-25 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 103.23 E-value: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDR--VLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGetvklasvdqfrdamdns 401
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILID------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 402 ktvweevsgGLDIMRIGNTEMPSR-AYVGR--FNFKGTdqgkrVGE--LSGGERGRLHLAKLLQVGGNVLLLDEPTNDLD 476
Cdd:cd03228 63 ---------GVDLRDLDLESLRKNiAYVPQdpFLFSGT-----IREniLSGGQRQRIAIARALLRDPPILILDEATSALD 128
|
170 180
....*....|....*....|....*
gi 489953208 477 IETLRALENALLEFPGCAMV--ISH 499
Cdd:cd03228 129 PETEALILEALRALAKGKTVivIAH 153
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
324-477 |
1.75e-25 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 105.17 E-value: 1.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLgetvklasvdqfrDAMDNSKT 403
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLV-------------DGLDVATT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 404 VWEEVSGGLDIMRIGNTeMPSRAYV------GRFNF-KG-------------------TD-QGKRVGELSGGERGRLHLA 456
Cdd:COG4604 69 PSRELAKRLAILRQENH-INSRLTVrelvafGRFPYsKGrltaedreiideaiayldlEDlADRYLDELSGGQRQRAFIA 147
|
170 180
....*....|....*....|.
gi 489953208 457 KLLQVGGNVLLLDEPTNDLDI 477
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDM 168
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
325-529 |
2.25e-25 |
|
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: 104.44 E-value: 2.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 325 EVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQ---------- 393
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFdGEDITGLPPHEiarlgigrtf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 394 -----FRDAmdnskTVWEEV--------SGGLDIMRIGNTEMPSRAYVGRF-NFKGTD--QGKRVGELSGGERGRLHLAK 457
Cdd:cd03219 82 qiprlFPEL-----TVLENVmvaaqartGSGLLLARARREEREARERAEELlERVGLAdlADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489953208 458 LLQVGGNVLLLDEPT---NDLDIETLRALENALLEFpGCA-MVISHDRWFLDRIATHI--LDYqdeGKVeFFEGNFTE 529
Cdd:cd03219 157 ALATDPKLLLLDEPAaglNPEETEELAELIRELRER-GITvLLVEHDMDVVMSLADRVtvLDQ---GRV-IAEGTPDE 229
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
320-520 |
2.33e-25 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 105.12 E-value: 2.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 320 GDKVVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQ----- 393
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFdGRDITGLPPHRiarlg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 394 ----------FRD--AMDN--------SKTVWEEVSGGLDIMRIGNTEMPSRAY--VGRFNFKGtDQGKRVGELSGGERG 451
Cdd:COG0411 81 iartfqnprlFPEltVLENvlvaaharLGRGLLAALLRLPRARREEREARERAEelLERVGLAD-RADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489953208 452 RLHLAKLLQVGGNVLLLDEPT---NDLDIETLRALENALLEFPGCAMV-ISHDRWFLDRIATHI--LDYqdeGKV 520
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAaglNPEETEELAELIRRLRDERGITILlIEHDMDLVMGLADRIvvLDF---GRV 231
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
324-490 |
2.56e-25 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 104.18 E-value: 2.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSG-----QEQPDSGSITL-GETVKLASVDQ---- 393
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLdGKDIYDLDVDVlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 394 ------FRDAMDNSKTVWEEVSGGLDIMRI-GNTEMPSRAYVGrfnFKGTDQGKRV------GELSGGERGRLHLAKLLQ 460
Cdd:cd03260 81 rrvgmvFQKPNPFPGSIYDNVAYGLRLHGIkLKEELDERVEEA---LRKAALWDEVkdrlhaLGLSGGQQQRLCLARALA 157
|
170 180 190
....*....|....*....|....*....|
gi 489953208 461 VGGNVLLLDEPTNDLDIETLRALENALLEF 490
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAEL 187
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
18-236 |
3.13e-25 |
|
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: 103.72 E-value: 3.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQpGI----------------KIGYLPQEPQLN 81
Cdd:cd03255 16 KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVD-GTdisklsekelaafrrrHIGFVFQSFNLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 82 PEHTVRESVEeavsevvnalkgldevyakyaepdadfdkLAAqqgkyeeIIQAHDGHNLNVQLERAADALRLPD-WDAKI 160
Cdd:cd03255 95 PDLTALENVE-----------------------------LPL-------LLAGVPKKERRERAEELLERVGLGDrLNHYP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 161 ANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDFEGTVVAITHDRyFLDNVAGWILELDRGE 236
Cdd:cd03255 139 SELSGGQQQRVAIARALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGK 217
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
17-218 |
4.61e-25 |
|
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: 102.13 E-value: 4.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEGEARPQPGIKIGYLPQepqlnpeht 85
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLlkpssgeilldGKDLASLSPKELARKIAYVPQ--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 86 vresveeaVSEVVNALKgldevyakyaepdadfdkLAAQQgkyeeiiqahdghnlnvqleraadalrlpdwdakIANLSG 165
Cdd:cd03214 81 --------ALELLGLAH------------------LADRP----------------------------------FNELSG 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489953208 166 GERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDFEGTVVAITHD 218
Cdd:cd03214 101 GERQRVLLARALAQEPPILLLDEPTSHLDiahqIELLELLRRLARERGKTVVMVLHD 157
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
16-226 |
5.36e-25 |
|
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: 108.45 E-value: 5.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGID--------------TDIEGEARPQPGIKIGYLPQEP--Q 79
Cdd:COG1123 275 KGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLrptsgsilfdgkdlTKLSRRSLRELRRRVQMVFQDPysS 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 80 LNPEHTVRESVEEAVsevvnalkgldEVYAKYAEPDADfdklaaqqgkyeeiiqahdghnlnvqlERAADALRLPDWDAK 159
Cdd:COG1123 355 LNPRMTVGDIIAEPL-----------RLHGLLSRAERR---------------------------ERVAELLERVGLPPD 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 160 IAN-----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAeSVAW-----LERFLHDFEGTVVAITHD----RYFLDNV 225
Cdd:COG1123 397 LADrypheLSGGQRQRVAIARALALEPKLLILDEPTSALDV-SVQAqilnlLRDLQRELGLTYLFISHDlavvRYIADRV 475
|
.
gi 489953208 226 A 226
Cdd:COG1123 476 A 476
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
324-523 |
5.56e-25 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 103.35 E-value: 5.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQFRD------ 396
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIdGEDISGLSEAELYRlrrrmg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 397 ------AMDNSKTVWEEVSGGLDImrigNTEMPSRAYVGRFNFK------GTDQGKRVGELSGGERGRLHLAKLLQVGGN 464
Cdd:cd03261 81 mlfqsgALFDSLTVFENVAFPLRE----HTRLSEEEIREIVLEKleavglRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489953208 465 VLLLDEPTNDLDIETLRALENALL----EFPGCAMVISHDRWFLDRIATHILdYQDEGKVEFF 523
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRslkkELGLTSIMVTHDLDTAFAIADRIA-VLYDGKIVAE 218
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
18-226 |
5.62e-25 |
|
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: 103.35 E-value: 5.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEG---EARPQPGIKIGYLPQEPQ--LN 81
Cdd:cd03257 17 SVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLlkptsgsiifdGKDLLKlsrRLRKIRRKEIQMVFQDPMssLN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 82 PEHTVRESVEEAVsevvnalkgldevyakyaepdadfdkLAAQQGKYEEIIQAHdGHNLNVQLERAADAL-RLPDWdaki 160
Cdd:cd03257 97 PRMTIGEQIAEPL--------------------------RIHGKLSKKEARKEA-VLLLLVGVGLPEEVLnRYPHE---- 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489953208 161 anLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD----FEGTVVAITHD----RYFLDNVA 226
Cdd:cd03257 146 --LSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKlqeeLGLTLLFITHDlgvvAKIADRVA 217
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
323-521 |
7.71e-25 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 103.04 E-value: 7.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 323 VVEVTNLRKSYGDR----VLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQFRDA 397
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVdGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 398 ------------MDNSKTVWEEVSGGLDIMRIGNTEMPSRAY-----VGRfnfkgTDQGKRV-GELSGGERGRLHLAKLL 459
Cdd:cd03258 81 rrrigmifqhfnLLSSRTVFENVALPLEIAGVPKAEIEERVLellelVGL-----EDKADAYpAQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489953208 460 QVGGNVLLLDEPTNDLDIETLRALENALL----EFPGCAMVISHDRWFLDRIATHILdYQDEGKVE 521
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLRdinrELGLTIVLITHEMEVVKRICDRVA-VMEKGEVV 220
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
21-251 |
8.23e-25 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 108.06 E-value: 8.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQPGIKIGYLPQEPqlnpehtvresveeavsevvna 100
Cdd:PRK15064 334 LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDH---------------------- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 101 lkgldevYAKYAEPDADFDKLA--AQQGKYEEIIQAHDGhnlnvQLERAADalrlpDWDAKIANLSGGERRRVALCRLLL 178
Cdd:PRK15064 392 -------AYDFENDLTLFDWMSqwRQEGDDEQAVRGTLG-----RLLFSQD-----DIKKSVKVLSGGEKGRMLFGKLMM 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489953208 179 EKPDMLLLDEPTNHLDAESVAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRGEGIPWEGNYSSWLEQK 251
Cdd:PRK15064 455 QKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLRSQ 527
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
325-483 |
1.86e-24 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 102.50 E-value: 1.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 325 EVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETvklaSVDQFRdAMDNSK-- 402
Cdd:COG4559 3 EAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGR----PLAAWS-PWELARrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 403 -------------TVWEEVSGGLDIMRIGNTEMPSRA-----------YVGRFnfkgtdqgkrVGELSGGERGRLHLAK- 457
Cdd:COG4559 78 avlpqhsslafpfTVEEVVALGRAPHGSSAAQDRQIVrealalvglahLAGRS----------YQTLSGGEQQRVQLARv 147
|
170 180 190
....*....|....*....|....*....|....*.
gi 489953208 458 LLQV------GGNVLLLDEPTNDLDI----ETLRAL 483
Cdd:COG4559 148 LAQLwepvdgGPRWLFLDEPTSALDLahqhAVLRLA 183
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
10-281 |
1.90e-24 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 107.73 E-value: 1.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 10 RVGKVV---------PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAgidtdieGEARPQPG-IKIG------Y 73
Cdd:PRK11147 314 RSGKIVfemenvnyqIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLML-------GQLQADSGrIHCGtklevaY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 74 LPQ-EPQLNPEHTVRESVEEavsevvnalkgldevyakyaepdadfdklaaqqGKYEEIIQAHDGHNLNVQLE------R 146
Cdd:PRK11147 387 FDQhRAELDPEKTVMDNLAE---------------------------------GKQEVMVNGRPRHVLGYLQDflfhpkR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 147 AadalRLPdwdakIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEGTVVAITHDRYFLDNVA 226
Cdd:PRK11147 434 A----MTP-----VKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTV 504
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 227 --GWILEldrGEGIpWE---GNYSSWLEQKDQRLAQEASQEAARRKSIEKELEWVRQGAK 281
Cdd:PRK11147 505 teCWIFE---GNGK-IGryvGGYHDARQQQAQYLALKQPAVKKKEEAAAPKAETVKRSSK 560
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
323-476 |
2.57e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 103.35 E-value: 2.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 323 VVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETV---------KLASVD 392
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcGEPVpsrarharqRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 393 QFrDAMDNSKTVWEE--VSG---GLDIMRIgNTEMPSRAYVGRFNFKGTdqgKRVGELSGGERGRLHLAKLLQVGGNVLL 467
Cdd:PRK13537 87 QF-DNLDPDFTVRENllVFGryfGLSAAAA-RALVPPLLEFAKLENKAD---AKVGELSGGMKRRLTLARALVNDPDVLV 161
|
....*....
gi 489953208 468 LDEPTNDLD 476
Cdd:PRK13537 162 LDEPTTGLD 170
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-235 |
2.63e-24 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 101.13 E-value: 2.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIE----GEARPQpgikIGYLPQEPQLNp 82
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLykptsgsvlldGTDIRqldpADLRRN----IGYVPQDVTLF- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 83 EHTVRESVEeavsevvnalkgldevyakYAEPDADFDKL--AAQQGKYEEIIQAH-DGHNLNVQlERAAdalrlpdwdak 159
Cdd:cd03245 91 YGTLRDNIT-------------------LGAPLADDERIlrAAELAGVTDFVNKHpNGLDLQIG-ERGR----------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 160 iaNLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVawlERFLHDFEG-----TVVAITHdRYFLDNVAGWILELDR 234
Cdd:cd03245 140 --GLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSE---ERLKERLRQllgdkTLIIITH-RPSLLDLVDRIIVMDS 213
|
.
gi 489953208 235 G 235
Cdd:cd03245 214 G 214
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-296 |
4.00e-24 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 106.41 E-value: 4.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQPGIKIGYLPQEpQL-------NP-EHTVRESV 90
Cdd:PRK10636 325 RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQH-QLeflradeSPlQHLARLAP 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 91 EEAVSEVVNALKGLDEVYAKYAEPDADFdklaaqqgkyeeiiqahdghnlnvqleraadalrlpdwdakianlSGGERRR 170
Cdd:PRK10636 404 QELEQKLRDYLGGFGFQGDKVTEETRRF---------------------------------------------SGGEKAR 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 171 VALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRGEGIPWEG---NYSSW 247
Cdd:PRK10636 439 LVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGdleDYQQW 518
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 489953208 248 L-EQKDQRLAQEASQEAARRKSIEKELEWVRQGAKGRQSKGKAR--LARFEE 296
Cdd:PRK10636 519 LsDVQKQENQTDEAPKENNANSAQARKDQKRREAELRTQTQPLRkeIARLEK 570
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
334-531 |
6.97e-24 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 106.02 E-value: 6.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 334 GDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETVKLASVDQFRDAMD-------------- 399
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPqpaleyvidgdrey 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 400 -------------NSKTVWEEVSGGLDIMRIGNTEMPSRAYVGRFNFKGTDQGKRVGELSGGERGRLHLAKLLQVGGNVL 466
Cdd:PRK10636 92 rqleaqlhdanerNDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489953208 467 LLDEPTNDLDIETLRALENALLEFPGCAMVISHDRWFLDRIATHILDYQDEGKVEfFEGNFTEYE 531
Cdd:PRK10636 172 LLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFE-YTGNYSSFE 235
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
324-484 |
7.37e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 103.77 E-value: 7.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVdqfRDAMDNSK 402
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVaGDDVEALSA---RAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 403 TVWEEVSGGLD-----IMRIGNTEMPSR---------AYVGR-FNFKGTDQ--GKRVGELSGGERGRLHLAKLLQVGGNV 465
Cdd:PRK09536 81 SVPQDTSLSFEfdvrqVVEMGRTPHRSRfdtwtetdrAAVERaMERTGVAQfaDRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180
....*....|....*....|
gi 489953208 466 LLLDEPTNDLDI-ETLRALE 484
Cdd:PRK09536 161 LLLDEPTASLDInHQVRTLE 180
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
324-499 |
1.20e-23 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 97.50 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVdqfRDAMDNsk 402
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVdGKEVSFASP---RDARRA-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 403 tvweevsggldimRIGntempsrayvgrfnfkgtdqgkRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLD------ 476
Cdd:cd03216 76 -------------GIA----------------------MVYQLSVGERQMVEIARALARNARLLILDEPTAALTpaever 120
|
170 180
....*....|....*....|....*
gi 489953208 477 -IETLRALENAllefpGCAMV-ISH 499
Cdd:cd03216 121 lFKVIRRLRAQ-----GVAVIfISH 140
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
8-236 |
1.74e-23 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 98.97 E-value: 1.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 8 MHRVGKVVPPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEAR---------PQPGI-----KIGY 73
Cdd:COG2884 4 FENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLvngqdlsrlKRREIpylrrRIGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 74 LPQEPQLNPEHTVRESVEeavsevvnalkgldevyakyaepdadfdkLAAQ-QGKYEEIIQahdghnlnvqlERAADALr 152
Cdd:COG2884 84 VFQDFRLLPDRTVYENVA-----------------------------LPLRvTGKSRKEIR-----------RRVREVL- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 153 lpDW-------DAKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EG-TVVAITHDRYFL 222
Cdd:COG2884 123 --DLvglsdkaKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEInrRGtTVLIATHDLELV 200
|
250
....*....|....
gi 489953208 223 DNVAGWILELDRGE 236
Cdd:COG2884 201 DRMPKRVLELEDGR 214
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
324-529 |
1.75e-23 |
|
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: 104.07 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGD-RVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGEtVKLASVDQfrdamdnsK 402
Cdd:COG4988 337 IELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILING-VDLSDLDP--------A 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 403 TVWEEVS----------GGL-DIMRIGNTEMPS--------RAYVGRFnFKGTDQG--KRVGE----LSGGERGRLHLAK 457
Cdd:COG4988 408 SWRRQIAwvpqnpylfaGTIrENLRLGRPDASDeeleaaleAAGLDEF-VAALPDGldTPLGEggrgLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489953208 458 LLQVGGNVLLLDEPTNDLDIETLRALENALLEFPG--CAMVISHdRWFLDRIATHILDYQDEGKVEffEGNFTE 529
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKgrTVILITH-RLALLAQADRILVLDDGRIVE--QGTHEE 557
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
18-218 |
1.88e-23 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 98.96 E-value: 1.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARpqpgI-------------------KIGYLPQEP 78
Cdd:COG1136 20 EVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVL----IdgqdisslserelarlrrrHIGFVFQFF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 79 QLNPEHTVRESVEeavseVVNALKGLDEVYAKyaepdadfdklaaqqgkyeeiiqahdghnlnvqlERAADALR---LPD 155
Cdd:COG1136 96 NLLPELTALENVA-----LPLLLAGVSRKERR----------------------------------ERARELLErvgLGD 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489953208 156 W-DAKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDFEGTVVAITHD 218
Cdd:COG1136 137 RlDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHD 204
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
19-236 |
2.07e-23 |
|
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: 97.07 E-value: 2.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG----------ID----TDIEGEARPQpgiKIGYLPQEPQLNPEh 84
Cdd:cd03228 15 KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRlydptsgeilIDgvdlRDLDLESLRK---NIAYVPQDPFLFSG- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 85 TVREsveeavsevvnalkgldevyakyaepdadfdklaaqqgkyeeiiqahdghNLnvqleraadalrlpdwdakianLS 164
Cdd:cd03228 91 TIRE--------------------------------------------------NI----------------------LS 98
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489953208 165 GGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEG--TVVAITHdRYFLDNVAGWILELDRGE 236
Cdd:cd03228 99 GGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKgkTVIVIAH-RLSTIRDADRIIVLDDGR 171
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
17-196 |
2.45e-23 |
|
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: 98.03 E-value: 2.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 17 PKRHILKNISLSFFPGAkIGVLGLNGAGKSTLLRIMAGIDTDIEG-------EARPQPGI---KIGYLPQEPQLNPEHTV 86
Cdd:cd03264 11 GKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGtiridgqDVLKQPQKlrrRIGYLPQEFGVYPNFTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 87 RESVEEAVsevvnALKGLdevyakyaePDADFDKLAaqqgkyEEIIQAhdghnlnVQLERAADAlrlpdwdaKIANLSGG 166
Cdd:cd03264 90 REFLDYIA-----WLKGI---------PSKEVKARV------DEVLEL-------VNLGDRAKK--------KIGSLSGG 134
|
170 180 190
....*....|....*....|....*....|
gi 489953208 167 ERRRVALCRLLLEKPDMLLLDEPTNHLDAE 196
Cdd:cd03264 135 MRRRVGIAQALVGDPSILIVDEPTAGLDPE 164
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
324-501 |
3.09e-23 |
|
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: 98.57 E-value: 3.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQ------FRD 396
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFgGEDATDVPVQErnvgfvFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 397 -AMDNSKTVWEEVSGGLDIMRIgnTEMPSRAYVGR-----FNFKGTDQ-GKRV-GELSGGERGRLHLAKLLQVGGNVLLL 468
Cdd:cd03296 83 yALFRHMTVFDNVAFGLRVKPR--SERPPEAEIRAkvhelLKLVQLDWlADRYpAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190
....*....|....*....|....*....|...
gi 489953208 469 DEPTNDLDIETLRALENALLEFpgcamvisHDR 501
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRL--------HDE 185
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
20-219 |
6.16e-23 |
|
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: 96.82 E-value: 6.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE---------ARPQPGIKIGYLPQEPQLNPEHTVRESV 90
Cdd:cd03259 14 RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEilidgrdvtGVPPERRNIGMVFQDYALFPHLTVAENI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 91 eeavsevvnalkgldeVYAkyaepdadfdkLAAQQGKYEEIIQahdghnlnvQLERAADALRLPDW-DAKIANLSGGERR 169
Cdd:cd03259 94 ----------------AFG-----------LKLRGVPKAEIRA---------RVRELLELVGLEGLlNRYPHELSGGQQQ 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489953208 170 RVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDFEGTVVAITHDR 219
Cdd:cd03259 138 RVALARALAREPSLLLLDEPLSALDAKLreelREELKELQRELGITTIYVTHDQ 191
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
22-508 |
1.69e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 100.87 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDT-D-----IEGEAR----PQPGIK--IGYLPQEPQLNPEHTVRES 89
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQpDsgeilIDGKPVrirsPRDAIAlgIGMVHQHFMLVPNLTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 90 VeeavsevvnALkGLDEVyakyAEPDADFDKLAAQqgkyeeiiqahdghnlnvqLERAADALRLP-DWDAKIANLSGGER 168
Cdd:COG3845 101 I---------VL-GLEPT----KGGRLDRKAARAR-------------------IRELSERYGLDvDPDAKVEDLSVGEQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 169 RRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EG-TVVAITHDryfLDNVagwiLEL-DR------GEGI 238
Cdd:COG3845 148 QRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLaaEGkSIIFITHK---LREV----MAIaDRvtvlrrGKVV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 239 pwegnysswleqkDQRLAQEASQEaarrksiekELewvrqgAK---GRqskgkarlarfeelnnteyqkrnETNELFIPP 315
Cdd:COG3845 221 -------------GTVDTAETSEE---------EL------AElmvGR-----------------------EVLLRVEKA 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 316 GARLGDKVVEVTNLR-KSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQ 393
Cdd:COG3845 250 PAEPGEVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLdGEDITGLSPRE 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 394 FRDA---------------MDNSktVWE----------EVSGGLdIMRIGNTEMPSRAYVGRFNFKGTDQGKRVGELSGG 448
Cdd:COG3845 330 RRRLgvayipedrlgrglvPDMS--VAEnlilgryrrpPFSRGG-FLDRKAIRAFAEELIEEFDVRTPGPDTPARSLSGG 406
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489953208 449 ERGRLHLAKLLQVGGNVLLLDEPTNDLDI-------ETLRALENAllefpGCA-MVISHDrwfL-------DRIA 508
Cdd:COG3845 407 NQQKVILARELSRDPKLLIAAQPTRGLDVgaiefihQRLLELRDA-----GAAvLLISED---LdeilalsDRIA 473
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
21-508 |
2.09e-22 |
|
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: 100.65 E-value: 2.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDtdiegEARPQPG---IKIGYLPQEPQLNPEHTVRESV----EEA 93
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMD-----QYEPTSGriiYHVALCEKCGYVERPSKVGEPCpvcgGTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 94 VSEVVNALKGLDEVYAKYAEPDADFDK----LAAQQGKYEEIIQA-HD-GHNLNVQLERAADALRLPDWDAKIA----NL 163
Cdd:TIGR03269 90 EPEEVDFWNLSDKLRRRIRKRIAIMLQrtfaLYGDDTVLDNVLEAlEEiGYEGKEAVGRAVDLIEMVQLSHRIThiarDL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 164 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESV----AWLERFLHDFEGTVVAITHDRYFLDNVAgwileldrgegip 239
Cdd:TIGR03269 170 SGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAklvhNALEEAVKASGISMVLTSHWPEVIEDLS------------- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 240 wegNYSSWLEQKdqrlaqEASQEAARRKSIEKELEWVRQgakgrqskgkarLARFEELnnteyqkrnetnelfippgaRL 319
Cdd:TIGR03269 237 ---DKAIWLENG------EIKEEGTPDEVVAVFMEGVSE------------VEKECEV--------------------EV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 320 GDKVVEVTNLRKSYG--DRVLI---DDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGS--ITLGE-------- 384
Cdd:TIGR03269 276 GEPIIKVRNVSKRYIsvDRGVVkavDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDewvdmtkp 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 385 --------TVKLASVDQ------FRDAMDN-SKTVWEEVSGGLDIMR-------IGNTEMPSRAYVGRFnfkgTDqgkrv 442
Cdd:TIGR03269 356 gpdgrgraKRYIGILHQeydlypHRTVLDNlTEAIGLELPDELARMKavitlkmVGFDEEKAEEILDKY----PD----- 426
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489953208 443 gELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIETLRALENALL----EFPGCAMVISHDRWFL----DRIA 508
Cdd:TIGR03269 427 -ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILkareEMEQTFIIVSHDMDFVldvcDRAA 499
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
320-499 |
2.51e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 100.49 E-value: 2.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 320 GDKVVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASvdqFRDAM 398
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIdGKPVRIRS---PRDAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 399 DN-------------SKTVWEEVSGGLDIMRIGNTEMPS-----RAYVGRFNFKgTDQGKRVGELSGGERGRLHLAKLLQ 460
Cdd:COG3845 79 ALgigmvhqhfmlvpNLTVAENIVLGLEPTKGGRLDRKAarariRELSERYGLD-VDPDAKVEDLSVGEQQRVEILKALY 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489953208 461 VGGNVLLLDEPT--------NDLdIETLRALENAllefpGCAMV-ISH 499
Cdd:COG3845 158 RGARILILDEPTavltpqeaDEL-FEILRRLAAE-----GKSIIfITH 199
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
16-238 |
3.13e-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: 94.63 E-value: 3.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE--------ARPQPGIKIGYLPQEPQlnpEHTVR 87
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSillngkpiKAKERRKSIGYVMQDVD---YQLFT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 88 ESVEEAVsevvnaLKGLDEVYAKYAEPDADFDKLaaqqgkyeEIIQAHDGHNLNvqleraadalrlpdwdakianLSGGE 167
Cdd:cd03226 87 DSVREEL------LLGLKELDAGNEQAETVLKDL--------DLYALKERHPLS---------------------LSGGQ 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489953208 168 RRRVALCRLLLEKPDMLLLDEPTNHLDA---ESVAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRGEGI 238
Cdd:cd03226 132 KQRLAIAAALLSGKDLLIFDEPTSGLDYknmERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
16-234 |
4.63e-22 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 99.67 E-value: 4.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE----ARPQPGIK-------IGYLPQEPQLnPEH 84
Cdd:TIGR02857 332 PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSiavnGVPLADADadswrdqIAWVPQHPFL-FAG 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 85 TVRESVeeavsevvnalkgldevyaKYAEPDADFDKL--AAQQGKYEEIIQAhdghnlnvqleraadalrLPD-WDAKI- 160
Cdd:TIGR02857 411 TIAENI-------------------RLARPDASDAEIreALERAGLDEFVAA------------------LPQgLDTPIg 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489953208 161 ---ANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEG--TVVAITHDRyfldnvaGWILELDR 234
Cdd:TIGR02857 454 eggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRL-------ALAALADR 525
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
332-500 |
5.08e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 93.84 E-value: 5.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 332 SYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETVKLASVDQfRDAMDNS--KTVWEEVS 409
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ-RSEVPDSlpLTVRDLVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 410 GGLdIMRIGNTEMPSRA----------YVGRFNFkgtdQGKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIET 479
Cdd:NF040873 80 MGR-WARRGLWRRLTRDdraavddaleRVGLADL----AGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154
|
170 180
....*....|....*....|....
gi 489953208 480 LRALENALLEFPG---CAMVISHD 500
Cdd:NF040873 155 RERIIALLAEEHArgaTVVVVTHD 178
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
324-520 |
5.39e-22 |
|
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: 94.13 E-value: 5.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETV---KLASVDQFRDAMD- 399
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKltdDKKNINELRQKVGm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 400 --------NSKTVWEEVSGGLDIMR-IGNTEMPSRAY-----VGRFNFKgtdqGKRVGELSGGERGRLHLAKLLQVGGNV 465
Cdd:cd03262 81 vfqqfnlfPHLTVLENITLAPIKVKgMSKAEAEERALellekVGLADKA----DAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489953208 466 LLLDEPTNDLDIETLRALENALLEFP--GCAMVI-SHDRWFLDRIATHILdYQDEGKV 520
Cdd:cd03262 157 MLFDEPTSALDPELVGEVLDVMKDLAeeGMTMVVvTHEMGFAREVADRVI-FMDDGRI 213
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
324-471 |
7.04e-22 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 94.53 E-value: 7.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGET--VKL------------- 388
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQdiTKLpmhkrarlgigyl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 389 ---ASVdqFRDAmdnskTVWEEVSGGLDIMRIGNTEMPSR--AYVGRFNFKGTdQGKRVGELSGGERGRLHLAKLLQVGG 463
Cdd:cd03218 81 pqeASI--FRKL-----TVEENILAVLEIRGLSKKEREEKleELLEEFHITHL-RKSKASSLSGGERRRVEIARALATNP 152
|
....*...
gi 489953208 464 NVLLLDEP 471
Cdd:cd03218 153 KFLLLDEP 160
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
323-394 |
8.68e-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: 8.68e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489953208 323 VVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQF 394
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWdGEPLDPEDRRRI 73
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
324-513 |
9.14e-22 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 93.41 E-value: 9.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDRVLIDDLTFSVPKGaIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETVKLASVDQFRDAM----- 398
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIgylpq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 399 ----DNSKTVWEEvsggLDIM----RIGNTEMPSRA-----YVGRFNFKgtdqGKRVGELSGGERGRLHLAKLLQVGGNV 465
Cdd:cd03264 80 efgvYPNFTVREF----LDYIawlkGIPSKEVKARVdevleLVNLGDRA----KKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489953208 466 LLLDEPTNDLDIETLRALENALLEfpgcamvISHDRWFLdrIATHILD 513
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSE-------LGEDRIVI--LSTHIVE 190
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
325-520 |
1.14e-21 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 93.09 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 325 EVTNLRKSYGDRVLI-DDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGEtVKLASVDQFRDA---MDN 400
Cdd:cd03226 1 RIENISFSYKKGTEIlDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG-KPIKAKERRKSIgyvMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 401 ------SKTVWEEVSGGLDIMRIGNTEmpSRAYVGRFN-FKGTDQGKRvgELSGGERGRLHLAKLLQVGGNVLLLDEPTN 473
Cdd:cd03226 80 vdyqlfTDSVREELLLGLKELDAGNEQ--AETVLKDLDlYALKERHPL--SLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489953208 474 DLDIETLRALENALLEFP--GCAM-VISHDRWFLDRIATHILdYQDEGKV 520
Cdd:cd03226 156 GLDYKNMERVGELIRELAaqGKAViVITHDYEFLAKVCDRVL-LLANGAI 204
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
14-235 |
1.17e-21 |
|
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: 98.57 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 14 VVPP--KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEGEARPQPGIKIGYLPQEPQL 80
Cdd:TIGR01842 324 IVPPggKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIwpptsgsvrldGADLKQWDRETFGKHIGYLPQDVEL 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 81 NPeHTVRESVeeavsevvnalkgldevyakyaepdADFDKLAAQqgkyEEIIQAhdghnlnvqlERAADA----LRLPD- 155
Cdd:TIGR01842 404 FP-GTVAENI-------------------------ARFGENADP----EKIIEA----------AKLAGVheliLRLPDg 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 156 WDAKI----ANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFE---GTVVAITHdRYFLDNVAGW 228
Cdd:TIGR01842 444 YDTVIgpggATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKargITVVVITH-RPSLLGCVDK 522
|
....*..
gi 489953208 229 ILELDRG 235
Cdd:TIGR01842 523 ILVLQDG 529
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
16-236 |
1.35e-21 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 98.31 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG----------ID-TDIE----GEARPQpgikIGYLPQEPQL 80
Cdd:COG1132 350 PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRfydptsgrilIDgVDIRdltlESLRRQ----IGVVPQDTFL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 81 NPEhTVRESVeeavsevvnalkgldevyaKYAEPDADFDKL--AAqqgkyeEIIQAHDghnlnvqleraaDALRLPD-WD 157
Cdd:COG1132 426 FSG-TIRENI-------------------RYGRPDATDEEVeeAA------KAAQAHE------------FIEALPDgYD 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 158 AKI----ANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAW----LERFLHDfeGTVVAITH--------DRyf 221
Cdd:COG1132 468 TVVgergVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALiqeaLERLMKG--RTTIVIAHrlstirnaDR-- 543
|
250
....*....|....*
gi 489953208 222 ldnvagwILELDRGE 236
Cdd:COG1132 544 -------ILVLDDGR 551
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
325-471 |
1.90e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 93.56 E-value: 1.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 325 EVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETV--KL-------------- 388
Cdd:COG1137 5 EAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDitHLpmhkrarlgigylp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 389 --ASVdqFRDAmdnskTVWEevsgglDIMRIGNTEMPSRAyvgrfnfkgtDQGKRVGEL-----------------SGGE 449
Cdd:COG1137 85 qeASI--FRKL-----TVED------NILAVLELRKLSKK----------EREERLEELleefgithlrkskayslSGGE 141
|
170 180
....*....|....*....|..
gi 489953208 450 RGRLHLAKLLQVGGNVLLLDEP 471
Cdd:COG1137 142 RRRVEIARALATNPKFILLDEP 163
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
324-479 |
1.98e-21 |
|
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: 92.82 E-value: 1.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETV---------KLASVDQ 393
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVaGHDVvreprevrrRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 394 FRdAMDNSKTVWEEVSGGLDIMRIGNTEMPSRA-----YVGRFNFKgtdqGKRVGELSGGERGRLHLAKLLQVGGNVLLL 468
Cdd:cd03265 81 DL-SVDDELTGWENLYIHARLYGVPGAERRERIdelldFVGLLEAA----DRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170
....*....|.
gi 489953208 469 DEPTNDLDIET 479
Cdd:cd03265 156 DEPTIGLDPQT 166
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
18-218 |
2.79e-21 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 92.36 E-value: 2.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 18 KRHILKNISLSF-FPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEAR---------------PQPGIKIGYLPQEPQLN 81
Cdd:cd03297 8 KRLPDFTLKIDFdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVlngtvlfdsrkkinlPPQQRKIGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 82 PEHTVRESVEeavsevvNALKGLDEvyakyaepdadfdklAAQQGKYEEIIQAhdghnlnVQLERAADAlrlpdwdaKIA 161
Cdd:cd03297 88 PHLNVRENLA-------FGLKRKRN---------------REDRISVDELLDL-------LGLDHLLNR--------YPA 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489953208 162 NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDFEGTVVAITHD 218
Cdd:cd03297 131 QLSGGEKQRVALARALAAQPELLLLDEPFSALDRALrlqlLPELKQIKKNLNIPVIFVTHD 191
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
323-512 |
4.80e-21 |
|
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: 91.80 E-value: 4.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 323 VVEVTNLRKSY----GDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETVKLASVDQ----- 393
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 394 -------FRDAM---DNSKTVWEEVSGGLDIMRIGNTEMPSRAYVGRfNFKGTDQGKRV-----GELSGGERGRLHLAKL 458
Cdd:cd03257 81 rkeiqmvFQDPMsslNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLL-LLVGVGLPEEVlnrypHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489953208 459 LQVGGNVLLLDEPTNDLD-------IETLRALENALlefpGCAMV-ISHDRWFLDRIATHIL 512
Cdd:cd03257 160 LALNPKLLIADEPTSALDvsvqaqiLDLLKKLQEEL----GLTLLfITHDLGVVAKIADRVA 217
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
18-217 |
6.42e-21 |
|
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: 91.12 E-value: 6.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEAR---------PQPGIKIGYLPQEPQLNPEHTVRE 88
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITfdgksyqknIEALRRIGALIEAPGFYPNLTARE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 89 SVeeavsevvnalkgldEVYAKYAepdadfdklaaqQGKYEEIIQAhdghnLNVQLERAADalrlpdwDAKIANLSGGER 168
Cdd:cd03268 92 NL---------------RLLARLL------------GIRKKRIDEV-----LDVVGLKDSA-------KKKVKGFSLGMK 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489953208 169 RRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLH---DFEGTVVAITH 217
Cdd:cd03268 133 QRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILslrDQGITVLISSH 184
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
5-217 |
8.75e-21 |
|
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: 90.30 E-value: 8.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 5 VYTMHRVGKVvppKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG--IDTDIEGE----ARPQPGIK----IGYL 74
Cdd:cd03213 11 VTVKSSPSKS---GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEvlinGRPLDKRSfrkiIGYV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 75 PQEPQLNPEHTVRESVEeavsevvnalkgldevYAkyaepdadfdklaaqqgkyeeiiqahdghnlnvqleraadalrlp 154
Cdd:cd03213 88 PQDDILHPTLTVRETLM----------------FA--------------------------------------------- 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489953208 155 dwdAKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD---AESVAWLERFLHDFEGTVVAITH 217
Cdd:cd03213 107 ---AKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDsssALQVMSLLRRLADTGRTIICSIH 169
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
9-218 |
9.37e-21 |
|
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: 91.48 E-value: 9.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 9 HRVGKVVPPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDI---EGEARPQPGIKIGYL 74
Cdd:cd03256 4 ENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLveptsgsvlidGTDInklKGKALRQLRRQIGMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 75 PQEPQLNPEHTVRESVEEAVSEVVNALKGLdevyakyaepdadfdklaAQQGKYEEIiqahdghnlnvqlERAADALR-- 152
Cdd:cd03256 84 FQQFNLIERLSVLENVLSGRLGRRSTWRSL------------------FGLFPKEEK-------------QRALAALErv 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489953208 153 --LPDWDAKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD---AESV-AWLERFLHDFEGTVVAITHD 218
Cdd:cd03256 133 glLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDpasSRQVmDLLKRINREEGITVIVSLHQ 204
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
18-236 |
1.03e-20 |
|
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: 89.55 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE-------------ARPQPGIKIGYLPQEPQLNPEH 84
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSilidgedltdledELPPLRRRIGMVFQDFALFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 85 TVRESVEEAvsevvnalkgldevyakyaepdadfdklaaqqgkyeeiiqahdghnlnvqleraadalrlpdwdakianLS 164
Cdd:cd03229 92 TVLENIALG---------------------------------------------------------------------LS 102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489953208 165 GGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERF---LHDFEG-TVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:cd03229 103 GGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALlksLQAQLGiTVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
17-218 |
1.09e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 89.99 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQPGIKIGYLPQEPQLNPEHTVResVEEAVSE 96
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSLPLT--VRDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 97 VVNALKGLdevyakYAEPDADfDKLAaqqgkyeeiiqahdghnlnvqLERAADALRLPDW-DAKIANLSGGERRRVALCR 175
Cdd:NF040873 81 GRWARRGL------WRRLTRD-DRAA---------------------VDDALERVGLADLaGRQLGELSGGQRQRALLAQ 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489953208 176 LLLEKPDMLLLDEPTNHLDAESVAWLE---RFLHDFEGTVVAITHD 218
Cdd:NF040873 133 GLAQEADLLLLDEPTTGLDAESRERIIallAEEHARGATVVVVTHD 178
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
306-500 |
1.38e-20 |
|
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: 95.67 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 306 NETNELFIPPGARLGDkvVEVTNLRKSYGDRV--LIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLG 383
Cdd:COG2274 458 REEGRSKLSLPRLKGD--IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILID 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 384 ----ETVKLAS-------VDQ----F----RD--AMDNS----KTVWE--EVSGGLD-IMRignteMPsrayvgrfnfKG 435
Cdd:COG2274 536 gidlRQIDPASlrrqigvVLQdvflFsgtiREniTLGDPdatdEEIIEaaRLAGLHDfIEA-----LP----------MG 600
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489953208 436 TDQgkRVGE----LSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIETLRALENALLE-FPGCAM-VISHD 500
Cdd:COG2274 601 YDT--VVGEggsnLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRlLKGRTViIIAHR 669
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
325-507 |
1.40e-20 |
|
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: 91.09 E-value: 1.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 325 EVTNLRKSYGD-RVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGET----VKLASVDQFR---- 395
Cdd:cd03256 2 EVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinkLKGKALRQLRrqig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 396 ------------DAMDN-------SKTVW---------EEVSGGLDIM-RIGnteMPSRAYvgrfnfkgtdqgKRVGELS 446
Cdd:cd03256 82 mifqqfnlierlSVLENvlsgrlgRRSTWrslfglfpkEEKQRALAALeRVG---LLDKAY------------QRADQLS 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489953208 447 GGERGRLHLAKLLQVGGNVLLLDEPTNDLDIETLRALENALLEFP---GCAMVIS-HD----RWFLDRI 507
Cdd:cd03256 147 GGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINreeGITVIVSlHQvdlaREYADRI 215
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
22-235 |
1.50e-20 |
|
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: 90.86 E-value: 1.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTD------IEGEARPQPGIK---IGYLPQEPQLNPEHTVREsvee 92
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPdsgtilFGGEDATDVPVQernVGFVFQHYALFRHMTVFD---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 93 avsevvNALKGLDEVYAKYAEPDADFDKlaaqqgKYEEIIQAhdghnlnVQLERAADalRLPdwdakiANLSGGERRRVA 172
Cdd:cd03296 94 ------NVAFGLRVKPRSERPPEAEIRA------KVHELLKL-------VQLDWLAD--RYP------AQLSGGQRQRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489953208 173 LCRLLLEKPDMLLLDEPTNHLDA----ESVAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRG 235
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAkvrkELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKG 213
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
324-513 |
1.64e-20 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 90.12 E-value: 1.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDR----VLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQFR--- 395
Cdd:cd03266 2 ITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVdGFDVVKEPAEARRrlg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 396 -----DAMDNSKTVWEEVS--GGLDIMRIGNTEMPSRAYVGRFNFKGTDQgKRVGELSGGERGRLHLAKLLQVGGNVLLL 468
Cdd:cd03266 82 fvsdsTGLYDRLTARENLEyfAGLYGLKGDELTARLEELADRLGMEELLD-RRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489953208 469 DEPTNDLDIETLRALENALLEF--PGCAMVIShdrwfldriaTHILD 513
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLraLGKCILFS----------THIMQ 197
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
324-501 |
1.77e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 92.86 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQfRD------ 396
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIdGEDVTHRSIQQ-RDicmvfq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 397 --AMDNSKTVWEEVSGGLDIMRIGNTEMPSR-----AYVGRFNFkgtdQGKRVGELSGGERGRLHLAKLLQVGGNVLLLD 469
Cdd:PRK11432 86 syALFPHMSLGENVGYGLKMLGVPKEERKQRvkealELVDLAGF----EDRYVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 489953208 470 EPTNDLDIETLRALENALLE----FPGCAMVISHDR 501
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRElqqqFNITSLYVTHDQ 197
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
19-217 |
2.85e-20 |
|
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: 90.14 E-value: 2.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------GIDTDIEGEARPQPGI-----KIGYLpqEPQLNPEHTV 86
Cdd:COG1119 16 KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITgdlpptyGNDVRLFGERRGGEDVwelrkRIGLV--SPALQLRFPR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 87 RESVEEAVsevvnaLKGLDEVYAKYAEPDADfdklaaqqgkyeeiiqahdghnlnvQLERAADALRLpdW------DAKI 160
Cdd:COG1119 94 DETVLDVV------LSGFFDSIGLYREPTDE-------------------------QRERARELLEL--LglahlaDRPF 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489953208 161 ANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDFEGTVVAITH 217
Cdd:COG1119 141 GTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGArellLALLDKLAAEGAPTLVLVTH 201
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
19-218 |
2.95e-20 |
|
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: 90.26 E-value: 2.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEGEARPQPGIKIGYLPQEPQLNPEHTVR 87
Cdd:TIGR03873 14 RLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGAlrpdagtvdlaGVDLHGLSRRARARRVALVEQDSDTAVPLTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 88 ESVeeavsevvnALKGLDEVYAKYAEPDADFDKLAAQQGKyeeiiqahdghnlnVQLERAADAlrlpDWDAkianLSGGE 167
Cdd:TIGR03873 94 DVV---------ALGRIPHRSLWAGDSPHDAAVVDRALAR--------------TELSHLADR----DMST----LSGGE 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489953208 168 RRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEG---TVVAITHD 218
Cdd:TIGR03873 143 RQRVHVARALAQEPKLLLLDEPTNHLDVRAQLETLALVRELAAtgvTVVAALHD 196
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
324-476 |
3.78e-20 |
|
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: 89.60 E-value: 3.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGEtVKLASVDQFRD------- 396
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG-KDITNLPPHKRpvntvfq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 397 --AMDNSKTVWEEVSGGLDIMRIGNTEMPSRA--YVGRFNFKGTDQgKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPT 472
Cdd:cd03300 80 nyALFPHLTVFENIAFGLRLKKLPKAEIKERVaeALDLVQLEGYAN-RKPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
....
gi 489953208 473 NDLD 476
Cdd:cd03300 159 GALD 162
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
325-499 |
6.22e-20 |
|
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: 87.27 E-value: 6.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 325 EVTNLRKSYGD--RVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQFRDamdns 401
Cdd:cd03246 2 EVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLdGADISQWDPNELGD----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 402 ktvweevsggldimRIGntempsraYVGRFN--FKGTdqgkrVGE--LSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDI 477
Cdd:cd03246 77 --------------HVG--------YLPQDDelFSGS-----IAEniLSGGQRQRLGLARALYGNPRILVLDEPNSHLDV 129
|
170 180
....*....|....*....|....*
gi 489953208 478 ETLRALENALLEFPGC---AMVISH 499
Cdd:cd03246 130 EGERALNQAIAALKAAgatRIVIAH 154
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
323-516 |
6.66e-20 |
|
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: 88.65 E-value: 6.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 323 VVEVTNLRKSY-----GDRVL--IDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL---GETVKLAS-- 390
Cdd:COG4778 4 LLEVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdGGWVDLAQas 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 391 --------------VDQFRDAMDNSKTvweevsggLDIMrigntEMPSRAyvgrfnfKGTDQG---KRVGEL-------- 445
Cdd:COG4778 84 preilalrrrtigyVSQFLRVIPRVSA--------LDVV-----AEPLLE-------RGVDREearARARELlarlnlpe 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 446 ----------SGGERGRLHLAKLLQVGGNVLLLDEPTNDLD-------IETLRALENAllefpGCAMV-ISHDRWFLDRI 507
Cdd:COG4778 144 rlwdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDaanravvVELIEEAKAR-----GTAIIgIFHDEEVREAV 218
|
....*....
gi 489953208 508 ATHILDYQD 516
Cdd:COG4778 219 ADRVVDVTP 227
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
19-242 |
6.86e-20 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 88.71 E-value: 6.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDT-----------DIEG--EARPQP-GIKIGYLPQEPQLNPEH 84
Cdd:cd03261 13 RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRpdsgevlidgeDISGlsEAELYRlRRRMGMLFQSGALFDSL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 85 TVRESVEEAVSEvvnalkgldevyaKYAEPDADFDKLAAqqgkyeEIIQAhdghnlnVQLERAADalRLPdwdakiANLS 164
Cdd:cd03261 93 TVFENVAFPLRE-------------HTRLSEEEIREIVL------EKLEA-------VGLRGAED--LYP------AELS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 165 GGERRRVALCRLLLEKPDMLLLDEPTNHLD---AESVAWLERFLHDFEG-TVVAITHDRYFLDNVAGWILELDRGEgIPW 240
Cdd:cd03261 139 GGMKKRVALARALALDPELLLYDEPTAGLDpiaSGVIDDLIRSLKKELGlTSIMVTHDLDTAFAIADRIAVLYDGK-IVA 217
|
..
gi 489953208 241 EG 242
Cdd:cd03261 218 EG 219
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
291-512 |
8.18e-20 |
|
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: 92.91 E-value: 8.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 291 LARFEELNNTEYQKRNETNELFIPPGARLgdkvvEVTNLRKSY--GDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRM 368
Cdd:COG4987 306 ARRLNELLDAPPAVTEPAEPAPAPGGPSL-----ELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLAL 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 369 MSGQEQPDSGSITLGET-VKLASVDQFRDAM-----DN---SKTVweevsggLDIMRIGN--------TEMPSRAYVGRF 431
Cdd:COG4987 381 LLRFLDPQSGSITLGGVdLRDLDEDDLRRRIavvpqRPhlfDTTL-------RENLRLARpdatdeelWAALERVGLGDW 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 432 nFKGTDQG--KRVGE----LSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIETLRALENALLE-FPGCAMV-ISHDRWF 503
Cdd:COG4987 454 -LAALPDGldTWLGEggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEaLAGRTVLlITHRLAG 532
|
....*....
gi 489953208 504 LDRiATHIL 512
Cdd:COG4987 533 LER-MDRIL 540
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
324-479 |
8.73e-20 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 90.52 E-value: 8.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSY----GDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQFRDA- 397
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVdGVDLTALSERELRAAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 398 ----M----DN---SKTVWEEVSGGLDIMRIGNTEMPSRA-----YVGRfnfkgTDQGKR-VGELSGGERGRLHLAKLLQ 460
Cdd:COG1135 82 rkigMifqhFNllsSRTVAENVALPLEIAGVPKAEIRKRVaelleLVGL-----SDKADAyPSQLSGGQKQRVGIARALA 156
|
170
....*....|....*....
gi 489953208 461 VGGNVLLLDEPTNDLDIET 479
Cdd:COG1135 157 NNPKVLLCDEATSALDPET 175
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
323-521 |
1.16e-19 |
|
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: 92.27 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 323 VVEVTNLRKSY--GDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPD---SGSITLGETVKLASVDQFR-- 395
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRgr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 396 -------DAMD--NSKTVWEEVSGGLDIMRIGNTEMPSRAY-----VGRFNFKgtdqGKRVGELSGGERGRLHLAKLLQV 461
Cdd:COG1123 84 rigmvfqDPMTqlNPVTVGDQIAEALENLGLSRAEARARVLelleaVGLERRL----DRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489953208 462 GGNVLLLDEPTNDLDIETLR---ALENALLEFPGCAMV-ISHDRWFLDRIATHILDYQDEGKVE 521
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAeilDLLRELQRERGTTVLlITHDLGVVAEIADRVVVMDDGRIVE 223
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
323-511 |
1.19e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 87.24 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 323 VVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL----GETVKLASVDQF---R 395
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLdggdIDDPDVAEACHYlghR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 396 DAMDNSKTVWEEVSGGLDIMriGNTEMPSRAYVGRFNFKGTdQGKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDL 475
Cdd:PRK13539 82 NAMKPALTVAENLEFWAAFL--GGEELDIAAALEAVGLAPL-AHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 489953208 476 DIETLRALENAL---LEFPGcaMVIshdrwfldrIATHI 511
Cdd:PRK13539 159 DAAAVALFAELIrahLAQGG--IVI---------AATHI 186
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
37-386 |
1.53e-19 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 91.61 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 37 VLGLNGAGKSTLLRIMAGIDTDIEGEArpqpgikigylpqepQLNPEHTVRESVEEA---VSEVV----NALKGLDEvya 109
Cdd:PRK10938 34 FVGANGSGKSALARALAGELPLLSGER---------------QSQFSHITRLSFEQLqklVSDEWqrnnTDMLSPGE--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 110 kyaepdADFDKLAAqqgkyeEIIQahDGHNLNVQLERAADALRLPDW-DAKIANLSGGERRRVALCRLLLEKPDMLLLDE 188
Cdd:PRK10938 96 ------DDTGRTTA------EIIQ--DEVKDPARCEQLAQQFGITALlDRRFKYLSTGETRKTLLCQALMSEPDLLILDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 189 PTNHLDAESVAWLERFLHDFEGTVVAIthdryfldnvagwILELDRGEGIPwegnysswleqkdqrlaqeasqEAARRKS 268
Cdd:PRK10938 162 PFDGLDVASRQQLAELLASLHQSGITL-------------VLVLNRFDEIP----------------------DFVQFAG 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 269 IEKELEWVRQGAKGR--QSKGKARLARFEELNNT------EYQKRNEtnelfIPPGA---RLGDKVVevtnlrkSYGDRV 337
Cdd:PRK10938 207 VLADCTLAETGEREEilQQALVAQLAHSEQLEGVqlpepdEPSARHA-----LPANEpriVLNNGVV-------SYNDRP 274
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 489953208 338 LIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQE-QPDSGSITL-------GETV 386
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHpQGYSNDLTLfgrrrgsGETI 331
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
323-512 |
1.61e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 87.42 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 323 VVEVTNLRKSY-GDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLG--ETVKLAS--------- 390
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNgqDLSRLKRreipylrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 391 ---VDQ-FRDAMDnsKTVWEEVSGGLDIMRIGNTEMPSRA-----YVGRFNFKgtdqGKRVGELSGGERGRLHLAKLLqV 461
Cdd:COG2884 81 igvVFQdFRLLPD--RTVYENVALPLRVTGKSRKEIRRRVrevldLVGLSDKA----KALPHELSGGEQQRVAIARAL-V 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489953208 462 ggN---VLLLDEPTNDLDIETLRALENALLEF--PGCAMVI-SHDRWFLDRIATHIL 512
Cdd:COG2884 154 --NrpeLLLADEPTGNLDPETSWEIMELLEEInrRGTTVLIaTHDLELVDRMPKRVL 208
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
16-218 |
1.73e-19 |
|
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: 91.65 E-value: 1.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE---------ARPQPGIK--IGYLPQEPQLNpEH 84
Cdd:TIGR02868 345 PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEvtldgvpvsSLDQDEVRrrVSVCAQDAHLF-DT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 85 TVRESVeeavsevvnalkgldevyaKYAEPDADFDKLAAQqgkyeeiiqahdghnlnvqLERA--ADALR-LPD-WDAKI 160
Cdd:TIGR02868 424 TVRENL-------------------RLARPDATDEELWAA-------------------LERVglADWLRaLPDgLDTVL 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489953208 161 ----ANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVawlERFLHDF-----EGTVVAITHD 218
Cdd:TIGR02868 466 geggARLSGGERQRLALARALLADAPILLLDEPTEHLDAETA---DELLEDLlaalsGRTVVLITHH 529
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
324-501 |
1.76e-19 |
|
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: 91.58 E-value: 1.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDR-VLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQFRDAMD-- 399
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVnGVPLADADADSWRDQIAwv 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 400 ------NSKTVWEEVsggldimRIGNTEMP--------SRAYVGRFnFKGTDQG--KRVGE----LSGGERGRLHLAKLL 459
Cdd:TIGR02857 402 pqhpflFAGTIAENI-------RLARPDASdaeirealERAGLDEF-VAALPQGldTPIGEggagLSGGQAQRLALARAF 473
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489953208 460 QVGGNVLLLDEPTNDLDIETLRALENALLEFPGCAMV--ISHDR 501
Cdd:TIGR02857 474 LRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVllVTHRL 517
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
8-236 |
4.36e-19 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 85.92 E-value: 4.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 8 MHRVGKVVPPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDT--------------DIEGEARPQPGIKIGY 73
Cdd:cd03292 3 FINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELptsgtirvngqdvsDLRGRAIPYLRRKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 74 LPQEPQLNPEHTVRESVEEAVsevvnalkgldevyakyaepdadfdklaaqqgkyeEIIqahdGHNLNVQLERAADALRL 153
Cdd:cd03292 83 VFQDFRLLPDRNVYENVAFAL-----------------------------------EVT----GVPPREIRKRVPAALEL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 154 PDWDAKI----ANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFE---GTVVAITHDRYFLDNVA 226
Cdd:cd03292 124 VGLSHKHralpAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINkagTTVVVATHAKELVDTTR 203
|
250
....*....|
gi 489953208 227 GWILELDRGE 236
Cdd:cd03292 204 HRVIALERGK 213
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
323-471 |
4.75e-19 |
|
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: 86.56 E-value: 4.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 323 VVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKL------------- 388
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIdGQDITHlpmherarlgigy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 389 ----ASVdqFRD--AMDNSKTVWEeVSGGLDIMRIgntEMPSRAYVGRFNFKgTDQGKRVGELSGGERGRLHLAKLLQVG 462
Cdd:TIGR04406 81 lpqeASI--FRKltVEENIMAVLE-IRKDLDRAER---EERLEALLEEFQIS-HLRDNKAMSLSGGERRRVEIARALATN 153
|
....*....
gi 489953208 463 GNVLLLDEP 471
Cdd:TIGR04406 154 PKFILLDEP 162
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
323-511 |
5.64e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 90.08 E-value: 5.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 323 VVEVTNLRKSYGD-RVLiDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVdqfRDAMDN 400
Cdd:COG1129 4 LLEMRGISKSFGGvKAL-DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLdGEPVRFRSP---RDAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 401 --SkTVWEEVS--GGLDI---MRIGNteMPSRAyvGRFNFKGT---------------DQGKRVGELSGGERGRLHLAKL 458
Cdd:COG1129 80 giA-IIHQELNlvPNLSVaenIFLGR--EPRRG--GLIDWRAMrrrarellarlgldiDPDTPVGDLSVAQQQLVEIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489953208 459 LQVGGNVLLLDEPTNDLD----------IETLRALenallefpGCAMV-ISHdrwFLD---RIATHI 511
Cdd:COG1129 155 LSRDARVLILDEPTASLTereverlfriIRRLKAQ--------GVAIIyISH---RLDevfEIADRV 210
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
20-219 |
5.69e-19 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 88.62 E-value: 5.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEG---EARPqpgikIGYLPQEPQLNPEHT 85
Cdd:COG3842 19 TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFetpdsgrilldGRDVTGlppEKRN-----VGMVFQDYALFPHLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 86 VRESVEeavsevvnalKGLDevyakyaepdadFDKLAAqqgkyEEIiqahdghnlnvqLERAADAL---RLPDW-DAKIA 161
Cdd:COG3842 94 VAENVA----------FGLR------------MRGVPK-----AEI------------RARVAELLelvGLEGLaDRYPH 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489953208 162 NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA---ESV-AWLERFLHDFEGTVVAITHDR 219
Cdd:COG3842 135 QLSGGQQQRVALARALAPEPRVLLLDEPLSALDAklrEEMrEELRRLQRELGITFIYVTHDQ 196
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
323-501 |
6.28e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 88.74 E-value: 6.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 323 VVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLgETVKLASVDQFR---DAMD 399
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML-DGVDLSHVPPYQrpiNMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 400 NS------KTVWEEVSGGLDIMRIGNTEMPSR-----AYVGRFNFKgtdqGKRVGELSGGERGRLHLAKLLQVGGNVLLL 468
Cdd:PRK11607 98 QSyalfphMTVEQNIAFGLKQDKLPKAEIASRvnemlGLVHMQEFA----KRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 489953208 469 DEPTNDLDiETLR---ALENA-LLEFPG--CAMViSHDR 501
Cdd:PRK11607 174 DEPMGALD-KKLRdrmQLEVVdILERVGvtCVMV-THDQ 210
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
14-238 |
7.58e-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: 83.74 E-value: 7.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 14 VVPPKRHIL-KNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQPGIKIGYLPQEPQLnPEHTVREsvee 92
Cdd:cd03223 8 LATPDGRVLlKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYL-PLGTLRE---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 93 avsevvnalkgldevyakyaepdadfdklaaqqgkyeeiiqahdghnlnvqleraadALRLPdWDAKianLSGGERRRVA 172
Cdd:cd03223 83 ---------------------------------------------------------QLIYP-WDDV---LSGGEQQRLA 101
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489953208 173 LCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEGTVVAITHdRYFLDNVAGWILELDRGEGI 238
Cdd:cd03223 102 FARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLDGEGGW 166
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-477 |
7.84e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 89.72 E-value: 7.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDT------DIEGEAR----PQPGIKIG-YL-PQEPQLNPEHTVRE 88
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPpdsgtlEIGGNPCarltPAKAHQLGiYLvPQEPLLFPNLSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 89 sveeavsevvNALKGLdevyakyaepdadfDKLAAQQGKYEEIIQAhdghnLNVQLeraadalrlpDWDAKIANLSGGER 168
Cdd:PRK15439 106 ----------NILFGL--------------PKRQASMQKMKQLLAA-----LGCQL----------DLDSSAGSLEVADR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 169 RRVALCRLLLEKPDMLLLDEPTNHLD-AESVAWLERF--LHDFEGTVVAITHDRYFLDNVAGWILELdRGEGIPWEGNYS 245
Cdd:PRK15439 147 QIVEILRGLMRDSRILILDEPTASLTpAETERLFSRIreLLAQGVGIVFISHKLPEIRQLADRISVM-RDGTIALSGKTA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 246 SWleqKDQRLAQEASQEAARRKSIEKELEWVR-QGAKGRQSKGKARLaRFEELnnteyqkrneTNELFIppgarlgdkvv 324
Cdd:PRK15439 226 DL---STDDIIQAITPAAREKSLSASQKLWLElPGNRRQQAAGAPVL-TVEDL----------TGEGFR----------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 325 evtnlrksygdrvlidDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVdqfRDAMDNSKT 403
Cdd:PRK15439 281 ----------------NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLnGKEINALST---AQRLARGLV 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 404 VWEE---VSG------------GLDIMRIGNTEMPSR--AYVGRF----NFKGTDQGKRVGELSGGERGRLHLAKLLQVG 462
Cdd:PRK15439 342 YLPEdrqSSGlyldaplawnvcALTHNRRGFWIKPARenAVLERYrralNIKFNHAEQAARTLSGGNQQKVLIAKCLEAS 421
|
490
....*....|....*
gi 489953208 463 GNVLLLDEPTNDLDI 477
Cdd:PRK15439 422 PQLLIVDEPTRGVDV 436
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
323-507 |
1.04e-18 |
|
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: 85.10 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 323 VVEVTNLRKSYGD-----RVLiDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSIT-LGETV-KLASVDqfR 395
Cdd:TIGR02211 1 LLKCENLGKRYQEgkldtRVL-KGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLfNGQSLsKLSSNE--R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 396 DAMDNSK--------------TVWEEVSGGLDIMRIGNTEMPSRAY-----VG---RFNfkgtdqgKRVGELSGGERGRL 453
Cdd:TIGR02211 78 AKLRNKKlgfiyqfhhllpdfTALENVAMPLLIGKKSVKEAKERAYemlekVGlehRIN-------HRPSELSGGERQRV 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489953208 454 HLAKLLQVGGNVLLLDEPTNDLDIETLRALENALLEF---PGCAMVI-SHDRWFLDRI 507
Cdd:TIGR02211 151 AIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELnreLNTSFLVvTHDLELAKKL 208
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
324-476 |
1.33e-18 |
|
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: 84.61 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETV--KLASVDqfRD-AM-- 398
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDvtDLPPKD--RDiAMvf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 399 DN-----SKTVWEEVSGGLDIMRIGNTEMPSRAY-VGRFNFKGTDQGKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPT 472
Cdd:cd03301 79 QNyalypHMTVYDNIAFGLKLRKVPKDEIDERVReVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
....
gi 489953208 473 NDLD 476
Cdd:cd03301 159 SNLD 162
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
20-190 |
1.59e-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: 84.41 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEG---EARPQPGikIGYLPQEPQLNPEHT 85
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLlpprsgsirfdGRDITGlppHERARAG--IGYVPEGRRIFPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 86 VRESVEEAVSEVVNALK--GLDEVYAKyaepdadFDKLAaqqgkyeeiiqahdghnlnvqlERaadalrlpdWDAKIANL 163
Cdd:cd03224 92 VEENLLLGAYARRRAKRkaRLERVYEL-------FPRLK----------------------ER---------RKQLAGTL 133
|
170 180
....*....|....*....|....*..
gi 489953208 164 SGGERRRVALCRLLLEKPDMLLLDEPT 190
Cdd:cd03224 134 SGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
328-477 |
1.80e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 85.07 E-value: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 328 NLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETV-----------KLASVDQFRD 396
Cdd:PRK11231 7 NLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPismlssrqlarRLALLPQHHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 397 AMDNSkTVWEEVSGGldimrigntEMPSRAYVGRFNFK------------GTDQ--GKRVGELSGGERGRLHLAKLLQVG 462
Cdd:PRK11231 87 TPEGI-TVRELVAYG---------RSPWLSLWGRLSAEdnarvnqameqtRINHlaDRRLTDLSGGQRQRAFLAMVLAQD 156
|
170
....*....|....*
gi 489953208 463 GNVLLLDEPTNDLDI 477
Cdd:PRK11231 157 TPVVLLDEPTTYLDI 171
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
19-257 |
3.20e-18 |
|
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: 84.26 E-value: 3.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG----------ID----TDIEGEARPQPGIKIGYLPQEPQL---- 80
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGllrpdsgeilVDgqdiTGLSEKELYELRRRIGMLFQGGALfdsl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 81 ----N---P--EHTV--RESVEEAVSEvvnalkgldevyakyaepdadfdKLAAqqgkyeeiiqahdghnlnVQLERAAD 149
Cdd:COG1127 98 tvfeNvafPlrEHTDlsEAEIRELVLE-----------------------KLEL------------------VGLPGAAD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 150 alRLPdwdakiANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD----FEGTVVAITHDRYFLDNV 225
Cdd:COG1127 137 --KMP------SELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRElrdeLGLTSVVVTHDLDSAFAI 208
|
250 260 270
....*....|....*....|....*....|..
gi 489953208 226 AGWILELDRGEgIPWEGNYSSWLEQKDQRLAQ 257
Cdd:COG1127 209 ADRVAVLADGK-IIAEGTPEELLASDDPWVRQ 239
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
323-524 |
3.29e-18 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 83.89 E-value: 3.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 323 VVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVklasvdqfrdamDNS 401
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVdGEDL------------TDS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 402 KTvweevsgglDIMRIgntempsRAYVG----RFN-F----------------KGTDQG----------KRVG------- 443
Cdd:COG1126 69 KK---------DINKL-------RRKVGmvfqQFNlFphltvlenvtlapikvKKMSKAeaeeramellERVGladkada 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 444 ---ELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIE-------TLRALENAllefpGCAMVI-SHDRWFLDRIATHIL 512
Cdd:COG1126 133 ypaQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPElvgevldVMRDLAKE-----GMTMVVvTHEMGFAREVADRVV 207
|
250
....*....|....*....
gi 489953208 513 dYQDEGKV-------EFFE 524
Cdd:COG1126 208 -FMDGGRIveegppeEFFE 225
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
18-219 |
3.59e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 86.29 E-value: 3.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE------------ARPQpgiKIGYLPQEPQLNPEHT 85
Cdd:PRK10851 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHirfhgtdvsrlhARDR---KVGFVFQHYALFRHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 86 VRESVEEAVSevvnalkgldeVYAKYAEPDAdfdklAAQQGKYEEIIQAhdghnlnVQLERAADalRLPdwdakiANLSG 165
Cdd:PRK10851 91 VFDNIAFGLT-----------VLPRRERPNA-----AAIKAKVTQLLEM-------VQLAHLAD--RYP------AQLSG 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489953208 166 GERRRVALCRLLLEKPDMLLLDEPTNHLDA----ESVAWLeRFLH-DFEGTVVAITHDR 219
Cdd:PRK10851 140 GQKQRVALARALAVEPQILLLDEPFGALDAqvrkELRRWL-RQLHeELKFTSVFVTHDQ 197
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
20-236 |
4.72e-18 |
|
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: 83.64 E-value: 4.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEGE---ARPQPGikIGYLPQEPQLNPEHT 85
Cdd:cd03219 14 VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFlrptsgsvlfdGEDITGLpphEIARLG--IGRTFQIPRLFPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 86 VRESVEeavsevvnalkgldevyakyaepdadfdkLAAQQGKYEEIIQAHDGHNLNVQLERAADALRL----PDWDAKIA 161
Cdd:cd03219 92 VLENVM-----------------------------VAAQARTGSGLLLARARREEREARERAEELLERvglaDLADRPAG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489953208 162 NLSGGERRRVALCRLLLEKPDMLLLDEPT---NHLDAESVAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:cd03219 143 ELSYGQQRRLEIARALATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGR 220
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
324-476 |
4.80e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 85.51 E-value: 4.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETV--KLASVDqfRD-AM-- 398
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDvtDLPPKD--RNiAMvf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 399 ------DNsKTVWEEVSGGLDIMRIGNTEMPSR-----------AYVGRfnfkgtdqgkRVGELSGGERGRLHLAKLLQV 461
Cdd:COG3839 82 qsyalyPH-MTVYENIAFPLKLRKVPKAEIDRRvreaaellgleDLLDR----------KPKQLSGGQRQRVALGRALVR 150
|
170
....*....|....*
gi 489953208 462 GGNVLLLDEPTNDLD 476
Cdd:COG3839 151 EPKVFLLDEPLSNLD 165
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-218 |
5.03e-18 |
|
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: 83.28 E-value: 5.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTD------IEGEARPQPGIKIGYLPQEPQLNPEHTVRESVEEAVS 95
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPtsggviLEGKQITEPGPDRMVVFQNYSLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 96 EVVNALKgldevyakyaepdadfdklaaqQGKYEEIIqahDGHNLNVQLERAADAlrlpdwdaKIANLSGGERRRVALCR 175
Cdd:TIGR01184 81 RVLPDLS----------------------KSERRAIV---EEHIALVGLTEAADK--------RPGQLSGGMKQRVAIAR 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489953208 176 LLLEKPDMLLLDEPTNHLDAESVAWLE----RFLHDFEGTVVAITHD 218
Cdd:TIGR01184 128 ALSIRPKVLLLDEPFGALDALTRGNLQeelmQIWEEHRVTVLMVTHD 174
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-239 |
5.72e-18 |
|
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: 87.15 E-value: 5.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 32 GAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEArpQPGIKIGYLPQEPQLNPEHTVRESVEEAVSEvvnalkGLDEVYAky 111
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDLKISYKPQYISPDYDGTVEEFLRSANTD------DFGSSYY-- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 112 aepdadfdklaaqqgkYEEIIQAhdghnlnVQLERAadalrlpdWDAKIANLSGGERRRVALCRLLLEKPDMLLLDEPTN 191
Cdd:COG1245 436 ----------------KTEIIKP-------LGLEKL--------LDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSA 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489953208 192 HLDAE---SVA-WLERFLHDFEGTVVAITHDRYFLDNVAgwilelDRG---EGIP 239
Cdd:COG1245 485 HLDVEqrlAVAkAIRRFAENRGKTAMVVDHDIYLIDYIS------DRLmvfEGEP 533
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
17-231 |
5.90e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 83.97 E-value: 5.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQpGIKIGYLPQEPQ----------------- 79
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWR-GEPLAKLNRAQRkafrrdiqmvfqdsisa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 80 LNPEHTVRESVEEAVSEvvnaLKGLDEvyakyaepdadfdklAAQQGKYEEIIQAhdghnlnVQLeRAADALRLPdwdak 159
Cdd:PRK10419 102 VNPRKTVREIIREPLRH----LLSLDK---------------AERLARASEMLRA-------VDL-DDSVLDKRP----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 160 iANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDFEGTVVAITHD----RYFLDNVA----G 227
Cdd:PRK10419 150 -PQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDlvlqAGVIRLLKKLQQQFGTACLFITHDlrlvERFCQRVMvmdnG 228
|
....
gi 489953208 228 WILE 231
Cdd:PRK10419 229 QIVE 232
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
20-218 |
6.17e-18 |
|
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: 83.25 E-value: 6.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE------------------ARPQpgiKIGYLPQEPQLN 81
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTvrlagqdlfaldedararLRAR---HVGFVFQSFQLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 82 PEHTVRESV----EEAvsevvnalkgldevyakyAEPDAdfdklaaqqgkyeeiiqahdghnlnvqLERAADAL------ 151
Cdd:COG4181 103 PTLTALENVmlplELA------------------GRRDA---------------------------RARARALLervglg 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489953208 152 -RLpdwDAKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA---ESVAWLERFLHDFEG-TVVAITHD 218
Cdd:COG4181 138 hRL---DHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAatgEQIIDLLFELNRERGtTLVLVTHD 206
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
18-236 |
6.23e-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: 82.58 E-value: 6.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDT------DIEGEARPQPGI-------KIGYLPQEPQLNPEH 84
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEpdsgtiIIDGLKLTDDKKninelrqKVGMVFQQFNLFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 85 TVRESVEEAVSEVvnalKGLDEVYAKyaepdadfdklaaqqgkyeeiiqahdghnlnvqlERAADALR---LPDW-DAKI 160
Cdd:cd03262 92 TVLENITLAPIKV----KGMSKAEAE----------------------------------ERALELLEkvgLADKaDAYP 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489953208 161 ANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EG-TVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:cd03262 134 AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLaeEGmTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-226 |
1.07e-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: 82.84 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 28 SFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEArPQPGIKIGYLPQEPQLNPEHTVREsveeAVSEVVNalkgldev 107
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI-EIELDTVSYKPQYIKADYEGTVRD----LLSSITK-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 108 yakyaepdadfDKLAAQQGKyEEIIQAhdghnlnVQLERAADAlRLPDwdakianLSGGERRRVALCRLLLEKPDMLLLD 187
Cdd:cd03237 88 -----------DFYTHPYFK-TEIAKP-------LQIEQILDR-EVPE-------LSGGELQRVAIAACLSKDADIYLLD 140
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489953208 188 EPTNHLDAE----SVAWLERFLHDFEGTVVAITHDRYFLDNVA 226
Cdd:cd03237 141 EPSAYLDVEqrlmASKVIRRFAENNEKTAFVVEHDIIMIDYLA 183
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
286-509 |
1.30e-17 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 85.99 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 286 KGKARLARFEELNNTEYQKRNETNELFIPPGArlGDkvVEVTNLRKSY-GDRVLIDDLTFSVPKGAIVGIIGPNGAGKST 364
Cdd:COG1132 306 RALASAERIFELLDEPPEIPDPPGAVPLPPVR--GE--IEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKST 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 365 LFRMMSGQEQPDSGSITLGET-VKLASVDQFRDAM-----DN---SKTVWEEVsggldimRIGNTEMP--------SRAY 427
Cdd:COG1132 382 LVNLLLRFYDPTSGRILIDGVdIRDLTLESLRRQIgvvpqDTflfSGTIRENI-------RYGRPDATdeeveeaaKAAQ 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 428 VGRF--NF-KGTDQgkRVGE----LSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIETLRALENALLEF-PGCAM-VIS 498
Cdd:COG1132 455 AHEFieALpDGYDT--VVGErgvnLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLmKGRTTiVIA 532
|
250
....*....|.
gi 489953208 499 HdrwfldRIAT 509
Cdd:COG1132 533 H------RLST 537
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
324-490 |
1.40e-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: 80.43 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYG--DRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETVKLASVDQFRDAMdns 401
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 402 ktvweevsggldimrignTEMPSRAYVgrfnFKGT---DQGKRvgeLSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIE 478
Cdd:cd03247 78 ------------------SVLNQRPYL----FDTTlrnNLGRR---FSGGERQRLALARILLQDAPIVLLDEPTVGLDPI 132
|
170
....*....|..
gi 489953208 479 TLRALENALLEF 490
Cdd:cd03247 133 TERQLLSLIFEV 144
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
324-490 |
1.49e-17 |
|
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: 82.00 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSY---------------------GDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL 382
Cdd:cd03267 1 IEVSNLSKSYrvyskepgligslkslfkrkyREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 383 GETV----KLASVDQFRDAMDNSKTVW---------------------------EEVSGGLDIMRIGNTemPSRayvgrf 431
Cdd:cd03267 81 AGLVpwkrRKKFLRRIGVVFGQKTQLWwdlpvidsfyllaaiydlpparfkkrlDELSELLDLEELLDT--PVR------ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489953208 432 nfkgtdqgkrvgELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIETLRALENALLEF 490
Cdd:cd03267 153 ------------QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEY 199
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
22-218 |
2.11e-17 |
|
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: 81.61 E-value: 2.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEAR-------PQPGIK--IGYLPQEPQLNPEHTVRESVEe 92
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILlngkditNLPPEKrdISYVPQNYALFPHMTVYKNIA- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 93 avsevvnalKGLDEVYAKYAEPDADFDKLAAQQGKyeeiiqahdGHNLNvqleraadalRLPdwdakiANLSGGERRRVA 172
Cdd:cd03299 94 ---------YGLKKRKVDKKEIERKVLEIAEMLGI---------DHLLN----------RKP------ETLSGGEQQRVA 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489953208 173 LCRLLLEKPDMLLLDEPTNHLDA---ESVAWLERFLHD-FEGTVVAITHD 218
Cdd:cd03299 140 IARALVVNPKILLLDEPFSALDVrtkEKLREELKKIRKeFGVTVLHVTHD 189
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
18-218 |
2.22e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 82.08 E-value: 2.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQPGIKIGYLPQEPQLNPehtvreSVEEAVSEV 97
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDT------TLPLTVNRF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 98 VNALKGLdevyakyaepdadfdklaaqqgKYEEIIQAhdghnlnvqLERAADALRLpdwDAKIANLSGGERRRVALCRLL 177
Cdd:PRK09544 90 LRLRPGT----------------------KKEDILPA---------LKRVQAGHLI---DAPMQKLSGGETQRVLLARAL 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489953208 178 LEKPDMLLLDEPTNHLDAESVAWL----ERFLHDFEGTVVAITHD 218
Cdd:PRK09544 136 LNRPQLLVLDEPTQGVDVNGQVALydliDQLRRELDCAVLMVSHD 180
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
330-524 |
2.54e-17 |
|
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: 81.04 E-value: 2.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 330 RKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLgeTVKLASVDQFRDAMDNSKTVWEEVS 409
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV--RGRVSSLLGLGGGFNPELTGRENIY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 410 GGLDIMRIGNTEMPSR-AYVGRFNFKGTDQGKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIETLRALENALL 488
Cdd:cd03220 107 LNGRLLGLSRKEIDEKiDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLR 186
|
170 180 190
....*....|....*....|....*....|....*....
gi 489953208 489 EF-PGCAMVI--SHDRWFLDRIATHILdYQDEGKVEFFE 524
Cdd:cd03220 187 ELlKQGKTVIlvSHDPSSIKRLCDRAL-VLEKGKIRFDG 224
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
30-226 |
2.78e-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: 83.61 E-value: 2.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 30 FPGAKIGVL-GLNGAGKSTLLRIMAGIDTDIEG--------------------EARPqpgikIGYLPQEPQLNPEHTVRE 88
Cdd:COG4148 22 LPGRGVTALfGPSGSGKTTLLRAIAGLERPDSGrirlggevlqdsargiflppHRRR-----IGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 89 sveeavsevvNALKGLDevYAKYAEPDADFDKLAAQQGkyeeiIQAHdghnlnvqLERaadalrlpdwdaKIANLSGGER 168
Cdd:COG4148 97 ----------NLLYGRK--RAPRAERRISFDEVVELLG-----IGHL--------LDR------------RPATLSGGER 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489953208 169 RRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERfLHD-FEGTVVAITHDryfLDNVA 226
Cdd:COG4148 140 QRVAIGRALLSSPRLLLMDEPLAALDlarkAEILPYLER-LRDeLDIPILYVSHS---LDEVA 198
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
9-218 |
3.03e-17 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 83.20 E-value: 3.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 9 HRVGKVvppkrHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG----------ID----TDIEGEARpqpgiKIGYL 74
Cdd:COG3839 11 KSYGGV-----EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGledptsgeilIGgrdvTDLPPKDR-----NIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 75 PQEPQLNPEHTVREsveeavsevvNALKGLdevyakyaepdadfdKLAaqqGKYEEIIQAhdghnlnvQLERAADALRLP 154
Cdd:COG3839 81 FQSYALYPHMTVYE----------NIAFPL---------------KLR---KVPKAEIDR--------RVREAAELLGLE 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489953208 155 DW-DAKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA--------EsvawLERFLHDFEGTVVAITHD 218
Cdd:COG3839 125 DLlDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAklrvemraE----IKRLHRRLGTTTIYVTHD 193
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
326-512 |
3.14e-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: 3.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 326 VTNLRKSYGDrvliDDLTFSVPKGA-----IVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLgETVKLASVDQFRDAmDN 400
Cdd:cd03237 1 YTYPTMKKTL----GEFTLEVEGGSiseseVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-ELDTVSYKPQYIKA-DY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 401 SKTVWEEVSGGLDIMRIG---NTEMpsrayvgrFNFKGTDQ--GKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDL 475
Cdd:cd03237 75 EGTVRDLLSSITKDFYTHpyfKTEI--------AKPLQIEQilDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489953208 476 DIE----TLRALENALLEFPGCAMVISHDRWFLDRIATHIL 512
Cdd:cd03237 147 DVEqrlmASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLI 187
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
321-499 |
3.16e-17 |
|
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: 81.28 E-value: 3.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 321 DKVVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSG-SIT-LGETVKLASVDQFR--- 395
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRlFGERRGGEDVWELRkri 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 396 --------DAMDNSKTVWEEV-SGGLDIMRIGNT---EMPSRA-----YVGRFNFKgtdqGKRVGELSGGERGRLHLAKL 458
Cdd:COG1119 81 glvspalqLRFPRDETVLDVVlSGFFDSIGLYREptdEQRERArelleLLGLAHLA----DRPFGTLSQGEQRRVLIARA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489953208 459 LQVGGNVLLLDEPTNDLDI---ETLRALENALLEFPGCAMV-ISH 499
Cdd:COG1119 157 LVKDPELLILDEPTAGLDLgarELLLALLDKLAAEGAPTLVlVTH 201
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
324-489 |
3.44e-17 |
|
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: 80.40 E-value: 3.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSI-TLGETVKLASVDQF-------- 394
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVlFDGKPLDIAARNRIgylpeerg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 395 ----RDAMDNSKTVweevsGGLDIMRIGNTEMPSRAYVGRFNFkGTDQGKRVGELSGGERGRLHLAKLLQVGGNVLLLDE 470
Cdd:cd03269 81 lypkMKVIDQLVYL-----AQLKGLKKEEARRRIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170
....*....|....*....
gi 489953208 471 PTNDLDIETLRALENALLE 489
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRE 173
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
20-218 |
3.49e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 80.95 E-value: 3.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE--------------ARPqpgIKIgyLPQEPQLNPEHT 85
Cdd:COG3840 13 DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRilwngqdltalppaERP---VSM--LFQENNLFPHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 86 VRESVeeavsevvnALkGLDevyakyaePDAdfdKL-AAQQGKYEEIIQahdghnlNVQLERAADalRLPdwdakiANLS 164
Cdd:COG3840 88 VAQNI---------GL-GLR--------PGL---KLtAEQRAQVEQALE-------RVGLAGLLD--RLP------GQLS 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489953208 165 GGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDFEGTVVAITHD 218
Cdd:COG3840 132 GGQRQRVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRERGLTVLMVTHD 189
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
319-521 |
3.85e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 81.55 E-value: 3.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 319 LGDKVVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGE-----------TVK 387
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgQLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 388 LASVDQFRDA------------MDNSKTVWEEV-SGGLDIMRIGNTEMPSRA--YVGRFNFKGTDQGKRVGELSGGERGR 452
Cdd:PRK10619 81 VADKNQLRLLrtrltmvfqhfnLWSHMTVLENVmEAPIQVLGLSKQEARERAvkYLAKVGIDERAQGKYPVHLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489953208 453 LHLAKLLQVGGNVLLLDEPTNDLDI----ETLRALENaLLEFPGCAMVISHDRWFLDRIATHILdYQDEGKVE 521
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPelvgEVLRIMQQ-LAEEGKTMVVVTHEMGFARHVSSHVI-FLHQGKIE 231
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
19-217 |
3.96e-17 |
|
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: 79.71 E-value: 3.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG----------IDTDIEGEARPQPGIKIGYLPQEPQLNPEHTVRE 88
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGllrpdsgevrWNGTPLAEQRDEPHENILYLGHLPGLKPELSALE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 89 SVeeavsevvnalkgldevyakyaepdaDFdklaaqqgkYEEIiqaHDGHNLNVqlERAADALRLPDW-DAKIANLSGGE 167
Cdd:TIGR01189 93 NL--------------------------HF---------WAAI---HGGAQRTI--EDALAAVGLTGFeDLPAAQLSAGQ 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489953208 168 RRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF---EGTVVAITH 217
Cdd:TIGR01189 133 QRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
19-217 |
4.39e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.92 E-value: 4.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG--------IDTDIEGEARPQPGIKIGYLPQEPQLNPEHTVRESV 90
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGllppaagtIKLDGGDIDDPDVAEACHYLGHRNAMKPALTVAENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 91 EEAvsevvnalkgldevyakyaepdADFdklaaqqgkyeeiiqaHDGHNLNVqlERAADALRLPD-WDAKIANLSGGERR 169
Cdd:PRK13539 95 EFW----------------------AAF----------------LGGEELDI--AAALEAVGLAPlAHLPFGYLSAGQKR 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489953208 170 RVALCRLLLEKPDMLLLDEPTNHLDAESVAwleRFLHDFE------GTVVAITH 217
Cdd:PRK13539 135 RVALARLLVSNRPIWILDEPTAALDAAAVA---LFAELIRahlaqgGIVIAATH 185
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
18-218 |
4.48e-17 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 80.30 E-value: 4.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEGEARPQPGI-------KIGYLPQEPq 79
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipgapdegEVLLDGKDIYDLDVdvlelrrRVGMVFQKP- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 80 lNPEH-TVRESVEEAVSevvnaLKGldevYAKYAEPDadfdklaaqqgkyeeiiqahdghnlnvqlERAADALRLPD-WD 157
Cdd:cd03260 91 -NPFPgSIYDNVAYGLR-----LHG----IKLKEELD-----------------------------ERVEEALRKAAlWD 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489953208 158 -----AKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EGTVVAITHD 218
Cdd:cd03260 132 evkdrLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELkkEYTIVIVTHN 199
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
7-217 |
5.06e-17 |
|
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: 80.32 E-value: 5.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 7 TMHRVGKVVPPKR---HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE--------------ARPQPGI 69
Cdd:cd03258 3 ELKNVSKVFGDTGgkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSvlvdgtdltllsgkELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 70 KIGYLPQEPQLNPEHTVRESVEEAVsevvnalkgldevyakyaepdadfdKLAAQQGKYEEiiqahdghnlnvqlERAAD 149
Cdd:cd03258 83 RIGMIFQHFNLLSSRTVFENVALPL-------------------------EIAGVPKAEIE--------------ERVLE 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489953208 150 ALRLPDW----DAKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD----FEGTVVAITH 217
Cdd:cd03258 124 LLELVGLedkaDAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDinreLGLTIVLITH 199
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
19-197 |
5.85e-17 |
|
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: 79.86 E-value: 5.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEA----------RPQPGIKIGYLPQEPQLNPEHTVRE 88
Cdd:cd03263 15 KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAyingysirtdRKAARQSLGYCPQFDALFDELTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 89 SVeeavsevvnalkgldEVYAKYaepdadfdklaaqQGKYEEIIqahdghnlNVQLERAADALRLPD-WDAKIANLSGGE 167
Cdd:cd03263 95 HL---------------RFYARL-------------KGLPKSEI--------KEEVELLLRVLGLTDkANKRARTLSGGM 138
|
170 180 190
....*....|....*....|....*....|
gi 489953208 168 RRRVALCRLLLEKPDMLLLDEPTNHLDAES 197
Cdd:cd03263 139 KRKLSLAIALIGGPSVLLLDEPTSGLDPAS 168
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
21-219 |
6.09e-17 |
|
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: 80.09 E-value: 6.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEA--RPQP-------------GIKIGYLPQEPQLNPEHT 85
Cdd:TIGR02211 20 VLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVlfNGQSlsklssneraklrNKKLGFIYQFHHLLPDFT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 86 VRESVeeavseVVNALKGldevyakyaepdaDFDKLAAQQGKYEEIIQAHDGHNLNvqleraadalrlpdwdAKIANLSG 165
Cdd:TIGR02211 100 ALENV------AMPLLIG-------------KKSVKEAKERAYEMLEKVGLEHRIN----------------HRPSELSG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489953208 166 GERRRVALCRLLLEKPDMLLLDEPTNHLD---AESVAWLERFLHDFEGT-VVAITHDR 219
Cdd:TIGR02211 145 GERQRVAIARALVNQPSLVLADEPTGNLDnnnAKIIFDLMLELNRELNTsFLVVTHDL 202
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
326-386 |
6.61e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 80.51 E-value: 6.61e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489953208 326 VTNLRKSYGDRVLI-DDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETV 386
Cdd:COG1134 28 LLRRRRTRREEFWAlKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRV 89
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
325-520 |
7.25e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 79.80 E-value: 7.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 325 EVTNLRKSYGDRVLidDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQ------FRDa 397
Cdd:COG3840 3 RLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWnGQDLTALPPAErpvsmlFQE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 398 mDN---SKTVWEEVSGGLDI-MRIGNTEmpsRAYV----GRFNFKGTDQgKRVGELSGGERGRLHLAKLLQVGGNVLLLD 469
Cdd:COG3840 80 -NNlfpHLTVAQNIGLGLRPgLKLTAEQ---RAQVeqalERVGLAGLLD-RLPGQLSGGQRQRVALARCLVRKRPILLLD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489953208 470 EPTNDLD----------IETLRALENALLefpgcaMVISHDrwfLD---RIATHILdYQDEGKV 520
Cdd:COG3840 155 EPFSALDpalrqemldlVDELCRERGLTV------LMVTHD---PEdaaRIADRVL-LVADGRI 208
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
14-217 |
8.80e-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: 78.03 E-value: 8.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 14 VVPP--KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEAR-----------PQPGIKIGYLPQEPQL 80
Cdd:cd03246 8 FRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRldgadisqwdpNELGDHVGYLPQDDEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 81 npehtvresveeavsevvnalkgldevyakyaepdadFDklaaqqGKYEEIIqahdghnlnvqleraadalrlpdwdaki 160
Cdd:cd03246 88 -------------------------------------FS------GSIAENI---------------------------- 96
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 161 anLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFE---GTVVAITH 217
Cdd:cd03246 97 --LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKaagATRIVIAH 154
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
7-235 |
9.73e-17 |
|
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: 79.40 E-value: 9.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 7 TMHRVGKVVPPkrhILKNISLSFFPGAKIGVLGLNGAGKSTLLRImagidtdIEGEARPQPGiKIGYLPQEPQLN----P 82
Cdd:COG4778 15 TLHLQGGKRLP---VLDGVSFSVAAGECVALTGPSGAGKSTLLKC-------IYGNYLPDSG-SILVRHDGGWVDlaqaS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 83 EHTV---RESVEEAVSEVVNAL---KGLDEVyakyAEPdadfdkLAAQqgkyeeiiqahdGHNLNVQLERAADALR---L 153
Cdd:COG4778 84 PREIlalRRRTIGYVSQFLRVIprvSALDVV----AEP------LLER------------GVDREEARARARELLArlnL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 154 PD--WDAKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EGT-VVAITHDRYFLDNVAGW 228
Cdd:COG4778 142 PErlWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAkaRGTaIIGIFHDEEVREAVADR 221
|
....*..
gi 489953208 229 ILELDRG 235
Cdd:COG4778 222 VVDVTPF 228
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
325-472 |
1.31e-16 |
|
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: 79.02 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 325 EVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLG----------ETVK--LASVD 392
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDgrditglpphERARagIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 393 QFRDAMDNsKTVWEE-VSGGLDIMRIGNTEMPSRAYvGRFNFKGTDQGKRVGELSGGERGRLHLAKLLQVGGNVLLLDEP 471
Cdd:cd03224 82 EGRRIFPE-LTVEENlLLGAYARRRAKRKARLERVY-ELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEP 159
|
.
gi 489953208 472 T 472
Cdd:cd03224 160 S 160
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
323-476 |
1.36e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 81.53 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 323 VVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQfRD----- 396
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLdGQDITHVPAEN-RHvntvf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 397 ---AMDNSKTVWEEVSGGLDIMRIGNTEMPSR-----AYVGRFNFKgtdqGKRVGELSGGERGRLHLAKLLQVGGNVLLL 468
Cdd:PRK09452 93 qsyALFPHMTVFENVAFGLRMQKTPAAEITPRvmealRMVQLEEFA----QRKPHQLSGGQQQRVAIARAVVNKPKVLLL 168
|
....*...
gi 489953208 469 DEPTNDLD 476
Cdd:PRK09452 169 DESLSALD 176
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
18-207 |
1.52e-16 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 79.26 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE-------ARPQPG---IKIGYLPQEPQLNPEHTVR 87
Cdd:TIGR03864 13 ARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQisvaghdLRRAPRaalARLGVVFQQPTLDLDLSVR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 88 ESVEEAVsevvnALKGLDEvyakyAEPDADFDKLAAQQGKYEeiiqahdghnlnvqleRAadalrlpdwDAKIANLSGGE 167
Cdd:TIGR03864 93 QNLRYHA-----ALHGLSR-----AEARARIAELLARLGLAE----------------RA---------DDKVRELNGGH 137
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489953208 168 RRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD 207
Cdd:TIGR03864 138 RRRVEIARALLHRPALLLLDEPTVGLDPASRAAITAHVRA 177
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
21-235 |
1.64e-16 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 79.29 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE-----------ARPQPGI------KIGYLPQEPQLNPE 83
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQlniaghqfdfsQKPSEKAirllrqKVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 84 HTVRESVEEAVSEVvnalkgldevyakyaepdadfdklaAQQGKYEEIIQAhdghnlNVQLERaadaLRLPDW-DAKIAN 162
Cdd:COG4161 97 LTVMENLIEAPCKV-------------------------LGLSKEQAREKA------MKLLAR----LRLTDKaDRFPLH 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489953208 163 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE---SVAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRG 235
Cdd:COG4161 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEitaQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKG 217
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
21-218 |
1.80e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 81.43 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEGEARPQPGIKIGYLPQEPQLNPEHTVRES 89
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTltptagtvlvaGDDVEALSARAASRRVASVPQDTSLSFEFDVRQV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 90 VEEAVSEVVNALKGLDEVyakyaepdadfDKLAAQQGkyeeiiqahdghnlnvqLERAaDALRLPDWDakIANLSGGERR 169
Cdd:PRK09536 98 VEMGRTPHRSRFDTWTET-----------DRAAVERA-----------------MERT-GVAQFADRP--VTSLSGGERQ 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489953208 170 RVALCRLLLEKPDMLLLDEPTNHLDA-ESVAWLE--RFLHDFEGTVVAITHD 218
Cdd:PRK09536 147 RVLLARALAQATPVLLLDEPTASLDInHQVRTLElvRRLVDDGKTAVAAIHD 198
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
21-236 |
1.96e-16 |
|
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: 77.89 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLriMAgidtdIEGEARPQPGI-----KIGYLPQEPQLNPEhTVREsveeavs 95
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLL--SA-----LLGELEKLSGSvsvpgSIAYVSQEPWIQNG-TIRE------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 96 evvNALKGldevyakyaepdADFDKlaaqqGKYEEIIQAhdghnlnVQLERaaDALRLPDWDA-----KIANLSGGERRR 170
Cdd:cd03250 85 ---NILFG------------KPFDE-----ERYEKVIKA-------CALEP--DLEILPDGDLteigeKGINLSGGQKQR 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489953208 171 VALCRLLLEKPDMLLLDEPTNHLDAESVAWLerFLHDFEG------TVVAITHDRYFLDNVAgWILELDRGE 236
Cdd:cd03250 136 ISLARAVYSDADIYLLDDPLSAVDAHVGRHI--FENCILGlllnnkTRILVTHQLQLLPHAD-QIVVLDNGR 204
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
21-203 |
2.40e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 79.85 E-value: 2.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEAR----PQPG------IKIGYLPQEPQLNPEHTVRESV 90
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgePVPSrarharQRVGVVPQFDNLDPDFTVRENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 91 eeavsevvnalkgldEVYAKYaepdadFDKLAAQqgkyeeiIQAHDGHNLN-VQLERAAdalrlpdwDAKIANLSGGERR 169
Cdd:PRK13537 102 ---------------LVFGRY------FGLSAAA-------ARALVPPLLEfAKLENKA--------DAKVGELSGGMKR 145
|
170 180 190
....*....|....*....|....*....|....*.
gi 489953208 170 RVALCRLLLEKPDMLLLDEPTNHLD--AESVAWlER 203
Cdd:PRK13537 146 RLTLARALVNDPDVLVLDEPTTGLDpqARHLMW-ER 180
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
19-234 |
2.47e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 77.91 E-value: 2.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI--------------DTDIEG---EARpqpgiKIGYLPQEPQLN 81
Cdd:COG4136 14 RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTlspafsasgevllnGRRLTAlpaEQR-----RIGILFQDDLLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 82 PEHTVREsveeavsevvNALKGLDEVYAKyaepdadfdklAAQQgkyEEIIQAHDGHNLnvqlerAADALRLPdwdakiA 161
Cdd:COG4136 89 PHLSVGE----------NLAFALPPTIGR-----------AQRR---ARVEQALEEAGL------AGFADRDP------A 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489953208 162 NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERF----LHDFEGTVVAITHDRyflDNV--AGWILELDR 234
Cdd:COG4136 133 TLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFvfeqIRQRGIPALLVTHDE---EDApaAGRVLDLGN 208
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
342-500 |
2.49e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 78.73 E-value: 2.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 342 LTFSVPKGAIVGIIGPNGAGKSTLFRMMSGqEQPDSGSITLGET----VKLASVDQFRD----------AMDnsktVWEE 407
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRplsdWSAAELARHRAylsqqqsppfAMP----VFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 408 VSggLDIMRIGNTEMPSRAY---VGRFNFkgTDQ-GKRVGELSGGERGRLHLAK-LLQV------GGNVLLLDEPTNDLD 476
Cdd:COG4138 90 LA--LHQPAGASSEAVEQLLaqlAEALGL--EDKlSRPLTQLSGGEWQRVRLAAvLLQVwptinpEGQLLLLDEPMNSLD 165
|
170 180
....*....|....*....|....*..
gi 489953208 477 IETLRALENALLEF--PGCAMVIS-HD 500
Cdd:COG4138 166 VAQQAALDRLLRELcqQGITVVMSsHD 192
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-225 |
2.83e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 79.38 E-value: 2.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEAR-------PQPGIKIGYLPQEPQLNPehtvRESV 90
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLwdgepldPEDRRRIGYLPEERGLYP----KMKV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 91 EE-----AvsevvnALKGLDEvyakyAEPDADFDKLaaqqgkyeeiiqahdghnlnvqLERaadaLRLPDW-DAKIANLS 164
Cdd:COG4152 89 GEqlvylA------RLKGLSK-----AEAKRRADEW----------------------LER----LGLGDRaNKKVEELS 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489953208 165 GGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EG-TVVAITHDryfLDNV 225
Cdd:COG4152 132 KGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELaaKGtTVIFSSHQ---MELV 192
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
335-519 |
3.18e-16 |
|
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: 76.42 E-value: 3.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 335 DRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGqeqpdsgsitlgetvklasvdqfrdamdnsktVWEEVSGGLDI 414
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG--------------------------------LWPWGSGRIGM 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 415 MRIGNTE-MPSRAYVGRFNFKgtDQ-----GKrvgELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIETLRALENALL 488
Cdd:cd03223 61 PEGEDLLfLPQRPYLPLGTLR--EQliypwDD---VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLK 135
|
170 180 190
....*....|....*....|....*....|..
gi 489953208 489 EFpGCAMV-ISHdRWFLDRIATHILDYQDEGK 519
Cdd:cd03223 136 EL-GITVIsVGH-RPSLWKFHDRVLDLDGEGG 165
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
19-218 |
3.41e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 78.57 E-value: 3.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE--------ARPQPGIKIGYlpQEPQLNPEHTVRESV 90
Cdd:PRK11247 25 RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEllagtaplAEAREDTRLMF--QDARLLPWKKVIDNV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 91 eeavsevvnalkGLdevyakyaepdadfdklaAQQGKYEEiiQAHDGhnlnvqLERAADALRLPDWDAKianLSGGERRR 170
Cdd:PRK11247 103 ------------GL------------------GLKGQWRD--AALQA------LAAVGLADRANEWPAA---LSGGQKQR 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489953208 171 VALCRLLLEKPDMLLLDEPTNHLDA----------ESVaWLErflHDFegTVVAITHD 218
Cdd:PRK11247 142 VALARALIHRPGLLLLDEPLGALDAltriemqdliESL-WQQ---HGF--TVLLVTHD 193
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
322-538 |
3.92e-16 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 81.83 E-value: 3.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 322 KVVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQ--------------EQPDSGSIT------ 381
Cdd:PLN03073 176 KDIHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHaidgipkncqilhvEQEVVGDDTtalqcv 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 382 ----------LGETVKLASVD---QFRDAMDNSKTV-------------WEEVSGGLDIMRIGNTEMPSRAYVGRFNFKG 435
Cdd:PLN03073 256 lntdiertqlLEEEAQLVAQQrelEFETETGKGKGAnkdgvdkdavsqrLEEIYKRLELIDAYTAEARAASILAGLSFTP 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 436 TDQGKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIETLRALENALLEFPGCAMVISHDRWFLDRIATHILDYQ 515
Cdd:PLN03073 336 EMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLH 415
|
250 260
....*....|....*....|...
gi 489953208 516 DEgKVEFFEGNFTEYEEYKKRTL 538
Cdd:PLN03073 416 GQ-KLVTYKGDYDTFERTREEQL 437
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
18-241 |
3.97e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 78.27 E-value: 3.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAgidtdieGEARPQPG-IKI-----------------GYLPQEPQ 79
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALS-------GELSPDSGeVRLngrpladwspaelarrrAVLPQHSS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 80 LNPEHTVResveeavsEVVnALkGLdevYAKYAEPDADfdklaaqqgkyEEIIQAhdghnlnvQLERA-ADALRlpdwDA 158
Cdd:PRK13548 87 LSFPFTVE--------EVV-AM-GR---APHGLSRAED-----------DALVAA--------ALAQVdLAHLA----GR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 159 KIANLSGGERRRVALCRLLL------EKPDMLLLDEPTNHLD---AESVAWLER-FLHDFEGTVVAITHD-----RYfld 223
Cdd:PRK13548 131 DYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDlahQHHVLRLARqLAHERGLAVIVVLHDlnlaaRY--- 207
|
250 260
....*....|....*....|..
gi 489953208 224 nvAGWILELDRG----EGIPWE 241
Cdd:PRK13548 208 --ADRIVLLHQGrlvaDGTPAE 227
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
18-189 |
4.24e-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: 77.58 E-value: 4.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEGE---ARPQPGikIGYLPQEPQLNPE 83
Cdd:cd03218 12 KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLvkpdsgkilldGQDITKLpmhKRARLG--IGYLPQEASIFRK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 84 HTVREsveeavsevvNALKGLDEVYAKYAEpdadfdklaaQQGKYEEIIQAhdghnlnVQLERAAdalrlpdwDAKIANL 163
Cdd:cd03218 90 LTVEE----------NILAVLEIRGLSKKE----------REEKLEELLEE-------FHITHLR--------KSKASSL 134
|
170 180
....*....|....*....|....*.
gi 489953208 164 SGGERRRVALCRLLLEKPDMLLLDEP 189
Cdd:cd03218 135 SGGERRRVEIARALATNPKFLLLDEP 160
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
21-235 |
5.41e-16 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 77.75 E-value: 5.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIM-------------AGIDTDIEGEARPQPGI----KIGYLPQEPQLNPE 83
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprsgtlniAGNHFDFSKTPSDKAIRelrrNVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 84 HTVRESVEEAVSEVVnalkGLDEVYAKyaepdADFDKLAAQqgkyeeiiqahdghnlnVQLERAADALRLpdwdakiaNL 163
Cdd:PRK11124 97 LTVQQNLIEAPCRVL----GLSKDQAL-----ARAEKLLER-----------------LRLKPYADRFPL--------HL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489953208 164 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEGT---VVAITHDRYFLDNVAGWILELDRG 235
Cdd:PRK11124 143 SGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETgitQVIVTHEVEVARKTASRVVYMENG 217
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
16-217 |
5.65e-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: 77.27 E-value: 5.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AG---ID-TDIEGEARPQPGIKIGYLPQEPQLNPEh 84
Cdd:cd03253 11 DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLfrfydvsSGsilIDgQDIREVTLDSLRRAIGVVPQDTVLFND- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 85 TVRESVeeavsevvnalkgldevyaKYAEPDADFDKL--AAQQGK-YEEIIQAHDGHNLNVQlERAadaLRLpdwdakia 161
Cdd:cd03253 90 TIGYNI-------------------RYGRPDATDEEVieAAKAAQiHDKIMRFPDGYDTIVG-ERG---LKL-------- 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489953208 162 nlSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD-FEG-TVVAITH 217
Cdd:cd03253 139 --SGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDvSKGrTTIVIAH 194
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
324-506 |
7.57e-16 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 76.68 E-value: 7.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDRVL-IDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGET----VKLASVDQFRDAM 398
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsdLRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 399 -----DN----SKTVWEEVSGGLDIMRIGNTEMPSRAyvgrfnfkgTDQGKRVG----------ELSGGERGRLHLAKLL 459
Cdd:cd03292 81 gvvfqDFrllpDRNVYENVAFALEVTGVPPREIRKRV---------PAALELVGlshkhralpaELSGGEQQRVAIARAI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489953208 460 QVGGNVLLLDEPTNDLDIETLRALENALLEF--PGCAMVIS-HDRWFLDR 506
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKInkAGTTVVVAtHAKELVDT 201
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
324-507 |
8.09e-16 |
|
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: 76.47 E-value: 8.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGD--RVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLgETVKLASVDQfRDAMDNS 401
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLL-DGTDIRQLDP-ADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 402 KTVWEEV---SGGL-DIMRIGNTEMPSRAYVGRFNFKGTDQ---------GKRVGE----LSGGERGRLHLAKLLQVGGN 464
Cdd:cd03245 81 GYVPQDVtlfYGTLrDNITLGAPLADDERILRAAELAGVTDfvnkhpnglDLQIGErgrgLSGGQRQAVALARALLNDPP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489953208 465 VLLLDEPTNDLDIETLRALENALLEFPG--CAMVISHDRWFL---DRI 507
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLLdlvDRI 208
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
18-218 |
8.68e-16 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 77.46 E-value: 8.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAgidtdieGEARPQPGiKIGY-------------------LPQEP 78
Cdd:COG4559 13 GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLT-------GELTPSSG-EVRLngrplaawspwelarrravLPQHS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 79 QLNPEHTVResveeavsEVVnALkGLdevyAKYAEPDADFDKLAAQqgkyeeiiqahdghnlnvQLERaADALRLpdWDA 158
Cdd:COG4559 85 SLAFPFTVE--------EVV-AL-GR----APHGSSAAQDRQIVRE------------------ALAL-VGLAHL--AGR 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489953208 159 KIANLSGGERRRVALCRLLL-------EKPDMLLLDEPTNHLDaesVAW---LERFLHDF---EGTVVAITHD 218
Cdd:COG4559 130 SYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALD---LAHqhaVLRLARQLarrGGGVVAVLHD 199
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
22-218 |
8.77e-16 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 76.99 E-value: 8.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARpqpgiKIGYLPQEPQlnPEHTVRESV----EEAVSEV 97
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVR-----VAGLVPWKRR--KKFLRRIGVvfgqKTQLWWD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 98 VNALKGLDEVYAKYAEPDADFDKlaaqqgkyeeiiqahdghnlnvQLERAADALRL-PDWDAKIANLSGGERRRVALCRL 176
Cdd:cd03267 110 LPVIDSFYLLAAIYDLPPARFKK----------------------RLDELSELLDLeELLDTPVRQLSLGQRMRAEIAAA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489953208 177 LLEKPDMLLLDEPTNHLDAESVAWLERFLHDF----EGTVVAITHD 218
Cdd:cd03267 168 LLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnrerGTTVLLTSHY 213
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
20-236 |
8.93e-16 |
|
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: 77.39 E-value: 8.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEG---EARPQPGIKIGYlpQEPQLNPEHT 85
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFyrptsgrilfdGRDITGlppHRIARLGIARTF--QNPRLFPELT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 86 VRESVeeavseVVNALKGLDEVYAkyaepdADFDKLAAQQGKYEEIIqahdghnlnvqlERAADALRL----PDWDAKIA 161
Cdd:COG0411 96 VLENV------LVAAHARLGRGLL------AALLRLPRARREEREAR------------ERAEELLERvglaDRADEPAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489953208 162 NLSGGERRRVALCRLLLEKPDMLLLDEPT---NHLDAESVAWLERFLHDFEG-TVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:COG0411 152 NLSYGQQRRLEIARALATEPKLLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLVMGLADRIVVLDFGR 230
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
22-241 |
9.68e-16 |
|
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: 76.25 E-value: 9.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEA--------RPQPGIK--IGYLPQEPQLNPEHTVRESVE 91
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRAtvaghdvvREPREVRrrIGIVFQDLSVDDELTGWENLY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 92 eavsevvnalkgldeVYAK-YAEPDADFDKLAAQQGKYeeiiqahdghnlnVQLERAADALrlpdwdakIANLSGGERRR 170
Cdd:cd03265 96 ---------------IHARlYGVPGAERRERIDELLDF-------------VGLLEAADRL--------VKTYSGGMRRR 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489953208 171 VALCRLLLEKPDMLLLDEPTNHLDAESVA--W--LERFLHDFEGTVVAITHDRYFLDNVAGWILELDRG----EGIPWE 241
Cdd:cd03265 140 LEIARSLVHRPEVLFLDEPTIGLDPQTRAhvWeyIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGriiaEGTPEE 218
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
20-224 |
1.29e-15 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 75.04 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRImagidtdIEGEARPQPGikigylpqEPQLN--PEHTVRESVEEAVSeV 97
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQL-------LTGDLKPQQG--------EITLDgvPVSDLEKALSSLIS-V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 98 VNalkglDEVYAkyaepdadFDklaaqqgkyeeiiqAHDGHNLNVQLeraadalrlpdwdakianlSGGERRRVALCRLL 177
Cdd:cd03247 80 LN-----QRPYL--------FD--------------TTLRNNLGRRF-------------------SGGERQRLALARIL 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489953208 178 LEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EGTVVAITH--------DR-YFLDN 224
Cdd:cd03247 114 LQDAPIVLLDEPTVGLDPITERQLLSLIFEVlkDKTLIWITHhltgiehmDKiLFLEN 171
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
324-489 |
1.29e-15 |
|
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: 76.50 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGD-RVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQFRDAM--- 398
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIdGQDIREVTLDSLRRAIgvv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 399 --DN---SKTVW------------EEVSGGLDIMRIGNTEMpsrayvgRFNFK-GTDQGKRVGELSGGERGRLHLAKLLQ 460
Cdd:cd03253 81 pqDTvlfNDTIGynirygrpdatdEEVIEAAKAAQIHDKIM-------RFPDGyDTIVGERGLKLSGGEKQRVAIARAIL 153
|
170 180
....*....|....*....|....*....
gi 489953208 461 VGGNVLLLDEPTNDLDIETLRALENALLE 489
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRD 182
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
3-195 |
1.53e-15 |
|
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: 75.77 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 3 QFVYTMHRVGKVVP---PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTD---------IEGEARPQPGIK 70
Cdd:cd03234 1 QRVLPWWDVGLKAKnwnKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggttsgqilFNGQPRKPDQFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 71 --IGYLPQEPQLNPEHTVRESVEEAVsevVNALKgldevyakYAEPDADFDKLAAQQGkyeeIIQAHDGHnlnvqleraa 148
Cdd:cd03234 81 kcVAYVRQDDILLPGLTVRETLTYTA---ILRLP--------RKSSDAIRKKRVEDVL----LRDLALTR---------- 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489953208 149 daLRlpdwDAKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA 195
Cdd:cd03234 136 --IG----GNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
21-203 |
1.69e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 77.95 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE----ARPQPG------IKIGYLPQEPQLNPEHTVREsv 90
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKitvlGVPVPArarlarARIGVVPQFDNLDLEFTVRE-- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 91 eeavsevvNALkgldeVYAKYAepdadfdKLAAQQgkYEEIIQAHdghnLN-VQLERAAdalrlpdwDAKIANLSGGERR 169
Cdd:PRK13536 134 --------NLL-----VFGRYF-------GMSTRE--IEAVIPSL----LEfARLESKA--------DARVSDLSGGMKR 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 489953208 170 RVALCRLLLEKPDMLLLDEPTNHLD--AESVAWlER 203
Cdd:PRK13536 180 RLTLARALINDPQLLILDEPTTGLDphARHLIW-ER 214
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
289-529 |
1.69e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 79.62 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 289 ARLARFEELNNTEYQKRNetnelfiPPGARLGDKV---VEVTNLRKSY-GDRVLIDDLTFSVPKGAIVGIIGPNGAGKST 364
Cdd:PRK13657 304 PKLEEFFEVEDAVPDVRD-------PPGAIDLGRVkgaVEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKST 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 365 LFRMMSGQEQPDSGSITL-GE---TVKLASVDQ-----FRDAMDNSKTVWEEVsggldimRIG-----NTEM---PSRAY 427
Cdd:PRK13657 377 LINLLQRVFDPQSGRILIdGTdirTVTRASLRRniavvFQDAGLFNRSIEDNI-------RVGrpdatDEEMraaAERAQ 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 428 VGRFNFK-----GTDQGKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIETLRALENALlefpGCAM------V 496
Cdd:PRK13657 450 AHDFIERkpdgyDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAAL----DELMkgrttfI 525
|
250 260 270
....*....|....*....|....*....|....
gi 489953208 497 ISHdRWFLDRIATHILdYQDEGK-VEffEGNFTE 529
Cdd:PRK13657 526 IAH-RLSTVRNADRIL-VFDNGRvVE--SGSFDE 555
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
324-476 |
1.78e-15 |
|
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: 75.61 E-value: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDRVLIDDLTFsvPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGEtVKLASVDQ--------FR 395
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLTF--AQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING-VDVTAAPPadrpvsmlFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 396 DA-----MDNSKTVWEEVSGGLDIMRIGNTEMPSRAyvGRFNFKGTDQgKRVGELSGGERGRLHLAKLLQVGGNVLLLDE 470
Cdd:cd03298 78 ENnlfahLTVEQNVGLGLSPGLKLTAEDRQAIEVAL--ARVGLAGLEK-RLPGELSGGERQRVALARVLVRDKPVLLLDE 154
|
....*.
gi 489953208 471 PTNDLD 476
Cdd:cd03298 155 PFAALD 160
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
24-217 |
2.04e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 75.23 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 24 NISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQpGIKIG-----------YLPQEPQLNPEHTVRESVee 92
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQ-GEPIRrqrdeyhqdllYLGHQPGIKTELTALENL-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 93 avsevvnalkgldevyakyaepdaDFdkLAAQQGKY--EEIIQAhdghnlnvqLERAADALRLpdwDAKIANLSGGERRR 170
Cdd:PRK13538 96 ------------------------RF--YQRLHGPGddEALWEA---------LAQVGLAGFE---DVPVRQLSAGQQRR 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489953208 171 VALCRLLLEKPDMLLLDEPTNHLDAESVAWLER-FLHDFE--GTVVAITH 217
Cdd:PRK13538 138 VALARLWLTRAPLWILDEPFTAIDKQGVARLEAlLAQHAEqgGMVILTTH 187
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
324-508 |
2.13e-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: 75.84 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDRVLiDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQfRD------ 396
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLnGKDITNLPPEK-RDisyvpq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 397 --AMDNSKTVWEEVSGGLDIMRIGNTEMPSRAY-VGRfnFKGTDQ--GKRVGELSGGERGRLHLAKLLQVGGNVLLLDEP 471
Cdd:cd03299 79 nyALFPHMTVYKNIAYGLKKRKVDKKEIERKVLeIAE--MLGIDHllNRKPETLSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489953208 472 TNDLDIET----LRALENALLEFPGCAMVISHD----RWFLDRIA 508
Cdd:cd03299 157 FSALDVRTkeklREELKKIRKEFGVTVLHVTHDfeeaWALADKVA 201
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-477 |
2.48e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 78.51 E-value: 2.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI---DT-DIE--GEARPQPGIK------IGYLPQEPQLNPEHTVRES 89
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIytrDAgSILylGKEVTFNGPKssqeagIGIIHQELNLIPQLTIAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 90 VEEAvSEVVNALKGLDevYAK-YAEPDADFDKLAAQqgkyeeiiqaHDGHNLnvqleraadalrlpdwdakIANLSGGER 168
Cdd:PRK10762 100 IFLG-REFVNRFGRID--WKKmYAEADKLLARLNLR----------FSSDKL-------------------VGELSIGEQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 169 RRVALCRLLLEKPDMLLLDEPTNHL-DAESVAwlerflhdfegtvvaithdryfLDNVagwILEL-DRGEGIPwegnYSS 246
Cdd:PRK10762 148 QMVEIAKVLSFESKVIIMDEPTDALtDTETES----------------------LFRV---IRELkSQGRGIV----YIS 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 247 wleqkdQRLaQEASQeaarrksIEKELEWVRQGakgrQSKGKARLARFEELNNTEYQKRNETNELFIPPGARLGDKVVEV 326
Cdd:PRK10762 199 ------HRL-KEIFE-------ICDDVTVFRDG----QFIAEREVADLTEDSLIEMMVGRKLEDQYPRLDKAPGEVRLKV 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 327 TNLRKSyGdrvlIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVK-------LA------SVD 392
Cdd:PRK10762 261 DNLSGP-G----VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLdGHEVVtrspqdgLAngivyiSED 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 393 QFRDAM-------DN-SKTVWEEVSGGLDIMRIGNTEMPSRAYVGRFNFKGTDQGKRVGELSGGERGRLHLAKLLQVGGN 464
Cdd:PRK10762 336 RKRDGLvlgmsvkENmSLTALRYFSRAGGSLKHADEQQAVSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPK 415
|
490
....*....|...
gi 489953208 465 VLLLDEPTNDLDI 477
Cdd:PRK10762 416 VLILDEPTRGVDV 428
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
16-205 |
2.49e-15 |
|
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: 75.10 E-value: 2.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 16 PPKRHI--LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------------GIDTDIE-GEARpqpgIKIGYLPQEPQ 79
Cdd:cd03266 13 DVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAgllepdagfatvdGFDVVKEpAEAR----RRLGFVSDSTG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 80 LNPEHTVRESVEeavseVVNALKGLDevyakyaepdadfdklaaqqgkyeeiiqahdGHNLNVQLERAADALRLPDW-DA 158
Cdd:cd03266 89 LYDRLTARENLE-----YFAGLYGLK-------------------------------GDELTARLEELADRLGMEELlDR 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489953208 159 KIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFL 205
Cdd:cd03266 133 RVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFI 179
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
323-500 |
2.72e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 76.27 E-value: 2.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 323 VVEVTNLRKSYGD-RVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVK-----LASVDQ-- 393
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIkGEPIKydkksLLEVRKtv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 394 ---FRDAMDN--SKTVWEEVSGGLDIMRIGNTEMPSRAyvgrfnfkgTDQGKRVG----------ELSGGERGRLHLAKL 458
Cdd:PRK13639 81 givFQNPDDQlfAPTVEEDVAFGPLNLGLSKEEVEKRV---------KEALKAVGmegfenkpphHLSGGQKKRVAIAGI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489953208 459 LQVGGNVLLLDEPTNDLDIETLRALENALLEF--PGCAMVIS-HD 500
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnkEGITIIIStHD 196
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
18-220 |
3.03e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 75.82 E-value: 3.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEGEARPQPGIKIGYLPQEPqLNPEH-T 85
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLltpqsgtvflgDKPISMLSSRQLARRLALLPQHH-LTPEGiT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 86 VRESVEEAVSEVVN---ALKGLDEVYAKYAEPDADFDKLAaqqgkyeeiiqahdghnlnvqleraadalrlpdwDAKIAN 162
Cdd:PRK11231 93 VRELVAYGRSPWLSlwgRLSAEDNARVNQAMEQTRINHLA----------------------------------DRRLTD 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489953208 163 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EG-TVVAITHD-----RY 220
Cdd:PRK11231 139 LSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELntQGkTVVTVLHDlnqasRY 204
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
17-236 |
3.04e-15 |
|
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: 75.20 E-value: 3.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMagidtdiEGEARPQPGIKIgyLPQEPQLNPEHTVRESVEEAVSE 96
Cdd:cd03248 25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALL-------ENFYQPQGGQVL--LDGKPISQYEHKYLHSKVSLVGQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 97 --VVNALKGLDEVyaKYAEPDADFDKLAAQQGKYeeiiqahDGHNLNVQLERAADAlrlpDWDAKIANLSGGERRRVALC 174
Cdd:cd03248 96 epVLFARSLQDNI--AYGLQSCSFECVKEAAQKA-------HAHSFISELASGYDT----EVGEKGSQLSGGQKQRVAIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489953208 175 RLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EGTVVAITHdRYFLDNVAGWILELDRGE 236
Cdd:cd03248 163 RALIRNPQVLILDEATSALDAESEQQVQQALYDWpeRRTVLVIAH-RLSTVERADQILVLDGGR 225
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
31-218 |
3.06e-15 |
|
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: 77.46 E-value: 3.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 31 PGAKI-GVLGLNGAGKSTLLRIMAGIDTDIEGE--------ARPQPGI-------KIGYLPQEPQLNPEHTVREsveeav 94
Cdd:TIGR02142 21 PGQGVtAIFGRSGSGKTTLIRLIAGLTRPDEGEivlngrtlFDSRKGIflppekrRIGYVFQEARLFPHLSVRG------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 95 sevvNALKGLDEVYAKYaepdadfdklaaQQGKYEEIIQAHD-GHNLNvqleraadalRLPdwdakiANLSGGERRRVAL 173
Cdd:TIGR02142 95 ----NLRYGMKRARPSE------------RRISFERVIELLGiGHLLG----------RLP------GRLSGGEKQRVAI 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489953208 174 CRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDFEGTVVAITHD 218
Cdd:TIGR02142 143 GRALLSSPRLLLMDEPLAALDdprkYEILPYLERLHAEFGIPILYVSHS 191
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
323-520 |
3.53e-15 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 75.13 E-value: 3.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 323 VVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGS-ITLGETVKLASVD--------- 392
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDlIVDGLKVNDPKVDerlirqeag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 393 ----QFR-----DAMDN-----------SKTVWEEVSGGLdIMRIGNTEmpsRAyvgrfnfkgtdqGKRVGELSGGERGR 452
Cdd:PRK09493 81 mvfqQFYlfphlTALENvmfgplrvrgaSKEEAEKQAREL-LAKVGLAE---RA------------HHYPSELSGGQQQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489953208 453 LHLAKLLQVGGNVLLLDEPTNDLDI----ETLRALENALLEfpGCAMVI-SHDRWFLDRIATHILdYQDEGKV 520
Cdd:PRK09493 145 VAIARALAVKPKLMLFDEPTSALDPelrhEVLKVMQDLAEE--GMTMVIvTHEIGFAEKVASRLI-FIDKGRI 214
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-217 |
3.60e-15 |
|
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: 73.23 E-value: 3.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEarpqpgIKIgylpqepqlnpehtvresveeavsevvn 99
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGE------ILV---------------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 100 alkgldevyakyaepdadfdklaaqqgkyeeiiqahDGHNlnVQLERAADALRlpdwdAKIA---NLSGGERRRVALCRL 176
Cdd:cd03216 60 ------------------------------------DGKE--VSFASPRDARR-----AGIAmvyQLSVGERQMVEIARA 96
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489953208 177 LLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EG-TVVAITH 217
Cdd:cd03216 97 LARNARLLILDEPTAALTPAEVERLFKVIRRLraQGvAVIFISH 140
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
324-501 |
3.75e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 77.05 E-value: 3.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETV--------KLASVDQ- 393
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFhGTDVsrlhardrKVGFVFQh 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 394 ---FRDaMdnskTVWEEVSGGLDIMRigNTEMPSRAYVGRfnfKGTDQGKRV----------GELSGGERGRLHLAKLLQ 460
Cdd:PRK10851 83 yalFRH-M----TVFDNIAFGLTVLP--RRERPNAAAIKA---KVTQLLEMVqlahladrypAQLSGGQKQRVALARALA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489953208 461 VGGNVLLLDEPTNDLDIET-------LRALENallEFPGCAMVISHDR 501
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVrkelrrwLRQLHE---ELKFTSVFVTHDQ 197
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
342-500 |
4.82e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 74.97 E-value: 4.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 342 LTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQeQPDSGSITLG----ETVKLASVDQFRD----------AMDnsktVWEE 407
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAgqplEAWSAAELARHRAylsqqqtppfAMP----VFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 408 VSggLDIMRIGNTEMPSRA--YVGRFnFKGTDQ-GKRVGELSGGERGRLHLAK-LLQV------GGNVLLLDEPTNDLDI 477
Cdd:PRK03695 90 LT--LHQPDKTRTEAVASAlnEVAEA-LGLDDKlGRSVNQLSGGEWQRVRLAAvVLQVwpdinpAGQLLLLDEPMNSLDV 166
|
170 180
....*....|....*....|....*.
gi 489953208 478 ETLRALENALLEFP--GCAMVIS-HD 500
Cdd:PRK03695 167 AQQAALDRLLSELCqqGIAVVMSsHD 192
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
323-482 |
4.91e-15 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 76.38 E-value: 4.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 323 VVEVTNLRKSY----GDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQFRDA 397
Cdd:PRK11153 1 MIELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVdGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 398 MDN------------SKTVWEEVSGGLDIMRIGNTEMPSR-----AYVGRfnfkgTDQGKRV-GELSGGERGRLHLAKLL 459
Cdd:PRK11153 81 RRQigmifqhfnllsSRTVFDNVALPLELAGTPKAEIKARvtellELVGL-----SDKADRYpAQLSGGQKQRVAIARAL 155
|
170 180
....*....|....*....|...
gi 489953208 460 QVGGNVLLLDEPTNDLDIETLRA 482
Cdd:PRK11153 156 ASNPKVLLCDEATSALDPATTRS 178
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
19-217 |
5.24e-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: 73.68 E-value: 5.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQPGikigylpqepqlnPEHTVRESVEEAVSEV- 97
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG-------------PLDFQRDSIARGLLYLg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 98 -VNALKGLDEVyakyaepdadfdklaaqqgkyEEIIQAHDGHNLNVQLERAADALRLPDW-DAKIANLSGGERRRVALCR 175
Cdd:cd03231 80 hAPGIKTTLSV---------------------LENLRFWHADHSDEQVEEALARVGLNGFeDRPVAQLSAGQQRRVALAR 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489953208 176 LLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF---EGTVVAITH 217
Cdd:cd03231 139 LLLSGRPLWILDEPTTALDKAGVARFAEAMAGHcarGGMVVLTTH 183
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
18-189 |
5.66e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 74.68 E-value: 5.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEGE---ARPQPGIkiGYLPQEP----Q 79
Cdd:COG1137 15 KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLvkpdsgrifldGEDITHLpmhKRARLGI--GYLPQEAsifrK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 80 LnpehtvreSVEE---AVSEVVNalkgldevyakyaepdadFDKlAAQQGKYEEIIQA-HDGHnlnvqleraadaLRlpd 155
Cdd:COG1137 93 L--------TVEDnilAVLELRK------------------LSK-KEREERLEELLEEfGITH------------LR--- 130
|
170 180 190
....*....|....*....|....*....|....
gi 489953208 156 wDAKIANLSGGERRRVALCRLLLEKPDMLLLDEP 189
Cdd:COG1137 131 -KSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
18-189 |
5.75e-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: 5.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 18 KRHILKNISLSFFPGAKIGVLGLNGAGKST-------LLRIMAGI----DTDI-----EGEARpqpgIKIGYLPQEPQLN 81
Cdd:TIGR04406 13 KRKVVNDVSLSVKSGEIVGLLGPNGAGKTTsfymivgLVRPDAGKilidGQDIthlpmHERAR----LGIGYLPQEASIF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 82 PEHTVRESVeEAVSEVVNalkgldevyakyaepdaDFDKlAAQQGKYEEIIQA-HDGHnlnvqleraadaLRlpdwDAKI 160
Cdd:TIGR04406 89 RKLTVEENI-MAVLEIRK-----------------DLDR-AEREERLEALLEEfQISH------------LR----DNKA 133
|
170 180
....*....|....*....|....*....
gi 489953208 161 ANLSGGERRRVALCRLLLEKPDMLLLDEP 189
Cdd:TIGR04406 134 MSLSGGERRRVEIARALATNPKFILLDEP 162
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
9-477 |
6.35e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 77.26 E-value: 6.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 9 HRVGKVVPPKRhILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE----ARPQ----------PGIKIGYl 74
Cdd:PRK11288 8 DGIGKTFPGVK-ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSilidGQEMrfasttaalaAGVAIIY- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 75 pQEPQLNPEHTVREsveeavsevvNALKGldevyakyaepdadfdKLAAQQG---KYEEIIQAHDghnlnvQLERAADAL 151
Cdd:PRK11288 86 -QELHLVPEMTVAE----------NLYLG----------------QLPHKGGivnRRLLNYEARE------QLEHLGVDI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 152 rlpDWDAKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EGTVVA-ITH--DRYFLDNVA 226
Cdd:PRK11288 133 ---DPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELraEGRVILyVSHrmEEIFALCDA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 227 GWILeldrgegipwegnysswleqKDQRLAQEASQEAA-RRKSIEKELewvrqgaKGRqskgkarlarfeELNNT-EYQK 304
Cdd:PRK11288 210 ITVF--------------------KDGRYVATFDDMAQvDRDQLVQAM-------VGR------------EIGDIyGYRP 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 305 RNetnelfippgarLGDKVVEVTNLRksyGDRvLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-G 383
Cdd:PRK11288 251 RP------------LGEVRLRLDGLK---GPG-LREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLdG 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 384 ETVKLASVdqfRDAM---------DNSK-------TVWEEVS---------GGLDIMRIGNTEMPSRaYVGRFNFKGTDQ 438
Cdd:PRK11288 315 KPIDIRSP---RDAIragimlcpeDRKAegiipvhSVADNINisarrhhlrAGCLINNRWEAENADR-FIRSLNIKTPSR 390
|
490 500 510
....*....|....*....|....*....|....*....
gi 489953208 439 GKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDI 477
Cdd:PRK11288 391 EQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDV 429
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
21-236 |
7.14e-15 |
|
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: 74.84 E-value: 7.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIdtdiegeARPQPGiKIGYLPQE-PQLNPEH--TVRESVEEAVSEV 97
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGL-------EKPAQG-TVSFRGQDlYQLDRKQrrAFRRDVQLVFQDS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 98 VNALKGLDEVYAKYAEPDADFDKL--AAQQGKYEEIIQAhdghnlnVQLeRAADALRLPdwdakiANLSGGERRRVALCR 175
Cdd:TIGR02769 98 PSAVNPRMTVRQIIGEPLRHLTSLdeSEQKARIAELLDM-------VGL-RSEDADKLP------RQLSGGQLQRINIAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489953208 176 LLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:TIGR02769 164 ALAVKPKLIVLDEAVSNLDmvlqAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQ 228
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
321-520 |
7.33e-15 |
|
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: 74.04 E-value: 7.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 321 DKVVEVTNLRKSY---GDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETV---------- 386
Cdd:cd03248 9 KGIVKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLdGKPIsqyehkylhs 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 387 KLASVDQfrDAMDNSKTVWEEVSGGL---DIMRIgnTEMPSRAYVGRFNFK-----GTDQGKRVGELSGGERGRLHLAKL 458
Cdd:cd03248 89 KVSLVGQ--EPVLFARSLQDNIAYGLqscSFECV--KEAAQKAHAHSFISElasgyDTEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489953208 459 LQVGGNVLLLDEPTNDLDIETLRALENALLEFPG--CAMVISHDRWFLDRiATHILdYQDEGKV 520
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPErrTVLVIAHRLSTVER-ADQIL-VLDGGRI 226
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
321-477 |
7.57e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.82 E-value: 7.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 321 DKVVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETV-----------KLA 389
Cdd:PRK10575 9 DTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPleswsskafarKVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 390 SVDQFRDAMDnSKTVWEEVSGGldimrigntEMPSRAYVGRFnfkGTDQGKRVGE-----------------LSGGERGR 452
Cdd:PRK10575 89 YLPQQLPAAE-GMTVRELVAIG---------RYPWHGALGRF---GAADREKVEEaislvglkplahrlvdsLSGGERQR 155
|
170 180
....*....|....*....|....*
gi 489953208 453 LHLAKLLQVGGNVLLLDEPTNDLDI 477
Cdd:PRK10575 156 AWIAMLVAQDSRCLLLDEPTSALDI 180
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
323-490 |
8.27e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 74.18 E-value: 8.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 323 VVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMM------------SGQEQPDSGSITLGETVKLAS 390
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlielypearvSGEVYLDGQDIFKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 391 VDQFRDAMDN---SKTVWEEVSGGLDIMRIGNT--EMPSRAYVGRFNFKGTDQGKR-----VGELSGGERGRLHLAKLLQ 460
Cdd:PRK14247 83 RVQMVFQIPNpipNLSIFENVALGLKLNRLVKSkkELQERVRWALEKAQLWDEVKDrldapAGKLSGGQQQRLCIARALA 162
|
170 180 190
....*....|....*....|....*....|
gi 489953208 461 VGGNVLLLDEPTNDLDIETLRALENALLEF 490
Cdd:PRK14247 163 FQPEVLLADEPTANLDPENTAKIESLFLEL 192
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
18-205 |
8.69e-15 |
|
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: 73.05 E-value: 8.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTD--IEGE----ARPQPG---IKIGYLPQEPQLNPEHTVRE 88
Cdd:cd03232 19 KRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEilinGRPLDKnfqRSTGYVEQQDVHSPNLTVRE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 89 SVEeavsevvnalkgldevyakyaepdadfdklaaqqgkyeeiiqahdghnlnvqleraadalrlpdWDAKIANLSGGER 168
Cdd:cd03232 99 ALR----------------------------------------------------------------FSALLRGLSVEQR 114
|
170 180 190
....*....|....*....|....*....|....*..
gi 489953208 169 RRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFL 205
Cdd:cd03232 115 KRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFL 151
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
20-190 |
9.02e-15 |
|
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: 73.86 E-value: 9.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEG---EARPQPGikIGYLPQEPQLNPEHT 85
Cdd:COG0410 17 HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLlpprsgsirfdGEDITGlppHRIARLG--IGYVPEGRRIFPSLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 86 VRESVE---EAVSEVVNALKGLDEVYAKyaepdadFDKLAaqqgkyeeiiqahdghnlnvqlERaadalrlpdWDAKIAN 162
Cdd:COG0410 95 VEENLLlgaYARRDRAEVRADLERVYEL-------FPRLK----------------------ER---------RRQRAGT 136
|
170 180
....*....|....*....|....*...
gi 489953208 163 LSGGERRRVALCRLLLEKPDMLLLDEPT 190
Cdd:COG0410 137 LSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
288-488 |
1.07e-14 |
|
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: 77.09 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 288 KARLA--RFEE--LNNTEYQKRNETNELFIPpgarLGDKVVEVTNLRKSYGDRVLiDDLTFSVPKGAIVGIIGPNGAGKS 363
Cdd:TIGR01193 440 AARVAnnRLNEvyLVDSEFINKKKRTELNNL----NGDIVINDVSYSYGYGSNIL-SDISLTIKMNSKTTIVGMSGSGKS 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 364 TLFRMMSGQEQPDSGSITLGETvKLASVD--QFRDA---------------MDN------SKTVWEEVSGGLDIMRI-GN 419
Cdd:TIGR01193 515 TLAKLLVGFFQARSGEILLNGF-SLKDIDrhTLRQFinylpqepyifsgsiLENlllgakENVSQDEIWAACEIAEIkDD 593
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489953208 420 TEMPSRAYvgrfnfkGTDQGKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIETLRALENALL 488
Cdd:TIGR01193 594 IENMPLGY-------QTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLL 655
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
21-217 |
1.17e-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: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEAR-------PQPGIKIGYLPQEPQLNPEHTVRESVEEA 93
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLfdgkpldIAARNRIGYLPEERGLYPKMKVIDQLVYL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 94 VSevvnaLKGLDEVYAKyaepdadfdklaaqqgkyeeiiqahdgHNLNVQLERaadaLRLPDW-DAKIANLSGGERRRVA 172
Cdd:cd03269 95 AQ-----LKGLKKEEAR---------------------------RRIDEWLER----LELSEYaNKRVEELSKGNQQKVQ 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489953208 173 LCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEG---TVVAITH 217
Cdd:cd03269 139 FIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARagkTVILSTH 186
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
17-218 |
1.19e-14 |
|
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: 73.06 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEarpqpgIKIGylpqepqlnpehtvresvEEAVSE 96
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGR------IYIG------------------GRDVTD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 97 VVNALKGLDEVYAKYAepdadfdkLAAQQGKYEEI-----IQAHDGHNLNVQLERAADALRLPDW-DAKIANLSGGERRR 170
Cdd:cd03301 67 LPPKDRDIAMVFQNYA--------LYPHMTVYDNIafglkLRKVPKDEIDERVREVAELLQIEHLlDRKPKQLSGGQRQR 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489953208 171 VALCRLLLEKPDMLLLDEPTNHLDA----ESVAWLERFLHDFEGTVVAITHD 218
Cdd:cd03301 139 VALGRAIVREPKVFLMDEPLSNLDAklrvQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
320-500 |
1.67e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 73.65 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 320 GDKVVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQFRDAM 398
Cdd:PRK11831 4 VANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFdGENIPAMSRSRLYTVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 399 DNSKTVWEevSGGL--DIMRIGNTEMPSRAY------------------VGrfnFKGTDQGKRvGELSGGERGRLHLAKL 458
Cdd:PRK11831 84 KRMSMLFQ--SGALftDMNVFDNVAYPLREHtqlpapllhstvmmkleaVG---LRGAAKLMP-SELSGGMARRAALARA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489953208 459 LQVGGNVLLLDEPTNDLDIETLRALENALLEFPGC----AMVISHD 500
Cdd:PRK11831 158 IALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlgvtCVVVSHD 203
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
19-236 |
1.73e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 75.26 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE--------------ARPqpgikIGYLPQEPQLNPEH 84
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQimldgvdlshvppyQRP-----INMMFQSYALFPHM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 85 TVREsveeavsevvNALKGLDEvyakyaepdadfDKLAAQQ--GKYEEIIQAhdghnlnVQLERAADalRLPDwdakiaN 162
Cdd:PRK11607 107 TVEQ----------NIAFGLKQ------------DKLPKAEiaSRVNEMLGL-------VHMQEFAK--RKPH------Q 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 163 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA--------ESVAWLERflhdFEGTVVAITHDRYFLDNVAGWILELDR 234
Cdd:PRK11607 150 LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKklrdrmqlEVVDILER----VGVTCVMVTHDQEEAMTMAGRIAIMNR 225
|
..
gi 489953208 235 GE 236
Cdd:PRK11607 226 GK 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-500 |
1.76e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.90 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 19 RHILKNISLSFFPGAKIGVLGLNGAGKS-TLLRIMAGIDT--------DI-----------EGEARPQPGIKIGYLPQEP 78
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSppvvypsgDIrfhgesllhasEQTLRGVRGNKIAMIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 79 --QLNPEHTVresvEEAVSEVVNALKGLDEVYAKyaepdadfdklaaqqgkyEEIIQAHDghnlNVQLERAADalRLPDW 156
Cdd:PRK15134 102 mvSLNPLHTL----EKQLYEVLSLHRGMRREAAR------------------GEILNCLD----RVGIRQAAK--RLTDY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 157 DAKianLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEG----TVVAITHD----RYFLDNVAgw 228
Cdd:PRK15134 154 PHQ---LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelnmGLLFITHNlsivRKLADRVA-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 229 ILELDRGegipwegnysswLEQKDQRLAQEASQEAARRKSIEKELEwvrqGAKGRQSKGKARLARFEELnnteyqkrnet 308
Cdd:PRK15134 229 VMQNGRC------------VEQNRAATLFSAPTHPYTQKLLNSEPS----GDPVPLPEPASPLLDVEQL----------- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 309 nELFIPPGARLgdkvvevtnLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKST----LFRMMSGQeqpdsGSITL-G 383
Cdd:PRK15134 282 -QVAFPIRKGI---------LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ-----GEIWFdG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 384 ETVKLASVDQ-----------FRD---AMDNSKTVWEEVSGGLDIMRIGNTEMPSRAYVGR-FNFKGTDQGKR---VGEL 445
Cdd:PRK15134 347 QPLHNLNRRQllpvrhriqvvFQDpnsSLNPRLNVLQIIEEGLRVHQPTLSAAQREQQVIAvMEEVGLDPETRhryPAEF 426
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 446 SGGERGRLHLAKLLQVGGNVLLLDEPTNDLDiETLRA----LENALLEFPGCAMV-ISHD 500
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLD-KTVQAqilaLLKSLQQKHQLAYLfISHD 485
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-218 |
1.86e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 73.34 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIdTDIEGEA----RPQPGIKI-------GYLPQ--EPQLN------- 81
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEIllngRPLSDWSAaelarhrAYLSQqqSPPFAmpvfqyl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 82 ----PEHTVRESVEEAVSEVVNALkGLDevyakyaepdadfDKLaaqqgkyeeiiqahdGHNLNvqleraadalrlpdwd 157
Cdd:COG4138 91 alhqPAGASSEAVEQLLAQLAEAL-GLE-------------DKL---------------SRPLT---------------- 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489953208 158 akiaNLSGGERRRVALCRLLLE-----KPD--MLLLDEPTNHLD-AESVA---WLERFlHDFEGTVVAITHD 218
Cdd:COG4138 126 ----QLSGGEWQRVRLAAVLLQvwptiNPEgqLLLLDEPMNSLDvAQQAAldrLLREL-CQQGITVVMSSHD 192
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
19-251 |
1.89e-14 |
|
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: 73.64 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDI---EGEARPQPGIKIGYLPQepqlNPEH 84
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLlkptsgtvtidGRDItakKKKKLKDLRKKVGLVFQ----FPEH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 85 TV-RESVEEavsEVVNALK--GLDEvyakyaepdadfdklaaqqgkyEEIiqahdghnlnvqLERAADALRLPDWDAKIA 161
Cdd:TIGR04521 94 QLfEETVYK---DIAFGPKnlGLSE----------------------EEA------------EERVKEALELVGLDEEYL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 162 -----NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES-VAWLERF--LHDFEG-TVVAITHDryfLDNVAGW---I 229
Cdd:TIGR04521 137 erspfELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGrKEILDLFkrLHKEKGlTVILVTHS---MEDVAEYadrV 213
|
250 260
....*....|....*....|....*..
gi 489953208 230 LELDRG----EGIPWE-GNYSSWLEQK 251
Cdd:TIGR04521 214 IVMHKGkivlDGTPREvFSDVDELEKI 240
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
341-498 |
2.07e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 73.76 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 341 DLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSIT-LGETVKLASVDQFRDAMDNSKTV-W------EEVS--- 409
Cdd:PRK15056 25 DASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISiLGQPTRQALQKNLVAYVPQSEEVdWsfpvlvEDVVmmg 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 410 --GGLDIMRIGNTEMPSR-----AYVGRFNFKgtdqGKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIETLRA 482
Cdd:PRK15056 105 ryGHMGWLRRAKKRDRQIvtaalARVDMVEFR----HRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEAR 180
|
170
....*....|....*...
gi 489953208 483 LENALLEF--PGCAMVIS 498
Cdd:PRK15056 181 IISLLRELrdEGKTMLVS 198
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
20-226 |
2.14e-14 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 74.32 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI--------------DTDI----EGEARPQPGIKIGYLPQEPQ-- 79
Cdd:COG0444 19 KAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLlpppgitsgeilfdGEDLlklsEKELRKIRGREIQMIFQDPMts 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 80 LNPEHTVRESVEEAvsevvnalkgldevyakyaepdadfdklaaqqgkyeeiIQAHDGHNLNVQLERAADALR---LPDw 156
Cdd:COG0444 99 LNPVMTVGDQIAEP--------------------------------------LRIHGGLSKAEARERAIELLErvgLPD- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 157 DAKIAN-----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDFEGTVVAITHD----RYFLD 223
Cdd:COG0444 140 PERRLDrypheLSGGMRQRVMIARALALEPKLLIADEPTTALDvtiqAQILNLLKDLQRELGLAILFITHDlgvvAEIAD 219
|
...
gi 489953208 224 NVA 226
Cdd:COG0444 220 RVA 222
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
325-487 |
2.25e-14 |
|
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: 72.14 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 325 EVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETVKLASVDQFRDAM------ 398
Cdd:cd03231 2 EADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLlylgha 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 399 DNSKTVWEEVSGGLDIMRIGNTEMPSRAyVGRFNFKGTDQgKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIE 478
Cdd:cd03231 82 PGIKTTLSVLENLRFWHADHSDEQVEEA-LARVGLNGFED-RPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
....*....
gi 489953208 479 TLRALENAL 487
Cdd:cd03231 160 GVARFAEAM 168
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
334-476 |
2.30e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 72.44 E-value: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 334 GDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQFRDAMDNS--------KTV 404
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFeGEDISTLKPEIYRQQVSYCaqtptlfgDTV 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489953208 405 WEEVSGGLDIMRIGNTEMPSRAYVGRFNFKGTDQGKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLD 476
Cdd:PRK10247 98 YDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
20-228 |
2.45e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 73.23 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTdiegearPQPGiKIGYLPQEPQLNPEHTVRESVeeavsevvn 99
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYL-------PQRG-RVKVMGREVNAENEKWVRSKV--------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 100 alkGL------DEVYAKYAEPDADFDKLAAQQGKyEEIiqahdghnlnvqLERAADALRLPD-WDAKIA---NLSGGERR 169
Cdd:PRK13647 82 ---GLvfqdpdDQVFSSTVWDDVAFGPVNMGLDK-DEV------------ERRVEEALKAVRmWDFRDKppyHLSYGQKK 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489953208 170 RVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERfLHDFEGTVVAITHDryfLDNVAGW 228
Cdd:PRK13647 146 RVAIAGVLAMDPDVIVLDEPMAYLDprgqETLMEILDR-LHNQGKTVIVATHD---VDLAAEW 204
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
321-508 |
2.46e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 73.61 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 321 DKVVEVTNLRKSYG---DRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQFRD 396
Cdd:PRK13650 2 SNIIEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIdGDLLTEENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 397 AM-------DNS---KTVWEEVSGGLDIMRIGNTEMPSR-----AYVGRFNFKGTDQGKrvgeLSGGERGRLHLAKLLQV 461
Cdd:PRK13650 82 KIgmvfqnpDNQfvgATVEDDVAFGLENKGIPHEEMKERvnealELVGMQDFKEREPAR----LSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489953208 462 GGNVLLLDEPTNDLD----IETLRALENALLEFPGCAMVISHDrwfLDRIA 508
Cdd:PRK13650 158 RPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHD---LDEVA 205
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
17-252 |
2.57e-14 |
|
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: 72.26 E-value: 2.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG----------ID-TDIEGEARPQPGIKIGYLPQEPQLNPEhT 85
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRfydpqkgqilIDgIDIRDISRKSLRSMIGVVLQDTFLFSG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 86 VRESVeeavsevvnalkgldevyaKYAEPDADFD---KLAAQQGKYEEIIQAHDGHNLNVQlERAAdalrlpdwdakiaN 162
Cdd:cd03254 93 IMENI-------------------RLGRPNATDEeviEAAKEAGAHDFIMKLPNGYDTVLG-ENGG-------------N 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 163 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD-FEG-TVVAITHDRYFLDNvAGWILELDRGEgIPW 240
Cdd:cd03254 140 LSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKlMKGrTSIIIAHRLSTIKN-ADKILVLDDGK-IIE 217
|
250
....*....|..
gi 489953208 241 EGNYSSWLEQKD 252
Cdd:cd03254 218 EGTHDELLAKKG 229
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
323-499 |
2.60e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 71.76 E-value: 2.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 323 VVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKlASVDQFRDAM--- 398
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWqGEPIR-RQRDEYHQDLlyl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 399 ------DNSKTVWEEVSGGLDIMRIGNTEMpSRAYVGRFNFKGTDQGKrVGELSGGERGRLHLAKLLQVGGNVLLLDEPT 472
Cdd:PRK13538 80 ghqpgiKTELTALENLRFYQRLHGPGDDEA-LWEALAQVGLAGFEDVP-VRQLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
170 180 190
....*....|....*....|....*....|
gi 489953208 473 NDLD---IETLRALENALLEFPGCAMVISH 499
Cdd:PRK13538 158 TAIDkqgVARLEALLAQHAEQGGMVILTTH 187
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
336-490 |
2.77e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 72.30 E-value: 2.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 336 RVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQE--QPDSGSItlgetvklasvdqfrDAMDNskTVWEEVSGGLD 413
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCV---------------DVPDN--QFGREASLIDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 414 IMRIGNT----EMPSRA-YVGRFNFKgtdqgKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIETLRALENALL 488
Cdd:COG2401 106 IGRKGDFkdavELLNAVgLSDAVLWL-----RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQ 180
|
..
gi 489953208 489 EF 490
Cdd:COG2401 181 KL 182
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
326-500 |
2.91e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 72.79 E-value: 2.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 326 VTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGeTVKLASVDQ-----FRDA-MD 399
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG-TAPLAEAREdtrlmFQDArLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 400 NSKTVWEEVSGGLDimriGNTEMPSR---AYVGRFNfkgtdqgkRVGE----LSGGERGRLHLAKLLQVGGNVLLLDEPT 472
Cdd:PRK11247 94 PWKKVIDNVGLGLK----GQWRDAALqalAAVGLAD--------RANEwpaaLSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190
....*....|....*....|....*....|..
gi 489953208 473 NDLD----IETLRALENALLEFPGCAMVISHD 500
Cdd:PRK11247 162 GALDaltrIEMQDLIESLWQQHGFTVLLVTHD 193
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-477 |
3.10e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.21 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 1 MAQFVYTMHRVGKVVPPKrHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI------DTDIEGEARP--------Q 66
Cdd:PRK09700 1 MATPYISMAGIGKSFGPV-HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIheptkgTITINNINYNkldhklaaQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 67 PGIKIGYlpQEPQLNPEHTVREsveeavsevvNALKGLDEVYAKYAEPDADFDKLaaqQGKYEEIIqahdghnLNVQLER 146
Cdd:PRK09700 80 LGIGIIY--QELSVIDELTVLE----------NLYIGRHLTKKVCGVNIIDWREM---RVRAAMML-------LRVGLKV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 147 aadalrlpDWDAKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EGT-VVAITH------ 217
Cdd:PRK09700 138 --------DLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLrkEGTaIVYISHklaeir 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 218 ---DRYfldnvagwileldrgeGIPWEGNYSSwleqkdQRLAQEASQEAARRKSIEKELEwvrqgakgrqskgkarlARF 294
Cdd:PRK09700 210 ricDRY----------------TVMKDGSSVC------SGMVSDVSNDDIVRLMVGRELQ-----------------NRF 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 295 EELNNTEYQKRNETnelfippgarlgdkVVEVTNLRKSygDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQ 374
Cdd:PRK09700 251 NAMKENVSNLAHET--------------VFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDK 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 375 PDSGSITL-GETVKLAS-VDQFRDAM--------DN--------------SKTVWEEVSGGLdiMRIGNTEMPSR---AY 427
Cdd:PRK09700 315 RAGGEIRLnGKDISPRSpLDAVKKGMayitesrrDNgffpnfsiaqnmaiSRSLKDGGYKGA--MGLFHEVDEQRtaeNQ 392
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 489953208 428 VGRFNFKGTDQGKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDI 477
Cdd:PRK09700 393 RELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDV 442
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
321-476 |
3.19e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 73.30 E-value: 3.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 321 DKVVEVTNLRKSYGD--RVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSG----QEQPDSGSITLGETVKLASVDQF 394
Cdd:PRK13640 3 DNIVEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpDDNPNSKITVDGITLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 395 RDAM-------DNS---KTVWEEVSGGLDIMRIGNTEMPS-----RAYVGRFNFkgtdQGKRVGELSGGERGRLHLAKLL 459
Cdd:PRK13640 83 REKVgivfqnpDNQfvgATVGDDVAFGLENRAVPRPEMIKivrdvLADVGMLDY----IDSEPANLSGGQKQRVAIAGIL 158
|
170
....*....|....*..
gi 489953208 460 QVGGNVLLLDEPTNDLD 476
Cdd:PRK13640 159 AVEPKIIILDESTSMLD 175
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
325-520 |
3.22e-14 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 71.40 E-value: 3.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 325 EVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQE--QPDSGSITL-GETVKLASVDQ-FRDAMDN 400
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFkGEDITDLPPEErARLGIFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 401 SKTVWEEVSG--GLDIMRigntempsraYVGrfnfkgtdqgkrVGeLSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIE 478
Cdd:cd03217 82 AFQYPPEIPGvkNADFLR----------YVN------------EG-FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489953208 479 TLRALENALLEF--PGCAM-VISHDRWFLDRIAT---HILdyqDEGKV 520
Cdd:cd03217 139 ALRLVAEVINKLreEGKSVlIITHYQRLLDYIKPdrvHVL---YDGRI 183
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
321-500 |
3.33e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 72.85 E-value: 3.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 321 DKVVEVTNLRKSY--GDRVLiDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSIT-LGETVKLASVDQ---- 393
Cdd:PRK13647 2 DNIIEVEDLHFRYkdGTKAL-KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKvMGREVNAENEKWvrsk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 394 ----FRDAMDN--SKTVWEEVSGGLDIMRIGNTEMPSRA-----YVGRFNFKgtdqGKRVGELSGGERGRLHLAKLLQVG 462
Cdd:PRK13647 81 vglvFQDPDDQvfSSTVWDDVAFGPVNMGLDKDEVERRVeealkAVRMWDFR----DKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489953208 463 GNVLLLDEPTNDLD---IETLRALENALLEFPGCAMVISHD 500
Cdd:PRK13647 157 PDVIVLDEPMAYLDprgQETLMEILDRLHNQGKTVIVATHD 197
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
334-523 |
3.51e-14 |
|
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: 75.17 E-value: 3.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 334 GDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGetvkLASVDQfrdamdnsktvWEEVSGG-- 411
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLD----GADLSQ-----------WDREELGrh 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 412 ----------LD------IMRIGNT---------------EMpsrayVGRFNfKGTDQgkRVGE----LSGGERGRLHLA 456
Cdd:COG4618 408 igylpqdvelFDgtiaenIARFGDAdpekvvaaaklagvhEM-----ILRLP-DGYDT--RIGEggarLSGGQRQRIGLA 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489953208 457 KLLQvgGN--VLLLDEPTNDLDIETLRALENALLEF---PGCAMVISHDRWFL---DRIAthILdyqDEGKVEFF 523
Cdd:COG4618 480 RALY--GDprLVVLDEPNSNLDDEGEAALAAAIRALkarGATVVVITHRPSLLaavDKLL--VL---RDGRVQAF 547
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
341-522 |
4.53e-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: 71.56 E-value: 4.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 341 DLTFSVPkGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETVKLASvdqfRDAMDNSK------------------ 402
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDS----RKKINLPPqqrkiglvfqqyalfphl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 403 TVWEEVSGGLDIMRIGNTEMPSRAYVGRFNFKGTdQGKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIETLRA 482
Cdd:cd03297 91 NVRENLAFGLKRKRNREDRISVDELLDLLGLDHL-LNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489953208 483 LENALLE----FPGCAMVISHDRWFLDRIATHILDYQDeGKVEF 522
Cdd:cd03297 170 LLPELKQikknLNIPVIFVTHDLSEAEYLADRIVVMED-GRLQY 212
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
325-472 |
4.53e-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: 4.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 325 EVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQ---------- 393
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFdGEDITGLPPHRiarlgigyvp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 394 -----FRDaMdnskTVWEevsggldimrigNTEMPSRAYVGRFNFKGT---------------DQgkRVGELSGGERGRL 453
Cdd:COG0410 85 egrriFPS-L----TVEE------------NLLLGAYARRDRAEVRADlervyelfprlkerrRQ--RAGTLSGGEQQML 145
|
170
....*....|....*....
gi 489953208 454 HLAKLLQVGGNVLLLDEPT 472
Cdd:COG0410 146 AIGRALMSRPKLLLLDEPS 164
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
321-476 |
4.94e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 72.33 E-value: 4.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 321 DKVVEVTNLRKSYGD--RVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQFRDA 397
Cdd:PRK13632 5 SVMIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIdGITISKENLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 398 M-------DNS---KTVWEEVSGGLDIMRIGNTEMPSRAYvgrfnfkgtDQGKRVG----------ELSGGERGRLHLAK 457
Cdd:PRK13632 85 IgiifqnpDNQfigATVEDDIAFGLENKKVPPKKMKDIID---------DLAKKVGmedyldkepqNLSGGQKQRVAIAS 155
|
170
....*....|....*....
gi 489953208 458 LLQVGGNVLLLDEPTNDLD 476
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLD 174
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
326-500 |
5.04e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 72.27 E-value: 5.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 326 VTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL----GETVKLASVD--QFRDAMd 399
Cdd:PRK11701 9 VRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrdGQLRDLYALSeaERRRLL- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 400 nsKTVW------------EEVSGGLDI----MRIGNtempsRAYvGRFNFKGTDQGKRV-----------GELSGGERGR 452
Cdd:PRK11701 88 --RTEWgfvhqhprdglrMQVSAGGNIgerlMAVGA-----RHY-GDIRATAGDWLERVeidaariddlpTTFSGGMQQR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489953208 453 LHLAKLLQVGGNVLLLDEPTNDLDI-------ETLRALENALlefpGCAMVI-SHD 500
Cdd:PRK11701 160 LQIARNLVTHPRLVFMDEPTGGLDVsvqarllDLLRGLVREL----GLAVVIvTHD 211
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
19-236 |
5.12e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 72.53 E-value: 5.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEA--RPQPGIKigylpqepqlnpeHTVREsVEEAVSE 96
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVliRGEPITK-------------ENIRE-VRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 97 VVNALKglDEVYAKYAEPDADFDKLaaQQGKYEEIIqAHdghnlnvQLERAADALRLPDWDAKIAN-LSGGERRRVALCR 175
Cdd:PRK13652 83 VFQNPD--DQIFSPTVEQDIAFGPI--NLGLDEETV-AH-------RVSSALHMLGLEELRDRVPHhLSGGEKKRVAIAG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489953208 176 LLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEG----TVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtygmTVIFSTHQLDLVPEMADYIYVMDKGR 215
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
319-500 |
6.09e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 72.36 E-value: 6.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 319 LGDKVVEVTNLRKSYGD--RVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLG------ETV---- 386
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGgmvlseETVwdvr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 387 -KLASVDQFRDAMDNSKTVWEEVSGGLDIMRIGNTEMPSR-----AYVGRFNFkGTDQGKRvgeLSGGERGRLHLAKLLQ 460
Cdd:PRK13635 81 rQVGMVFQNPDNQFVGATVQDDVAFGLENIGVPREEMVERvdqalRQVGMEDF-LNREPHR---LSGGQKQRVAIAGVLA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489953208 461 VGGNVLLLDEPTNDLD-------IETLRALENAllefpGCAMVIS--HD 500
Cdd:PRK13635 157 LQPDIIILDEATSMLDprgrrevLETVRQLKEQ-----KGITVLSitHD 200
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
323-500 |
6.61e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 71.68 E-value: 6.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 323 VVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETVKLASVDQfRDAMDnsk 402
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQ-KLYLD--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 403 tvweevsggldimrignTEMPsrAYVGRF-----NFKGTDQG---KRVG----------ELSGGERGRLHLAKLLQVGGN 464
Cdd:PRK09544 80 -----------------TTLP--LTVNRFlrlrpGTKKEDILpalKRVQaghlidapmqKLSGGETQRVLLARALLNRPQ 140
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489953208 465 VLLLDEPTNDLDIE---TLRALENALLEFPGCA-MVISHD 500
Cdd:PRK09544 141 LLVLDEPTQGVDVNgqvALYDLIDQLRRELDCAvLMVSHD 180
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
18-241 |
7.68e-14 |
|
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: 71.69 E-value: 7.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIM-------------AGIDTDIEG---EARPqpgiKIGYLPQepqlN 81
Cdd:TIGR04520 14 EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLnglllptsgkvtvDGLDTLDEEnlwEIRK----KVGMVFQ----N 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 82 PEH-----TVRESV-----------EEAVSEVVNALK--GLDEvYAKYaEPdadfdklaaqqgkyeeiiqahdghnlnvq 143
Cdd:TIGR04520 86 PDNqfvgaTVEDDVafglenlgvprEEMRKRVDEALKlvGMED-FRDR-EP----------------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 144 leraadalrlpdwdakiANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES---VAWLERFLHDFEG-TVVAITHDr 219
Cdd:TIGR04520 135 -----------------HLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGrkeVLETIRKLNKEEGiTVISITHD- 196
|
250 260
....*....|....*....|....*...
gi 489953208 220 yfLDNV--AGWILELDRG----EGIPWE 241
Cdd:TIGR04520 197 --MEEAvlADRVIVMNKGkivaEGTPRE 222
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
328-520 |
1.11e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 71.17 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 328 NLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETV-KLASVDQFRD----AMDNS 401
Cdd:PRK10253 12 QLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLdGEHIqHYASKEVARRigllAQNAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 402 K----TVWEEVSGGldimRIGNTEMPSR-------AYVGRFNFKGTDQ--GKRVGELSGGERGRLHLAKLLQVGGNVLLL 468
Cdd:PRK10253 92 TpgdiTVQELVARG----RYPHQPLFTRwrkedeeAVTKAMQATGITHlaDQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489953208 469 DEPTNDLDIE---TLRALENALLEFPGCAM-VISHDRWFLDRIATHILDYQDeGKV 520
Cdd:PRK10253 168 DEPTTWLDIShqiDLLELLSELNREKGYTLaAVLHDLNQACRYASHLIALRE-GKI 222
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-500 |
1.12e-13 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 73.57 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 19 RHILKNISLSFFPGAKIGVLGLNGAGKS----TLLRIMAGIDTDIEGEAR---------PQP------GIKIGYLPQEPQ 79
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILfdgqdllglSERelrrirGNRIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 80 --LNPEHTVresvEEAVSEVVNALKGLDevyakyaepdadfdKLAAQQgkyeeiiqahdghnlnvqleRAADALR---LP 154
Cdd:COG4172 103 tsLNPLHTI----GKQIAEVLRLHRGLS--------------GAAARA--------------------RALELLErvgIP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 155 DwDAKIAN-----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDFEGTVVAITHD----RYF 221
Cdd:COG4172 145 D-PERRLDayphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDvtvqAQILDLLKDLQRELGMALLLITHDlgvvRRF 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 222 LDNVA----GWILEldRGEgipwegnysswleqkdqrLAQ--EASQEAARRKSIEKElewvrqgakgrqSKGKARLArfe 295
Cdd:COG4172 224 ADRVAvmrqGEIVE--QGP------------------TAElfAAPQHPYTRKLLAAE------------PRGDPRPV--- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 296 elnnteyqkrnetnelfiPPGARLgdkVVEVTNLRKSY-----------GDRVLIDDLTFSVPKGAIVGIIGPNGAGKST 364
Cdd:COG4172 269 ------------------PPDAPP---LLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKST 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 365 LFRMMSGQeQPDSGSITL-GETVKLASVDQFRD--------------AMDNSKTVWEEVSGGLDIMRIGNTEMPSRAYVG 429
Cdd:COG4172 328 LGLALLRL-IPSEGEIRFdGQDLDGLSRRALRPlrrrmqvvfqdpfgSLSPRMTVGQIIAEGLRVHGPGLSAAERRARVA 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 430 RFNfkgtdqgKRVG-----------ELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLD-------IETLRALENALlefp 491
Cdd:COG4172 407 EAL-------EEVGldpaarhryphEFSGGQRQRIAIARALILEPKLLVLDEPTSALDvsvqaqiLDLLRDLQREH---- 475
|
570
....*....|
gi 489953208 492 GCAMV-ISHD 500
Cdd:COG4172 476 GLAYLfISHD 485
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
323-381 |
1.23e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 72.04 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 323 VVEVTNLRKSYgdRVLI-----------------------DDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGS 379
Cdd:COG4586 1 IIEVENLSKTY--RVYEkepglkgalkglfrreyreveavDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGE 78
|
..
gi 489953208 380 IT 381
Cdd:COG4586 79 VR 80
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
324-483 |
1.27e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 70.93 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETVKLAS---------VDQF 394
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTArslsqqkglIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 395 RDAMD---------NSKTVWEEVSGGLDIMR---IGNTEMPSRAYVGRFNFKGTDQG--KRvgeLSGGERGRLHLAKLLQ 460
Cdd:PRK11264 84 RQHVGfvfqnfnlfPHRTVLENIIEGPVIVKgepKEEATARARELLAKVGLAGKETSypRR---LSGGQQQRVAIARALA 160
|
170 180 190
....*....|....*....|....*....|
gi 489953208 461 VGGNVLLLDEPTNDLDIE-------TLRAL 483
Cdd:PRK11264 161 MRPEVILFDEPTSALDPElvgevlnTIRQL 190
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
323-498 |
1.31e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 71.37 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 323 VVEVTNLRKSY-GDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQFR----- 395
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrGEPITKENIREVRkfvgl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 396 -----DAMDNSKTVWEEVSGGLDIMRIGNTEMPSRAYVGRFNFKGTDQGKRV-GELSGGERGRLHLAKLLQVGGNVLLLD 469
Cdd:PRK13652 83 vfqnpDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVpHHLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190
....*....|....*....|....*....|..
gi 489953208 470 EPTNDLDIETLRAL---ENALLEFPGCAMVIS 498
Cdd:PRK13652 163 EPTAGLDPQGVKELidfLNDLPETYGMTVIFS 194
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
20-218 |
1.61e-13 |
|
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: 70.34 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQPGIKIGYLPQEPQLNpehTVRESveeavsevvn 99
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVN---TVFQN---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 100 alkgldevYAKYaePDAD-FDKLA---AQQGKYEEIIQahdghnlnvqlERAADALRLPDWDA----KIANLSGGERRRV 171
Cdd:cd03300 81 --------YALF--PHLTvFENIAfglRLKKLPKAEIK-----------ERVAEALDLVQLEGyanrKPSQLSGGQQQRV 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489953208 172 ALCRLLLEKPDMLLLDEPTNHLDAESVAWLE---RFLHDFEG-TVVAITHD 218
Cdd:cd03300 140 AIARALVNEPKVLLLDEPLGALDLKLRKDMQlelKRLQKELGiTFVFVTHD 190
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
329-508 |
1.69e-13 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 70.75 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 329 LRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQFRD----------- 396
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIdGQDIAAMSRKELRElrrkkismvfq 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 397 --AMDNSKTVWEEVSGGLDIMRIGNTEMPSRA-----YVGRFNFKGtdqgKRVGELSGGERGRLHLAKLLQVGGNVLLLD 469
Cdd:cd03294 110 sfALLPHRTVLENVAFGLEVQGVPRAEREERAaealeLVGLEGWEH----KYPDELSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489953208 470 EPTNDLDIETLRALENALL----EFPGCAMVISHDrwfL-------DRIA 508
Cdd:cd03294 186 EAFSALDPLIRREMQDELLrlqaELQKTIVFITHD---LdealrlgDRIA 232
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
320-490 |
1.78e-13 |
|
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: 69.00 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 320 GDKVVEVTNLrkSYGDRVliDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQFRDA- 397
Cdd:cd03215 1 GEPVLEVRGL--SVKGAV--RDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLdGKPVTRRSPRDAIRAg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 398 -----MDNSKTvweevsGGLDIMRIG-NTEMPSRayvgrfnfkgtdqgkrvgeLSGGERGRLHLAKLLQVGGNVLLLDEP 471
Cdd:cd03215 77 iayvpEDRKRE------GLVLDLSVAeNIALSSL-------------------LSGGNQQKVVLARWLARDPRVLILDEP 131
|
170
....*....|....*....
gi 489953208 472 TNDLDIETLRALENALLEF 490
Cdd:cd03215 132 TRGVDVGAKAEIYRLIREL 150
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-217 |
1.80e-13 |
|
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: 70.26 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKST----LLR---------IMAGIDT-DIEGEARPQpgiKIGYLPQEPQLNp 82
Cdd:cd03249 14 PDVPILKGLSLTIPPGKTVALVGSSGCGKSTvvslLERfydptsgeiLLDGVDIrDLNLRWLRS---QIGLVSQEPVLF- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 83 EHTVRESVEeavsevvnalkgldevYAKYAEPDADFDKLAAQQGKYEEIIQAHDGHNLNVqleraadalrlpdwDAKIAN 162
Cdd:cd03249 90 DGTIAENIR----------------YGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLV--------------GERGSQ 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489953208 163 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF-EG-TVVAITH 217
Cdd:cd03249 140 LSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAmKGrTTIVIAH 196
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
325-500 |
1.86e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 70.50 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 325 EVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQ---------- 393
Cdd:PRK11248 3 QISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdGKPVEGPGAERgvvfqnegll 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 394 -FRDAMDNsktvweeVSGGLDIMRIGNTEMPSRA--YVGRFNFKGTDQgKRVGELSGGERGRLHLAKLLQVGGNVLLLDE 470
Cdd:PRK11248 83 pWRNVQDN-------VAFGLQLAGVEKMQRLEIAhqMLKKVGLEGAEK-RYIWQLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190
....*....|....*....|....*....|....
gi 489953208 471 PTNDLDIETLRALENALL----EFPGCAMVISHD 500
Cdd:PRK11248 155 PFGALDAFTREQMQTLLLklwqETGKQVLLITHD 188
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
328-521 |
2.08e-13 |
|
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: 71.68 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 328 NLRKSYGDRVLidDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETVkLASVDQ-------------- 393
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRT-LFDSRKgiflppekrrigyv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 394 FRDA-MDNSKTVWEEVSGGLDIMRIGNTEMPSRAYVGRFNFkGTDQGKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPT 472
Cdd:TIGR02142 81 FQEArLFPHLSVRGNLRYGMKRARPSERRISFERVIELLGI-GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489953208 473 NDLDI----ETLRALENALLEFPGCAMVISHDRWFLDRIATHILDYQDeGKVE 521
Cdd:TIGR02142 160 AALDDprkyEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLED-GRVA 211
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
324-488 |
2.22e-13 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 72.78 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSY-GDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQFR------ 395
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLdGVPVSSLDQDEVRrrvsvc 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 396 --DAMDNSKTVweevsggLDIMRIGN--------TEMPSRAYVGRF-----NFKGTDQGKRVGELSGGERGRLHLAKLLQ 460
Cdd:TIGR02868 415 aqDAHLFDTTV-------RENLRLARpdatdeelWAALERVGLADWlralpDGLDTVLGEGGARLSGGERQRLALARALL 487
|
170 180
....*....|....*....|....*...
gi 489953208 461 VGGNVLLLDEPTNDLDIETLRALENALL 488
Cdd:TIGR02868 488 ADAPILLLDEPTEHLDAETADELLEDLL 515
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
17-218 |
2.71e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 70.20 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEA--RPQP---------GIKIGYLPQepQLNPEH- 84
Cdd:PRK10575 22 PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIllDAQPleswsskafARKVAYLPQ--QLPAAEg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 85 -TVRESVeeAVsevvnalkgldevyAKYAEPDADFDKLAAQQGKYEEIIQAhdghnlnVQLERAADalRLPDwdakiaNL 163
Cdd:PRK10575 100 mTVRELV--AI--------------GRYPWHGALGRFGAADREKVEEAISL-------VGLKPLAH--RLVD------SL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489953208 164 SGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDFEGTVVAITHD 218
Cdd:PRK10575 149 SGGERQRAWIAMLVAQDSRCLLLDEPTSALDiahqVDVLALVHRLSQERGLTVIAVLHD 207
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
21-218 |
2.81e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 69.46 E-value: 2.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEA--RPQP-------------GIKIGYLPQEPQLNPEHT 85
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifNGQPmsklssaakaelrNQKLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 86 VRESVeeavsevvnalkgldevyakyAEPDADFDKLAAQ-QGKYEEIIQAhdghnlnVQLERAADAlrlpdwdaKIANLS 164
Cdd:PRK11629 104 ALENV---------------------AMPLLIGKKKPAEiNSRALEMLAA-------VGLEHRANH--------RPSELS 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489953208 165 GGERRRVALCRLLLEKPDMLLLDEPTNHLD---AESVAWLERFLHDFEGTV-VAITHD 218
Cdd:PRK11629 148 GGERQRVAIARALVNNPRLVLADEPTGNLDarnADSIFQLLGELNRLQGTAfLVVTHD 205
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
325-476 |
2.92e-13 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 69.89 E-value: 2.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 325 EVTNLRKSYG----DRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQ---FR- 395
Cdd:COG4525 5 TVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLdGVPVTGPGADRgvvFQk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 396 DAMDNSKTVWEEVSGGLDIMRIGNTEMPSRA-----YVGRFNFkgtdQGKRVGELSGGERGRLHLAKLLQVGGNVLLLDE 470
Cdd:COG4525 85 DALLPWLNVLDNVAFGLRLRGVPKAERRARAeellaLVGLADF----ARRRIWQLSGGMRQRVGIARALAADPRFLLMDE 160
|
....*.
gi 489953208 471 PTNDLD 476
Cdd:COG4525 161 PFGALD 166
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
339-500 |
3.00e-13 |
|
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: 69.42 E-value: 3.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 339 IDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQFRDAMDNS----KTVWEEVSGGLD 413
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILeGKQITEPGPDRMVVFQNYSllpwLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 414 IMRIGNTEMPSRAYVgRFNFK----GTDQGKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIETLRALENALLE 489
Cdd:TIGR01184 81 RVLPDLSKSERRAIV-EEHIAlvglTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQ 159
|
170
....*....|....*.
gi 489953208 490 F-----PGCAMViSHD 500
Cdd:TIGR01184 160 IweehrVTVLMV-THD 174
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
290-522 |
3.03e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 72.15 E-value: 3.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 290 RLARFEELNNTEYQKRNETNELFIPPGARLgdkvvEVTNLR-KSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRM 368
Cdd:COG4178 334 RLAGFEEALEAADALPEAASRIETSEDGAL-----ALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRA 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 369 MSGQEQPDSGSITLGETVKL---------------------ASVDQFRDAMdnSKTVWEEVsgGLDimrigntempsrAY 427
Cdd:COG4178 409 IAGLWPYGSGRIARPAGARVlflpqrpylplgtlreallypATAEAFSDAE--LREALEAV--GLG------------HL 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 428 VGRFnfkgtDQGKRVG-ELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIETLRALENALL-EFPGCAMV-ISHdRWFL 504
Cdd:COG4178 473 AERL-----DEEADWDqVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLReELPGTTVIsVGH-RSTL 546
|
250
....*....|....*...
gi 489953208 505 DRIATHILDYQDEGKVEF 522
Cdd:COG4178 547 AAFHDRVLELTGDGSWQL 564
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
26-194 |
3.19e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 69.23 E-value: 3.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 26 SLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE--------------ARPqpgikIGYLPQEPQLNPEHTVRESVe 91
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSltlngqdhtttppsRRP-----VSMLFQENNLFSHLTVAQNI- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 92 eavsevvnALkGLDevyakyaePDADFDklAAQQGKYEEIIQahdghnlNVQLEraaDAL-RLPdwdakiANLSGGERRR 170
Cdd:PRK10771 93 --------GL-GLN--------PGLKLN--AAQREKLHAIAR-------QMGIE---DLLaRLP------GQLSGGQRQR 137
|
170 180
....*....|....*....|....
gi 489953208 171 VALCRLLLEKPDMLLLDEPTNHLD 194
Cdd:PRK10771 138 VALARCLVREQPILLLDEPFSALD 161
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
20-236 |
4.12e-13 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 69.25 E-value: 4.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDT------DIEGEARPQPGI-------KIGYLPQEPQLNPEHTV 86
Cdd:COG1126 15 EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEpdsgtiTVDGEDLTDSKKdinklrrKVGMVFQQFNLFPHLTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 87 RESVEEAVSEVvnalKGLDEVYAKyaepdadfdklaaqqgkyeeiiqahdghnlnvqlERAADALR---LPD-WDAKIAN 162
Cdd:COG1126 95 LENVTLAPIKV----KKMSKAEAE----------------------------------ERAMELLErvgLADkADAYPAQ 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489953208 163 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EG-TVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:COG1126 137 LSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLakEGmTMVVVTHEMGFAREVADRVVFMDGGR 213
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
18-64 |
4.25e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 69.34 E-value: 4.25e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 489953208 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEAR 64
Cdd:COG1134 38 EFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
324-487 |
4.46e-13 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 68.80 E-value: 4.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGD--RVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLG----ETVKLAS------- 390
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDghdvRDYTLASlrrqigl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 391 VDQfrDAMDNSKTVWEEVSGG---------LDIMRIGN-----TEMPsrayvgrfnfKGTDQ--GKRVGELSGGERGRLH 454
Cdd:cd03251 81 VSQ--DVFLFNDTVAENIAYGrpgatreevEEAARAANahefiMELP----------EGYDTviGERGVKLSGGQRQRIA 148
|
170 180 190
....*....|....*....|....*....|...
gi 489953208 455 LAKLLQVGGNVLLLDEPTNDLDIETLRALENAL 487
Cdd:cd03251 149 IARALLKDPPILILDEATSALDTESERLVQAAL 181
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
21-236 |
4.56e-13 |
|
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: 68.67 E-value: 4.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 21 ILKNISLSFFPGAKIGVLGLNGAGKST----LLRIM---AG---IDT-DIEGEARPQPGIKIGYLPQEPQLNpEHTVRES 89
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLVelsSGsilIDGvDISKIGLHDLRSRISIIPQDPVLF-SGTIRSN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 90 veeavsevvnalkgLDEvYAKYAEpdadfdklaaqqgkyEEIIQAHDghnlNVQLERAADALRLPDwDAKIA----NLSG 165
Cdd:cd03244 98 --------------LDP-FGEYSD---------------EELWQALE----RVGLKEFVESLPGGL-DTVVEeggeNLSV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 166 GERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EGTVVAITH--------DRyfldnvagwILELDRG 235
Cdd:cd03244 143 GQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAfkDCTVLTIAHrldtiidsDR---------ILVLDKG 213
|
.
gi 489953208 236 E 236
Cdd:cd03244 214 R 214
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-508 |
4.96e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.81 E-value: 4.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 22 LKNISLSFFPGAKIGVLGLNGAGKS----TLLRIMAGIDTDIEGEA---------------------RPQPGIKIGYLPQ 76
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAGGLVQCDKmllrrrsrqvielseqsaaqmRHVRGADMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 77 EP--QLNPEHTVRESVEEAVsevvnalkgldevyakyaepdadfdKLAAQQGKYEEIIQAhdghnlnvqlERAADALRLP 154
Cdd:PRK10261 112 EPmtSLNPVFTVGEQIAESI-------------------------RLHQGASREEAMVEA----------KRMLDQVRIP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 155 DWDAKIA----NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDFEGTVVAITHDRYFLDNVA 226
Cdd:PRK10261 157 EAQTILSryphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDvtiqAQILQLIKVLQKEMSMGVIFITHDMGVVAEIA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 227 GWILELDRGEGIPwegnySSWLEQKDQRLAQEASQEAarrksiekeLEWV-RQGAKgrqsKGKARLARFEELNNTEYQKR 305
Cdd:PRK10261 237 DRVLVMYQGEAVE-----TGSVEQIFHAPQHPYTRAL---------LAAVpQLGAM----KGLDYPRRFPLISLEHPAKQ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 306 NETNE--LFIPpgarlGDKVVEVTNL------RKSYGDRV-----LIDDLTFSVPKGAIVGIIGPNGAGKST----LFRM 368
Cdd:PRK10261 299 EPPIEqdTVVD-----GEPILQVRNLvtrfplRSGLLNRVtrevhAVEKVSFDLWPGETLSLVGESGSGKSTtgraLLRL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 369 MSGQEqpdsGSITL-GETVKLASVDQ-----------FRD---AMDNSKTVWEEVSGGLDIMRIGNTEMPSRA---YVGR 430
Cdd:PRK10261 374 VESQG----GEIIFnGQRIDTLSPGKlqalrrdiqfiFQDpyaSLDPRQTVGDSIMEPLRVHGLLPGKAAAARvawLLER 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 431 FNFKGTDQGKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIETLRALENALL----EFPGCAMVISHDRWFLDR 506
Cdd:PRK10261 450 VGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLdlqrDFGIAYLFISHDMAVVER 529
|
..
gi 489953208 507 IA 508
Cdd:PRK10261 530 IS 531
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-218 |
5.04e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 68.65 E-value: 5.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 2 AQFVYTMHRVGKVVPPKRH---ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEG--------------EAR 64
Cdd:PRK10584 3 AENIVEVHHLKKSVGQGEHelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGevslvgqplhqmdeEAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 65 PQPGIK-IGYLPQEPQLNPEHTVRESVEeavseVVNALKGldevyakyaEPDADFDKLAAQqgkyeeiiqahdghnLNVQ 143
Cdd:PRK10584 83 AKLRAKhVGFVFQSFMLIPTLNALENVE-----LPALLRG---------ESSRQSRNGAKA---------------LLEQ 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489953208 144 LERAADALRLPdwdakiANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFL----HDFEGTVVAITHD 218
Cdd:PRK10584 134 LGLGKRLDHLP------AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHD 206
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
21-251 |
5.75e-13 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 68.41 E-value: 5.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AG---ID-TDIEGEARPQPGIKIGYLPQEPQLNPEhTVRES 89
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIprfydvdSGrilIDgHDVRDYTLASLRRQIGLVSQDVFLFND-TVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 90 VeeavsevvnalkgldevyaKYAEPDADfdklaaqqgkYEEIIQAhdghnlnvqlERAADAL----RLPD-WDAKIA--- 161
Cdd:cd03251 96 I-------------------AYGRPGAT----------REEVEEA----------ARAANAHefimELPEgYDTVIGerg 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 162 -NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDfeGTVVAITHDRYFLDNvAGWILELDRGE 236
Cdd:cd03251 137 vKLSGGQRQRIAIARALLKDPPILILDEATSALDTESerlvQAALERLMKN--RTTFVIAHRLSTIEN-ADRIVVLEDGK 213
|
250
....*....|....*
gi 489953208 237 gIPWEGNYSSWLEQK 251
Cdd:cd03251 214 -IVERGTHEELLAQG 227
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-229 |
8.78e-13 |
|
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: 68.55 E-value: 8.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 31 PGAKIGVLGLNGAGKSTLLRIMAGidtdiegEARPQPGikigylpqEPQLNPEHTvresveeavsEVVNALKG--LDEVY 108
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAG-------KLKPNLG--------KFDDPPDWD----------EILDEFRGseLQNYF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 109 AKYAEPDAD-------FDKLAAQ-QGKYEEIIQAHDGHNlnvQLERAADALRL-PDWDAKIANLSGGERRRVALCRLLLE 179
Cdd:cd03236 80 TKLLEGDVKvivkpqyVDLIPKAvKGKVGELLKKKDERG---KLDELVDQLELrHVLDRNIDQLSGGELQRVAIAAALAR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489953208 180 KPDMLLLDEPTNHLDAE---SVAWLERFLHDFEGTVVAITHDRYFLDNVAGWI 229
Cdd:cd03236 157 DADFYFFDEPSSYLDIKqrlNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
323-485 |
1.00e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 70.91 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 323 VVEVTNLRKSY---GDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETV----------KL 388
Cdd:TIGR00958 478 LIEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLdGVPLvqydhhylhrQV 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 389 ASVDQFRDAMdnSKTVWEEVSGGLDIM---RIGNTEMPSRA--YVGRF-NFKGTDQGKRVGELSGGERGRLHLAKLLQVG 462
Cdd:TIGR00958 558 ALVGQEPVLF--SGSVRENIAYGLTDTpdeEIMAAAKAANAhdFIMEFpNGYDTEVGEKGSQLSGGQKQRIAIARALVRK 635
|
170 180
....*....|....*....|...
gi 489953208 463 GNVLLLDEPTNDLDIETLRALEN 485
Cdd:TIGR00958 636 PRVLILDEATSALDAECEQLLQE 658
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
321-511 |
1.14e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 67.83 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 321 DKVVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGET----------VKL-- 388
Cdd:COG4674 8 GPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTdltgldeheiARLgi 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 389 ------ASVdqFRDAmdnskTVWE--EVSGGLD------IMRIGNTEMPSR-----AYVGRfnfkGTDQGKRVGELSGGE 449
Cdd:COG4674 88 grkfqkPTV--FEEL-----TVFEnlELALKGDrgvfasLFARLTAEERDRieevlETIGL----TDKADRLAGLLSHGQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489953208 450 RGRLHLAKLLQVGGNVLLLDEPTNDL-DIETLR--ALENALLEfpGCA-MVISHDRWFLDRIATHI 511
Cdd:COG4674 157 KQWLEIGMLLAQDPKLLLLDEPVAGMtDAETERtaELLKSLAG--KHSvVVVEHDMEFVRQIARKV 220
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
16-236 |
1.28e-12 |
|
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: 67.17 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDT------DIEGEARPQPGIKIGylpqepqLNPEHTVRES 89
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPpdsgtvTVRGRVSSLLGLGGG-------FNPELTGREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 90 VeeavsEVVNALKGLDevyakYAEPDAdfdklaaqqgKYEEIIQ-AhdghnlnvQLERAAdalrlpdwDAKIANLSGGER 168
Cdd:cd03220 105 I-----YLNGRLLGLS-----RKEIDE----------KIDEIIEfS--------ELGDFI--------DLPVKTYSSGMK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489953208 169 RRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF---EGTVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:cd03220 149 ARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELlkqGKTVILVSHDPSSIKRLCDRALVLEKGK 219
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-257 |
1.41e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 70.24 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAgidtdiegeaR---PQPG-IKIGYLP----QEPQLNPEHTVresve 91
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT----------RawdPQQGeILLNGQPiadySEAALRQAISV----- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 92 eaVSEVVNALKGLDEVYAKYAEPDADFDKLAA--QQGKYEEIIQAHDGhnLNVQLeraADALRLpdwdakianLSGGERR 169
Cdd:PRK11160 419 --VSQRVHLFSATLRDNLLLAAPNASDEALIEvlQQVGLEKLLEDDKG--LNAWL---GEGGRQ---------LSGGEQR 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 170 RVALCRLLLEKPDMLLLDEPTNHLDAESvawlER----FLHDF--EGTVVAITHDRYFLDNVAGWILeLDRGEGIPwEGN 243
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLDAET----ERqileLLAEHaqNKTVLMITHRLTGLEQFDRICV-MDNGQIIE-QGT 556
|
250
....*....|....
gi 489953208 244 YSSwLEQKDQRLAQ 257
Cdd:PRK11160 557 HQE-LLAQQGRYYQ 569
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
22-228 |
1.47e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 68.57 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEarpqpgIKIGYLPQEPQlnpehTVRESVEEAVSEVV--- 98
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGT------IEWIFKDEKNK-----KKTKEKEKVLEKLViqk 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 99 ---NALKGLDEV---------YAKYA------EPDADFDKLAAQQGKYEeiiqahdghnlnvQLERAADALRLPDWDAKI 160
Cdd:PRK13651 92 trfKKIKKIKEIrrrvgvvfqFAEYQlfeqtiEKDIIFGPVSMGVSKEE-------------AKKRAAKYIELVGLDESY 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489953208 161 A-----NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVA-WLERF--LHDFEGTVVAITHDryfLDNVAGW 228
Cdd:PRK13651 159 LqrspfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKeILEIFdnLNKQGKTIILVTHD---LDNVLEW 231
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
328-476 |
1.52e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 67.61 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 328 NLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSIT------------------LGETVKLA 389
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIiddedisllplhararrgIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 390 SVdqFRDAmdnskTVWEEVSGGLDIMRIGNTEM-PSRAYVGRFNFKGTDQGKRVGE-LSGGERGRLHLAKLLQVGGNVLL 467
Cdd:PRK10895 88 SI--FRRL-----SVYDNLMAVLQIRDDLSAEQrEDRANELMEEFHIEHLRDSMGQsLSGGERRRVEIARALAANPKFIL 160
|
....*....
gi 489953208 468 LDEPTNDLD 476
Cdd:PRK10895 161 LDEPFAGVD 169
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
325-487 |
1.57e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.94 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 325 EVTNLRKSY-GDRVLiDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVdqfRDAMDN-- 400
Cdd:PRK11288 6 SFDGIGKTFpGVKAL-DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIdGQEMRFAST---TAALAAgv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 401 -----------SKTVWEEVSGGldimrigntEMPSRAYV---GRFNFKGTDQGKRVGE----------LSGGERGRLHLA 456
Cdd:PRK11288 82 aiiyqelhlvpEMTVAENLYLG---------QLPHKGGIvnrRLLNYEAREQLEHLGVdidpdtplkyLSIGQRQMVEIA 152
|
170 180 190
....*....|....*....|....*....|....
gi 489953208 457 KLLQVGGNVLLLDEPTNDL---DIETLRALENAL 487
Cdd:PRK11288 153 KALARNARVIAFDEPTSSLsarEIEQLFRVIREL 186
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-241 |
1.70e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 68.12 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIdtdiegeARPQPG-IKIGYLPqepqLNPEhTVREsVEEAVSE 96
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGL-------LLPEAGtITVGGMV----LSEE-TVWD-VRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 97 VvnalkgldevyakYAEPDADF------DKLA----AQQGKYEEIIqahdghnlnvqlERAADALRL----PDWDAKIAN 162
Cdd:PRK13635 86 V-------------FQNPDNQFvgatvqDDVAfgleNIGVPREEMV------------ERVDQALRQvgmeDFLNREPHR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 163 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA---ESVAWLERFLHDFEG-TVVAITHDryfLDNVAGW--ILELDRG- 235
Cdd:PRK13635 141 LSGGQKQRVAIAGVLALQPDIIILDEATSMLDPrgrREVLETVRQLKEQKGiTVLSITHD---LDEAAQAdrVIVMNKGe 217
|
....*....
gi 489953208 236 ---EGIPWE 241
Cdd:PRK13635 218 ileEGTPEE 226
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
19-218 |
2.04e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 67.54 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGidtDIEGEARPQpGIKIgylPQEPQLNPEHTVRESVEEavsevv 98
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG---DLTGGGAPR-GARV---TGDVTLNGEPLAAIDAPR------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 99 naLKGLDEVYAKYAEPDADF--DKLAAqQGKYEEIIQA-----HDGHNLNVQLERA-ADALRLPDwdakIANLSGGERRR 170
Cdd:PRK13547 81 --LARLRAVLPQAAQPAFAFsaREIVL-LGRYPHARRAgalthRDGEIAWQALALAgATALVGRD----VTTLSGGELAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489953208 171 VALCRLLLE---------KPDMLLLDEPTNHLD-------AESVAWLERflhDFEGTVVAITHD 218
Cdd:PRK13547 154 VQFARVLAQlwpphdaaqPPRYLLLDEPTAALDlahqhrlLDTVRRLAR---DWNLGVLAIVHD 214
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-195 |
2.06e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 69.69 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLL-----RIMAGIDTD----IEGEARPQPGIKI--GYLPQEPQLNPEHT 85
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMnalafRSPKGVKGSgsvlLNGMPIDAKEMRAisAYVQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 86 VRESVeeavseVVNALKGLDEVYAKyaepdadfdklAAQQGKYEEIIQAhdghnlnVQLERAADAL-RLPDwdaKIANLS 164
Cdd:TIGR00955 116 VREHL------MFQAHLRMPRRVTK-----------KEKRERVDEVLQA-------LGLRKCANTRiGVPG---RVKGLS 168
|
170 180 190
....*....|....*....|....*....|.
gi 489953208 165 GGERRRVALCRLLLEKPDMLLLDEPTNHLDA 195
Cdd:TIGR00955 169 GGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
324-499 |
2.10e-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: 69.75 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYG--DRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLG----ETVKLAS------- 390
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDghdlADYTLASlrrqval 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 391 VDQfrDAMDNSKTVWEEVsggldimRIGNTEMPSRAYVGR-------FNF-----KGTDQ--GKRVGELSGGERGRLHLA 456
Cdd:TIGR02203 411 VSQ--DVVLFNDTIANNI-------AYGRTEQADRAEIERalaaayaQDFvdklpLGLDTpiGENGVLLSGGQRQRLAIA 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489953208 457 KLLQVGGNVLLLDEPTNDLDIETLRALENALLEF-PG-CAMVISH 499
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDNESERLVQAALERLmQGrTTLVIAH 526
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
21-247 |
2.22e-12 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 69.89 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQPGIKIGYLPQepqlnpeHTVresveEAVSEVVNA 100
Cdd:PLN03073 524 LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQ-------HHV-----DGLDLSSNP 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 101 LkgldeVYAKYAEPDADFDKLAAQQGKYeeiiqahdGHNLNVQLEraadalrlpdwdaKIANLSGGERRRVALCRLLLEK 180
Cdd:PLN03073 592 L-----LYMMRCFPGVPEQKLRAHLGSF--------GVTGNLALQ-------------PMYTLSGGQKSRVAFAKITFKK 645
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489953208 181 PDMLLLDEPTNHLDAESVAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRGEGIPWEGNYSSW 247
Cdd:PLN03073 646 PHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDY 712
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
324-484 |
2.30e-12 |
|
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: 66.94 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGD-RVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQFRDAM--- 398
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIdGEDIREQDPVELRRKIgyv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 399 -------------DNSKTV-----WEE------VSGGLDIMRignteMPSRAYVGRFNfkgtdqgkrvGELSGGERGRLH 454
Cdd:cd03295 81 iqqiglfphmtveENIALVpkllkWPKekirerADELLALVG-----LDPAEFADRYP----------HELSGGQQQRVG 145
|
170 180 190
....*....|....*....|....*....|
gi 489953208 455 LAKLLQVGGNVLLLDEPTNDLDIETLRALE 484
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDPITRDQLQ 175
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
230-297 |
2.35e-12 |
|
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: 62.59 E-value: 2.35e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 230 LELDRGEGIPWEGNYSSWLEQKDQRLAQEASQEAARRKSIEKELEWV-RQGAKG-RQSKGKARLARFEEL 297
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIdRFRAKAsKAKQAQSRIKALEKM 70
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
324-489 |
2.45e-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: 66.48 E-value: 2.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSY-GDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL----GETVKLAS-------V 391
Cdd:cd03254 3 IEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIdgidIRDISRKSlrsmigvV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 392 DQ----FRDA-MDN--------SKTVWEEVS---GGLD-IMRIGN---TEMpsrayvgrfnfkgtdqGKRVGELSGGERG 451
Cdd:cd03254 83 LQdtflFSGTiMENirlgrpnaTDEEVIEAAkeaGAHDfIMKLPNgydTVL----------------GENGGNLSQGERQ 146
|
170 180 190
....*....|....*....|....*....|....*...
gi 489953208 452 RLHLAKLLQVGGNVLLLDEPTNDLDIETLRALENALLE 489
Cdd:cd03254 147 LLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEK 184
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
324-520 |
2.85e-12 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 66.57 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLG-------ETVKLASVDQFR- 395
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAghqfdfsQKPSEKAIRLLRq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 396 ---------------DAMDN------------SKTVWEEVSGGLDIMRIGNtempsraYVGRFNFkgtdqgkrvgELSGG 448
Cdd:COG4161 83 kvgmvfqqynlwphlTVMENlieapckvlglsKEQAREKAMKLLARLRLTD-------KADRFPL----------HLSGG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489953208 449 ERGRLHLAKLLQVGGNVLLLDEPTNDLDIETLRALENALLEFPGCAM---VISHDRWFLDRIATHILdYQDEGKV 520
Cdd:COG4161 146 QQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGItqvIVTHEVEFARKVASQVV-YMEKGRI 219
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
20-236 |
3.72e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 68.13 E-value: 3.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDtDIE------GEAR----PQPGIKIGYLPQEPQLNPEHTVREs 89
Cdd:PRK11000 17 VISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLE-DITsgdlfiGEKRmndvPPAERGVGMVFQSYALYPHLSVAE- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 90 veeavsevvNALKGLDEVYAKYAEPDADFDKLAaqqgkyeEIIQ-AHdghnlnvQLERAADAlrlpdwdakianLSGGER 168
Cdd:PRK11000 95 ---------NMSFGLKLAGAKKEEINQRVNQVA-------EVLQlAH-------LLDRKPKA------------LSGGQR 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489953208 169 RRVALCRLLLEKPDMLLLDEPTNHLDAE-------SVAWLERFLhdfEGTVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:PRK11000 140 QRVAIGRTLVAEPSVFLLDEPLSNLDAAlrvqmriEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGR 211
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
322-499 |
3.97e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 68.66 E-value: 3.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 322 KVVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGE------TVKLA------ 389
Cdd:PRK09700 4 PYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynklDHKLAaqlgig 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 390 ------SVDQFRDAMDN-------SKTVWeevsgGLDImrIGNTEMPSRAYV--GRFNFKgTDQGKRVGELSGGERGRLH 454
Cdd:PRK09700 84 iiyqelSVIDELTVLENlyigrhlTKKVC-----GVNI--IDWREMRVRAAMmlLRVGLK-VDLDEKVANLSISHKQMLE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489953208 455 LAKLLQVGGNVLLLDEPTNDL---DIETLRALENALLEfPGCAMV-ISH 499
Cdd:PRK09700 156 IAKTLMLDAKVIIMDEPTSSLtnkEVDYLFLIMNQLRK-EGTAIVyISH 203
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
37-217 |
4.07e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 67.59 E-value: 4.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 37 VLGLNGAGKSTLLRIMAGIDTDIEGEAR--------PQPGI-------KIGYLPQEPQLNPEHTVREsveeavsevvNAL 101
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVlngrvlfdAEKGIclppekrRIGYVFQDARLFPHYKVRG----------NLR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 102 KGLDEVYakyaepDADFDKLAAQQGkyeeiIqahdGHNLNvqleraadalRLPdwdakiANLSGGERRRVALCRLLLEKP 181
Cdd:PRK11144 99 YGMAKSM------VAQFDKIVALLG-----I----EPLLD----------RYP------GSLSGGEKQRVAIGRALLTAP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489953208 182 DMLLLDEPTNHLDA----ESVAWLERFLHDFEGTVVAITH 217
Cdd:PRK11144 148 ELLLMDEPLASLDLprkrELLPYLERLAREINIPILYVSH 187
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
330-483 |
4.14e-12 |
|
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: 65.76 E-value: 4.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 330 RKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQpdSGSITLGETV-------------KLASVDQFrD 396
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVE--GGGTTSGQILfngqprkpdqfqkCVAYVRQD-D 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 397 AMDNSKTVWEEVSGGLdIMRIGNtEMPSRAYVGRFNFKGTDQ-------GKRVGELSGGERGRLHLAKLLQVGGNVLLLD 469
Cdd:cd03234 91 ILLPGLTVRETLTYTA-ILRLPR-KSSDAIRKKRVEDVLLRDlaltrigGNLVKGISGGERRRVSIAVQLLWDPKVLILD 168
|
170 180
....*....|....*....|.
gi 489953208 470 EPTNDLD-------IETLRAL 483
Cdd:cd03234 169 EPTSGLDsftalnlVSTLSQL 189
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-236 |
4.42e-12 |
|
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: 65.97 E-value: 4.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEA---------------RPQpgikIGYLPQEPQL 80
Cdd:cd03252 12 PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlvdghdlaladpawlRRQ----VGVVLQENVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 81 NpEHTVRESVeeavsevvnALkgldevyakyAEPDADFDKL---AAQQGKYEEIIQAHDGHNLNVQlERAAdalrlpdwd 157
Cdd:cd03252 88 F-NRSIRDNI---------AL----------ADPGMSMERVieaAKLAGAHDFISELPEGYDTIVG-EQGA--------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 158 akiaNLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEG--TVVAITHdRYFLDNVAGWILELDRG 235
Cdd:cd03252 138 ----GLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAgrTVIIIAH-RLSTVKNADRIIVMEKG 212
|
.
gi 489953208 236 E 236
Cdd:cd03252 213 R 213
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
324-513 |
4.97e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 68.31 E-value: 4.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDR--VLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQFRDAMdn 400
Cdd:PRK11160 339 LTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLnGQPIADYSEAALRQAI-- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 401 sKTVWEEV---SGGL-DIMRIGN--------TEMPSRayVGRFNFKGTDQGKR--VGE----LSGGERGRLHLAKLLQVG 462
Cdd:PRK11160 417 -SVVSQRVhlfSATLrDNLLLAApnasdealIEVLQQ--VGLEKLLEDDKGLNawLGEggrqLSGGEQRRLGIARALLHD 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489953208 463 GNVLLLDEPTNDLDIETLRALENALLEFpgCA----MVISHDRWFL---DRIatHILD 513
Cdd:PRK11160 494 APLLLLDEPTEGLDAETERQILELLAEH--AQnktvLMITHRLTGLeqfDRI--CVMD 547
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
321-529 |
5.05e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 66.80 E-value: 5.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 321 DKVVEVTNLRKSYGDRV-LIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSI---------------TLGE 384
Cdd:PRK13636 3 DYILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdgkpidysrkglmKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 385 TVKLasVDQFRDAMDNSKTVWEEVSGGLDIMRIGNTEMPSRAyvgRFNFKGTD----QGKRVGELSGGERGRLHLAKLLQ 460
Cdd:PRK13636 83 SVGM--VFQDPDNQLFSASVYQDVSFGAVNLKLPEDEVRKRV---DNALKRTGiehlKDKPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 461 VGGNVLLLDEPTNDLD---IETLRALENALLEFPGCAMVishdrwfldrIATHILD----------YQDEGKVeFFEGNF 527
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDpmgVSEIMKLLVEMQKELGLTII----------IATHDIDivplycdnvfVMKEGRV-ILQGNP 226
|
..
gi 489953208 528 TE 529
Cdd:PRK13636 227 KE 228
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
19-195 |
5.14e-12 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 66.42 E-value: 5.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI------DTDIEGEARPQPGIKIGYLPQEPQLNPEHTVRESVEE 92
Cdd:COG4525 20 QPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFlapssgEITLDGVPVTGPGADRGVVFQKDALLPWLNVLDNVAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 93 AVSevvnaLKGLDEvyakyaepdadfdklAAQQGKYEEIIQAhdghnlnVQLERAADAlrlpdwdaKIANLSGGERRRVA 172
Cdd:COG4525 100 GLR-----LRGVPK---------------AERRARAEELLAL-------VGLADFARR--------RIWQLSGGMRQRVG 144
|
170 180
....*....|....*....|...
gi 489953208 173 LCRLLLEKPDMLLLDEPTNHLDA 195
Cdd:COG4525 145 IARALAADPRFLLMDEPFGALDA 167
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
26-242 |
5.23e-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: 65.21 E-value: 5.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 26 SLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQpGIKIGYLP----------QEPQLNPEHTVRESVEEAVS 95
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLIN-GVDVTAAPpadrpvsmlfQENNLFAHLTVEQNVGLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 96 evvnalKGLdevyakyaepdadfdKLAAQQGKYEEIIQAhdghnlnvQLERAADALRLPDwdakiaNLSGGERRRVALCR 175
Cdd:cd03298 97 ------PGL---------------KLTAEDRQAIEVALA--------RVGLAGLEKRLPG------ELSGGERQRVALAR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489953208 176 LLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRGEgIPWEG 242
Cdd:cd03298 142 VLVRDKPVLLLDEPFAALDpalrAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGR-IAAQG 211
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
324-520 |
5.23e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 65.81 E-value: 5.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSIT-------LGETVKLASVDQFRD 396
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNiagnhfdFSKTPSDKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 397 ----------------AMDNSKTVWEEVSGgldimrIGNTEMPSRA-----------YVGRFNFkgtdqgkrvgELSGGE 449
Cdd:PRK11124 83 nvgmvfqqynlwphltVQQNLIEAPCRVLG------LSKDQALARAekllerlrlkpYADRFPL----------HLSGGQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489953208 450 RGRLHLAKLLQVGGNVLLLDEPTNDLDIETLRALENALLEFPGCAM---VISHDRWFLDRIATHILdYQDEGKV 520
Cdd:PRK11124 147 QQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGItqvIVTHEVEVARKTASRVV-YMENGHI 219
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
15-217 |
6.79e-12 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 68.72 E-value: 6.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 15 VPPKR-HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTD--IEGEARPQPGIKI--------GYLPQEPQLNPE 83
Cdd:PLN03140 888 VTEDRlQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGFPKKqetfarisGYCEQNDIHSPQ 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 84 HTVRESVeeavsevvnalkgldeVYAKyaepdadFDKLAAQQGKYEEIIQAHDGHNLnVQLERAADAL-RLPDwdakIAN 162
Cdd:PLN03140 968 VTVRESL----------------IYSA-------FLRLPKEVSKEEKMMFVDEVMEL-VELDNLKDAIvGLPG----VTG 1019
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489953208 163 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLH---DFEGTVVAITH 217
Cdd:PLN03140 1020 LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRntvDTGRTVVCTIH 1077
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
17-197 |
7.71e-12 |
|
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: 67.92 E-value: 7.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AG---ID-TDIegeaR--PQPGIK--IGYLPQEPQL- 80
Cdd:COG5265 369 PERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLfrfydvtSGrilIDgQDI----RdvTQASLRaaIGIVPQDTVLf 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 81 NpeHTVRESVeeavsevvnalkgldevyaKYAEPDADfdklaaqqgkYEEIiqahdghnlnvqlERAADA-------LRL 153
Cdd:COG5265 445 N--DTIAYNI-------------------AYGRPDAS----------EEEV-------------EAAARAaqihdfiESL 480
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489953208 154 PD-WDAKIA----NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 197
Cdd:COG5265 481 PDgYDTRVGerglKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRT 529
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
324-476 |
8.47e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 65.49 E-value: 8.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYG-----DRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQ---- 393
Cdd:COG1101 2 LELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIdGKDVTKLPEYKraky 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 394 ----FRDAMDN---SKTVWEEVS--------GGLdimRIGNTempsRAYVGRFN--FKGTDQG------KRVGELSGGER 450
Cdd:COG1101 82 igrvFQDPMMGtapSMTIEENLAlayrrgkrRGL---RRGLT----KKRRELFRelLATLGLGlenrldTKVGLLSGGQR 154
|
170 180
....*....|....*....|....*...
gi 489953208 451 GRLHL--AKLLQVggNVLLLDEPTNDLD 476
Cdd:COG1101 155 QALSLlmATLTKP--KLLLLDEHTAALD 180
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-223 |
8.52e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.98 E-value: 8.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGidtdiegEARPQPGIKIGYLPQEpQLNPEHTVRESV--EEAVS 95
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG-------ALKGTPVAGCVDVPDN-QFGREASLIDAIgrKGDFK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 96 EVVNALK--GLDEVYAkyaepdadfdklaaqqgkyeeiiqahdghnlnvqleraadalrlpdWDAKIANLSGGERRRVAL 173
Cdd:COG2401 114 DAVELLNavGLSDAVL----------------------------------------------WLRRFKELSTGQKFRFRL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489953208 174 CRLLLEKPDMLLLDEPTNHLD---AESVAW-LERFLHDFEGTVVAITHDRYFLD 223
Cdd:COG2401 148 ALLLAERPKLLVIDEFCSHLDrqtAKRVARnLQKLARRAGITLVVATHHYDVID 201
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
323-516 |
9.67e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 64.20 E-value: 9.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 323 VVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVK--LASVDQ------ 393
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFeRQSIKkdLCTYQKqlcfvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 394 FRDAMDNSKTVWEEV-------SGGLDImrignTEMPSRAYVGRF-NFKgtdqgkrVGELSGGERGRLHLAKLLQVGGNV 465
Cdd:PRK13540 81 HRSGINPYLTLRENClydihfsPGAVGI-----TELCRLFSLEHLiDYP-------CGLLSSGQKRQVALLRLWMSKAKL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489953208 466 LLLDEPTNDLD---IETLRALENALLEFPGCAMVISHDRWFLDRIathilDYQD 516
Cdd:PRK13540 149 WLLDEPLVALDelsLLTIITKIQEHRAKGGAVLLTSHQDLPLNKA-----DYEE 197
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
9-386 |
1.03e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 67.84 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 9 HRVGKVVPpkrhiLKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-----------IDTDI-EGEARPQPGIKIGYLPQ 76
Cdd:NF033858 9 HRYGKTVA-----LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGarkiqqgrvevLGGDMaDARHRRAVCPRIAYMPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 77 E--PQLNPEHTVRESVEeavseVVNALKGLDEvyakyAEPDADFDKLAAQQGkyeeiiqahdghnLNVQLERAAdalrlp 154
Cdd:NF033858 84 GlgKNLYPTLSVFENLD-----FFGRLFGQDA-----AERRRRIDELLRATG-------------LAPFADRPA------ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 155 dwdakiANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVA--W--LERFLHDFEG-TVVAITHdryFLDNVAG-- 227
Cdd:NF033858 135 ------GKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRqfWelIDRIRAERPGmSVLVATA---YMEEAERfd 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 228 WILELDRGegipwegnysswleqkdQRLAQEASQEAARRKsiekelewvrqgakGRQSKGKARLARFEElnnteyQKRNE 307
Cdd:NF033858 206 WLVAMDAG-----------------RVLATGTPAELLART--------------GADTLEAAFIALLPE------EKRRG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 308 TNELFIPPGARLGDK--VVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GE 384
Cdd:NF033858 249 HQPVVIPPRPADDDDepAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfGQ 328
|
..
gi 489953208 385 TV 386
Cdd:NF033858 329 PV 330
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-238 |
1.21e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 64.86 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIdTDIEGEARPQPGIKI-GYLPQEPQLNPEHtVRESVEeAVSEVV 98
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRL-LELNEEARVEGEVRLfGRNIYSPDVDPIE-VRREVG-MVFQYP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 99 NALKGLdEVYAKYAePDADFDKLAAQQGKYEEIIQAhdghnlnvQLERAA--DAL--RLPDWDAkiaNLSGGERRRVALC 174
Cdd:PRK14267 95 NPFPHL-TIYDNVA-IGVKLNGLVKSKKELDERVEW--------ALKKAAlwDEVkdRLNDYPS---NLSGGQRQRLVIA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489953208 175 RLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EGTVVAITHDRYFLDNVAGWILELDRGEGI 238
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFELkkEYTIVLVTHSPAQAARVSDYVAFLYLGKLI 227
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
324-483 |
1.27e-11 |
|
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: 63.72 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDRVLiDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQ--EQPDSGSITL-GETVKLAS-------VDQ 393
Cdd:cd03213 11 VTVKSSPSKSGKQLL-KNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLInGRPLDKRSfrkiigyVPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 394 fRDAMDNSKTVWE--EVSGGLdimrigntempsrayvgrfnfKGtdqgkrvgeLSGGERGRLHLAKLLQVGGNVLLLDEP 471
Cdd:cd03213 90 -DDILHPTLTVREtlMFAAKL---------------------RG---------LSGGERKRVSIALELVSNPSLLFLDEP 138
|
170
....*....|....*....
gi 489953208 472 TNDLD-------IETLRAL 483
Cdd:cd03213 139 TSGLDsssalqvMSLLRRL 157
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
10-218 |
1.57e-11 |
|
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: 64.63 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 10 RVGKVVPPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE-------ARPQPGI----KIGYLPQEP 78
Cdd:cd03295 5 NVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEifidgedIREQDPVelrrKIGYVIQQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 79 QLNPEHTVRESVEeavseVVNALKGLDEvyAKYAEPDADFDKLaaqqgkyeeiiqahdghnlnVQLERAADALRLPDwda 158
Cdd:cd03295 85 GLFPHMTVEENIA-----LVPKLLKWPK--EKIRERADELLAL--------------------VGLDPAEFADRYPH--- 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489953208 159 kiaNLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA-------ESVAWLERFLHDfegTVVAITHD 218
Cdd:cd03295 135 ---ELSGGQQQRVGVARALAADPPLLLMDEPFGALDPitrdqlqEEFKRLQQELGK---TIVFVTHD 195
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
17-217 |
1.58e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 67.05 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE----ARPQPGI-------KIGYLPQEPQLnpeht 85
Cdd:TIGR00958 492 PDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQvlldGVPLVQYdhhylhrQVALVGQEPVL----- 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 86 VRESVEEavsevvNALKGLDEVyakyaePDADFDKLAAQQGKYEEIIQAHDGHNLNVqleraadalrlpdwDAKIANLSG 165
Cdd:TIGR00958 567 FSGSVRE------NIAYGLTDT------PDEEIMAAAKAANAHDFIMEFPNGYDTEV--------------GEKGSQLSG 620
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489953208 166 GERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEGTVVAITH 217
Cdd:TIGR00958 621 GQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
324-499 |
1.67e-11 |
|
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: 66.75 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQ--PDSGSI--------------------- 380
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 381 ---TLGETVKLASVD-------QFRD-------------AMDNSKTVWEEVSGGLDimrigNTEMPSRAYVGRFN--FKG 435
Cdd:TIGR03269 81 pcpVCGGTLEPEEVDfwnlsdkLRRRirkriaimlqrtfALYGDDTVLDNVLEALE-----EIGYEGKEAVGRAVdlIEM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489953208 436 TDQGKRVG----ELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIETLRALENALLEF---PGCAMVI-SH 499
Cdd:TIGR03269 156 VQLSHRIThiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkaSGISMVLtSH 227
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-477 |
1.88e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.49 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 1 MAQFVYTMHRVGKVVPPKRhILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI------DTDIEGEARP--------- 65
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVK-ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVyphgtyEGEIIFEGEElqasnirdt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 66 -QPGIKIGYlpQEPQLNPEHTVRESV---EEAVSevvNALKGLDEVYAKYaepdadfDKLAAQQgkyeeiiqahdghNLN 141
Cdd:PRK13549 80 eRAGIAIIH--QELALVKELSVLENIflgNEITP---GGIMDYDAMYLRA-------QKLLAQL-------------KLD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 142 VqleraadalrlpDWDAKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEGTVVA---ITHD 218
Cdd:PRK13549 135 I------------NPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIAciyISHK 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 219 ryfLDNV---AGWILELDRGEGIpwegnysswleqkDQRLAQEASQEAARRKSIEKELewvrqgakgrqskgkarlarfe 295
Cdd:PRK13549 203 ---LNEVkaiSDTICVIRDGRHI-------------GTRPAAGMTEDDIITMMVGREL---------------------- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 296 elnnteyqkrnetNELFIPPGARLGDKVVEVTNL---RKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGK----STLFRM 368
Cdd:PRK13549 245 -------------TALYPREPHTIGEVILEVRNLtawDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRtelvQCLFGA 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 369 MSGQEQpdsGSITL-GETVKLASVdqfRDAMDNSKTVWEE---VSGGLDIMRIG-NTEMPS------------------- 424
Cdd:PRK13549 312 YPGRWE---GEIFIdGKPVKIRNP---QQAIAQGIAMVPEdrkRDGIVPVMGVGkNITLAAldrftggsriddaaelkti 385
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 489953208 425 RAYVGRFNFKGTDQGKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDI 477
Cdd:PRK13549 386 LESIQRLKVKTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDV 438
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-477 |
1.96e-11 |
|
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: 66.39 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI------DTDI--EGEARPQPGIK------IGYLPQEPQLNPEHTVR 87
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVyphgtwDGEIywSGSPLKASNIRdteragIVIIHQELTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 88 EsveeavsevvNALKGlDEVyakyaepdadfdKLAAQQGKYEEIIqaHDGHNLNVQLERAADALRLPdwdakIANLSGGE 167
Cdd:TIGR02633 97 E----------NIFLG-NEI------------TLPGGRMAYNAMY--LRAKNLLRELQLDADNVTRP-----VGDYGGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 168 RRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEGTVVAITHDRYFLDNVAGWIlelDRGEGIpwegnyssw 247
Cdd:TIGR02633 147 QQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVC---DTICVI--------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 248 leqkdqRLAQEASQEAARRKSIEKELEWVrqgaKGRqskgkarlarfeelnnteyqkrnETNELFIPPGARLGDKVVEVT 327
Cdd:TIGR02633 215 ------RDGQHVATKDMSTMSEDDIITMM----VGR-----------------------EITSLYPHEPHEIGDVILEAR 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 328 NLRKSYGD---RVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSG-------------QEQPDSGSITLGETVKLASV 391
Cdd:TIGR02633 262 NLTCWDVInphRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGaypgkfegnvfinGKPVDIRNPAQAIRAGIAMV 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 392 --DQFRDAMDNSKTVWEEVS-GGLD----IMRIGN-TEMPS-RAYVGRFNFKGTDQGKRVGELSGGERGRLHLAKLLQVG 462
Cdd:TIGR02633 342 peDRKRHGIVPILGVGKNITlSVLKsfcfKMRIDAaAELQIiGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTN 421
|
490
....*....|....*
gi 489953208 463 GNVLLLDEPTNDLDI 477
Cdd:TIGR02633 422 PRVLILDEPTRGVDV 436
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
324-490 |
2.06e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 64.48 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGEtVKLASVDQFRDAMDNSK- 402
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGE-VRLFGRNIYSPDVDPIEv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 403 -----------------TVWEEVSGGLDIMRI--GNTEMPSRAyvgRFNFKGTDQGKRV--------GELSGGERGRLHL 455
Cdd:PRK14267 84 rrevgmvfqypnpfphlTIYDNVAIGVKLNGLvkSKKELDERV---EWALKKAALWDEVkdrlndypSNLSGGQRQRLVI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 489953208 456 AKLLQVGGNVLLLDEPTNDLDIETLRALENALLEF 490
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFEL 195
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
18-198 |
2.25e-11 |
|
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: 64.20 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGID----------------TDIEGEARPQPGIKIGYlpQEPQLN 81
Cdd:TIGR01978 12 DKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPsyevtsgtilfkgqdlLELEPDERARAGLFLAF--QYPEEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 82 PEHTVRESVEEAVSEVVNAlKGLDEVyakyaePDADFDKLAAQQGKYEEIIQAHDGHNLNVqleraadalrlpdwdakia 161
Cdd:TIGR01978 90 PGVSNLEFLRSALNARRSA-RGEEPL------DLLDFEKLLKEKLALLDMDEEFLNRSVNE------------------- 143
|
170 180 190
....*....|....*....|....*....|....*..
gi 489953208 162 NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESV 198
Cdd:TIGR01978 144 GFSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDAL 180
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
21-239 |
2.37e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 64.22 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE----------ARPQPG--------------IKIGYLPQ 76
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSivvngqtinlVRDKDGqlkvadknqlrllrTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 77 EPQLNPEHTVRESVEEAVSEVVNALKGLDEVYAKYAEPDADFDKlaAQQGKYEeiiqahdghnlnvqleraadalrlpdw 156
Cdd:PRK10619 100 HFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDE--RAQGKYP--------------------------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 157 dakiANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EG-TVVAITHDRYFLDNVAGWILELD 233
Cdd:PRK10619 151 ----VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLaeEGkTMVVVTHEMGFARHVSSHVIFLH 226
|
250
....*....|
gi 489953208 234 RG----EGIP 239
Cdd:PRK10619 227 QGkieeEGAP 236
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
333-485 |
2.51e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 64.75 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 333 YGDRVLIDdLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETV---------------KLASVDQFRDA 397
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVvsstskqkeikpvrkKVGVVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 398 MDNSKTVWEEVSGGLDIMRIGNTEMPSRAyVGRFNFKGTDQ---GKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTND 474
Cdd:PRK13643 96 QLFEETVLKDVAFGPQNFGIPKEKAEKIA-AEKLEMVGLADefwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170
....*....|....*
gi 489953208 475 LD----IETLRALEN 485
Cdd:PRK13643 175 LDpkarIEMMQLFES 189
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
323-487 |
2.76e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 64.26 E-value: 2.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 323 VVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMS----GQEQPDSGSITLGETVKLAS-------- 390
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSglitGDKSAGSHIELLGRTVQREGrlardirk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 391 --------VDQFRdaMDNSKTVWEEVSGGL--------DIMRIGNTEMPSRAY-----VGRFNFKgtdqGKRVGELSGGE 449
Cdd:PRK09984 84 srantgyiFQQFN--LVNRLSVLENVLIGAlgstpfwrTCFSWFTREQKQRALqaltrVGMVHFA----HQRVSTLSGGQ 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 489953208 450 RGRLHLAKLLQVGGNVLLLDEPTNDLDIETLRALENAL 487
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTL 195
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
324-500 |
3.09e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 65.05 E-value: 3.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETvKLASVDQ--------FR 395
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK-RMNDVPPaergvgmvFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 396 D-AMDNSKTVWEEVSGGLDIMRIGNTEMPSRA-YVGRFNFKGTDQGKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTN 473
Cdd:PRK11000 83 SyALYPHLSVAENMSFGLKLAGAKKEEINQRVnQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 489953208 474 DLD--------IETLRaLENALlefpGCAMV-ISHD 500
Cdd:PRK11000 163 NLDaalrvqmrIEISR-LHKRL----GRTMIyVTHD 193
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-243 |
3.31e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 63.57 E-value: 3.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 1 MAQFVYTMHRVGKVVppkrhILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQpGIKIgylpqepqL 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQ-----VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVD-GLKV--------N 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 81 NPEHTVRESVEEA--VSEVVN---ALKGLDEVYakyaepdadFDKLAAQ-QGKYEEIIQAHDghnLNVQLERAADALRLP 154
Cdd:PRK09493 67 DPKVDERLIRQEAgmVFQQFYlfpHLTALENVM---------FGPLRVRgASKEEAEKQARE---LLAKVGLAERAHHYP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 155 dwdakiANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EG-TVVAITHDRYFLDNVAGWILE 231
Cdd:PRK09493 135 ------SELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLaeEGmTMVIVTHEIGFAEKVASRLIF 208
|
250
....*....|..
gi 489953208 232 LDRGeGIPWEGN 243
Cdd:PRK09493 209 IDKG-RIAEDGD 219
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
25-218 |
3.35e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 63.80 E-value: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 25 ISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIdTDIEGEAR---------PQPGIKI--GYLPQE--PQLN---------- 81
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQfagqpleawSAAELARhrAYLSQQqtPPFAmpvfqyltlh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 82 -PEHTVRESVEEAVSEVVNALKgLDevyakyaepdadfDKLAAQqgkyeeiiqahdghnlnvqleraadalrlpdwdakI 160
Cdd:PRK03695 94 qPDKTRTEAVASALNEVAEALG-LD-------------DKLGRS-----------------------------------V 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489953208 161 ANLSGGERRRVALCRLLLE-----KPD--MLLLDEPTNHLDAESVAWLERFLHDFE---GTVVAITHD 218
Cdd:PRK03695 125 NQLSGGEWQRVRLAAVVLQvwpdiNPAgqLLLLDEPMNSLDVAQQAALDRLLSELCqqgIAVVMSSHD 192
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
343-489 |
5.15e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 62.68 E-value: 5.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 343 TFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQFRDAM---DNS----KTVWEEVSGGLD- 413
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLnGQDHTTTPPSRRPVSMlfqENNlfshLTVAQNIGLGLNp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 414 ------IMRIGNTEMPSRayVGRfnfkgTDQGKRV-GELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDietlRALENA 486
Cdd:PRK10771 99 glklnaAQREKLHAIARQ--MGI-----EDLLARLpGQLSGGQRQRVALARCLVREQPILLLDEPFSALD----PALRQE 167
|
...
gi 489953208 487 LLE 489
Cdd:PRK10771 168 MLT 170
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
21-236 |
5.55e-11 |
|
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: 62.04 E-value: 5.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 21 ILKNISLSFFPGAKIGVLGLNGAGKSTL----LRIMAGIDTDIEGEARPQPGI-------KIGYLPQEPQLNpEHTVRES 89
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLilalFRFLEAEEGKIEIDGIDISTIpledlrsSLTIIPQDPTLF-SGTIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 90 VEeavsevvnalkgldeVYAKYAEpdadfdklaaqqgkyEEIIQAhdghnlnvqLERAADALrlpdwdakiaNLSGGERR 169
Cdd:cd03369 102 LD---------------PFDEYSD---------------EEIYGA---------LRVSEGGL----------NLSQGQRQ 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489953208 170 RVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD-FEG-TVVAITHDryfLDNVAGW--ILELDRGE 236
Cdd:cd03369 133 LLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREeFTNsTILTIAHR---LRTIIDYdkILVMDAGE 200
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
323-383 |
6.26e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.15 E-value: 6.26e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489953208 323 VVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSIT-LG 383
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvLG 62
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-190 |
6.30e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 64.65 E-value: 6.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEAR----------PQPGIK--IGYLPQEPQ---LNPE 83
Cdd:COG1129 265 GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRldgkpvrirsPRDAIRagIAYVPEDRKgegLVLD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 84 HTVRESVEEAVSEVVNALKGLDEvyakyaepdadfdklAAQQGKYEEIIQAhdghnLNVqleraadalRLPDWDAKIANL 163
Cdd:COG1129 345 LSIRENITLASLDRLSRGGLLDR---------------RRERALAEEYIKR-----LRI---------KTPSPEQPVGNL 395
|
170 180
....*....|....*....|....*..
gi 489953208 164 SGGERRRVALCRLLLEKPDMLLLDEPT 190
Cdd:COG1129 396 SGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
22-275 |
7.81e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 63.08 E-value: 7.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 22 LKNISLSFFPGAKIGVLGLNGAGKSTL-------LR------IMAGIDTdieGEARPQPGIK--IGYLPQEPQlnpEHTV 86
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLalhlnglLRpqkgkvLVSGIDT---GDFSKLQGIRklVGIVFQNPE---TQFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 87 RESVEEAVSevvnalKGLDEVYAKYAEPDADFDKLAAQQG--KYEEiiqahdghnlnvqleraadalRLPDwdakiaNLS 164
Cdd:PRK13644 92 GRTVEEDLA------FGPENLCLPPIEIRKRVDRALAEIGleKYRH---------------------RSPK------TLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 165 GGERRRVALCRLLLEKPDMLLLDEPTNHLDAES-VAWLERF--LHDFEGTVVAITHDRYFLdNVAGWILELDRG----EG 237
Cdd:PRK13644 139 GGQGQCVALAGILTMEPECLIFDEVTSMLDPDSgIAVLERIkkLHEKGKTIVYITHNLEEL-HDADRIIVMDRGkivlEG 217
|
250 260 270
....*....|....*....|....*....|....*....
gi 489953208 238 IPweGNYSSWLEQKDQRLAQEASQEAARR-KSIEKELEW 275
Cdd:PRK13644 218 EP--ENVLSDVSLQTLGLTPPSLIELAENlKMHGVVIPW 254
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
18-217 |
8.07e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 62.49 E-value: 8.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDtdiegearpqpgikigylpqepQLNPEHTVRESVEeavsev 97
Cdd:PRK14239 17 KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMN----------------------DLNPEVTITGSIV------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 98 vnaLKGLDeVYAkyaePDADFDKLAAQQGK------------YEEIIQA------HDGHNLNVQLERAADALRLpdWD-- 157
Cdd:PRK14239 69 ---YNGHN-IYS----PRTDTVDLRKEIGMvfqqpnpfpmsiYENVVYGlrlkgiKDKQVLDEAVEKSLKGASI--WDev 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489953208 158 -----AKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEG--TVVAITH 217
Cdd:PRK14239 139 kdrlhDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDdyTMLLVTR 205
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
323-499 |
8.31e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 64.25 E-value: 8.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 323 VVEVTNLRKSY-GDRVLiDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSIT-LGETVKLASVDQFRDA--- 397
Cdd:PRK10762 4 LLQLKGIDKAFpGVKAL-SGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILyLGKEVTFNGPKSSQEAgig 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 398 -------MDNSKTVWEEVSGGLDIM----RIGNTEMPSRA--YVGRFNFKGTDQgKRVGELSGGERGRLHLAKLLQVGGN 464
Cdd:PRK10762 83 iihqelnLIPQLTIAENIFLGREFVnrfgRIDWKKMYAEAdkLLARLNLRFSSD-KLVGELSIGEQQMVEIAKVLSFESK 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 489953208 465 VLLLDEPTNDL-DIETlRALENAL--LEFPGCAMV-ISH 499
Cdd:PRK10762 162 VIIMDEPTDALtDTET-ESLFRVIreLKSQGRGIVyISH 199
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
329-520 |
9.09e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 62.78 E-value: 9.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 329 LRKSYGDRVLiDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSIT-LGETV-KLASVDQ----------FRD 396
Cdd:PRK10419 19 SGKHQHQTVL-NNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSwRGEPLaKLNRAQRkafrrdiqmvFQD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 397 ---AMDNSKTVWEEVSGGL-DIMRIGNTEMPSRA-----YVGrfnFKGTDQGKRVGELSGGERGRLHLAKLLQVGGNVLL 467
Cdd:PRK10419 98 sisAVNPRKTVREIIREPLrHLLSLDKAERLARAsemlrAVD---LDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489953208 468 LDEPTNDLDI----ETLRALENALLEFPGCAMVISHDRWFLDRIATHILdYQDEGKV 520
Cdd:PRK10419 175 LDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVM-VMDNGQI 230
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
320-511 |
9.74e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 62.37 E-value: 9.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 320 GDKVVEVTNLRKSY---GDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETVKLASVDQFR- 395
Cdd:PRK14246 4 GKSAEDVFNISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 396 DAMDNSK---TVWEEVSGGLDIMRIGNTEMPSRAY------------------VGRFNFKGTDQGKRVGELSGGERGRLH 454
Cdd:PRK14246 84 DAIKLRKevgMVFQQPNPFPHLSIYDNIAYPLKSHgikekreikkiveeclrkVGLWKEVYDRLNSPASQLSGGQQQRLT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489953208 455 LAKLLQVGGNVLLLDEPTNDLDIETLRALENALLEFPG--CAMVISHDRWFLDRIATHI 511
Cdd:PRK14246 164 IARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYV 222
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-236 |
9.83e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 62.72 E-value: 9.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIdtdiegeARPQPGikiGYLPQEPQLNPEHTVRESVEEAVSEVvna 100
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGL-------LRPQKG---AVLWQGKPLDYSKRGLLALRQQVATV--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 101 lkgldevyakYAEPDadfdklaaQQGKYEEIIQ--AHDGHNLNVQLE----RAADALRLPDWD----AKIANLSGGERRR 170
Cdd:PRK13638 83 ----------FQDPE--------QQIFYTDIDSdiAFSLRNLGVPEAeitrRVDEALTLVDAQhfrhQPIQCLSHGQKKR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489953208 171 VALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHdfEGTVVAI-THDRYFLDNVAGWILELDRGE 236
Cdd:PRK13638 145 VAIAGALVLQARYLLLDEPTAGLDpagrTQMIAIIRRIVA--QGNHVIIsSHDIDLIYEISDAVYVLRQGQ 213
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
341-476 |
1.04e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 62.73 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 341 DLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETV---------------KLASVDQFRDAMDNSKTVW 405
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVitagkknkklkplrkKVGIVFQFPEHQLFEETVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 406 EEVSGGldIMRIGNTEMPSRAyvgrfnfKGTDQGKRVG-----------ELSGGERGRLHLAKLLQVGGNVLLLDEPTND 474
Cdd:PRK13634 105 KDICFG--PMNFGVSEEDAKQ-------KAREMIELVGlpeellarspfELSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
..
gi 489953208 475 LD 476
Cdd:PRK13634 176 LD 177
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
21-218 |
1.10e-10 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 62.02 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE----------------ARpqpgiKIGYLPQEPQLNPEH 84
Cdd:COG4604 16 VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEvlvdgldvattpsrelAK-----RLAILRQENHINSRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 85 TVRESVEeavsevvnalkgldevyakyaepdadFDKLAAQQGKYEEIIQAHdghnlnvqLERAADALRLPDW-DAKIANL 163
Cdd:COG4604 91 TVRELVA--------------------------FGRFPYSKGRLTAEDREI--------IDEAIAYLDLEDLaDRYLDEL 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489953208 164 SGGERRRVALCRLLLEKPDMLLLDEPTNHLD-AESVAW---LERFLHDFEGTVVAITHD 218
Cdd:COG4604 137 SGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDmKHSVQMmklLRRLADELGKTVVIVLHD 195
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-246 |
1.12e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 64.10 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---------ID----TDIEGEARPQpgiKIGYLPQEPQLnPEHTVR 87
Cdd:PRK11174 365 LAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGflpyqgslkINgielRELDPESWRK---HLSWVGQNPQL-PHGTLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 88 ESVeeavsevvnALkgldevyakyAEPDADFDKL--AAQQGKYEEIIQAHDgHNLNVQL-ERAAdalrlpdwdakiaNLS 164
Cdd:PRK11174 441 DNV---------LL----------GNPDASDEQLqqALENAWVSEFLPLLP-QGLDTPIgDQAA-------------GLS 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 165 GGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD--FEGTVVAITHDryfLDNVAGW--ILELDRGEgIPW 240
Cdd:PRK11174 488 VGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAasRRQTTLMVTHQ---LEDLAQWdqIWVMQDGQ-IVQ 563
|
....*.
gi 489953208 241 EGNYSS 246
Cdd:PRK11174 564 QGDYAE 569
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
14-217 |
1.15e-10 |
|
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: 64.38 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 14 VVPPKRHILKNiSLSF-FP-GAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE-ARPQPGiKIGYLPQEPQLNpEHTVRESV 90
Cdd:TIGR00954 459 LVTPNGDVLIE-SLSFeVPsGNNLLICGPNGCGKSSLFRILGELWPVYGGRlTKPAKG-KLFYVPQRPYMT-LGTLRDQI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 91 eeavsevvnalkgldeVYakyaePDA--DFDKLAAQQGKYEEIIQAHDGHNLnVQLERAADALRlpDWdakIANLSGGER 168
Cdd:TIGR00954 536 ----------------IY-----PDSseDMKRRGLSDKDLEQILDNVQLTHI-LEREGGWSAVQ--DW---MDVLSGGEK 588
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489953208 169 RRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEGTVVAITH 217
Cdd:TIGR00954 589 QRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
325-512 |
1.15e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 62.01 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 325 EVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQE--QPDSGSITL-GETVKLASVDQfRD----- 396
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLdGEDILELSPDE-RAragif 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 397 -AMDNSktvwEEVSG--GLDIMR-----IGNTEMPSRAYVGRFNFKGTDQG------KR---VGeLSGGERGRLHLAKLL 459
Cdd:COG0396 81 lAFQYP----VEIPGvsVSNFLRtalnaRRGEELSAREFLKLLKEKMKELGldedflDRyvnEG-FSGGEKKRNEILQML 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489953208 460 QVGGNVLLLDEPTNDLDIETLRALENALLEF--PGCAM-VISHDRWFLDRIA---THIL 512
Cdd:COG0396 156 LLEPKLAILDETDSGLDIDALRIVAEGVNKLrsPDRGIlIITHYQRILDYIKpdfVHVL 214
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
18-225 |
1.17e-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: 61.00 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGID----------------TDIEGEARPQPGIKIGYlpQEPqln 81
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyevtegeilfkgediTDLPPEERARLGIFLAF--QYP--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 82 pehtvresveEAVSEVVNA--LKGLDEvyakyaepdadfdklaaqqgkyeeiiqahdghnlnvqleraadalrlpdwdak 159
Cdd:cd03217 87 ----------PEIPGVKNAdfLRYVNE----------------------------------------------------- 103
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489953208 160 iaNLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERF---LHDFEGTVVAITHDRYFLDNV 225
Cdd:cd03217 104 --GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVinkLREEGKSVLIITHYQRLLDYI 170
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
324-522 |
1.20e-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: 61.36 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSY---GDRVLiDDLTFSVPKGAIVGIIGPNGAGKST----LFRMMsgqeQPDSGSITLGEtVKLASVD--QF 394
Cdd:cd03244 3 IEFKNVSLRYrpnLPPVL-KNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILIDG-VDISKIGlhDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 395 RDAMD-----------------------------------NSKTVWEEVSGGLDiMRIgntempsrayvgrfnfkgTDQG 439
Cdd:cd03244 77 RSRISiipqdpvlfsgtirsnldpfgeysdeelwqalervGLKEFVESLPGGLD-TVV------------------EEGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 440 KrvgELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIETLRALENAL-LEFPGCAMV-ISHdrwfldRIAThILDYQ-- 515
Cdd:cd03244 138 E---NLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIrEAFKDCTVLtIAH------RLDT-IIDSDri 207
|
250
....*....|.
gi 489953208 516 ---DEGKV-EF 522
Cdd:cd03244 208 lvlDKGRVvEF 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
22-218 |
1.38e-10 |
|
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: 62.28 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDI----EGEARPQPGIKIGYLPQEPQLNPEHTV 86
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLieptsgkvlidGQDIaamsRKELRELRRKKISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 87 REsveeavsevvNALKGLDevyakyaepdadfdklaaqqgkyeeiIQahdGHNLNVQLERAADALR---LPDW-DAKIAN 162
Cdd:cd03294 120 LE----------NVAFGLE--------------------------VQ---GVPRAEREERAAEALElvgLEGWeHKYPDE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 163 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDFEGTVVAITHD 218
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDplirREMQDELLRLQAELQKTIVFITHD 220
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
321-476 |
1.38e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 62.08 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 321 DKVVEVTNLRKSY-GDRVL-IDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGEtvKLASVDQFRDAM 398
Cdd:PRK13648 5 NSIIVFKNVSFQYqSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNN--QAITDDNFEKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 399 ----------DNS---KTVWEEVSGGLDIMRIGNTEMPSRAYVGRFNFKGTDQGK-RVGELSGGERGRLHLAKLLQVGGN 464
Cdd:PRK13648 83 khigivfqnpDNQfvgSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADyEPNALSGGQKQRVAIAGVLALNPS 162
|
170
....*....|..
gi 489953208 465 VLLLDEPTNDLD 476
Cdd:PRK13648 163 VIILDEATSMLD 174
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
22-236 |
1.39e-10 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 62.32 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 22 LKNISLSFFPGAKIGVL-GLNGAGKSTLLRIMA----GIDTDIEGEARPQPGIKIGYLPQEPQL----NPEHTVRESVEE 92
Cdd:COG3950 14 FEDLEIDFDNPPRLTVLvGENGSGKTTLLEAIAlalsGLLSRLDDVKFRKLLIRNGEFGDSAKLilyyGTSRLLLDGPLK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 93 AVSEVVNALKGLDEVYAKYAEPDADFDKLAAQQGKYEEIIQAHDGHNLNVQLERAADALR--LPDWDA------------ 158
Cdd:COG3950 94 KLERLKEEYFSRLDGYDSLLDEDSNLREFLEWLREYLEDLENKLSDELDEKLEAVREALNklLPDFKDiridrdpgrlvi 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 159 --------KIANLSGGERRRVALC-----RLLLEKPDM---------LLLDEPTNHLdaeSVAWLERFLHDFEGT----- 211
Cdd:COG3950 174 ldkngeelPLNQLSDGERSLLALVgdlarRLAELNPALenplegegiVLIDEIDLHL---HPKWQRRILPDLRKIfpniq 250
|
250 260
....*....|....*....|....*.
gi 489953208 212 VVAITHDRYFLDNV-AGWILELDRGE 236
Cdd:COG3950 251 FIVTTHSPLILSSLeDEEVIVLERDE 276
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
19-198 |
1.40e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 61.83 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIE---GEARPQPGikIGYLPQEPQLnpeh 84
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIvprdagniiidDEDISllpLHARARRG--IGYLPQEASI---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 85 TVRESVEEAVSEVVNALKGLDEvyakyaepdadfdklAAQQGKYEEIIQAHDGHNLNVQLERAadalrlpdwdakianLS 164
Cdd:PRK10895 90 FRRLSVYDNLMAVLQIRDDLSA---------------EQREDRANELMEEFHIEHLRDSMGQS---------------LS 139
|
170 180 190
....*....|....*....|....*....|....
gi 489953208 165 GGERRRVALCRLLLEKPDMLLLDEPTNHLDAESV 198
Cdd:PRK10895 140 GGERRRVEIARALAANPKFILLDEPFAGVDPISV 173
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
336-483 |
1.44e-10 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 61.73 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 336 RVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSItLGETVKLASVDQ----------FRDAMDNSKTVW 405
Cdd:cd03252 15 PVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRV-LVDGHDLALADPawlrrqvgvvLQENVLFNRSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 406 EEVSggldimrIGNTEMPSRAYV------GRFNF-----KGTDQ--GKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPT 472
Cdd:cd03252 94 DNIA-------LADPGMSMERVIeaaklaGAHDFiselpEGYDTivGEQGAGLSGGQRQRIAIARALIHNPRILIFDEAT 166
|
170
....*....|.
gi 489953208 473 NDLDIETLRAL 483
Cdd:cd03252 167 SALDYESEHAI 177
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
324-476 |
1.52e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 62.37 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYG-----DRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL------GETVKLAS-- 390
Cdd:PRK13637 3 IKIENLTHIYMegtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIdgvditDKKVKLSDir 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 391 -----VDQFRDAMDNSKTVWEEVSGGLDIMRIGNTEMPSRAYVGrFNFKGTD----QGKRVGELSGGERGRLHLAKLLQV 461
Cdd:PRK13637 83 kkvglVFQYPEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRA-MNIVGLDyedyKDKSPFELSGGQKRRVAIAGVVAM 161
|
170
....*....|....*
gi 489953208 462 GGNVLLLDEPTNDLD 476
Cdd:PRK13637 162 EPKILILDEPTAGLD 176
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
21-194 |
1.89e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 62.66 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQpGIKIGYLPQEPQ----------LNPEHTVRESV 90
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLD-GQDITHVPAENRhvntvfqsyaLFPHMTVFENV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 91 -----------EEAVSEVVNALKgldevyakyaepdadfdklaaqqgkyeeiiqahdghnlNVQLERAADAlrlpdwdaK 159
Cdd:PRK09452 108 afglrmqktpaAEITPRVMEALR--------------------------------------MVQLEEFAQR--------K 141
|
170 180 190
....*....|....*....|....*....|....*
gi 489953208 160 IANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 194
Cdd:PRK09452 142 PHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
327-507 |
1.97e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 60.98 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 327 TNLRKSYGD-RVLID---DLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSI--------TLGETVK------- 387
Cdd:PRK11629 9 DNLCKRYQEgSVQTDvlhNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifngqpmsKLSSAAKaelrnqk 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 388 LASVDQFRDAMDNSkTVWEEVSGGLDIMRIGNTEMPSRAY-----VG---RFNfkgtdqgKRVGELSGGERGRLHLAKLL 459
Cdd:PRK11629 89 LGFIYQFHHLLPDF-TALENVAMPLLIGKKKPAEINSRALemlaaVGlehRAN-------HRPSELSGGERQRVAIARAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489953208 460 QVGGNVLLLDEPTNDLDIETLRALENALLEF---PGCA-MVISHDRWFLDRI 507
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELnrlQGTAfLVVTHDLQLAKRM 212
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
325-532 |
1.98e-10 |
|
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: 61.12 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 325 EVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQE--QPDSGSITLGETVKLA------------- 389
Cdd:TIGR01978 2 KIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPsyEVTSGTILFKGQDLLElepderaraglfl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 390 -----------SVDQFRDAMDNSKTVwEEVSGGLDIMRIgNTEMPSRAYVGRFNFKGTDQGKRVGeLSGGERGRLHLAKL 458
Cdd:TIGR01978 82 afqypeeipgvSNLEFLRSALNARRS-ARGEEPLDLLDF-EKLLKEKLALLDMDEEFLNRSVNEG-FSGGEKKRNEILQM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 459 LQVGGNVLLLDEPTNDLDIETLRALENALLEF--PGCAM-VISHDRWFLDRIA---THILdyqDEGKVeFFEGNFTEYEE 532
Cdd:TIGR01978 159 ALLEPKLAILDEIDSGLDIDALKIVAEGINRLrePDRSFlIITHYQRLLNYIKpdyVHVL---LDGRI-VKSGDVELAKE 234
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-194 |
2.16e-10 |
|
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: 63.78 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRImagidtdIEGEARPQPG-IK----IGYLPQEPQLNPeHTVREsveeavs 95
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMM-------IMGELEPSEGkIKhsgrISFSPQTSWIMP-GTIKD------- 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 96 evvNALKGLDevYAKYaepdadfdklaaqqgKYEEIIQAhdghnlnVQLERaaDALRLPDWDAKI-----ANLSGGERRR 170
Cdd:TIGR01271 506 ---NIIFGLS--YDEY---------------RYTSVIKA-------CQLEE--DIALFPEKDKTVlgeggITLSGGQRAR 556
|
170 180
....*....|....*....|....
gi 489953208 171 VALCRLLLEKPDMLLLDEPTNHLD 194
Cdd:TIGR01271 557 ISLARAVYKDADLYLLDSPFTHLD 580
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
321-489 |
2.22e-10 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 61.21 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 321 DKVVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLF----RMmsGQEQPD---SGSITL-GETVKLASVD 392
Cdd:COG1117 9 EPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLrclnRM--NDLIPGarvEGEILLdGEDIYDPDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 393 Q----------------------------FRDAMDNSKTV--------------WEEVSGGLDimrigntempsrayvgr 430
Cdd:COG1117 87 VvelrrrvgmvfqkpnpfpksiydnvaygLRLHGIKSKSEldeiveeslrkaalWDEVKDRLK----------------- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 431 fnfkgtdqgKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLD-IETLRaLENALLE 489
Cdd:COG1117 150 ---------KSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpISTAK-IEELILE 199
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
346-511 |
2.38e-10 |
|
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: 63.26 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 346 VPK-GAIVGIIGPNGAGKSTLFRMMSGQEQPDsgsitLGETVKLASVDQ-------------FRDAMDNSKTVweevsgg 411
Cdd:COG1245 95 VPKkGKVTGILGPNGIGKSTALKILSGELKPN-----LGDYDEEPSWDEvlkrfrgtelqdyFKKLANGEIKV------- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 412 ldIMRIGNTEMPSRAYVGRFN--FKGTDQ-----------------GKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPT 472
Cdd:COG1245 163 --AHKPQYVDLIPKVFKGTVRelLEKVDErgkldelaeklglenilDRDISELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489953208 473 NDLDI-ETLRA--LENALLEFPGCAMVISHDRWFLDRIATHI 511
Cdd:COG1245 241 SYLDIyQRLNVarLIRELAEEGKYVLVVEHDLAILDYLADYV 282
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
22-218 |
2.48e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 61.25 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQpGIKIGYlPQEPQLNpehtVRESVeeavsevvnal 101
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIK-GEPIKY-DKKSLLE----VRKTV----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 102 kGL------DEVYAKYAEPDADFDKLaaQQGKYEEIIQahdghnlnvqlERAADALR---LPDWDAKIAN-LSGGERRRV 171
Cdd:PRK13639 81 -GIvfqnpdDQLFAPTVEEDVAFGPL--NLGLSKEEVE-----------KRVKEALKavgMEGFENKPPHhLSGGQKKRV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489953208 172 ALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EG-TVVAITHD 218
Cdd:PRK13639 147 AIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnkEGiTIIISTHD 196
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
314-487 |
2.53e-10 |
|
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: 62.92 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 314 PPGAR---LGDKVVEVTNLRKSY-GDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLG----ET 385
Cdd:COG5265 345 APDAPplvVGGGEVRFENVSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDgqdiRD 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 386 VKLAS-------VDQ----FRDamdnskTVWEEVSGGldimRIGNTE-----MPSRAYVGRFnFKGTDQG--KRVGE--- 444
Cdd:COG5265 425 VTQASlraaigiVPQdtvlFND------TIAYNIAYG----RPDASEeeveaAARAAQIHDF-IESLPDGydTRVGErgl 493
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489953208 445 -LSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIETLRALENAL 487
Cdd:COG5265 494 kLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAAL 537
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-218 |
2.58e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 61.26 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG----------ID-TDIEGEARPQPGIKIGYLPQEPQLN--PEHT 85
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGslppdsgsilIDgKDVTKLPEYKRAKYIGRVFQDPMMGtaPSMT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 86 VREsveeavsevvNALkgldevyakyaepdadfdkLAAQQGK---------------YEEIIQAhdghnLNVQLERaada 150
Cdd:COG1101 99 IEE----------NLA-------------------LAYRRGKrrglrrgltkkrrelFRELLAT-----LGLGLEN---- 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489953208 151 lRLpdwDAKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD---AESVAWL-ERFLHDFEGTVVAITHD 218
Cdd:COG1101 141 -RL---DTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDpktAALVLELtEKIVEENNLTTLMVTHN 208
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
321-509 |
2.64e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 61.26 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 321 DKVVEVTNLRKSY---GDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQFRD 396
Cdd:PRK13642 2 NKILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIdGELLTAENVWNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 397 AM-------DNS---KTVWEEVSGGLDIMRIGNTEMPSRA-----YVGRFNFKGTDQGKrvgeLSGGERGRLHLAKLLQV 461
Cdd:PRK13642 82 KIgmvfqnpDNQfvgATVEDDVAFGMENQGIPREEMIKRVdeallAVNMLDFKTREPAR----LSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489953208 462 GGNVLLLDEPTNDLD----IETLRALENALLEFPGCAMVISHDrwfLDRIAT 509
Cdd:PRK13642 158 RPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHD---LDEAAS 206
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
339-522 |
2.79e-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: 59.64 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 339 IDDLTFSVPKGAIVGIIGPNGAGKSTLFR---MMSGQEQPDSGSITLGETvKLASVDQFRDAMDNsktvweevsgGLDIM 415
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNeglYASGKARLISFLPKFSRN-KLIFIDQLQFLIDV----------GLGYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 416 RIGNtEMPSrayvgrfnfkgtdqgkrvgeLSGGERGRLHLAKLLQVG--GNVLLLDEPTNDLDIETLRALENALLEFPGC 493
Cdd:cd03238 80 TLGQ-KLST--------------------LSGGELQRVKLASELFSEppGTLFILDEPSTGLHQQDINQLLEVIKGLIDL 138
|
170 180 190
....*....|....*....|....*....|....*..
gi 489953208 494 A---MVISHDRWFLDRiATHILDY-----QDEGKVEF 522
Cdd:cd03238 139 GntvILIEHNLDVLSS-ADWIIDFgpgsgKSGGKVVF 174
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
21-194 |
3.99e-10 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 61.03 E-value: 3.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRImagidtdIEGEARPQPGI-----KIGYLPQEPQLNPeHTVRESVEEAVS 95
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLML-------ILGELEPSEGKikhsgRISFSSQFSWIMP-GTIKENIIFGVS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 96 evvnalkgldevYAKYaepdadfdklaaqqgKYEEIIQAhdghnlnVQLERaaDALRLPDWDAKI-----ANLSGGERRR 170
Cdd:cd03291 124 ------------YDEY---------------RYKSVVKA-------CQLEE--DITKFPEKDNTVlgeggITLSGGQRAR 167
|
170 180
....*....|....*....|....
gi 489953208 171 VALCRLLLEKPDMLLLDEPTNHLD 194
Cdd:cd03291 168 ISLARAVYKDADLYLLDSPFGYLD 191
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
21-235 |
6.54e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 59.76 E-value: 6.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDT---------DIEGEA----RPQPGI------KIGYLPQEPQLN 81
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQpeagtirvgDITIDTarslSQQKGLirqlrqHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 82 PEHTVRESVEEAVSEVvnalKGldevyakyaEPDADFDKLAaqqgkyEEIIQahdghnlNVQLERAADALrlPdwdakiA 161
Cdd:PRK11264 98 PHRTVLENIIEGPVIV----KG---------EPKEEATARA------RELLA-------KVGLAGKETSY--P------R 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489953208 162 NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLE---RFLHDFEGTVVAITHDRYFLDNVAGWILELDRG 235
Cdd:PRK11264 144 RLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLntiRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQG 220
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
328-484 |
8.21e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 59.72 E-value: 8.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 328 NLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETVKLA-SVDQFRDAMDNSKTVwe 406
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGrSIFNYRDVLEFRRRV-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 407 evsgGLDIMR--------IGNTEMPSRAY--VGRFNFKGTDQGK--RVG--------------ELSGGERGRLHLAKLLQ 460
Cdd:PRK14271 104 ----GMLFQRpnpfpmsiMDNVLAGVRAHklVPRKEFRGVAQARltEVGlwdavkdrlsdspfRLSGGQQQLLCLARTLA 179
|
170 180
....*....|....*....|....
gi 489953208 461 VGGNVLLLDEPTNDLDIETLRALE 484
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIE 203
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
324-520 |
1.01e-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: 58.58 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDRV--LIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLgetvklasvdqfrDAMDNS 401
Cdd:cd03369 7 IEVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEI-------------DGIDIS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 402 KTVWEEVSGGLDIMRIGNTEMPS--RAYVGRFNFKGTDQ---GKRVGE----LSGGERGRLHLAKLLQVGGNVLLLDEPT 472
Cdd:cd03369 74 TIPLEDLRSSLTIIPQDPTLFSGtiRSNLDPFDEYSDEEiygALRVSEgglnLSQGQRQLLCLARALLKRPRVLVLDEAT 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489953208 473 NDLDIETLRALENALLE-FPGCAMV-ISHdrwfldRIAThILDYQ-----DEGKV 520
Cdd:cd03369 154 ASIDYATDALIQKTIREeFTNSTILtIAH------RLRT-IIDYDkilvmDAGEV 201
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
22-218 |
1.26e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 59.34 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARpqpgikigylpqepqLNPEHTVRESVEEAVSEVVNAL 101
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVK---------------IDGELLTAENVWNLRRKIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 102 KGLDEVY-AKYAEPDADFDkLAAQQGKYEEIIQahdghnlnvQLERAADALRLPDWDAK-IANLSGGERRRVALCRLLLE 179
Cdd:PRK13642 88 QNPDNQFvGATVEDDVAFG-MENQGIPREEMIK---------RVDEALLAVNMLDFKTRePARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489953208 180 KPDMLLLDEPTNHLDAESVAWLERFLHDFEG----TVVAITHD 218
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIHEIKEkyqlTVLSITHD 200
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
17-218 |
1.27e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 58.94 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDT------DIEGEARPQPGIKIGYLPQEPQLNPEHTVRESV 90
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPyqhgsiTLDGKPVEGPGAERGVVFQNEGLLPWRNVQDNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 91 EeavsevvnalkgldevyakyaepdadFDKLAAQQGKYEeiiqahdghnlnvQLERAADALRLPDWDA----KIANLSGG 166
Cdd:PRK11248 92 A--------------------------FGLQLAGVEKMQ-------------RLEIAHQMLKKVGLEGaekrYIWQLSGG 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489953208 167 ERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFL----HDFEGTVVAITHD 218
Cdd:PRK11248 133 QRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLlklwQETGKQVLLITHD 188
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
329-517 |
1.30e-09 |
|
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: 57.58 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 329 LRKSYGD-RVLIDDLTFSvpKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLgETVKLASVDQFRDamdnsktvwee 407
Cdd:cd03222 6 CVKRYGVfFLLVELGVVK--EGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW-DGITPVYKPQYID----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 408 vsggldimrigntempsrayvgrfnfkgtdqgkrvgeLSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIE----TLRAL 483
Cdd:cd03222 72 -------------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnAARAI 114
|
170 180 190
....*....|....*....|....*....|....
gi 489953208 484 ENALLEFPGCAMVISHDRWFLDRIATHILDYQDE 517
Cdd:cd03222 115 RRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
10-219 |
1.70e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 59.73 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 10 RVGKVVppkrhILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEarpqpgIKIgylpqepqlNPEHTVRES 89
Cdd:PRK11432 15 RFGSNT-----VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQ------IFI---------DGEDVTHRS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 90 VEEavsevvnalKGLDEVYAKYAepdadfdkLAAQQGKYEEIiqahdGHNLNVQ-------LERAADALRLPDW----DA 158
Cdd:PRK11432 75 IQQ---------RDICMVFQSYA--------LFPHMSLGENV-----GYGLKMLgvpkeerKQRVKEALELVDLagfeDR 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489953208 159 KIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAEsvawLERFLHD--------FEGTVVAITHDR 219
Cdd:PRK11432 133 YVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDAN----LRRSMREkirelqqqFNITSLYVTHDQ 197
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
21-219 |
1.85e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 58.19 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQpGIKIGYLPQEpqlnpehTVRESVEEAVSevVNA 100
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFE-GEDISTLKPE-------IYRQQVSYCAQ--TPT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 101 LKGlDEVYAKYAEPdadfdklaaqqgkYEEIIQAHDGHNLNVQLERaadaLRLPD--WDAKIANLSGGERRRVALCRLLL 178
Cdd:PRK10247 92 LFG-DTVYDNLIFP-------------WQIRNQQPDPAIFLDDLER----FALPDtiLTKNIAELSGGEKQRISLIRNLQ 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489953208 179 EKPDMLLLDEPTNHLDAESVAWLERFLH----DFEGTVVAITHDR 219
Cdd:PRK10247 154 FMPKVLLLDEITSALDESNKHNVNEIIHryvrEQNIAVLWVTHDK 198
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
339-499 |
1.88e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 60.42 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 339 IDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETV---KLAS-------VDQ----FRDAMDNSKT 403
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLdGHDLrdyTLASlrnqvalVSQnvhlFNDTIANNIA 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 404 -VWEEVSGGLDIMRIGntEMpsrAYVGRFnFKGTDQG--KRVGE----LSGGERGRLHLAKLLQVGGNVLLLDEPTNDLD 476
Cdd:PRK11176 439 yARTEQYSREQIEEAA--RM---AYAMDF-INKMDNGldTVIGEngvlLSGGQRQRIAIARALLRDSPILILDEATSALD 512
|
170 180
....*....|....*....|....*
gi 489953208 477 IETLRALENALLEFPG--CAMVISH 499
Cdd:PRK11176 513 TESERAIQAALDELQKnrTSLVIAH 537
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-218 |
1.98e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 59.33 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEAR-----PQP---------GIKIGylpQEPQLNPEHTVR 87
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvlgyvPFKrrkefarriGVVFG---QRSQLWWDLPAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 88 ESVEeavsevVNAlkgldevyAKYAEPDADFDKlaaqqgkyeeiiqahdghnlnvQLERAADALRLPD-WDAKIANLSGG 166
Cdd:COG4586 115 DSFR------LLK--------AIYRIPDAEYKK----------------------RLDELVELLDLGElLDTPVRQLSLG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489953208 167 ERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD----FEGTVVAITHD 218
Cdd:COG4586 159 QRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEynreRGTTILLTSHD 214
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
337-522 |
2.08e-09 |
|
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: 60.15 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 337 VLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETVKLASVDQfRDAMDNsKTVWEEV---SGGLD 413
Cdd:TIGR00954 466 VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQ-RPYMTL-GTLRDQIiypDSSED 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 414 IMRIGNTEMPSRAYVGrfNFKGTDQGKRVG----------ELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIETLRAL 483
Cdd:TIGR00954 544 MKRRGLSDKDLEQILD--NVQLTHILEREGgwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYM 621
|
170 180 190
....*....|....*....|....*....|....*....
gi 489953208 484 ENALLEFPGCAMVISHdRWFLDRIATHILDYQDEGKVEF 522
Cdd:TIGR00954 622 YRLCREFGITLFSVSH-RKSLWKYHEYLLYMDGRGGYQF 659
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
18-197 |
2.09e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 60.28 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-------IDTDIEGEARPQPGI--KIGYLPQEPQLNPEHTVRE 88
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGriqgnnfTGTILANNRKPTKQIlkRTGFVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 89 SVeeavseVVNALKGLDEVYAKYaepdadfDKLAAQQGKYEEIIQAHDGHNLNvqleraadalrlpdWDAKIANLSGGER 168
Cdd:PLN03211 160 TL------VFCSLLRLPKSLTKQ-------EKILVAESVISELGLTKCENTII--------------GNSFIRGISGGER 212
|
170 180
....*....|....*....|....*....
gi 489953208 169 RRVALCRLLLEKPDMLLLDEPTNHLDAES 197
Cdd:PLN03211 213 KRVSIAHEMLINPSLLILDEPTSGLDATA 241
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
19-194 |
2.12e-09 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 60.14 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEGEARPQPGIKIGYLPQEPQL------- 80
Cdd:TIGR01193 487 SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFfqarsgeillnGFSLKDIDRHTLRQFINYLPQEPYIfsgsile 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 81 -----NPEHTVRESVEEAVSevvnalkgldevyakYAEPDADFDKLaaQQGkYEEIIQAHDGhnlnvqleraadalrlpd 155
Cdd:TIGR01193 567 nlllgAKENVSQDEIWAACE---------------IAEIKDDIENM--PLG-YQTELSEEGS------------------ 610
|
170 180 190
....*....|....*....|....*....|....*....
gi 489953208 156 wdakiaNLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 194
Cdd:TIGR01193 611 ------SISGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
322-384 |
2.24e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 58.46 E-value: 2.24e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489953208 322 KVVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGE 384
Cdd:PRK11300 4 PLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRG 66
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
19-235 |
2.45e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 57.58 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE------------ARPQPGIK--IGYLPQEPQLNPEH 84
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKiwfsghditrlkNREVPFLRrqIGMIFQDHHLLMDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 85 TVRESVeeavsevvnalkgldevyakyAEPdadfdklaaqqgkyeEIIQAHDGHNLNVQLERAADALRLPDwdaKIAN-- 162
Cdd:PRK10908 95 TVYDNV---------------------AIP---------------LIIAGASGDDIRRRVSAALDKVGLLD---KAKNfp 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489953208 163 --LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEG---TVVAITHDRYFLDNVAGWILELDRG 235
Cdd:PRK10908 136 iqLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
346-512 |
3.19e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.44 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 346 VPK-GAIVGIIGPNGAGKSTLFRMMSGQEQPDsgsitLGETVKLASVDQ-------------FRDAMDNSKTVweevsgg 411
Cdd:PRK13409 95 IPKeGKVTGILGPNGIGKTTAVKILSGELIPN-----LGDYEEEPSWDEvlkrfrgtelqnyFKKLYNGEIKV------- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 412 ldIMRIGNTEMPSRAYVGRFN--FKGTDQ-----------------GKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPT 472
Cdd:PRK13409 163 --VHKPQYVDLIPKVFKGKVRelLKKVDErgkldevverlglenilDRDISELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489953208 473 NDLDI-ETLRAlENALLEF-PGCA-MVISHDRWFLDRIA--THIL 512
Cdd:PRK13409 241 SYLDIrQRLNV-ARLIRELaEGKYvLVVEHDLAVLDYLAdnVHIA 284
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
326-501 |
3.54e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 59.92 E-value: 3.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 326 VTNLRKSY--GDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTL----FRMMS--GQEQPDS---GSITLGETVKLASV--- 391
Cdd:TIGR01271 1220 VQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLlsalLRLLSteGEIQIDGvswNSVTLQTWRKAFGVipq 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 392 ------DQFRDAMD-----NSKTVW---EEVsgGLDIMrigntempSRAYVGRFNFKGTDQGKRvgeLSGGERGRLHLAK 457
Cdd:TIGR01271 1300 kvfifsGTFRKNLDpyeqwSDEEIWkvaEEV--GLKSV--------IEQFPDKLDFVLVDGGYV---LSNGHKQLMCLAR 1366
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489953208 458 LLQVGGNVLLLDEPTNDLDIETLRALENALLE-FPGCAMVISHDR 501
Cdd:TIGR01271 1367 SILSKAKILLLDEPSAHLDPVTLQIIRKTLKQsFSNCTVILSEHR 1411
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
339-476 |
5.01e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 57.53 E-value: 5.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 339 IDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETV--------------KLASVDQFRDAMDNSKT 403
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIaGYHItpetgnknlkklrkKVSLVFQFPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 404 VWEEVSGGldIMRIGNTEMPSRAyvgrfnfKGTDQGKRVG-----------ELSGGERGRLHLAKLLQVGGNVLLLDEPT 472
Cdd:PRK13641 103 VLKDVEFG--PKNFGFSEDEAKE-------KALKWLKKVGlsedliskspfELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
....
gi 489953208 473 NDLD 476
Cdd:PRK13641 174 AGLD 177
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-200 |
5.42e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 59.35 E-value: 5.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTD--IEGEARPQPGIK--------IGYLPQEPQLNPEHTVR 87
Cdd:TIGR00956 775 KRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgvITGGDRLVNGRPldssfqrsIGYVQQQDLHLPTSTVR 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 88 ESVEeavsevvnalkgldevYAKYAEPDADFDKlaAQQGKY-EEIIQAhdghnlnVQLERAADAL-RLPDwdakiANLSG 165
Cdd:TIGR00956 855 ESLR----------------FSAYLRQPKSVSK--SEKMEYvEEVIKL-------LEMESYADAVvGVPG-----EGLNV 904
|
170 180 190
....*....|....*....|....*....|....*.
gi 489953208 166 GERRRVALCRLLLEKPDMLL-LDEPTNHLDAESvAW 200
Cdd:TIGR00956 905 EQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQT-AW 939
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
11-218 |
5.48e-09 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 57.78 E-value: 5.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 11 VGKVVPPKR---HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG----------ID-TDIEG-------EARPqpgi 69
Cdd:COG1135 7 LSKTFPTKGgpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLlerptsgsvlVDgVDLTAlserelrAARR---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 70 KIGYLPQEPQLNPEHTVRESVEEAvsevvnaLKgldevYAKYaepdadfDKlAAQQGKYEEIIQahdghnLnVQLERAAD 149
Cdd:COG1135 83 KIGMIFQHFNLLSSRTVAENVALP-------LE-----IAGV-------PK-AEIRKRVAELLE------L-VGLSDKAD 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489953208 150 ALrlPdwdakiANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE---SVAWLERFLHDFEG-TVVAITHD 218
Cdd:COG1135 136 AY--P------SQLSGGQKQRVGIARALANNPKVLLCDEATSALDPEttrSILDLLKDINRELGlTIVLITHE 200
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
323-499 |
6.27e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.40 E-value: 6.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 323 VVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQeQPD---SGSITL-GETVKLASVdqfRD-- 396
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFeGEELQASNI---RDte 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 397 -----------AMDNSKTVWEEVSGGLDIMRIGNT---EMPSRAY--VGRFNFkGTDQGKRVGELSGGERGRLHLAKLLQ 460
Cdd:PRK13549 81 ragiaiihqelALVKELSVLENIFLGNEITPGGIMdydAMYLRAQklLAQLKL-DINPATPVGNLGLGQQQLVEIAKALN 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489953208 461 VGGNVLLLDEPTNDL---DIETLRALENALLEfPGCAMV-ISH 499
Cdd:PRK13549 160 KQARLLILDEPTASLtesETAVLLDIIRDLKA-HGIACIyISH 201
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
16-218 |
7.01e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 56.92 E-value: 7.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEGEARPQPGIKIGYLPQepqlNPEH 84
Cdd:PRK13632 19 NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLlkpqsgeikidGITISKENLKEIRKKIGIIFQ----NPDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 85 T-VRESVEEAVSevvnalKGLDEVYAKYAEPDADFDKLAAQqgkyeeiiqahdghnlnVQLERAADalRLPDwdakiaNL 163
Cdd:PRK13632 95 QfIGATVEDDIA------FGLENKKVPPKKMKDIIDDLAKK-----------------VGMEDYLD--KEPQ------NL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489953208 164 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEG----TVVAITHD 218
Cdd:PRK13632 144 SGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrkkTLISITHD 202
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
314-489 |
7.38e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 57.55 E-value: 7.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 314 PPGARLGDKVVEVTNLRKSYGDR-----VLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETV-- 386
Cdd:PRK13631 12 VPNPLSDDIILRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYig 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 387 ------------------------KLAS-VDQFRDAMDNSKTVWEEVSGGLDIMRIGNTEMPSRA--YVGRFNFKGTDQG 439
Cdd:PRK13631 92 dkknnhelitnpyskkiknfkelrRRVSmVFQFPEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAkfYLNKMGLDDSYLE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489953208 440 KRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIETLRALENALLE 489
Cdd:PRK13631 172 RSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD 221
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-240 |
7.57e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 56.46 E-value: 7.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----DTDIEGEArpqpgikigYLP-QEPQLNPEHTVRESVEeAV 94
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEV---------YLDgQDIFKMDVIELRRRVQ-MV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 95 SEVVNALKGLdEVYAKYAEpDADFDKLAAQQGKYEEIIQAhdghnlnvQLERAADALRLPD-WDAKIANLSGGERRRVAL 173
Cdd:PRK14247 88 FQIPNPIPNL-SIFENVAL-GLKLNRLVKSKKELQERVRW--------ALEKAQLWDEVKDrLDAPAGKLSGGQQQRLCI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489953208 174 CRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EGTVVAITHDRYFLDNVAGWILELDRGEGIPW 240
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELkkDMTIVLVTHFPQQAARISDYVAFLYKGQIVEW 226
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
338-516 |
8.02e-09 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 55.94 E-value: 8.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 338 LIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETVklASVDQ--------------FRDAMDNSKt 403
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSI--AYVSQepwiqngtirenilFGKPFDEER- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 404 vWEEV------SGGLDIMRIG-NTEmpsrayvgrfnfkgtdqgkrVGE----LSGGERGRLHLAKLLQVGGNVLLLDEPT 472
Cdd:cd03250 97 -YEKVikacalEPDLEILPDGdLTE--------------------IGEkginLSGGQKQRISLARAVYSDADIYLLDDPL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489953208 473 NDLDIETLRAL-ENAL---LEFPGCAMVISHDRWFLDRiATHILDYQD 516
Cdd:cd03250 156 SAVDAHVGRHIfENCIlglLLNNKTRILVTHQLQLLPH-ADQIVVLDN 202
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
19-226 |
9.07e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 56.66 E-value: 9.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI------DTDIEGEARPQPGI-----KIGYLPQEPQlnpEHTVR 87
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLleaesgQIIIDGDLLTEENVwdirhKIGMVFQNPD---NQFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 88 ESVEEAVSEVVNAlKGLDevyakyaepdadfdklaaqqgkYEEIIqahdghnlnvqlERAADALRLPDW----DAKIANL 163
Cdd:PRK13650 97 ATVEDDVAFGLEN-KGIP----------------------HEEMK------------ERVNEALELVGMqdfkEREPARL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489953208 164 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDFEGTVVAITHDryfLDNVA 226
Cdd:PRK13650 142 SGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGrlelIKTIKGIRDDYQMTVISITHD---LDEVA 205
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
24-226 |
1.14e-08 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 57.05 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 24 NISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQpGIKIGYLP---------------QEPQ--LNPEHTV 86
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFD-GQDITGLSgrelrplrrrmqmvfQDPYasLNPRMTV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 87 RESVEEA--VSEVVNAlkgldevyakyaepdadfdklAAQQGKYEEIIQAhdghnlnVQLeRAADALRLPdwdakiANLS 164
Cdd:COG4608 115 GDIIAEPlrIHGLASK---------------------AERRERVAELLEL-------VGL-RPEHADRYP------HEFS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 165 GGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDFEGTVVAITHD----RYFLDNVA 226
Cdd:COG4608 160 GGQRQRIGIARALALNPKLIVCDEPVSALDvsiqAQVLNLLEDLQDELGLTYLFISHDlsvvRHISDRVA 229
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
31-205 |
1.16e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 55.63 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 31 PGAKIGVLGLNGAGKSTLLRIMAG--------IDTDIEGEARPQPGIKIGYLPQEPQLNPEHTVRESVEeavseVVNALK 102
Cdd:PRK13543 36 AGEALLVQGDNGAGKTTLLRVLAGllhvesgqIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLENLH-----FLCGLH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 103 GLdevYAKYAEPDAdfdkLAAqqgkyeeiiqahdghnlnVQLERAADALrlpdwdakIANLSGGERRRVALCRLLLEKPD 182
Cdd:PRK13543 111 GR---RAKQMPGSA----LAI------------------VGLAGYEDTL--------VRQLSAGQKKRLALARLWLSPAP 157
|
170 180
....*....|....*....|...
gi 489953208 183 MLLLDEPTNHLDAESVAWLERFL 205
Cdd:PRK13543 158 LWLLDEPYANLDLEGITLVNRMI 180
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
325-476 |
1.30e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 57.81 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 325 EVTNLRKSY----GDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGsitlgeTVKLASVDQfrDAMDN 400
Cdd:PRK10535 6 ELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSG------TYRVAGQDV--ATLDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 401 SKtvweevsggLDIMR-------------------IGNTEMP--------------SRAYVGRFNFkgtdqGKRV----G 443
Cdd:PRK10535 78 DA---------LAQLRrehfgfifqryhllshltaAQNVEVPavyaglerkqrllrAQELLQRLGL-----EDRVeyqpS 143
|
170 180 190
....*....|....*....|....*....|...
gi 489953208 444 ELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLD 476
Cdd:PRK10535 144 QLSGGQQQRVSIARALMNGGQVILADEPTGALD 176
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
342-515 |
1.36e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 55.24 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 342 LTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQFRDAMDNSKTVWEEVSG--------GL 412
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIdGKTATRGDRSRFMAYLGHLPGLKADLSTlenlhflcGL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 413 DIMRIGNTEMPSRAYVGRFNFKGTdqgkRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIETLRALENAL---LE 489
Cdd:PRK13543 110 HGRRAKQMPGSALAIVGLAGYEDT----LVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMIsahLR 185
|
170 180
....*....|....*....|....*.
gi 489953208 490 FPGCAMVISHDRWFLDRIATHILDYQ 515
Cdd:PRK13543 186 GGGAALVTTHGAYAAPPVRTRMLTLE 211
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
21-241 |
1.86e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 56.01 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLrimagidTDIEGEARPQPG-IKIGYLPQEPQLNPEHTVRESVEEAVSEVVN 99
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLV-------THFNGLIKSKYGtIQVGDIYIGDKKNNHELITNPYSKKIKNFKE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 100 ALKGLDEVYA--KYA------EPDADFDKLAAQQGKYEEIIQAhdghnlNVQLERAAdaLRLPDWDAKIANLSGGERRRV 171
Cdd:PRK13631 114 LRRRVSMVFQfpEYQlfkdtiEKDIMFGPVALGVKKSEAKKLA------KFYLNKMG--LDDSYLERSPFGLSGGQKRRV 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489953208 172 ALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEG---TVVAITHDRYFLDNVAGWILELDRGE----GIPWE 241
Cdd:PRK13631 186 AIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAnnkTVFVITHTMEHVLEVADEVIVMDKGKilktGTPYE 262
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-219 |
2.02e-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: 57.23 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRI---MAGIDTDIEGEARPQPGIKI-------GYLPQEPQLNpEHTVRe 88
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSAllrLLSTEGEIQIDGVSWNSVTLqtwrkafGVIPQKVFIF-SGTFR- 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 89 sveeavsevvnalKGLDEvYAKYAepDADFDKLAAQQGKYEEIIQAHDghNLNVQLERAADAlrlpdwdakianLSGGER 168
Cdd:TIGR01271 1310 -------------KNLDP-YEQWS--DEEIWKVAEEVGLKSVIEQFPD--KLDFVLVDGGYV------------LSNGHK 1359
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489953208 169 RRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFL-HDFEGTVVAITHDR 219
Cdd:TIGR01271 1360 QLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLkQSFSNCTVILSEHR 1411
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
21-218 |
2.03e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 57.04 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARpQPGIKIGYLPQE--PQLNPEHtvresveeavsevv 98
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYR-VAGQDVATLDADalAQLRREH-------------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 99 nalkgLDEVYAKYAEpdadFDKLAAQQGKyeEIIQAHDGHNLNVQLERAADAL-RL---PDWDAKIANLSGGERRRVALC 174
Cdd:PRK10535 88 -----FGFIFQRYHL----LSHLTAAQNV--EVPAVYAGLERKQRLLRAQELLqRLgleDRVEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489953208 175 RLLLEKPDMLLLDEPTNHLDAES---VAWLERFLHDFEGTVVAITHD 218
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSgeeVMAILHQLRDRGHTVIIVTHD 203
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
7-216 |
2.11e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 55.40 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 7 TMHRVGKVVPPKRH--ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIdtdIEGEARPQPGIKI------------- 71
Cdd:PRK09984 3 TIIRVEKLAKTFNQhqALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL---ITGDKSAGSHIELlgrtvqregrlar 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 72 ---------GYLPQEPQLNPEHTVRESVeeavseVVNALkGLDEVYAKYAEPDADFDKLAAQQGkYEEIIQAHDGHNlnv 142
Cdd:PRK09984 80 dirksrantGYIFQQFNLVNRLSVLENV------LIGAL-GSTPFWRTCFSWFTREQKQRALQA-LTRVGMVHFAHQ--- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489953208 143 qleraadalrlpdwdaKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF---EGTVVAIT 216
Cdd:PRK09984 149 ----------------RVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInqnDGITVVVT 209
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
324-512 |
2.28e-08 |
|
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: 54.54 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRkSYGDRVLIDdltFSVPkgaIVGIIGPNGAGKSTLF-------------RMMSGQEQPDsgsiTLGETVKLAS 390
Cdd:cd03240 4 LSIRNIR-SFHERSEIE---FFSP---LTLIVGQNGAGKTTIIealkyaltgelppNSKGGAHDPK----LIREGEVRAQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 391 VD-QFRDAMDNSKTVWEEvsggLDIMRigntempSRAYV--GRFNFKGTDQgkrVGELSGGERG------RLHLAKLLQV 461
Cdd:cd03240 73 VKlAFENANGKKYTITRS----LAILE-------NVIFChqGESNWPLLDM---RGRCSGGEKVlasliiRLALAETFGS 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489953208 462 GGNVLLLDEPTNDLD-----------IETLRALENALLefpgcaMVISHDRWFLDRiATHIL 512
Cdd:cd03240 139 NCGILALDEPTTNLDeenieeslaeiIEERKSQKNFQL------IVITHDEELVDA-ADHIY 193
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
18-236 |
2.37e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 55.58 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIdtdiegearpqpgikigYLPQEpqlNPEHTVRESVEEAVSEV 97
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGL-----------------LLPDD---NPNSKITVDGITLTAKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 98 VNALKglDEVYAKYAEPDADF------DKLA----AQQGKYEEIIQAhdghnlnvqLERAADALRLPDW-DAKIANLSGG 166
Cdd:PRK13640 79 VWDIR--EKVGIVFQNPDNQFvgatvgDDVAfgleNRAVPRPEMIKI---------VRDVLADVGMLDYiDSEPANLSGG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489953208 167 ERRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDFEGTVVAITHDryfLD--NVAGWILELDRGE 236
Cdd:PRK13640 148 QKQRVAIAGILAVEPKIIILDESTSMLDPAGkeqiLKLIRKLKKKNNLTVISITHD---IDeaNMADQVLVLDDGK 220
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
324-476 |
2.50e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 56.01 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSY-GDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETVklasVDQF----RD-A 397
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRV----VNELepadRDiA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 398 M--DN-----SKTVWEEVSGGLDIMRIGNTEMPSR-----------AYVGRfnfkgtdqgkRVGELSGGERGRLHLAKLL 459
Cdd:PRK11650 80 MvfQNyalypHMSVRENMAYGLKIRGMPKAEIEERvaeaarilelePLLDR----------KPRELSGGQRQRVAMGRAI 149
|
170
....*....|....*..
gi 489953208 460 QVGGNVLLLDEPTNDLD 476
Cdd:PRK11650 150 VREPAVFLFDEPLSNLD 166
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
16-272 |
2.69e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 56.51 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AG---ID-TDIEGEARPQPGIKIGYLPQEPQLnpeh 84
Cdd:PRK13657 345 DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLqrvfdpqSGrilIDgTDIRTVTRASLRRNIAVVFQDAGL---- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 85 tVRESVEEavsevvNALKGldevyakyaEPDA-DFDKLAAQqgkyeEIIQAHDghnlnvQLERAADALrlpdwDAKIAN- 162
Cdd:PRK13657 421 -FNRSIED------NIRVG---------RPDAtDEEMRAAA-----ERAQAHD------FIERKPDGY-----DTVVGEr 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 163 ---LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF-EG-TVVAITHDryfLDNV--AGWILELDRG 235
Cdd:PRK13657 469 grqLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELmKGrTTFIIAHR---LSTVrnADRILVFDNG 545
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 489953208 236 EGIPwEGNYSSwLEQKDQRLAQEA-----SQEAARRKSIEKE 272
Cdd:PRK13657 546 RVVE-SGSFDE-LVARGGRFAALLraqgmLQEDERRKQPAAE 585
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-240 |
3.23e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 54.67 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI----DTDIEGEArpqpgiKIGYLPQEpqlnpehTVResveeav 94
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiyDSKIKVDG------KVLYFGKD-------IFQ------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 95 sevVNALKGLDEVYAKYAEPDAdFDKLAAqqgkYEEIIQAHDGHNLNVQLER---AADALR-LPDW-------DAKIANL 163
Cdd:PRK14246 83 ---IDAIKLRKEVGMVFQQPNP-FPHLSI----YDNIAYPLKSHGIKEKREIkkiVEECLRkVGLWkevydrlNSPASQL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489953208 164 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EGTVVAITHDRYFLDNVAGWILELDRGEGIPW 240
Cdd:PRK14246 155 SGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELknEIAIVIVSHNPQQVARVADYVAFLYNGELVEW 233
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
24-227 |
3.60e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 55.50 E-value: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 24 NISLSffPGAKIGVLGLNGAGKS-TLLRIMA-----GIdtdIEGEARPQpGIKIGYLP----------------QEP--Q 79
Cdd:PRK09473 36 NFSLR--AGETLGIVGESGSGKSqTAFALMGllaanGR---IGGSATFN-GREILNLPekelnklraeqismifQDPmtS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 80 LNPEHTVRESVeeavSEVVNALKGLDEVYAkyaepdadfdklaaqqgkYEEIIqahdghnlnvqleRAADALRLPDWDAK 159
Cdd:PRK09473 110 LNPYMRVGEQL----MEVLMLHKGMSKAEA------------------FEESV-------------RMLDAVKMPEARKR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489953208 160 IA----NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDFEGTVVAITHDryfLDNVAG 227
Cdd:PRK09473 155 MKmyphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDvtvqAQIMTLLNELKREFNTAIIMITHD---LGVVAG 227
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
324-489 |
3.62e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 56.01 E-value: 3.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLR-KSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQeQPDSGSI---------------------- 380
Cdd:PRK11174 350 IEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLkingielreldpeswrkhlswv 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 381 ---------TLGETVKLASVD----QFRDAMDNSKtVWEEVSG---GLDimrigntempsrayvgrfnfkgTDQGKRVGE 444
Cdd:PRK11174 429 gqnpqlphgTLRDNVLLGNPDasdeQLQQALENAW-VSEFLPLlpqGLD----------------------TPIGDQAAG 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489953208 445 LSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIETLRALENALLE 489
Cdd:PRK11174 486 LSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNA 530
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
321-489 |
3.68e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 54.80 E-value: 3.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 321 DKVVEVTNLRKSYGDRV---------LIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLgETVKLASV 391
Cdd:PRK15112 2 ETLLEVRNLSKTFRYRTgwfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLI-DDHPLHFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 392 DQ----------FRDAmDNSKTVWEEVSGGLDIMRIGNTEMPSRAYVGRFNfkgtDQGKRVG-----------ELSGGER 450
Cdd:PRK15112 81 DYsyrsqrirmiFQDP-STSLNPRQRISQILDFPLRLNTDLEPEQREKQII----ETLRQVGllpdhasyyphMLAPGQK 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 489953208 451 GRLHLAKLLQVGGNVLLLDEPTNDLDIETLRALENALLE 489
Cdd:PRK15112 156 QRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLE 194
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
16-228 |
4.00e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 54.74 E-value: 4.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQpGIKIGYLPQEPQLNPehtVRESV----- 90
Cdd:PRK13643 16 PFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG-DIVVSSTSKQKEIKP---VRKKVgvvfq 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 91 ---EEAVSEVVnaLKGLDEVYAKYAEPDADFDKLAAQqgKYEEIiqahdghnlnvqleraadALRLPDWDAKIANLSGGE 167
Cdd:PRK13643 92 fpeSQLFEETV--LKDVAFGPQNFGIPKEKAEKIAAE--KLEMV------------------GLADEFWEKSPFELSGGQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489953208 168 RRRVALCRLLLEKPDMLLLDEPTNHLDAES-VAWLERF--LHDFEGTVVAITHdryFLDNVAGW 228
Cdd:PRK13643 150 MRRVAIAGILAMEPEVLVLDEPTAGLDPKArIEMMQLFesIHQSGQTVVLVTH---LMDDVADY 210
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
348-515 |
4.12e-08 |
|
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: 52.38 E-value: 4.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 348 KGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSitlgetVKLASVDQFRDAMDNSktvweevsggldimrigntempsray 427
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGG------VIYIDGEDILEEVLDQ-------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 428 vgrfnFKGTDQGKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIET---------LRALENALLEFPGCAMVIS 498
Cdd:smart00382 49 -----LLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQeallllleeLRLLLLLKSEKNLTVILTT 123
|
170
....*....|....*...
gi 489953208 499 HDR-WFLDRIATHILDYQ 515
Cdd:smart00382 124 NDEkDLGPALLRRRFDRR 141
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-194 |
4.29e-08 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 55.85 E-value: 4.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 12 GKVVPPKRhILKNISLSFFPGAKIGVLGLNGAGKSTLLR-IMAGIDTdiEGEARPQpGIKIGYLP--------------- 75
Cdd:COG4172 293 RRTVGHVK-AVDGVSLTLRRGETLGLVGESGSGKSTLGLaLLRLIPS--EGEIRFD-GQDLDGLSrralrplrrrmqvvf 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 76 QEP--QLNPEHTVRESVEEavsevvnalkGLDevyakyaepdADFDKLAAQQgkyeeiiqahdghnlnvQLERAADALRL 153
Cdd:COG4172 369 QDPfgSLSPRMTVGQIIAE----------GLR----------VHGPGLSAAE-----------------RRARVAEALEE 411
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489953208 154 PDWDAKIAN-----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 194
Cdd:COG4172 412 VGLDPAARHrypheFSGGQRQRIAIARALILEPKLLVLDEPTSALD 457
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
321-484 |
4.49e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 54.40 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 321 DKVVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFR-------MMSGQEQpdSGSITL-GETVKLASVD 392
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTFhGKNLYAPDVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 393 Q----------FRDAMDNSKTVWEEVSGGLDI--MRIGNTEMPSRAYVGRFNFKGT-DQGKRVG-ELSGGERGRLHLAKL 458
Cdd:PRK14243 86 PvevrrrigmvFQKPNPFPKSIYDNIAYGARIngYKGDMDELVERSLRQAALWDEVkDKLKQSGlSLSGGQQQRLCIARA 165
|
170 180
....*....|....*....|....*..
gi 489953208 459 LQVGGNVLLLDEPTNDLD-IETLRALE 484
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDpISTLRIEE 192
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
336-500 |
4.66e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.45 E-value: 4.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 336 RVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGqEQPDS---------GSITL-GEtvKLASVDQFRDAMDNSK--- 402
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGGgaprgarvtGDVTLnGE--PLAAIDAPRLARLRAVlpq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 403 --------TVWEEVSGGL--DIMRIGNTEMPSRAYVGR-FNFKGTDQ--GKRVGELSGGERGRLHLAKLL---------Q 460
Cdd:PRK13547 91 aaqpafafSAREIVLLGRypHARRAGALTHRDGEIAWQaLALAGATAlvGRDVTTLSGGELARVQFARVLaqlwpphdaA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489953208 461 VGGNVLLLDEPTNDLD-------IETLRALENallEFPGCAMVISHD 500
Cdd:PRK13547 171 QPPRYLLLDEPTAALDlahqhrlLDTVRRLAR---DWNLGVLAIVHD 214
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
11-195 |
4.83e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 55.23 E-value: 4.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 11 VGKVVPPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEarpqpgIKIGylpqepqlnpehtvresv 90
Cdd:PRK11650 9 VRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGE------IWIG------------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 91 eeavSEVVNALKGLDE----VYAKYA-EPDAD-FDKLA-----AQQGKyEEIIQahdghnlnvQLERAADALRL-PDWDA 158
Cdd:PRK11650 65 ----GRVVNELEPADRdiamVFQNYAlYPHMSvRENMAyglkiRGMPK-AEIEE---------RVAEAARILELePLLDR 130
|
170 180 190
....*....|....*....|....*....|....*..
gi 489953208 159 KIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA 195
Cdd:PRK11650 131 KPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDA 167
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
18-217 |
5.91e-08 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 53.89 E-value: 5.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----DTDIEGEAR------PQPGI-------KIGYLPQEPq 79
Cdd:COG1117 23 DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndlipGARVEGEILldgediYDPDVdvvelrrRVGMVFQKP- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 80 lNP-EHTVRESV---------------EEAVSEvvnALK--GL-DEVYakyaepdadfDKLaaqqgkyeeiiqaHDghnl 140
Cdd:COG1117 102 -NPfPKSIYDNVayglrlhgikskselDEIVEE---SLRkaALwDEVK----------DRL-------------KK---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 141 nvqleraaDALrlpdwdakiaNLSGGERRRvaLC--RLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEG--TVVAIT 216
Cdd:COG1117 151 --------SAL----------GLSGGQQQR--LCiaRALAVEPEVLLMDEPTSALDPISTAKIEELILELKKdyTIVIVT 210
|
.
gi 489953208 217 H 217
Cdd:COG1117 211 H 211
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
331-476 |
5.96e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 53.73 E-value: 5.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 331 KSY-GDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLG--ETVKLASVDQ----------FRD- 396
Cdd:PRK10908 9 KAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSghDITRLKNREVpflrrqigmiFQDh 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 397 --AMDnsKTVWEEVSGGLDIMRIGNTEMPSRAYVGRFNFKGTDQGKRVG-ELSGGERGRLHLAKLLQVGGNVLLLDEPTN 473
Cdd:PRK10908 89 hlLMD--RTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPiQLSGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
...
gi 489953208 474 DLD 476
Cdd:PRK10908 167 NLD 169
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
324-487 |
7.76e-08 |
|
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: 53.31 E-value: 7.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDR--VLI-DDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQFRDAM- 398
Cdd:cd03249 1 IEFKNVSFRYPSRpdVPIlKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLdGVDIRDLNLRWLRSQIg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 399 --------------------DNSKTVWEEVSGGLD------IMRIGNtempsrayvgRFNfkgTDQGKRVGELSGGERGR 452
Cdd:cd03249 81 lvsqepvlfdgtiaenirygKPDATDEEVEEAAKKanihdfIMSLPD----------GYD---TLVGERGSQLSGGQKQR 147
|
170 180 190
....*....|....*....|....*....|....*
gi 489953208 453 LHLAKLLQVGGNVLLLDEPTNDLDIETLRALENAL 487
Cdd:cd03249 148 IAIARALLRNPKILLLDEATSALDAESEKLVQEAL 182
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
323-383 |
8.12e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.06 E-value: 8.12e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489953208 323 VVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLG 383
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIG 71
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-286 |
8.63e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 55.34 E-value: 8.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 16 PPKrhiLKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQPgiKIGYLPQEPQLNPEhTVRESVeeavs 95
Cdd:TIGR00957 651 PPT---LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG--SVAYVPQQAWIQND-SLRENI----- 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 96 evvnalkgldeVYAKYAEPDadfdklaaqqgKYEEIIQAhdghnlnvqLERAADALRLPDWD-----AKIANLSGGERRR 170
Cdd:TIGR00957 720 -----------LFGKALNEK-----------YYQQVLEA---------CALLPDLEILPSGDrteigEKGVNLSGGQKQR 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 171 VALCRLLLEKPDMLLLDEPTNHLDA-------ESVAWLERFLHDfeGTVVAITHDRYFLDNVaGWILELDRGEgIPWEGN 243
Cdd:TIGR00957 769 VSLARAVYSNADIYLFDDPLSAVDAhvgkhifEHVIGPEGVLKN--KTRILVTHGISYLPQV-DVIIVMSGGK-ISEMGS 844
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 489953208 244 YSSWLeQKDQRLAQEASQEAARRKSIEKELEWVR-QGAKGRQSK 286
Cdd:TIGR00957 845 YQELL-QRDGAFAEFLRTYAPDEQQGHLEDSWTAlVSGEGKEAK 887
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
22-241 |
8.74e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 53.60 E-value: 8.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEA--RPQP-------GIK--IGYLPQepqlNPEHtvresv 90
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfyNNQAitddnfeKLRkhIGIVFQ----NPDN------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 91 eEAVSEVVnalkgldevyaKYaepDADFDkLAAQQGKYEEIiqahdgHNLNVQLERAADALRLPDWDAKiaNLSGGERRR 170
Cdd:PRK13648 95 -QFVGSIV-----------KY---DVAFG-LENHAVPYDEM------HRRVSEALKQVDMLERADYEPN--ALSGGQKQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 171 VALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLH----DFEGTVVAITHDryfLDNVAG--WILELDRG----EGIPW 240
Cdd:PRK13648 151 VAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRkvksEHNITIISITHD---LSEAMEadHVIVMNKGtvykEGTPT 227
|
.
gi 489953208 241 E 241
Cdd:PRK13648 228 E 228
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
339-488 |
9.52e-08 |
|
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: 55.40 E-value: 9.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 339 IDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETVKLASVD----------QFrDAMDNSKT----- 403
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISdvhqnmgycpQF-DAIDDLLTgrehl 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 404 -VWEEVSG--GLDIMRIGNTEMPS---RAYVGRFnfkgtdqgkrVGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDI 477
Cdd:TIGR01257 2034 yLYARLRGvpAEEIEKVANWSIQSlglSLYADRL----------AGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDP 2103
|
170
....*....|.
gi 489953208 478 ETLRALENALL 488
Cdd:TIGR01257 2104 QARRMLWNTIV 2114
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
324-500 |
9.75e-08 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 52.71 E-value: 9.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRkSYGDRVLIDdltFSvpkGAIVGIIGPNGAGKSTLF------------RMMSGQEQ-----PDSGSITL---- 382
Cdd:COG0419 5 LRLENFR-SYRDTETID---FD---DGLNLIVGPNGAGKSTILeairyalygkarSRSKLRSDlinvgSEEASVELefeh 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 383 -----------GETVKLAS---------------VDQFRDAMDNSKTVWEEVSGGLDimRIGNTEMPSRAYVGRFNfkgt 436
Cdd:COG0419 78 ggkryrierrqGEFAEFLEakpserkealkrllgLEIYEELKERLKELEEALESALE--ELAELQKLKQEILAQLS---- 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489953208 437 dQGKRVGELSGGERGRLHLAKLLQvggnvLLLDepTNDLDIETLRALENALLEfpgcAMVISHD 500
Cdd:COG0419 152 -GLDPIETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEE----LAIITHV 203
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
341-520 |
1.07e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 53.47 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 341 DLTFSvpKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETVKLASVDQFRDAMD--------------------- 399
Cdd:PRK13645 31 SLTFK--KNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVKRlrkeiglvfqfpeyqlfqeti 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 400 -------------NSKTVWEEVSGGLDIMRIgntempSRAYVGRFNFkgtdqgkrvgELSGGERGRLHLAKLLQVGGNVL 466
Cdd:PRK13645 109 ekdiafgpvnlgeNKQEAYKKVPELLKLVQL------PEDYVKRSPF----------ELSGGQKRRVALAGIIAMDGNTL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489953208 467 LLDEPTNDLDIETLRALENALL----EFPGCAMVISHDRWFLDRIATHILdYQDEGKV 520
Cdd:PRK13645 173 VLDEPTGGLDPKGEEDFINLFErlnkEYKKRIIMVTHNMDQVLRIADEVI-VMHEGKV 229
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
21-216 |
1.24e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.04 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQPG------------IKIGYLPQEPQLnpehtVRE 88
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkdinlkwwrSKIGVVSQDPLL-----FSN 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 89 SVEEAVSEVVNALKGLDEV--------YAKYAEPDADFDKLAAQQGKYEEIIQAHDGHNL-----NVQLERAADALR--- 152
Cdd:PTZ00265 475 SIKNNIKYSLYSLKDLEALsnyynedgNDSQENKNKRNSCRAKCAGDLNDMSNTTDSNELiemrkNYQTIKDSEVVDvsk 554
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489953208 153 ----------LPD-WDAKI----ANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEGTVVAIT 216
Cdd:PTZ00265 555 kvlihdfvsaLPDkYETLVgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRIT 633
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
341-476 |
1.41e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 53.21 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 341 DLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETV---------------KLASVDQFRDAMDNSKTVW 405
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitstsknkdikqirkKVGLVFQFPESQLFEETVL 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489953208 406 EEVSGGLDIMRIGNTEMPSRAYvGRFNFKGTDQ---GKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLD 476
Cdd:PRK13649 105 KDVAFGPQNFGVSQEEAEALAR-EKLALVGISEslfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
321-535 |
1.57e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 52.86 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 321 DKVVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMS--GQEQPD---SGSITL-GETVKLASVDQ- 393
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYnGHNIYSPRTDTv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 394 ---------FRDAMDNSKTVWEEVSGGLDIMRIGNTEMPSRAyVGRfNFKGTDQGKRVGE--------LSGGERGRLHLA 456
Cdd:PRK14239 83 dlrkeigmvFQQPNPFPMSIYENVVYGLRLKGIKDKQVLDEA-VEK-SLKGASIWDEVKDrlhdsalgLSGGQQQRVCIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 457 KLLQVGGNVLLLDEPTNDLDIETLRALENALLEFPG--CAMVISHDRWFLDRIAThildyqdegKVEFF-EGNFTEYEEY 533
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDdyTMLLVTRSMQQASRISD---------RTGFFlDGDLIEYNDT 231
|
..
gi 489953208 534 KK 535
Cdd:PRK14239 232 KQ 233
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-218 |
1.67e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 52.73 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIdTDIEGEARPQPgiKIGYLPQ---EPQLNpehtvresveeavsev 97
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEG--RVEFFNQniyERRVN---------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 98 VNALKglDEVYAKYAEPD----ADFDKLAAQQgkyeEIIQAHDGHNLNVQLERAADALRLpdWDA------KIA-NLSGG 166
Cdd:PRK14258 83 LNRLR--RQVSMVHPKPNlfpmSVYDNVAYGV----KIVGWRPKLEIDDIVESALKDADL--WDEikhkihKSAlDLSGG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489953208 167 ERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF----EGTVVAITHD 218
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlrsELTMVIVSHN 210
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
327-499 |
2.06e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.58 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 327 TNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSIT-LGETVKLASVdqfRDAMDNS-KTV 404
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILfQGKEIDFKSS---KEALENGiSMV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 405 WEEVSGGLDIMRIGNTempsraYVGRFNFKG--TDQGK--------------------RVGELSGGERGRLHLAKLLQVG 462
Cdd:PRK10982 79 HQELNLVLQRSVMDNM------WLGRYPTKGmfVDQDKmyrdtkaifdeldididpraKVATLSVSQMQMIEIAKAFSYN 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489953208 463 GNVLLLDEPTNDL---DIETLRALENALLEfPGCAMV-ISH 499
Cdd:PRK10982 153 AKIVIMDEPTSSLtekEVNHLFTIIRKLKE-RGCGIVyISH 192
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
320-476 |
2.07e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 52.78 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 320 GDKVVEVTNLRKSYGD------RVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLG--ETVKLASV 391
Cdd:PRK13633 1 MNEMIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDglDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 392 DQFRDAM-------DN---SKTVWEEVSGGLDIMRIGNTEMPSRA-----YVGRFNFKgtDQGKRVgeLSGGERGRLHLA 456
Cdd:PRK13633 81 WDIRNKAgmvfqnpDNqivATIVEEDVAFGPENLGIPPEEIRERVdeslkKVGMYEYR--RHAPHL--LSGGQKQRVAIA 156
|
170 180
....*....|....*....|
gi 489953208 457 KLLQVGGNVLLLDEPTNDLD 476
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLD 176
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
324-526 |
2.24e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 52.35 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDS-----GSITL-GETV--KLASVDQFR 395
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFfNQNIyeRRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 396 D--AMDNSK------TVWEEVSGGLDImrIGNTEMPSRAYVGRFNFKGTDQGKRVG--------ELSGGERGRLHLAKLL 459
Cdd:PRK14258 88 RqvSMVHPKpnlfpmSVYDNVAYGVKI--VGWRPKLEIDDIVESALKDADLWDEIKhkihksalDLSGGQQQRLCIARAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489953208 460 QVGGNVLLLDEPTNDLD------IETLraLENALLEFPGCAMVISHDRWFLDRIAthilDYqdegkVEFFEGN 526
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDpiasmkVESL--IQSLRLRSELTMVIVSHNLHQVSRLS----DF-----TAFFKGN 227
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
22-235 |
2.29e-07 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 51.95 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEG---------------EARPQPGIKIGYLPQEPQLnpehtV 86
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGkvhwsnknesepsfeATRSRNRYSVAYAAQKPWL-----L 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 87 RESVEEAVSevvnalkgldevyakYAEPdadFDKlaaqqGKYEEIIQAhdghnlnVQLERAADALRLPDwDAKIA----N 162
Cdd:cd03290 92 NATVEENIT---------------FGSP---FNK-----QRYKAVTDA-------CSLQPDIDLLPFGD-QTEIGergiN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 163 LSGGERRRVALCRLLLEKPDMLLLDEP--------TNHLDAESVAwleRFLHDFEGTVVAITHDRYFLDNvAGWILELDR 234
Cdd:cd03290 141 LSGGQRQRICVARALYQNTNIVFLDDPfsaldihlSDHLMQEGIL---KFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKD 216
|
.
gi 489953208 235 G 235
Cdd:cd03290 217 G 217
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
323-472 |
2.39e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 51.80 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 323 VVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLG-------ETVKL-----AS 390
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDgkditdwQTAKImreavAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 391 VDQFRDAMdNSKTVWEEVS-GGLDIMRIGNTEMPSRAYvGRFNFKGTDQGKRVGELSGGERGRLHLAKLLQVGGNVLLLD 469
Cdd:PRK11614 85 VPEGRRVF-SRMTVEENLAmGGFFAERDQFQERIKWVY-ELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLD 162
|
...
gi 489953208 470 EPT 472
Cdd:PRK11614 163 EPS 165
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
318-477 |
2.41e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 53.25 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 318 RLGDKVVEVTNLR---KSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLfrMMS------GQEQpdSGSITL-GETVK 387
Cdd:NF040905 252 KIGEVVFEVKNWTvyhPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTEL--AMSvfgrsyGRNI--SGTVFKdGKEVD 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 388 LASVdqfRDAMDNS-KTVWEEVSG-GL----DIMRigNTEMPS-------------------RAYVGRFNFKGTDQGKRV 442
Cdd:NF040905 328 VSTV---SDAIDAGlAYVTEDRKGyGLnlidDIKR--NITLANlgkvsrrgvideneeikvaEEYRKKMNIKTPSVFQKV 402
|
170 180 190
....*....|....*....|....*....|....*
gi 489953208 443 GELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDI 477
Cdd:NF040905 403 GNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDV 437
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
22-251 |
2.44e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 53.48 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 22 LKNISLSFFPGAKIGVLGLNGAGKSTllriMAGIDT---DI-EGEarpqpgIKI-GYLPQEPQLNpehTVRESVEeAVSE 96
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKST----IANLLTrfyDIdEGE------ILLdGHDLRDYTLA---SLRNQVA-LVSQ 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 97 VVNALKgldevyakyaepdadfDKLA-----AQQGKY--EEIIQAhdghnlnvqlERAADAL----RLPD-WDAKI---- 160
Cdd:PRK11176 425 NVHLFN----------------DTIAnniayARTEQYsrEQIEEA----------ARMAYAMdfinKMDNgLDTVIgeng 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 161 ANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEG--TVVAITHDRYFLDNvAGWILELDRGEgI 238
Cdd:PRK11176 479 VLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKnrTSLVIAHRLSTIEK-ADEILVVEDGE-I 556
|
250
....*....|...
gi 489953208 239 PWEGNYSSWLEQK 251
Cdd:PRK11176 557 VERGTHAELLAQN 569
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
324-501 |
2.61e-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: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSY--GDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLF----RMMS--GQEQPDS---GSITLGETVKLASV- 391
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLsaflRLLNteGDIQIDGvswNSVPLQKWRKAFGVi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 392 --------DQFRDAMD-----NSKTVW---EEVSGGLDImrigntempsRAYVGRFNFKGTDQGKrvgELSGGERGRLHL 455
Cdd:cd03289 83 pqkvfifsGTFRKNLDpygkwSDEEIWkvaEEVGLKSVI----------EQFPGQLDFVLVDGGC---VLSHGHKQLMCL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489953208 456 AKLLQVGGNVLLLDEPTNDLDIETLRALENALLE-FPGCAMVISHDR 501
Cdd:cd03289 150 ARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQaFADCTVILSEHR 196
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
341-396 |
2.80e-07 |
|
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: 53.26 E-value: 2.80e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 489953208 341 DLTFSvpKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQFRD 396
Cdd:COG4615 352 DLTIR--RGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLdGQPVTADNREAYRQ 406
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
339-476 |
2.89e-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: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 339 IDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETVklASVDQfrDAMDNSKTVWEEVSGG--LDIMR 416
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSV--AYVPQ--QAWIQNDSLRENILFGkaLNEKY 729
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489953208 417 IGNTeMPSRAYVGRFNFKGTDQGKRVGE----LSGGERGRLHLAKLLQVGGNVLLLDEPTNDLD 476
Cdd:TIGR00957 730 YQQV-LEACALLPDLEILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
21-223 |
3.62e-07 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 51.61 E-value: 3.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGID----------------TDIEGEARPQPGIKIGYlpQEPQLNPEH 84
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyevtsgsilldgediLELSPDERARAGIFLAF--QYPVEIPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 85 TVRESVEEAVsevvNALKGLDEvyakyaePDADFDKLaaqqgkyeeiiqahdghnlnvqLERAADALRLpdwDAKIAN-- 162
Cdd:COG0396 93 SVSNFLRTAL----NARRGEEL-------SAREFLKL----------------------LKEKMKELGL---DEDFLDry 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489953208 163 ----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES---VAWLERFLHDFEGTVVAITHDRYFLD 223
Cdd:COG0396 137 vnegFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDAlriVAEGVNKLRSPDRGILIITHYQRILD 204
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
327-476 |
3.65e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 51.93 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 327 TNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSI-------------TLGETVKLASVDQ 393
Cdd:PRK13638 5 SDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwqgkpldyskrgLLALRQQVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 394 FRDAMDNSKTVWEEVSGGLDIMRIGNTEMPSR-----AYVGRFNFKgtdqGKRVGELSGGERGRLHLAKLLQVGGNVLLL 468
Cdd:PRK13638 85 DPEQQIFYTDIDSDIAFSLRNLGVPEAEITRRvdealTLVDAQHFR----HQPIQCLSHGQKKRVAIAGALVLQARYLLL 160
|
....*...
gi 489953208 469 DEPTNDLD 476
Cdd:PRK13638 161 DEPTAGLD 168
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
346-511 |
4.02e-07 |
|
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: 51.60 E-value: 4.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 346 VPK-GAIVGIIGPNGAGKSTLFRMMSGQEQPDSGsitlgetvKLASVDQFRDAMDNSK-TVWEE-----VSGGLD-IMRI 417
Cdd:cd03236 22 VPReGQVLGLVGPNGIGKSTALKILAGKLKPNLG--------KFDDPPDWDEILDEFRgSELQNyftklLEGDVKvIVKP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 418 GNTEMPSRAYVGRF--NFKGTDQ-----------------GKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIE 478
Cdd:cd03236 94 QYVDLIPKAVKGKVgeLLKKKDErgkldelvdqlelrhvlDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 489953208 479 ---TLRALENALLEFPGCAMVISHDRWFLDRIATHI 511
Cdd:cd03236 174 qrlNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
21-219 |
4.14e-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: 51.78 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRI---MAGIDTDIEGEARPQPGIKI-------GYLPQEPQLNpEHTVResv 90
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAflrLLNTEGDIQIDGVSWNSVPLqkwrkafGVIPQKVFIF-SGTFR--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 91 eeavsevvnalKGLDEvYAKYAEpdadfdklaaqqgkyEEIIQAHDGHNLNVQLERAADALRLPDWDAKIAnLSGGERRR 170
Cdd:cd03289 95 -----------KNLDP-YGKWSD---------------EEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCV-LSHGHKQL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489953208 171 VALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFL-HDFEGTVVAITHDR 219
Cdd:cd03289 147 MCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLkQAFADCTVILSEHR 196
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
162-217 |
4.15e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.11 E-value: 4.15e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 162 NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF----EGTVVAITH 217
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdkaDKTIITIAH 1417
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-236 |
5.44e-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: 52.64 E-value: 5.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQpGI------------KIGYLPQEPQLNpEHTVRE 88
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIID-GLniakiglhdlrfKITIIPQDPVLF-SGSLRM 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 89 SVEEavsevvnalkgldevYAKYAEpdadfdklaaqqgkyEEIIQAHDGHNLNVQLERAADALrlpdwDAKIA----NLS 164
Cdd:TIGR00957 1379 NLDP---------------FSQYSD---------------EEVWWALELAHLKTFVSALPDKL-----DHECAeggeNLS 1423
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489953208 165 GGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLH-DFEG-TVVAITHDryfLDNVAGW--ILELDRGE 236
Cdd:TIGR00957 1424 VGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRtQFEDcTVLTIAHR---LNTIMDYtrVIVLDKGE 1496
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
321-507 |
7.39e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.80 E-value: 7.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 321 DKVVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGqeQPdSGSITLGETVklasvdqFRDAMDN 400
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HP-AYKILEGDIL-------FKGESIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 401 SKTVWEEVSGGL--------DIMRIGNTEMPSRAYVGRFNFKGTDQ------------------------GKRVGE-LSG 447
Cdd:CHL00131 75 DLEPEERAHLGIflafqypiEIPGVSNADFLRLAYNSKRKFQGLPEldplefleiineklklvgmdpsflSRNVNEgFSG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489953208 448 GERGRLHLAKLLQVGGNVLLLDEPTNDLDIETLRALE---NALLEFPGCAMVISHDRWFLDRI 507
Cdd:CHL00131 155 GEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAegiNKLMTSENSIILITHYQRLLDYI 217
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
22-197 |
8.17e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.87 E-value: 8.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE-----------ARPQpgikIGYLPQEPQLNPEHTVRESv 90
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNiyykncninniAKPY----CTYIGHNLGLKLEMTVFEN- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 91 eeavsevvnaLKGLDEVYAKyaepdadfdklaaqqgkyEEIIQAhdghnlnvqlerAADALRLPDW-DAKIANLSGGERR 169
Cdd:PRK13541 91 ----------LKFWSEIYNS------------------AETLYA------------AIHYFKLHDLlDEKCYSLSSGMQK 130
|
170 180
....*....|....*....|....*...
gi 489953208 170 RVALCRLLLEKPDMLLLDEPTNHLDAES 197
Cdd:PRK13541 131 IVAIARLIACQSDLWLLDEVETNLSKEN 158
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-249 |
9.72e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.09 E-value: 9.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 17 PKRhILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGiDTDIEgEARPQPGIKIGYLPQEPQ-LNPehTVRESV----E 91
Cdd:PTZ00243 672 PKV-LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLS-QFEIS-EGRVWAERSIAYVPQQAWiMNA--TVRGNIlffdE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 92 EAVSEVVNALKgldevyakYAEPDADFDKLAAqqGKYEEIIQahdghnlnvqleraadalrlpdwdaKIANLSGGERRRV 171
Cdd:PTZ00243 747 EDAARLADAVR--------VSQLEADLAQLGG--GLETEIGE-------------------------KGVNLSGGQKARV 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 172 ALCRLLLEKPDMLLLDEPTNHLDAEsVAwlERFLHD-FEG-----TVVAITHDRYFLDNvAGWILELDRGEgIPWEGNYS 245
Cdd:PTZ00243 792 SLARAVYANRDVYLLDDPLSALDAH-VG--ERVVEEcFLGalagkTRVLATHQVHVVPR-ADYVVALGDGR-VEFSGSSA 866
|
....
gi 489953208 246 SWLE 249
Cdd:PTZ00243 867 DFMR 870
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
339-380 |
1.09e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 51.43 E-value: 1.09e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 489953208 339 IDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSI 380
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV 81
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
323-499 |
1.13e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 51.36 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 323 VVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSG-------------QEQP-DSGSITLGETVKL 388
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyphgtwdgeiywSGSPlKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 389 ASVDQfRDAMDNSKTVWEEVSGGLDIM----RIGNTEMPSRAY--VGRFNFKGTDQGKRVGELSGGERGRLHLAKLLQVG 462
Cdd:TIGR02633 81 VIIHQ-ELTLVPELSVAENIFLGNEITlpggRMAYNAMYLRAKnlLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489953208 463 GNVLLLDEPTNDLDIETLRALENAL--LEFPGCAMV-ISH 499
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIrdLKAHGVACVyISH 199
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
17-198 |
1.22e-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: 49.18 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI---DTDIEG----------EARPQPGIKIGYLPQEPQLNPE 83
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegNVSVEGdihyngipykEFAEKYPGEIIYVSEEDVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 84 HTVRESVEEAVSevvnaLKGldevyakyaepdadfdklaaqqgkyeeiiqahdghnlnvqleraadalrlpdwDAKIANL 163
Cdd:cd03233 98 LTVRETLDFALR-----CKG-----------------------------------------------------NEFVRGI 119
|
170 180 190
....*....|....*....|....*....|....*
gi 489953208 164 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESV 198
Cdd:cd03233 120 SGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTA 154
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-477 |
1.37e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.88 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEarpqpgikIGYLPQEPQLnpeHTVRESVEEAVSEVVNAL 101
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGS--------ILFQGKEIDF---KSSKEALENGISMVHQEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 102 KG------LDEVY-AKYAE--PDADFDKLaaqqgkYEEIIQAHDGHNLNVqleraadalrlpDWDAKIANLSGGERRRVA 172
Cdd:PRK10982 83 NLvlqrsvMDNMWlGRYPTkgMFVDQDKM------YRDTKAIFDELDIDI------------DPRAKVATLSVSQMQMIE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 173 LCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEgtvvaithdryfldnvagwilelDRGEGIPwegnYSSWLEQKD 252
Cdd:PRK10982 145 IAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLK-----------------------ERGCGIV----YISHKMEEI 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 253 QRLAQEASqeaarrksIEKELEWVR-QGAKGRQSKGKARLARFEELNNTEYQKRNETNELfippgarlgdkVVEVTNLrk 331
Cdd:PRK10982 198 FQLCDEIT--------ILRDGQWIAtQPLAGLTMDKIIAMMVGRSLTQRFPDKENKPGEV-----------ILEVRNL-- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 332 SYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDqfrDAMDNS-KTVWEE-- 407
Cdd:PRK10982 257 TSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLhGKKINNHNAN---EAINHGfALVTEErr 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 408 ---VSGGLDI--------MR--------IGNTEMPS--RAYVGRFNFKGTDQGKRVGELSGGERGRLHLAKLLQVGGNVL 466
Cdd:PRK10982 334 stgIYAYLDIgfnslisnIRnyknkvglLDNSRMKSdtQWVIDSMRVKTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEIL 413
|
490
....*....|.
gi 489953208 467 LLDEPTNDLDI 477
Cdd:PRK10982 414 MLDEPTRGIDV 424
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
324-499 |
1.52e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 50.87 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSY-GDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSI--------TLGETV---KLASV 391
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIrldgrplsSLSHSVlrqGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 392 DQfrDAMDNSKTVWEEVSGGLDIMRIG---NTEMPSRAYVGRfnfkGTDQG--KRVGE----LSGGERGRLHLAKLLQVG 462
Cdd:PRK10790 421 QQ--DPVVLADTFLANVTLGRDISEEQvwqALETVQLAELAR----SLPDGlyTPLGEqgnnLSVGQKQLLALARVLVQT 494
|
170 180 190
....*....|....*....|....*....|....*....
gi 489953208 463 GNVLLLDEPTNDLDIETLRALENALLEFPGCA--MVISH 499
Cdd:PRK10790 495 PQILILDEATANIDSGTEQAIQQALAAVREHTtlVVIAH 533
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
320-500 |
1.84e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 49.96 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 320 GDKVVEVTNLRKSY--------GDRVL--IDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKL 388
Cdd:PRK11308 2 QQPLLQAIDLKKHYpvkrglfkPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYqGQDLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 389 ASVDQFRD--------------AMDNSKTVWEEVSGGLDImrigNTEMPS-------RAYVGRFNFKgTDQGKRVGEL-S 446
Cdd:PRK11308 82 ADPEAQKLlrqkiqivfqnpygSLNPRKKVGQILEEPLLI----NTSLSAaerrekaLAMMAKVGLR-PEHYDRYPHMfS 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 447 GGERGRLHLAKLLQVGGNVLLLDEPTNDLDIeTLRALENALL-----EFpGCAMV-ISHD 500
Cdd:PRK11308 157 GGQRQRIAIARALMLDPDVVVADEPVSALDV-SVQAQVLNLMmdlqqEL-GLSYVfISHD 214
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
336-476 |
2.39e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.55 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 336 RVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETVklASVDQFRDAM-----DNSKTVWEEVSG 410
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSI--AYVPQQAWIMnatvrGNILFFDEEDAA 750
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489953208 411 GL-DIMRIGNTEMPSRAYVGRFNfkgTDQGKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLD 476
Cdd:PTZ00243 751 RLaDAVRVSQLEADLAQLGGGLE---TEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
22-194 |
2.42e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 49.58 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE--------ARPQPGI------KIGYLPQEP--QLNPEHT 85
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGElyyqgqdlLKADPEAqkllrqKIQIVFQNPygSLNPRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 86 VRESVEEAVseVVNAlkgldevyakyaepdadfdKLAAQQGKyeeiiqahdghnlnvqlERAAD-----ALRLPDWDAKI 160
Cdd:PRK11308 111 VGQILEEPL--LINT-------------------SLSAAERR-----------------EKALAmmakvGLRPEHYDRYP 152
|
170 180 190
....*....|....*....|....*....|....
gi 489953208 161 ANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 194
Cdd:PRK11308 153 HMFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
295-516 |
2.51e-06 |
|
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: 50.78 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 295 EELNNTEYQKrnETNELFIP---PGARLGDKVVEVTNLRKSYGdRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSG 371
Cdd:TIGR01257 902 EEMEDPEHPE--GINDSFFErelPGLVPGVCVKNLVKIFEPSG-RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTG 978
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 372 QEQPDSGSITLGETVKLASVDQFRDAMD---------NSKTV--------------WEEVSGGLDIMrIGNTEMPSRayv 428
Cdd:TIGR01257 979 LLPPTSGTVLVGGKDIETNLDAVRQSLGmcpqhnilfHHLTVaehilfyaqlkgrsWEEAQLEMEAM-LEDTGLHHK--- 1054
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 429 grfnfkgtdQGKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIETLRALENALLEFPGCAMVIshdrwfldrIA 508
Cdd:TIGR01257 1055 ---------RNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTII---------MS 1116
|
....*...
gi 489953208 509 THILDYQD 516
Cdd:TIGR01257 1117 THHMDEAD 1124
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
324-490 |
2.63e-06 |
|
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: 48.48 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYG-DRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGEtvKLASVDQFRDAMDNSK 402
Cdd:cd03290 1 VQVTNGYFSWGsGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSN--KNESEPSFEATRSRNR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 403 ---------------TVWEEVSGG--------------------LDIMRIGNTempsrayvgrfnfkgTDQGKRVGELSG 447
Cdd:cd03290 79 ysvayaaqkpwllnaTVEENITFGspfnkqrykavtdacslqpdIDLLPFGDQ---------------TEIGERGINLSG 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489953208 448 GERGRLHLAKLLQVGGNVLLLDEPTNDLDIE-TLRALENALLEF 490
Cdd:cd03290 144 GQRQRICVARALYQNTNIVFLDDPFSALDIHlSDHLMQEGILKF 187
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-198 |
2.64e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.41 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIdtdiegeARPQPG--------IKIGYLPQEPQL---------NPE 83
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGL-------LNPEKGeilferqsIKKDLCTYQKQLcfvghrsgiNPY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 84 HTVRESVEEAVSEVVNALkGLDEVYAKYaepdadfdKLaaqqgkyeeiiqahdGHNLnvqleraadalrlpdwDAKIANL 163
Cdd:PRK13540 89 LTLRENCLYDIHFSPGAV-GITELCRLF--------SL---------------EHLI----------------DYPCGLL 128
|
170 180 190
....*....|....*....|....*....|....*
gi 489953208 164 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESV 198
Cdd:PRK13540 129 SSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSL 163
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
19-214 |
2.69e-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: 50.10 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIdtdiegearpqpgikigYLPQEPQ-LNPEHTVRESVeeavsev 97
Cdd:TIGR02203 345 RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRF-----------------YEPDSGQiLLDGHDLADYT------- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 98 vnalkgLDEVYAKYAEPDAD---FDKLAAQQGKYEEIIQAHDGhnlnvQLERAADAL-------RLPD-WDAKI----AN 162
Cdd:TIGR02203 401 ------LASLRRQVALVSQDvvlFNDTIANNIAYGRTEQADRA-----EIERALAAAyaqdfvdKLPLgLDTPIgengVL 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489953208 163 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDFEGTVVA 214
Cdd:TIGR02203 470 LSGGQRQRLAIARALLKDAPILILDEATSALDNESerlvQAALERLMQGRTTLVIA 525
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
20-226 |
2.72e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 49.08 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEarpqpgIKIGYLPQEPQLNPEHTVRESVEEAVSEVVN 99
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGR------ILFDGKPIDYSRKGLMKLRESVGMVFQDPDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 100 ALkgldevYAKYAEPDADFDKLAAQQGKYEeiIQAHDGHnlnvQLERAADAlrlPDWDAKIANLSGGERRRVALCRLLLE 179
Cdd:PRK13636 94 QL------FSASVYQDVSFGAVNLKLPEDE--VRKRVDN----ALKRTGIE---HLKDKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489953208 180 KPDMLLLDEPTNHLD----AESVAWLERFLHDFEGTVVAITHDryfLDNVA 226
Cdd:PRK13636 159 EPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHD---IDIVP 206
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
13-241 |
2.78e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 49.24 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 13 KVVPPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----DTDIEGEARPQPGIK-----------IGYLPQ 76
Cdd:PRK13645 18 KKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiisetGQTIVGDYAIPANLKkikevkrlrkeIGLVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 77 EPQLnpeHTVRESVEEAVS-EVVNALKGLDEVYAKYAEpdadfdklaaqqgkyeeiiqahdghnlnvqlerAADALRLPD 155
Cdd:PRK13645 98 FPEY---QLFQETIEKDIAfGPVNLGENKQEAYKKVPE---------------------------------LLKLVQLPE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 156 WDAKIA--NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDFEGTVVAITHDRYFLDNVAGWI 229
Cdd:PRK13645 142 DYVKRSpfELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGeedfINLFERLNKEYKKRIIMVTHNMDQVLRIADEV 221
|
250
....*....|....*.
gi 489953208 230 LELDRGE----GIPWE 241
Cdd:PRK13645 222 IVMHEGKvisiGSPFE 237
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
313-479 |
2.82e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 49.73 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 313 IPPGARlgdKVVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAG--KSTLFRMMSGqeqPDSGSITLGETVKLAS 390
Cdd:NF000106 6 ISNGAR---NAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWRF*TWCAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 391 VDQFRDAMDNSKTV----WEEVSGGLDIMRIGNTEMPSRA--------YVGRFNFKGTdQGKRVGELSGGERGRLHLAKL 458
Cdd:NF000106 80 RRALRRTIG*HRPVr*grRESFSGRENLYMIGR*LDLSRKdararadeLLERFSLTEA-AGRAAAKYSGGMRRRLDLAAS 158
|
170 180
....*....|....*....|.
gi 489953208 459 LQVGGNVLLLDEPTNDLDIET 479
Cdd:NF000106 159 MIGRPAVLYLDEPTTGLDPRT 179
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
9-217 |
2.93e-06 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 49.41 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 9 HRVGKVVP-PKRHI--LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE------------------ARPQp 67
Cdd:PRK11153 5 KNISKVFPqGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRvlvdgqdltalsekelrkARRQ- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 68 gikIGYLPQEPQLNPEHTVRESV----------EEAVSEVVNALkgLDEVyakyaepdadfdKLAAQQGKYeeiiqahdg 137
Cdd:PRK11153 84 ---IGMIFQHFNLLSSRTVFDNValplelagtpKAEIKARVTEL--LELV------------GLSDKADRY--------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 138 hnlnvqleraadalrlPdwdakiANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE---SV-AWLERFLHDFEGTVV 213
Cdd:PRK11153 138 ----------------P------AQLSGGQKQRVAIARALASNPKVLLCDEATSALDPAttrSIlELLKDINRELGLTIV 195
|
....
gi 489953208 214 AITH 217
Cdd:PRK11153 196 LITH 199
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
330-476 |
2.94e-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: 48.03 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 330 RKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPD---SGSITL-GETVKLASVDQFRDAMDNSktvw 405
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYnGIPYKEFAEKYPGEIIYVS---- 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489953208 406 EEvsgglDImrigntEMPSRAyVGR-FNFKGTDQGKR-VGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLD 476
Cdd:cd03233 90 EE-----DV------HFPTLT-VREtLDFALRCKGNEfVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-218 |
3.09e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 48.94 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 1 MAQFVYTMHRVGKVVppkrhiLKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQPGI----------- 69
Cdd:PRK14271 22 MAAVNLTLGFAGKTV------LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLlggrsifnyrd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 70 ------KIGYLPQEPQLNPehtvresveeaVSEVVNALKGldeVYAKYAEPDADFDKLAaqQGKYEEIiqahdghnlnvq 143
Cdd:PRK14271 96 vlefrrRVGMLFQRPNPFP-----------MSIMDNVLAG---VRAHKLVPRKEFRGVA--QARLTEV------------ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489953208 144 leRAADAL--RLPDWDAKianLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEG--TVVAITHD 218
Cdd:PRK14271 148 --GLWDAVkdRLSDSPFR---LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHN 221
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
9-217 |
3.22e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 48.86 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 9 HRVGKVVPPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEarpqpgIKIGylpqepqlnpEHTVRE 88
Cdd:PRK13634 10 HRYQYKTPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGT------VTIG----------ERVITA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 89 SVEEavsevvNALKGL-DEVYAKYAEPDADFdklaaqqgkYEEIIQ---AHDGHNLNVQ----LERAADALRLPDWDAKI 160
Cdd:PRK13634 74 GKKN------KKLKPLrKKVGIVFQFPEHQL---------FEETVEkdiCFGPMNFGVSeedaKQKAREMIELVGLPEEL 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489953208 161 A-----NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA----ESVAWLERfLHDFEG-TVVAITH 217
Cdd:PRK13634 139 LarspfELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPkgrkEMMEMFYK-LHKEKGlTTVLVTH 204
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
163-226 |
3.38e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 48.97 E-value: 3.38e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489953208 163 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERF---LHDFEGTVVAITHdryFLDNVA 226
Cdd:PRK13649 146 LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLfkkLHQSGMTIVLVTH---LMDDVA 209
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
163-238 |
3.79e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 48.67 E-value: 3.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 163 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEG---TVVAITHDryfLDNVAGW---ILELDRGE 236
Cdd:PRK13641 146 LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaghTVILVTHN---MDDVAEYaddVLVLEHGK 222
|
..
gi 489953208 237 GI 238
Cdd:PRK13641 223 LI 224
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
22-218 |
3.89e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 48.62 E-value: 3.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 22 LKNISLSFfPGAKI-GVLGLNGAGKSTLLRIMAGIDTDIEGeARPQPgiKIGYLPQE---PQLNPEHtVRESVeeavsev 97
Cdd:PRK14243 26 VKNVWLDI-PKNQItAFIGPSGCGKSTILRCFNRLNDLIPG-FRVEG--KVTFHGKNlyaPDVDPVE-VRRRI------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 98 vnalkGLdeVYAK-YAEPDADFDKLAaqqgkYEEIIQAHDGhNLNVQLERAADALRLpdWDA---KI----ANLSGGERR 169
Cdd:PRK14243 94 -----GM--VFQKpNPFPKSIYDNIA-----YGARINGYKG-DMDELVERSLRQAAL--WDEvkdKLkqsgLSLSGGQQQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489953208 170 RVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EGTVVAITHD 218
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELkeQYTIIIVTHN 209
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
160-223 |
3.95e-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: 47.99 E-value: 3.95e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489953208 160 IANLSGGERR------RVALCRLLLEKPDMLLLDEPTNHLDAESVAW-----LERFLHDFEGTVVAITHDRYFLD 223
Cdd:cd03240 113 RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEEslaeiIEERKSQKNFQLIVITHDEELVD 187
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
22-241 |
4.39e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 48.55 E-value: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEArpqpgikigYLPQEPQLNPEHT--VRESVEEAVSEVVN 99
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKV---------YVDGLDTSDEENLwdIRNKAGMVFQNPDN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 100 alkgldEVYAKYAEPDADF--DKLAAQQgkyEEIiqahdghnlnvqLERAADAL-RLPDWDAKIAN---LSGGERRRVAL 173
Cdd:PRK13633 97 ------QIVATIVEEDVAFgpENLGIPP---EEI------------RERVDESLkKVGMYEYRRHAphlLSGGQKQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489953208 174 CRLLLEKPDMLLLDEPTNHLDA----ESVAWLERFLHDFEGTVVAITHdryFLDNV--AGWILELDRG----EGIPWE 241
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPsgrrEVVNTIKELNKKYGITIILITH---YMEEAveADRIIVMDSGkvvmEGTPKE 230
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
339-520 |
5.49e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 48.24 E-value: 5.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 339 IDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGE-TV--------------KLASVDQFRDAMDNSKT 403
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDiTIthktkdkyirpvrkRIGMVFQFPESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 404 VWEEVSGGLDIMRIGNTEMPSRAY--VGRFNFKGTDQGKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLD----I 477
Cdd:PRK13646 103 VEREIIFGPKNFKMNLDEVKNYAHrlLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDpqskR 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489953208 478 ETLRALENALLEFPGCAMVISHDrwfLDRIAThildYQDEGKV 520
Cdd:PRK13646 183 QVMRLLKSLQTDENKTIILVSHD---MNEVAR----YADEVIV 218
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
22-236 |
6.12e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.81 E-value: 6.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEArpqpgikigYLPQEPqlnpehtVRESVEEAVSEVVNAL 101
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI---------LLDGKP-------VTAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 102 kgLDEVYAkyaepdadFDKLAAQQGKY--EEIIQAhdghnlnvQLER--AADALRLPDWdaKIAN--LSGGERRRVALCR 175
Cdd:PRK10522 403 --FTDFHL--------FDQLLGPEGKPanPALVEK--------WLERlkMAHKLELEDG--RISNlkLSKGQKKRLALLL 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489953208 176 LLLEKPDMLLLDE------PtnHLDAESVAWLERFLHDFEGTVVAITHDRYFLDNvAGWILELDRGE 236
Cdd:PRK10522 463 ALAEERDILLLDEwaadqdP--HFRREFYQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQ 526
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
323-485 |
7.35e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 47.67 E-value: 7.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 323 VVEVTNLRKSYGDRV-LIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-----GETVKLASVDQ--- 393
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVsgidtGDFSKLQGIRKlvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 394 --FRDAMDN--SKTVWEEVSGGLDIMRIGNTEMPSRAYVGRFNFK-GTDQGKRVGELSGGERGRLHLAKLLQVGGNVLLL 468
Cdd:PRK13644 81 ivFQNPETQfvGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGlEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170
....*....|....*...
gi 489953208 469 DEPTNDLDIETLRA-LEN 485
Cdd:PRK13644 161 DEVTSMLDPDSGIAvLER 178
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
321-500 |
1.06e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 47.80 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 321 DKVVEVTNLRKSY----GDRVLIDDLTFSVPKGAIVGIIGPNGAGKS-TLFRMM---------------SGQE------- 373
Cdd:PRK09473 10 DALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMgllaangriggsatfNGREilnlpek 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 374 --------------QPDSGSIT----LGEtvKLASVDQFRDAMDNSkTVWEEVSGGLDIMRignteMP-SRayvgrfnfk 434
Cdd:PRK09473 90 elnklraeqismifQDPMTSLNpymrVGE--QLMEVLMLHKGMSKA-EAFEESVRMLDAVK-----MPeAR--------- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489953208 435 gtdqgKRVG----ELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLDIeTLRALENALL-----EFPGCAMVISHD 500
Cdd:PRK09473 153 -----KRMKmyphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDV-TVQAQIMTLLnelkrEFNTAIIMITHD 221
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
324-485 |
1.18e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 47.39 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 324 VEVTNLRKSYGDRV-----LIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSI------------------ 380
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 381 ---------TLGETVKLAS--------VDQFRDAMDNSKTVWEEVSGGLDIMRIGNTEMPSRA------------YVGRF 431
Cdd:PRK13651 83 vleklviqkTRFKKIKKIKeirrrvgvVFQFAEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAakyielvgldesYLQRS 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489953208 432 NFkgtdqgkrvgELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLD----IETLRALEN 485
Cdd:PRK13651 163 PF----------ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgvKEILEIFDN 210
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
339-500 |
1.57e-05 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 47.34 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 339 IDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLASVDQFRD-------------AMDNSKTV 404
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIdGVDIAKISDAELREvrrkkiamvfqsfALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 405 WEEVSGGLDIMRIGNTEMPSRAYvgrfnfkgtDQGKRVG----------ELSGGERGRLHLAKLLQVGGNVLLLDEPTND 474
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKAL---------DALRQVGlenyahsypdELSGGMRQRVGLARALAINPDILLMDEAFSA 194
|
170 180 190
....*....|....*....|....*....|
gi 489953208 475 LDIETLRALENALLEFPG----CAMVISHD 500
Cdd:PRK10070 195 LDPLIRTEMQDELVKLQAkhqrTIVFISHD 224
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
336-500 |
1.61e-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: 45.43 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 336 RVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMsgqeqpdsGSITLGETVKLASVDQFRdAMDNSKTVweevSGGLDIM 415
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAI--------GLALGGAQSATRRRSGVK-AGCIVAAV----SAELIFT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 416 RIGntempsrayvgrfnfkgtdqgkrvgeLSGGERGRLHLAKLLQ----VGGNVLLLDEPTNDLDIETLRALENALLEF- 490
Cdd:cd03227 75 RLQ--------------------------LSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQALAEAILEHl 128
|
170
....*....|..
gi 489953208 491 -PGC-AMVISHD 500
Cdd:cd03227 129 vKGAqVIVITHL 140
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
120-223 |
2.31e-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: 44.67 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 120 KLAAQQGKYEEIIQAHDGhnlNVQLERAADALRLPDWDAKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVA 199
Cdd:smart00382 21 ALARELGPPGGGVIYIDG---EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEA 97
|
90 100 110
....*....|....*....|....*....|...
gi 489953208 200 WL---------ERFLHDFEGTVVAITHDRYFLD 223
Cdd:smart00382 98 LLllleelrllLLLKSEKNLTVILTTNDEKDLG 130
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
16-236 |
2.34e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 46.19 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLR-------------IMAGID-TDIE---GEARPQPGIKIGYlpqep 78
Cdd:PRK13637 17 PFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQhlngllkptsgkiIIDGVDiTDKKvklSDIRKKVGLVFQY----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 79 qlnPEHTV-RESVEEAVSEVVNALkGLDEvyakyaepdadfdklaaqqgkyEEIiqahdghnlNVQLERAADALRLPDWD 157
Cdd:PRK13637 92 ---PEYQLfEETIEKDIAFGPINL-GLSE----------------------EEI---------ENRVKRAMNIVGLDYED 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 158 AKIAN---LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA---ESVAWLERFLHD-FEGTVVAITHDRYFLDNVAGWIL 230
Cdd:PRK13637 137 YKDKSpfeLSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPkgrDEILNKIKELHKeYNMTIILVSHSMEDVAKLADRII 216
|
....*.
gi 489953208 231 ELDRGE 236
Cdd:PRK13637 217 VMNKGK 222
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
162-226 |
3.33e-05 |
|
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: 44.49 E-value: 3.33e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489953208 162 NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE----SVAWLERFLHDFEGTVVAITHDRYFLDNVA 226
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnAARAIRRLSEEGKKTALVVEHDLAVLDYLS 139
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
24-218 |
3.55e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 45.89 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 24 NISLSFFPGAKIGVLGLNGAGKS-TLLRIMAGID--------------TDI----EGEARPQPGIKIGYLPQEP--QLNP 82
Cdd:PRK11022 25 RISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDypgrvmaeklefngQDLqrisEKERRNLVGAEVAMIFQDPmtSLNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 83 EHTVRESVEEAvsevvnalkgldevyakyaepdadfdklaaqqgkyeeiIQAHDGHNLNVQLERAADALRL---PDWDAK 159
Cdd:PRK11022 105 CYTVGFQIMEA--------------------------------------IKVHQGGNKKTRRQRAIDLLNQvgiPDPASR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489953208 160 IAN----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEG----TVVAITHD 218
Cdd:PRK11022 147 LDVyphqLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkenmALVLITHD 213
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
21-223 |
4.21e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 45.40 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-----------------IdTDIEGEARPQPGIKIGYlpQEPqlnpe 83
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpaykilegdilfkgesI-LDLEPEERAHLGIFLAF--QYP----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 84 htvresVEeaVSEVVNalkgldevyakyaepdADFDKLA-----AQQGKYE-------EIIQahdghnlnvqleraaDAL 151
Cdd:CHL00131 94 ------IE--IPGVSN----------------ADFLRLAynskrKFQGLPEldpleflEIIN---------------EKL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 152 RLPDWDAKIAN------LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF---EGTVVAITHDRYFL 222
Cdd:CHL00131 135 KLVGMDPSFLSrnvnegFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLmtsENSIILITHYQRLL 214
|
.
gi 489953208 223 D 223
Cdd:CHL00131 215 D 215
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
159-238 |
4.41e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 44.24 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 159 KIANLSGGERRRVALCRLLLE--KPDMLLLDEPTNHLDAESvawLERFLHDFEG------TVVAITHDRYFLDNvAGWIL 230
Cdd:cd03238 84 KLSTLSGGELQRVKLASELFSepPGTLFILDEPSTGLHQQD---INQLLEVIKGlidlgnTVILIEHNLDVLSS-ADWII 159
|
....*...
gi 489953208 231 ELDRGEGI 238
Cdd:cd03238 160 DFGPGSGK 167
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
22-218 |
4.68e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 45.26 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 22 LKNISLSFfPGAKIGVL-GLNGAGKSTLLRIMAGIDTDIEGEAR--PQPGIK------IGYLPQEPQlnpehtVRESVEE 92
Cdd:PRK15056 23 LRDASFTV-PGGSIAALvGVNGSGKSTLFKALMGFVRLASGKISilGQPTRQalqknlVAYVPQSEE------VDWSFPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 93 AVSEVVnalkgldevyakyaepdadfdklaaQQGKYEE-----IIQAHDGHNLNVQLERAaDALRLPDwdAKIANLSGGE 167
Cdd:PRK15056 96 LVEDVV-------------------------MMGRYGHmgwlrRAKKRDRQIVTAALARV-DMVEFRH--RQIGELSGGQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489953208 168 RRRVALCRLLLEKPDMLLLDEPTNHLDAESVAW---LERFLHDFEGTVVAITHD 218
Cdd:PRK15056 148 KKRVFLARAIAQQGQVILLDEPFTGVDVKTEARiisLLRELRDEGKTMLVSTHN 201
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
22-213 |
5.02e-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: 44.35 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE--------ARPQPG----IKIGYLPQEPQ---LNPEHTV 86
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEitldgkpvTRRSPRdairAGIAYVPEDRKregLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 87 REsveeavsevvnalkgldevyakyaepdadfdklaaqqgkyeeiiqahdghNLNvqleraadalrLPDWdakianLSGG 166
Cdd:cd03215 96 AE--------------------------------------------------NIA-----------LSSL------LSGG 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489953208 167 ERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EGTVV 213
Cdd:cd03215 109 NQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELadAGKAV 157
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
14-194 |
5.05e-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: 45.97 E-value: 5.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 14 VVPPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-DTDIEGEA----------RPQPGIKIGYLpqepqLNP 82
Cdd:TIGR02633 268 VINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVfingkpvdirNPAQAIRAGIA-----MVP 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 83 EHTVRESVEEAVSEVVNALKGLDEVYAKYAEPDAdfdklAAQQGKYEEIIQahdghnlnvQLERAADALRLPdwdakIAN 162
Cdd:TIGR02633 343 EDRKRHGIVPILGVGKNITLSVLKSFCFKMRIDA-----AAELQIIGSAIQ---------RLKVKTASPFLP-----IGR 403
|
170 180 190
....*....|....*....|....*....|..
gi 489953208 163 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 194
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
341-518 |
5.20e-05 |
|
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: 44.91 E-value: 5.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 341 DLTFSVPKGAIVGIIGPNGAGKSTLF----------RMMSGQEQPDS-GSITLGETV-KLASVDQ-------------FR 395
Cdd:cd03271 13 NIDVDIPLGVLTCVTGVSGSGKSSLIndtlypalarRLHLKKEQPGNhDRIEGLEHIdKVIVIDQspigrtprsnpatYT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 396 DAMDNSKTVWEEVSGG-------LDIMRIGNT-----EMPsrAYVGRFNFKGTDQGKR-------VG-----------EL 445
Cdd:cd03271 93 GVFDEIRELFCEVCKGkrynretLEVRYKGKSiadvlDMT--VEEALEFFENIPKIARklqtlcdVGlgyiklgqpatTL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 446 SGGERGRLHLAKLLQ---VGGNVLLLDEPTNDL---DIETLRALENALLEFPGCAMVISHDrwfLD--RIATHILDYQDE 517
Cdd:cd03271 171 SGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLhfhDVKKLLEVLQRLVDKGNTVVVIEHN---LDviKCADWIIDLGPE 247
|
.
gi 489953208 518 G 518
Cdd:cd03271 248 G 248
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
328-488 |
7.45e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.09 E-value: 7.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 328 NLRKSYGDRVLIDdLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSI--------------------TLGETVK 387
Cdd:PRK13541 6 QLQFNIEQKNLFD-LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIyykncninniakpyctyighNLGLKLE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 388 LASVDQFRdamdnsktVWEEVSGGLDIMrigntempsraYVGRFNFKGTD-QGKRVGELSGGERGRLHLAKLLQVGGNVL 466
Cdd:PRK13541 85 MTVFENLK--------FWSEIYNSAETL-----------YAAIHYFKLHDlLDEKCYSLSSGMQKIVAIARLIACQSDLW 145
|
170 180
....*....|....*....|..
gi 489953208 467 LLDEPTNDLDIETlRALENALL 488
Cdd:PRK13541 146 LLDEVETNLSKEN-RDLLNNLI 166
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
163-226 |
7.65e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 44.77 E-value: 7.65e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489953208 163 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFE----GTVVAITHDryfLDNVA 226
Cdd:PRK13646 146 MSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdenKTIILVSHD---MNEVA 210
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
339-381 |
7.98e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.42 E-value: 7.98e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 489953208 339 IDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSIT 381
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD 82
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
312-395 |
1.04e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 44.96 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 312 FIPPGARLGDKVVEVTNLRKSYGDRVL-IDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL-GETVKLA 389
Cdd:PRK10522 311 FPRPQAFPDWQTLELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLdGKPVTAE 390
|
....*.
gi 489953208 390 SVDQFR 395
Cdd:PRK10522 391 QPEDYR 396
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
35-218 |
1.42e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 43.08 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 35 IGVLGLNGAGKSTLLRimaGIDTDIEGEARPQPGIkigylpqepqlnPEHTVRESVEEAVSEVVNALKGldEVYaKYAEP 114
Cdd:COG0419 26 NLIVGPNGAGKSTILE---AIRYALYGKARSRSKL------------RSDLINVGSEEASVELEFEHGG--KRY-RIERR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 115 DADFDKLAAQQGK--------------YEEIIQahDGHNLNVQLERAADAL------------RLPDWDAkIANLSGGER 168
Cdd:COG0419 88 QGEFAEFLEAKPSerkealkrllgleiYEELKE--RLKELEEALESALEELaelqklkqeilaQLSGLDP-IETLSGGER 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489953208 169 RRVALCRLLlekpdMLLLDepTNHLDAESvawLERFLHDFEGTVVaITHD 218
Cdd:COG0419 165 LRLALADLL-----SLILD--FGSLDEER---LERLLDALEELAI-ITHV 203
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
19-218 |
1.66e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 43.38 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGidtdiegEARPQPGiKIGYLPQEPQLNPEHTVRESVEEAVSE-- 96
Cdd:PRK11701 19 RKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSA-------RLAPDAG-EVHYRMRDGQLRDLYALSEAERRRLLRte 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 97 --VV--NALKGLD-EVYA--KYAEPdadfdkLAAQQGKYEEIIQAHDGHNL-NVQLeraaDALRLPDwdaKIANLSGGER 168
Cdd:PRK11701 91 wgFVhqHPRDGLRmQVSAggNIGER------LMAVGARHYGDIRATAGDWLeRVEI----DAARIDD---LPTTFSGGMQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489953208 169 RRVALCRLLLEKPDMLLLDEPTNHLDAeSVA-----WLERFLHDFEGTVVAITHD 218
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLDV-SVQarlldLLRGLVRELGLAVVIVTHD 211
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
163-241 |
1.89e-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: 44.23 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 163 LSGGERRRVALCRLLLEK---PDMLLLDEPTNHLDAESVAWLERFLH---DFEGTVVAITHDryfLD--NVAGWILEL-- 232
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQrlvDKGNTVVVIEHN---LDviKTADYIIDLgp 906
|
90
....*....|....*..
gi 489953208 233 ---DRG-----EGIPWE 241
Cdd:TIGR00630 907 eggDGGgtvvaSGTPEE 923
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
328-523 |
1.97e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 43.71 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 328 NLRKSYGDRVLidDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITLGETVkLASVDQ-------------- 393
Cdd:PRK11144 5 NFKQQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRV-LFDAEKgiclppekrrigyv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 394 FRDA---------------MDNSKTV-WEEVSGGLDImrigntempsRAYVGRFNfkgtdqgkrvGELSGGERGRLHLAK 457
Cdd:PRK11144 82 FQDArlfphykvrgnlrygMAKSMVAqFDKIVALLGI----------EPLLDRYP----------GSLSGGEKQRVAIGR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489953208 458 LLQVGGNVLLLDEPTNDLDI----ETLRALENALLEFPGCAMVISHDrwfLD---RIATHILdYQDEGKVEFF 523
Cdd:PRK11144 142 ALLTAPELLLMDEPLASLDLprkrELLPYLERLAREINIPILYVSHS---LDeilRLADRVV-VLEQGKVKAF 210
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
323-514 |
2.78e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.86 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 323 VVEVTNLRKSYGDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQE--QPDSGSITL--GETVKLASVDQFRDAM 398
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFkgKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 399 DNSKTVWEEVSGGLDIMRIGNTEMPSRAYVG-----RFNFKGTDQGK---------------RVGeLSGGERGRLHLAKL 458
Cdd:PRK09580 81 FMAFQYPVEIPGVSNQFFLQTALNAVRSYRGqepldRFDFQDLMEEKiallkmpedlltrsvNVG-FSGGEKKRNDILQM 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489953208 459 LQVGGNVLLLDEPTNDLDIETLRALENallefpGCAMVISHDRWFLdrIATH---ILDY 514
Cdd:PRK09580 160 AVLEPELCILDESDSGLDIDALKIVAD------GVNSLRDGKRSFI--IVTHyqrILDY 210
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
349-485 |
4.10e-04 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 43.11 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 349 GAIVGIIGPNGAGKSTL-----FRMMSGQEQpdSGSITL-GETVKL-------ASVDQFrDAMDNSKTVWEevsgglDIM 415
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLmnalaFRSPKGVKG--SGSVLLnGMPIDAkemraisAYVQQD-DLFIPTLTVRE------HLM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 416 RIGNTEMPSRAY--------------VGRFNFKGT--DQGKRVGELSGGERGRLHLAKLLQVGGNVLLLDEPTNDLD--- 476
Cdd:TIGR00955 122 FQAHLRMPRRVTkkekrervdevlqaLGLRKCANTriGVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDsfm 201
|
170
....*....|...
gi 489953208 477 ----IETLRALEN 485
Cdd:TIGR00955 202 aysvVQVLKGLAQ 214
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
334-381 |
4.71e-04 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 41.46 E-value: 4.71e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 489953208 334 GDRVLIDDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSGQEqpDSGSIT 381
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRK--TAGVIT 63
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
340-371 |
4.83e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.85 E-value: 4.83e-04
10 20 30
....*....|....*....|....*....|..
gi 489953208 340 DDLTFSVPKGAIVGIIGPNGAGKSTLFRMMSG 371
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
160-223 |
6.34e-04 |
|
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: 41.99 E-value: 6.34e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 160 IANLSGGERR---RVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFL---HDFEGTVVAITHDRYFLD 223
Cdd:pfam13304 234 AFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLkelSRNGAQLILTTHSPLLLD 303
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
331-363 |
7.40e-04 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 40.91 E-value: 7.40e-04
10 20 30
....*....|....*....|....*....|...
gi 489953208 331 KSYGDRVLIDdltfsVPKGaIVGIIGPNGAGKS 363
Cdd:cd03278 10 KSFADKTTIP-----FPPG-LTAIVGPNGSGKS 36
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
19-251 |
7.61e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 42.40 E-value: 7.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARpqpgikigyLPQEPQLNPEHTV-RESVeeavsev 97
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIR---------LDGRPLSSLSHSVlRQGV------- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 98 vnALKGLDEVYAKyaepDADFDKLAAQQGKYEEII-QAHDghnlNVQLerAADALRLPD-WDAKIA----NLSGGERRRV 171
Cdd:PRK10790 418 --AMVQQDPVVLA----DTFLANVTLGRDISEEQVwQALE----TVQL--AELARSLPDgLYTPLGeqgnNLSVGQKQLL 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 172 ALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EGTVVAITHDryfLDNV--AGWILELDRGEGIPwEGNYSSW 247
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVreHTTLVVIAHR---LSTIveADTILVLHRGQAVE-QGTHQQL 561
|
....
gi 489953208 248 LEQK 251
Cdd:PRK10790 562 LAAQ 565
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
298-392 |
7.61e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.71 E-value: 7.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 298 NNTEYQKRNE-TNELF----IPP-------GARLGD-KVVEVTNLRKSYGDRVLID---DLTFSVPKGAIVGIIGPNGAG 361
Cdd:PTZ00265 344 NITEYMKSLEaTNSLYeiinRKPlvennddGKKLKDiKKIQFKNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCG 423
|
90 100 110
....*....|....*....|....*....|.
gi 489953208 362 KSTLFRMMSGQEQPDSGSITLGETVKLASVD 392
Cdd:PTZ00265 424 KSTILKLIERLYDPTEGDIIINDSHNLKDIN 454
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
146-194 |
9.64e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.70 E-value: 9.64e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 489953208 146 RAADALRLPDWDAKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 194
Cdd:NF040905 388 RKKMNIKTPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
22-63 |
1.54e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.41 E-value: 1.54e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 489953208 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI------DTDIEGEA 63
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVtmpnkgTVDIKGSA 87
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
145-218 |
1.93e-03 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 40.79 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 145 ERAADALR----------LPDwdakiaNLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDFEG 210
Cdd:PRK10070 143 EKALDALRqvglenyahsYPD------ELSGGMRQRVGLARALAINPDILLMDEAFSALDplirTEMQDELVKLQAKHQR 216
|
....*...
gi 489953208 211 TVVAITHD 218
Cdd:PRK10070 217 TIVFISHD 224
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
21-173 |
2.27e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 21 ILKNISLSFFPGAKIgVLGLNGAGKSTLLR-IMAGIDTDIEGEA----RPQPGIKIGYLPQEPQLNPEHTVRESVEEAVS 95
Cdd:COG4717 13 KFRDRTIEFSPGLNV-IYGPNEAGKSTLLAfIRAMLLERLEKEAdelfKPQGRKPELNLKELKELEEELKEAEEKEEEYA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 96 EVVNALKGLDEvyaKYAEPDADFDKLAAQQGKYEEIIQAHDGHNLNVQLERAADAL--RLPDWDAKIANLSGGERRRVAL 173
Cdd:COG4717 92 ELQEELEELEE---ELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELpeRLEELEERLEELRELEEELEEL 168
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
24-218 |
2.61e-03 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 39.97 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 24 NISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEGearpQPGIKIGYLP-----QEPQLNPEHTVR 87
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFykptggtillrGQHIEG----LPGHQIARMGvvrtfQHVRLFREMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 88 ESVEEAVSEVVNA--LKGLDEVYA-KYAEPDAdfdklaaqqgkyeeiiqahdghnlnvqLERAA---DALRLPDWDAKIA 161
Cdd:PRK11300 99 ENLLVAQHQQLKTglFSGLLKTPAfRRAESEA---------------------------LDRAAtwlERVGLLEHANRQA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489953208 162 -NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFL----HDFEGTVVAITHD 218
Cdd:PRK11300 152 gNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIaelrNEHNVTVLLIEHD 213
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
445-518 |
2.98e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.38 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 445 LSGGERGRLHLAKLLQ---VGGNVLLLDEPTNDL---DIETLRALENALLEFPGCAMVISHDrwfLDRI--ATHILDYQD 516
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLhfdDIKKLLEVLQRLVDKGNTVVVIEHN---LDVIktADYIIDLGP 906
|
..
gi 489953208 517 EG 518
Cdd:TIGR00630 907 EG 908
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
22-225 |
3.38e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 39.99 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 22 LKNISLSFFPGakIGVL-GLNGAGKSTLLRIMAGIdtdIEGEARPQPGIKIGYLPQEPQLnPEHTVRESVEEAVSEVVNA 100
Cdd:COG3593 14 IKDLSIELSDD--LTVLvGENNSGKSSILEALRLL---LGPSSSRKFDEEDFYLGDDPDL-PEIEIELTFGSLLSRLLRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 101 LKGL---DEVYAKYAEPDADFDKLAAQqgkYEEIIQAH---DGHNLNVQLERAADA---------LRLPDWDA-KIANLS 164
Cdd:COG3593 88 LLKEedkEELEEALEELNEELKEALKA---LNELLSEYlkeLLDGLDLELELSLDEledllkslsLRIEDGKElPLDRLG 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489953208 165 GGERRRV--ALCRLLLE-----KPDMLLLDEPTNHLDAESVAWLERFLHDFEGT---VVAITHDRYFLDNV 225
Cdd:COG3593 165 SGFQRLIllALLSALAElkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKpnqVIITTHSPHLLSEV 235
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
22-62 |
3.73e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.41 E-value: 3.73e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 489953208 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE 62
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK 80
|
|
| COG4928 |
COG4928 |
Predicted P-loop ATPase, KAP-like [General function prediction only]; |
330-501 |
3.95e-03 |
|
Predicted P-loop ATPase, KAP-like [General function prediction only];
Pssm-ID: 443956 Cd Length: 386 Bit Score: 39.89 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 330 RKSYGDRV--LIDDLtfSVPKGAIVGIIGPNGAGKSTLFRMMSGQEQPDSGSITL---------GETVKLASVDQFRDAM 398
Cdd:COG4928 10 RKKYAESLanLIKSS--DADEPLVIGLDGEWGSGKTSFLNLIEKELESNEKVIVVyfnawlydgEEDLLAALLSEIAAEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 399 DNSKTVWEEVSGGL-DIMRIGNTEMPSRAYVGRFNFKGTDQGKRVGELSGGERG------RLHLAKLLQVGGN---VLLL 468
Cdd:COG4928 88 EKKKKKDKKAAKKLkKYAKRLSKLALKAGLLGGPAEAVAEALKALLKKEYKSKKksieafREELEELLKELKGkrlVVFI 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489953208 469 DeptnDLD-------IETLRALeNALLEFPGCAMVISHDR 501
Cdd:COG4928 168 D----DLDrcepdeaIEVLELI-KLFFDFPNVVFVLAFDR 202
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
331-363 |
4.23e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.04 E-value: 4.23e-03
10 20 30
....*....|....*....|....*....|...
gi 489953208 331 KSYGDRVLIDdltfsVPKGaIVGIIGPNGAGKS 363
Cdd:TIGR02168 11 KSFADPTTIN-----FDKG-ITGIVGPNGCGKS 37
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-113 |
5.07e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 39.76 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489953208 21 ILKNISLSFFPGAKIGVLGLNGAGKST-LLRIMAGIDTdIEGEARPQpGIKIG------------YLPQEPQLNpEHTVR 87
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTlLLTFMRMVEV-CGGEIRVN-GREIGayglrelrrqfsMIPQDPVLF-DGTVR 1401
|
90 100 110
....*....|....*....|....*....|..
gi 489953208 88 ESVE---EAVSEVVNA---LKGLDEVYAKYAE 113
Cdd:PTZ00243 1402 QNVDpflEASSAEVWAaleLVGLRERVASESE 1433
|
|
| |
